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Conserved domains on  [gi|1972253235|ref|NP_001379057|]
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RING-type domain-containing protein [Caenorhabditis elegans]

Protein Classification

RING finger protein 11( domain architecture ID 11613368)

RING finger protein 11 (RNF11) is an E3 ubiquitin-protein ligase that acts both as an adaptor and a modulator of itch-mediated control of ubiquitination events underlying membrane traffic

CATH:  3.30.40.10
Gene Ontology:  GO:0008270|GO:0061630
PubMed:  10673045|11007473
SCOP:  3000160

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RING-H2_RNF11 cd16468
RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 ...
94-136 3.37e-23

RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 is an E3 ubiquitin-protein ligase that acts both as an adaptor and a modulator of itch-mediated control of ubiquitination events underlying membrane traffic. It acts downstream of an enzymatic cascade for the ubiquitination of specific substrates. It is also a molecular adaptor of homologous to E6-associated protein C-terminus (HECT)-type ligases. RNF11 has been implicated in the regulation of several signaling pathways. It enhances transforming growth factor receptor (TGFR) signaling by both abrogating Smurf2-mediated receptor ubiquitination and by promoting the Smurf2-mediated degradation of AMSH (associated molecule with the SH3 domain of STAM), a de-ubiquitinating enzyme that enhances TGF-beta signaling and epidermal growth factor receptor (EGFR) endosomal recycling. It also acts directly on Smad4 to enhance Smad4 function, and plays a role in prolonged TGF-beta signaling. RNF11 also functions as a critical component of the A20 ubiquitin-editing protein complex that negatively regulates tumor necrosis factor (TNF)-mediated nuclear factor (NF)-kappaB activation. It interacts with Smad anchor for receptor activation (SARA) and the endosomal sorting complex required for transport (ESCRT)-0 complex, thus participating in the regulation of lysosomal degradation of EGFR. RNF11 acts as a novel GGA cargo actively participating in regulating the ubiquitination of the GGA protein family. RNF11 functions together with TAX1BP1 to target TANK-binding kinase 1 (TBK1)/IkappaB kinase IKKi, and further restricts antiviral signaling and type I interferon (IFN)-beta production. RNF11 contains an N-terminal PPPY motif that binds WW domain-containing proteins such as AIP4/itch, Nedd4 and Smurf1/2 (SMAD-specific E3 ubiquitin-protein ligase 1/2), and a C-terminal C3H2C3-type RING-H2 finger that functions as a scaffold for the coordinated transfer of ubiquitin to substrate proteins together with the E2 enzymes UbcH527 and Ubc13.


:

Pssm-ID: 438131 [Multi-domain]  Cd Length: 43  Bit Score: 86.26  E-value: 3.37e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCL 136
Cdd:cd16468     1 ECVICMADFVVGDPIRYLPCMHIYHVDCIDDWLMRSFTCPSCM 43
 
Name Accession Description Interval E-value
RING-H2_RNF11 cd16468
RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 ...
94-136 3.37e-23

RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 is an E3 ubiquitin-protein ligase that acts both as an adaptor and a modulator of itch-mediated control of ubiquitination events underlying membrane traffic. It acts downstream of an enzymatic cascade for the ubiquitination of specific substrates. It is also a molecular adaptor of homologous to E6-associated protein C-terminus (HECT)-type ligases. RNF11 has been implicated in the regulation of several signaling pathways. It enhances transforming growth factor receptor (TGFR) signaling by both abrogating Smurf2-mediated receptor ubiquitination and by promoting the Smurf2-mediated degradation of AMSH (associated molecule with the SH3 domain of STAM), a de-ubiquitinating enzyme that enhances TGF-beta signaling and epidermal growth factor receptor (EGFR) endosomal recycling. It also acts directly on Smad4 to enhance Smad4 function, and plays a role in prolonged TGF-beta signaling. RNF11 also functions as a critical component of the A20 ubiquitin-editing protein complex that negatively regulates tumor necrosis factor (TNF)-mediated nuclear factor (NF)-kappaB activation. It interacts with Smad anchor for receptor activation (SARA) and the endosomal sorting complex required for transport (ESCRT)-0 complex, thus participating in the regulation of lysosomal degradation of EGFR. RNF11 acts as a novel GGA cargo actively participating in regulating the ubiquitination of the GGA protein family. RNF11 functions together with TAX1BP1 to target TANK-binding kinase 1 (TBK1)/IkappaB kinase IKKi, and further restricts antiviral signaling and type I interferon (IFN)-beta production. RNF11 contains an N-terminal PPPY motif that binds WW domain-containing proteins such as AIP4/itch, Nedd4 and Smurf1/2 (SMAD-specific E3 ubiquitin-protein ligase 1/2), and a C-terminal C3H2C3-type RING-H2 finger that functions as a scaffold for the coordinated transfer of ubiquitin to substrate proteins together with the E2 enzymes UbcH527 and Ubc13.


Pssm-ID: 438131 [Multi-domain]  Cd Length: 43  Bit Score: 86.26  E-value: 3.37e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCL 136
Cdd:cd16468     1 ECVICMADFVVGDPIRYLPCMHIYHVDCIDDWLMRSFTCPSCM 43
zf-RING_2 pfam13639
Ring finger domain;
93-135 2.47e-13

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 60.88  E-value: 2.47e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  93 NECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:pfam13639   1 DECPICLEEFEEGDKVVVLPCGHHFHRECLDKWLRSSNTCPLC 43
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
94-139 7.17e-11

RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 59.24  E-value: 7.17e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMK-SFTCPSCLEPV 139
Cdd:COG5540   325 ECAICMSNFIKNDRLRVLPCDHRFHVGCVDKWLLGySNKCPVCRTAI 371
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
95-135 2.16e-07

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 45.19  E-value: 2.16e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1972253235   95 CAICMIDFEpgERIRFLPCMHSFHQECVDEWLM-KSFTCPSC 135
Cdd:smart00184   1 CPICLEEYL--KDPVILPCGHTFCRSCIRKWLEsGNNTCPIC 40
PHA02929 PHA02929
N1R/p28-like protein; Provisional
94-145 8.30e-04

N1R/p28-like protein; Provisional


Pssm-ID: 222944 [Multi-domain]  Cd Length: 238  Bit Score: 38.61  E-value: 8.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972253235  94 ECAICM-IDFEPGERIRF---LP-CMHSFHQECVDEWLMKSFTCPSCLEPVDSTILS 145
Cdd:PHA02929  176 ECAICMeKVYDKEIKNMYfgiLSnCNHVFCIECIDIWKKEKNTCPVCRTPFISVIKS 232
 
Name Accession Description Interval E-value
RING-H2_RNF11 cd16468
RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 ...
94-136 3.37e-23

RING finger, H2 subclass, found in RING finger protein 11 (RNF11) and similar proteins; RNF11 is an E3 ubiquitin-protein ligase that acts both as an adaptor and a modulator of itch-mediated control of ubiquitination events underlying membrane traffic. It acts downstream of an enzymatic cascade for the ubiquitination of specific substrates. It is also a molecular adaptor of homologous to E6-associated protein C-terminus (HECT)-type ligases. RNF11 has been implicated in the regulation of several signaling pathways. It enhances transforming growth factor receptor (TGFR) signaling by both abrogating Smurf2-mediated receptor ubiquitination and by promoting the Smurf2-mediated degradation of AMSH (associated molecule with the SH3 domain of STAM), a de-ubiquitinating enzyme that enhances TGF-beta signaling and epidermal growth factor receptor (EGFR) endosomal recycling. It also acts directly on Smad4 to enhance Smad4 function, and plays a role in prolonged TGF-beta signaling. RNF11 also functions as a critical component of the A20 ubiquitin-editing protein complex that negatively regulates tumor necrosis factor (TNF)-mediated nuclear factor (NF)-kappaB activation. It interacts with Smad anchor for receptor activation (SARA) and the endosomal sorting complex required for transport (ESCRT)-0 complex, thus participating in the regulation of lysosomal degradation of EGFR. RNF11 acts as a novel GGA cargo actively participating in regulating the ubiquitination of the GGA protein family. RNF11 functions together with TAX1BP1 to target TANK-binding kinase 1 (TBK1)/IkappaB kinase IKKi, and further restricts antiviral signaling and type I interferon (IFN)-beta production. RNF11 contains an N-terminal PPPY motif that binds WW domain-containing proteins such as AIP4/itch, Nedd4 and Smurf1/2 (SMAD-specific E3 ubiquitin-protein ligase 1/2), and a C-terminal C3H2C3-type RING-H2 finger that functions as a scaffold for the coordinated transfer of ubiquitin to substrate proteins together with the E2 enzymes UbcH527 and Ubc13.


Pssm-ID: 438131 [Multi-domain]  Cd Length: 43  Bit Score: 86.26  E-value: 3.37e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCL 136
Cdd:cd16468     1 ECVICMADFVVGDPIRYLPCMHIYHVDCIDDWLMRSFTCPSCM 43
RING-H2_SIS3 cd23118
RING finger, H2 subclass, found in Arabidopsis thaliana protein SUGAR INSENSITIVE 3 (SIS3) and ...
94-135 1.73e-17

RING finger, H2 subclass, found in Arabidopsis thaliana protein SUGAR INSENSITIVE 3 (SIS3) and similar proteins; SIS3 is an E3 ubiquitin-protein ligase that acts as a positive regulator of sugar signaling during early seedling development. SIS3 contains a C3H2C3-type RING-H2 finger.


Pssm-ID: 438480 [Multi-domain]  Cd Length: 47  Bit Score: 71.63  E-value: 1.73e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd23118     2 TCTICLEDFEDGEKLRVLPCQHQFHSECVDQWLRRNPKCPVC 43
RING-H2_EL5-like cd16461
RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins; ...
94-135 8.12e-17

RING finger, H2 subclass, found in rice E3 ubiquitin-protein ligase EL5 and similar proteins; EL5, also known as protein ELICITOR 5, is an E3 ubiquitin-protein ligase containing an N-terminal transmembrane domain and a C3H2C3-type RING-H2 finger that is a binding site for ubiquitin-conjugating enzyme (E2). It can be rapidly induced by N-acetylchitooligosaccharide elicitor. EL5 catalyzes polyubiquitination via the Lys48 residue of ubiquitin, and thus plays a crucial role as a membrane-anchored E3 in the maintenance of cell viability after the initiation of root primordial formation in rice. It also acts as an anti-cell death enzyme that might be responsible for mediating the degradation of cytotoxic proteins produced in root cells after the actions of phytohormones. Moreover, EL5 interacts with UBC5b, a rice ubiquitin carrier protein, through its RING-H2 finger. EL5 is an unstable protein, and its degradation is regulated by the C3H2C3-type RING-H2 finger in a proteasome-independent manner.


Pssm-ID: 438124 [Multi-domain]  Cd Length: 44  Bit Score: 69.98  E-value: 8.12e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  94 ECAICMIDFEPGERIRFLP-CMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16461     1 ECAICLSDYENGEELRRLPeCKHAFHKECIDEWLKSNSTCPLC 43
RING-H2_RNF111-like cd16474
RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; ...
95-135 7.78e-16

RING finger, H2 subclass, found in RING finger proteins RNF111, RNF165, and similar proteins; The family includes RING finger proteins RNF111, RNF165, and similar proteins. RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It also interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. The N-terminal half of RNF111 harbors three SUMO-interacting motifs (SIMs). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). RNF165, also known as Arkadia-like 2, Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to the C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. Both RNF165 and RNF111 contain a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438137 [Multi-domain]  Cd Length: 46  Bit Score: 67.43  E-value: 7.78e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16474     3 CTICLSDFEEGEDVRRLPCMHLFHQECVDQWLSTNKRCPIC 43
RING-H2_PA-TM-RING cd16454
RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING ...
94-135 4.19e-15

RING finger, H2 subclass, found in the PA-TM-RING ubiquitin ligase family; The PA-TM-RING family represents a group of transmembrane-type E3 ubiquitin ligases, which has been characterized by an N-terminal transient signal peptide, a PA (protease-associated) domain, a TM (transmembrane) domain, as well as a C-terminal C3H2C3-type RING-H2 finger domain. It includes RNF13, RNF167, ZNRF4 (zinc and RING finger 4), GRAIL (gene related to anergy in lymphocytes)/RNF128, RNF130, RNF133, RNF148, RNF149 and RNF150 (which are more closely related), as well as RNF43 and ZNRF3, which have substantially longer C-terminal tail extensions compared with the others. PA-TM-RING proteins are expressed at low levels in all mammalian tissues and species, but they are not present in yeast. They play a common regulatory role in intracellular trafficking/sorting, suggesting that abrogation of their function may result in dysregulation of cellular signaling events in cancer.


Pssm-ID: 438118 [Multi-domain]  Cd Length: 43  Bit Score: 65.37  E-value: 4.19e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16454     1 TCAICLEEFKEGEKVRVLPCNHLFHKDCIDPWLEQHNTCPLC 42
RING-H2_RNF38-like cd16472
RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; ...
94-135 6.65e-15

RING finger, H2 subclass, found in RING finger proteins RNF38, RNF44, and similar proteins; This subfamily includes RING finger proteins RNF38, RNF44, and similar proteins. RNF38 is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 is an uncharacterized RING finger protein that shows high sequence similarity to RNF38. Both RNF38 and RNF44 contain a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C3-type RING-H2 finger. In addition, RNF38 harbors two potential nuclear localization signals.


Pssm-ID: 438135 [Multi-domain]  Cd Length: 46  Bit Score: 65.05  E-value: 6.65e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16472     4 QCVVCMCDYEKRQLLRVLPCSHEFHAKCIDKWLKTNRTCPIC 45
RING-H2_RNF103 cd16473
RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; ...
92-139 2.39e-14

RING finger, H2 subclass, found in RING finger protein 103 (RNF103) and similar proteins; RNF103, also known as KF-1 or zinc finger protein 103 homolog (Zfp-103), is an endoplasmic reticulum (ER)-resident E3 ubiquitin-protein ligase that is widely expressed in many different organs, including brain, heart, kidney, spleen, and lung. It is involved in the ER-associated degradation (ERAD) pathway by interacting with components of the ERAD pathway, including Derlin-1 and VCP. RNF103 contains several hydrophobic regions at its N-terminal and middle regions, as well as a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438136 [Multi-domain]  Cd Length: 55  Bit Score: 63.83  E-value: 2.39e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1972253235  92 SNECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSF-TCPSCLEPV 139
Cdd:cd16473     4 CEECAICLENYQNGDLLRGLPCGHVFHQNCIDVWLERDNhCCPVCRWPV 52
RING-H2_RNF6-like cd16467
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6, RNF12, and similar ...
94-135 2.51e-14

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6, RNF12, and similar proteins; RNF6 is an androgen receptor (AR)-associated protein that induces AR ubiquitination and promotes AR transcriptional activity. RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity by modulating cofactor recruitment. RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. RNF6 also regulates local serine/threonine kinase LIM kinase 1 (LIMK1) levels in axonal growth cones. RNF6-induced LIMK1 polyubiquitination is mediated via K48 of ubiquitin and leads to proteasomal degradation of the kinase. RNF6 binds and upregulates the Inha promoter, and functions as a transcription regulatory protein in the mouse sertoli cell. It acts as a potential tumor suppressor gene involved in the pathogenesis of esophageal squamous cell carcinoma (ESCC). RNF12, also known as LIM domain-interacting RING finger protein, or RING finger LIM domain-binding protein (R-LIM), is an E3 ubiquitin-protein ligase encoded by gene RLIM that is crucial for normal embryonic development in some species and for normal X inactivation in mice. It thus functions as a major sex-specific epigenetic regulator of female mouse nurturing tissues. RNF12 is widely expressed during embryogenesis, and mainly localizes to the cell nucleus, where it regulates the levels of many proteins, including CLIM, LMO, HDAC2, TRF1, SMAD7, and REX1, by proteasomal degradation. Both RNF6 and RNF12 contain a well conserved C3H2C3-type RING-H2 finger.


Pssm-ID: 438130 [Multi-domain]  Cd Length: 43  Bit Score: 63.63  E-value: 2.51e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16467     1 ECTICLGEYETGEKLRRLPCSHEFHSECVDRWLKENSSCPIC 42
RING-H2 cd16448
H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ...
95-135 2.84e-14

H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers: some have different Cys/His patterns while some lack a single Cys or His residue at typical Zn ligand positions (the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can indeed chelate Zn in a RING finger as well). This family corresponds to the H2 subclass of RING (RING-H2) finger proteins that are characterized by containing C3H2C3-type canonical RING-H2 fingers or noncanonical RING-H2 finger variants, including C4HC3- (RING-CH alias RINGv), C3H3C2-, C3H2C2D-, C3DHC3-, and C4HC2H-type modified RING-H2 fingers. The canonical RING-H2 finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-H-X2-C-X(4-48)-C-X2-C, X is any amino acid and the number of X residues varies in different fingers. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-H2 finger can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serves as a scaffold for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438112 [Multi-domain]  Cd Length: 43  Bit Score: 63.19  E-value: 2.84e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLM-KSFTCPSC 135
Cdd:cd16448     1 CVICLEEFEEGDVVRLLPCGHVFHLACILRWLEsGNNTCPLC 42
RING-H2_RNF111 cd16681
RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; ...
89-143 1.85e-13

RING finger, H2 subclass, found in RING finger protein 111 (RNF111) and similar proteins; RNF111, also known as Arkadia, is a nuclear E3 ubiquitin-protein ligase that targets intracellular effectors and modulators of transforming growth factor beta (TGF-beta)/Nodal-related signaling for polyubiquitination and proteasome-dependent degradation. It acts as an amplifier of Nodal signals, and enhances the dorsalizing activity of limiting amounts of Xnr1, a Nodal homolog, and requires Nodal signaling for its function. The loss of RNF111 results in early embryonic lethality, with defects attributed to compromised Nodal signaling. RNF111 also regulates tumor metastasis by modulation of the TGF-beta pathway. Its ubiquitination can be modulated by the four and a half LIM-only protein 2 (FHL2) that activates TGF-beta signal transduction. Furthermore, RNF111 interacts with the clathrin-adaptor 2 (AP2) complex and regulates endocytosis of certain cell surface receptors, leading to modulation of epidermal growth factor (EGF) and possibly other signaling pathways. In addition, RNF111 has been identified as a small ubiquitin-like modifier (SUMO)-binding protein with clustered SUMO-interacting motifs (SIMs) that together form a SUMO-binding domain (SBD). It thus functions as a SUMO-targeted ubiquitin ligase (STUbL) that directly links nonproteolytic ubiquitylation and SUMOylation in the DNA damage response, as well as triggers degradation of signal-induced polysumoylated proteins, such as the promyelocytic leukemia protein (PML). The N-terminal half of RNF111 harbors three SIMs. Its C-terminal half show high sequence similarity with RING finger protein 165 (RNF165), where it contains two serine rich domains, two nuclear localization signals, an NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is required for polyubiqutination and proteasome-dependent degradation of phosphorylated forms of Smad2/3 and three major negative regulators of TGF-beta signaling, Smad7, SnoN and c-Ski.


Pssm-ID: 438343 [Multi-domain]  Cd Length: 61  Bit Score: 61.62  E-value: 1.85e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972253235  89 DMTSNECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPVDSTI 143
Cdd:cd16681     7 EDTEEKCTICLSILEEGEDVRRLPCMHLFHQVCVDQWLITNKKCPICRVDIEAQL 61
zf-RING_2 pfam13639
Ring finger domain;
93-135 2.47e-13

Ring finger domain;


Pssm-ID: 433370 [Multi-domain]  Cd Length: 44  Bit Score: 60.88  E-value: 2.47e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  93 NECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:pfam13639   1 DECPICLEEFEEGDKVVVLPCGHHFHRECLDKWLRSSNTCPLC 43
RING-H2_RNF167 cd16797
RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; ...
95-135 2.71e-13

RING finger, H2 subclass, found in RING finger protein 167 (RNF167) and similar proteins; RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) ubiquitination. It ubiquitinates AMPA-type glutamate receptor subunit GluA2 and regulates its surface expression, and thus acts as a selective regulator of AMPAR-mediated neurotransmission. It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. RNF167 is widely conserved in metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, two transmembrane domains (TM1 and TM2), and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319711 [Multi-domain]  Cd Length: 46  Bit Score: 60.83  E-value: 2.71e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSF-TCPSC 135
Cdd:cd16797     3 CAICLDEYEEGDKLRVLPCSHAYHSKCVDPWLTQTKkTCPVC 44
RING-H2_BB-like cd23115
RING finger, H2 subclass, found in Arabidopsis thaliana RING-type E3 ubiquitin transferase BIG ...
89-135 8.51e-13

RING finger, H2 subclass, found in Arabidopsis thaliana RING-type E3 ubiquitin transferase BIG BROTHER (BB) and similar proteins; BB (also known as protein ENHANCER OF DA1-1 or EOD1) is an E3 ubiquitin-protein ligase that limits organ size, and possibly seed size, in a dose-dependent manner. It negatively regulates the duration of cell proliferation in leaves and petals independently of the major phytohormones (e.g. auxin, cytokinin, gibberellin, brassinosteroids, ethylene, abscisic acid, jasmonic acid), probably by targeting growth stimulators for degradation. It limits the proliferation of root meristematic cells. BB polyubiquitinates DA1. It is involved in the promotion of leaf senescence, in addition to its function in restricting plant growth. BB-related is an E3 ubiquitin-ligase probably involved in organ size regulation. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438477 [Multi-domain]  Cd Length: 52  Bit Score: 59.77  E-value: 8.51e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1972253235  89 DMTSNECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd23115     1 DEDNERCVICRLEYEEGEDLLTLPCKHCYHSECIQQWLQINKVCPVC 47
RING-H2_RNF43-like cd16666
RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; ...
95-136 1.27e-12

RING finger, H2 subclass, found in RING finger proteins RNF43, ZNRF3, and similar proteins; RNF43 and ZNRF3 (also known as RNF203) are transmembrane E3 ubiquitin-protein ligases that belong to the PA-TM-RING ubiquitin ligase family, characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger followed by a long C-terminal region. Both RNF43 and RNF203 function as tumor suppressors involved in the regulation of Wnt/beta-catenin signaling. They negatively regulate Wnt signaling by interacting with complexes of frizzled (FZD) receptors and low-density lipoprotein receptor-related protein (LRP) 5/6, which leads to ubiquitination of FZD and endocytosis of the Wnt receptor. Dishevelled (DVL), a positive Wnt regulator, is required for ZNRF3/RNF43-mediated ubiquitination and degradation of FZD. They also associate with R-spondin 1 (RSPO1). This interaction may block FZD ubiquitination and enhances Wnt signaling.


Pssm-ID: 438328 [Multi-domain]  Cd Length: 45  Bit Score: 59.01  E-value: 1.27e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCL 136
Cdd:cd16666     2 CAICLEEYEEGQELRVLPCQHEFHRKCVDPWLLQNHTCPLCL 43
RING-H2_RNF13 cd16796
RING finger, H2 subclass, found in RING finger protein 13 (RNF13) and similar proteins; RNF13 ...
95-139 1.69e-12

RING finger, H2 subclass, found in RING finger protein 13 (RNF13) and similar proteins; RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that is functionally significant in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. It functions as an important regulator of inositol-requiring transmembrane kinase/endonuclease IRE1alpha, mediating endoplasmic reticulum (ER) stress-induced apoptosis through the activation of the IRE1alpha-TRAF2-JNK signaling pathway. Moreover, RNF13 is involved in the regulation of the soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor (SNARE) complex via the ubiquitination of snapin, a SNAP25-interacting protein, which thereby controls synaptic function. In addition, RNF13 participates in regulating the function of satellite cells by modulating cytokine composition. RNF13 is evolutionarily conserved among many metazoans and contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 438450 [Multi-domain]  Cd Length: 59  Bit Score: 59.29  E-value: 1.69e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKS-FTCPSCLEPV 139
Cdd:cd16796    11 CAICLDEYEEGDKLRILPCSHAYHCKCVDPWLTKTkKTCPVCKQKV 56
RING-H2_RNF6 cd16673
RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins; RNF6 ...
95-142 2.39e-12

RING finger, H2 subclass, found in E3 ubiquitin-protein ligase RNF6 and similar proteins; RNF6 is an androgen receptor (AR)-associated protein that induces AR ubiquitination and promotes AR transcriptional activity. RNF6-induced ubiquitination may regulate AR transcriptional activity and specificity by modulating cofactor recruitment. RNF6 is overexpressed in hormone-refractory human prostate cancer tissues and required for prostate cancer cell growth under androgen-depleted conditions. Moreover, RNF6 regulates local serine/threonine kinase LIM kinase 1 (LIMK1) levels in axonal growth cones. RNF6-induced LIMK1 polyubiquitination is mediated via K48 of ubiquitin and leads to proteasomal degradation of the kinase. RNF6 also binds and upregulates the Inha promoter, and functions as a transcription regulatory protein in the mouse sertoli cell. RNF6 also acts as a potential tumor suppressor gene involved in the pathogenesis of esophageal squamous cell carcinoma (ESCC). RNF6 contains an N-terminal coiled-coil domain, a Lys-X-X-Leu/Ile-X-X-Leu/Ile (KIL) motif, and a C-terminal C3H2C3-type RING-H2 finger which is responsible for its ubiquitin ligase activity. The KIL motif is present in a subset of RING-H2 proteins from organisms as evolutionarily diverse as human, mouse, chicken, Drosophila, Caenorhabditis elegans, and Arabidopsis thaliana.


Pssm-ID: 438335 [Multi-domain]  Cd Length: 52  Bit Score: 58.43  E-value: 2.39e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPVDST 142
Cdd:cd16673     3 CSVCINEYATGNKLRRLPCAHEFHIHCIDRWLSENSTCPICRQPVLGS 50
RING-H2_RNF165 cd16682
RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins; ...
91-135 3.48e-12

RING finger, H2 subclass, found in RING finger protein 165 (RNF165) and similar proteins; RNF165, also known as Arkadia-like 2, Arkadia2, or Ark2C, is an E3 ubiquitin ligase with homology to the C-terminal half of RNF111. It is expressed specifically in the nervous system, and can serve to amplify neuronal responses to specific signals. It acts as a positive regulator of bone morphogenetic protein (BMP)-Smad signaling that is involved in motor neuron (MN) axon elongation. RNF165 contains two serine rich domains, a nuclear localization signal, an NRG-TIER domain, and a C-terminal C3H2C3-type RING-H2 finger that is responsible for the enhancement of BMP-Smad1/5/8 signaling in the spinal cord.


Pssm-ID: 438344 [Multi-domain]  Cd Length: 59  Bit Score: 58.55  E-value: 3.48e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972253235  91 TSNECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16682     6 TDEKCTICLSMLEDGEDVRRLPCMHLFHQLCVDQWLAMSKKCPIC 50
RING-H2_RNF130-like cd16668
RING finger, H2 subclass, found in RING finger proteins, RNF130, RNF149, RNF150 and similar ...
95-135 4.68e-12

RING finger, H2 subclass, found in RING finger proteins, RNF130, RNF149, RNF150 and similar proteins; This subfamily includes RING finger proteins, RNF130, RNF149 and RNF150, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence. RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128. It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property and controls the development of T cell clonal anergy by ubiquitination. RNF133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase that may play a role in sperm maturation through an ER-associated degradation (ERAD) pathway. RNF149, also known as DNA polymerase-transactivated protein 2, is an E3 ubiquitin-protein ligase that induces the ubiquitination of wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF) and promotes its proteasome-dependent degradation. RNF150 polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. This subfamily also includes Drosophila melanogaster protein goliath (d-goliath), also known as protein g1, which is one of the founding members of the group. It was originally identified as a transcription factor involved in the embryo mesoderm formation.


Pssm-ID: 438330 [Multi-domain]  Cd Length: 46  Bit Score: 57.79  E-value: 4.68e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16668     2 CAVCIEPYKPSDVIRILPCKHIFHKSCVDPWLLEHRTCPMC 42
RING-H2_RNF13-like cd16665
RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 ...
95-135 4.75e-12

RING finger, H2 subclass, found in RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), and similar proteins; This subfamily includes RING finger protein 13 (RNF13), RING finger protein 167 (RNF167), Zinc/RING finger protein 4 (ZNRF4), and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane domain (TM), and a C-terminal C3H2C3-type RING-H2 finger followed by a putative PEST sequence. RNF13 is a widely expressed membrane-associated E3 ubiquitin-protein ligase that functions in the regulation of cancer development, muscle cell growth, and neuronal development. Its expression is developmentally regulated during myogenesis and is upregulated in various tumors. RNF13 negatively regulates cell proliferation through its E3 ligase activity. RNF167, also known as RING105, is an endosomal/lysosomal E3 ubiquitin-protein ligase involved in the ubiquitination of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR). It acts as an endosomal membrane protein which ubiquitylates vesicle-associated membrane protein 3 (VAMP3) and regulates endosomal trafficking. Moreover, RNF167 plays a role in the regulation of TSSC5 (tumor-suppressing subchromosomal transferable fragment cDNA, also known as ORCTL2/IMPT1/BWR1A/SLC22A1L), which can function in concert with the ubiquitin-conjugating enzyme UbcH6. ZNRF4, also known as RING finger protein 204 (RNF204), or Nixin, is an endoplasmic reticulum (ER) membrane-anchored ubiquitin ligase that physically interacts with the ER-localized chaperone calnexin in a glycosylation-independent manner, inducing calnexin ubiquitination, and p97-dependent degradation. The murine protein sperizin (spermatid-specific ring zinc finger) is a homolog of human ZNRF4. It is specifically expressed in Haploid germ cells and is involved in spermatogenesis.


Pssm-ID: 438327 [Multi-domain]  Cd Length: 46  Bit Score: 57.44  E-value: 4.75e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKS-FTCPSC 135
Cdd:cd16665     3 CAICLDDYEEGDKLRILPCSHAYHCKCIDPWLTKNkRTCPVC 44
RING-H2_RNF43 cd16798
RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 ...
95-136 9.96e-12

RING finger, H2 subclass, found in RING finger protein 43 (RNF43) and similar proteins; RNF43 is a transmembrane E3 ubiquitin-protein ligase that plays an important role in frizzled (FZD)-dependent regulation of the Wnt/beta-catenin pathway. It functions as a tumor suppressor that inhibits Wnt/beta-catenin signaling by ubiquitinating FZD receptor and targeting it to the lysosomal pathway for degradation. miR-550a-5p directly targeted the 3'-UTR of gene RNF43 and regulated its expression. Moreover, RNF43 interacts with NEDD-4-like ubiquitin-protein ligase-1 (NEDL1) and regulates p53-mediated transcription. It may also be involved in cell growth control through the interaction with HAP95, a chromatin-associated protein interfacing the nuclear envelope. Mutations of RNF43 have been identified in various tumors, including colorectal cancer (CRC), endometrial cancer, mucinous ovarian tumors, gastric adenocarcinoma, pancreatic ductal adenocarcinoma, liver fluke-associated cholangiocarcinoma, hepatocellular carcinoma, and glioma. RNF43 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger followed by a long C-terminal region.


Pssm-ID: 438451 [Multi-domain]  Cd Length: 53  Bit Score: 56.79  E-value: 9.96e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCL 136
Cdd:cd16798     6 CAICLEEFSEGQELRIISCSHEFHRECVDPWLHQHRTCPLCM 47
RING-H2_RNF181 cd16669
RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; ...
94-135 9.99e-12

RING finger, H2 subclass, found in RING finger protein 181 (RNF181) and similar proteins; RNF181, also known as HSPC238, is a platelet E3 ubiquitin-protein ligase containing a C3H2C3-type RING-H2 finger. It interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3, suggesting a role for RNF181-mediated ubiquitination in integrin and platelet signaling. It also suppresses the tumorigenesis of hepatocellular carcinoma (HCC) through the inhibition of extracellular signal-regulated kinase/mitogen-activated protein kinase (ERK/MAPK) signaling in the liver.


Pssm-ID: 438331 [Multi-domain]  Cd Length: 46  Bit Score: 56.61  E-value: 9.99e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16669     1 KCPICLLEFEEGETVKQLPCKHSFHSDCILPWLGKTNSCPLC 42
RING-H2_RNF215 cd16670
RING finger, H2 subclass, found in RING finger protein 215 (RNF215) and similar proteins; This ...
95-135 2.95e-11

RING finger, H2 subclass, found in RING finger protein 215 (RNF215) and similar proteins; This family includes uncharacterized protein RNF215 and similar proteins. Although its biological function remains unclear, RNF215 shares high sequence similarity with PA-TM-RING ubiquitin ligases, which have been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438332 [Multi-domain]  Cd Length: 50  Bit Score: 55.54  E-value: 2.95e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16670     3 CAVCLDQFYKNQCLRVLPCLHEFHRDCVDPWLLLQQTCPLC 43
RING-H2_ZNRF3 cd16799
RING finger, H2 subclass, found in zinc/RING finger protein 3 (ZNRF3) and similar proteins; ...
94-135 4.44e-11

RING finger, H2 subclass, found in zinc/RING finger protein 3 (ZNRF3) and similar proteins; ZNRF3, also known as RING finger protein 203 (RNF203), is a homolog of Ring finger protein 43 (RNF43). It is a transmembrane E3 ubiquitin-protein ligase that is associated with the Wnt receptor complex, and negatively regulates Wnt signaling by promoting the turnover of frizzled and lipoprotein receptor-related protein LRP6 in an R-spondin-sensitive manner. It inhibits gastric cancer cell growth and promotes cell apoptosis by affecting the Wnt/beta-catenin/TCF signaling pathway. ZNRF3 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C3H2C3-type RING-H2 finger followed by a long C-terminal region.


Pssm-ID: 319713 [Multi-domain]  Cd Length: 45  Bit Score: 55.03  E-value: 4.44e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16799     1 DCAICLEKYIDGEELRVIPCTHRFHKKCVDPWLLQHHTCPHC 42
mRING-CH-C4HC2H_ZNRF cd16489
Modified RING-CH finger, H2 subclass (C4HC2H-type), found in the ZNRF family; The ZNRF family ...
94-133 5.16e-11

Modified RING-CH finger, H2 subclass (C4HC2H-type), found in the ZNRF family; The ZNRF family includes zinc/RING finger proteins ZNRF1, ZNRF2, and similar proteins. It has been characterized by containing a unique combination of zinc finger-RING finger motifs in the C-terminal region, which is evolutionarily conserved in a wide range of species, including Caenorhabditis elegans and Drosophila. ZNRF proteins function as E3 ubiquitin ligases and are highly expressed in central nervous system (CNS) and peripheral nervous system (PNS) neurons, particularly during development and in adulthood. ZNRF1 and ZNRF2 are differentially localized within the synaptic region. ZNRF1 is associated with synaptic vesicle membranes, whereas ZNRF2 is present in presynaptic plasma membranes. They are N-myrisotoylated and also located in the endosome-lysosome compartment in fibroblasts. ZNRF proteins may play a role in the establishment and maintenance of neuronal transmission and plasticity via their ubiquitin ligase activity, as well as in regulating Ca2+-dependent exocytosis. The RING fingers found in ZNRF proteins are modified as C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of the RING-H2 finger.


Pssm-ID: 438152 [Multi-domain]  Cd Length: 43  Bit Score: 54.62  E-value: 5.16e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCP 133
Cdd:cd16489     1 ECVICLEELEAGDTIARLPCLCIYHKKCIDDWFEVNRSCP 40
RING-H2_RNF149 cd16804
RING finger, H2 subclass, found in RING finger protein 149 (RNF149) and similar proteins; ...
95-135 5.97e-11

RING finger, H2 subclass, found in RING finger protein 149 (RNF149) and similar proteins; RNF149, also known as DNA polymerase-transactivated protein 2, is an E3 ubiquitin-protein ligase that interacts with wild-type v-Raf murine sarcoma viral oncogene homolog B1 (BRAF), a RING domain-containing E3 ubiquitin ligase involved in control of gene transcription, translation, cytoskeletal organization, cell adhesion, and epithelial development. RNF149 induces the ubiquitination of wild-type BRAF and promotes its proteasome-dependent degradation. Mutated RNF149 has been found in some human breast, ovarian, and colorectal cancers. RNF149 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 438455 [Multi-domain]  Cd Length: 48  Bit Score: 54.91  E-value: 5.97e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16804     2 CAVCIENYKSKDVVRILPCKHVFHRICIDPWLLEHRTCPMC 42
RING-H2_RNF44 cd16680
RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins; RNF44 ...
95-135 6.20e-11

RING finger, H2 subclass, found in RING finger protein 44 (RNF44) and similar proteins; RNF44 is an uncharacterized RING finger protein that shows high sequence similarity with RNF38, which is a nuclear E3 ubiquitin protein ligase that plays a role in regulating p53. RNF44 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), and a C3H2C2-type RING-H2 finger.


Pssm-ID: 438342 [Multi-domain]  Cd Length: 62  Bit Score: 55.07  E-value: 6.20e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16680    10 CVVCFSDFESRQLLRVLPCNHEFHTKCVDKWLKTNRTCPIC 50
RING-H2_DZIP3 cd16460
RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) ...
95-139 6.26e-11

RING finger, H2 subclass, found in DAZ (deleted in azoospermia)-interacting protein 3 (DZIP3) and similar proteins; DZIP3, also known as RNA-binding ubiquitin ligase of 138 kDa (RUL138) or 2A-HUB protein, is an RNA-binding E3 ubiquitin-protein ligase that interacts with coactivator-associated arginine methyltransferase 1 (CARM1) and acts as a transcriptional coactivator of estrogen receptor (ER) alpha. It is also a histone H2A ubiquitin ligase that catalyzes monoubiquitination of H2A at lysine 119, functioning as a combinatorial component of the repression machinery required for repressing a specific chemokine gene expression program, critically modulating migratory responses to Toll-like receptors (TLR) activation. DZIP3 contains a C3H2C3-type RING-H2 finger at the C-terminus.


Pssm-ID: 438123 [Multi-domain]  Cd Length: 47  Bit Score: 54.85  E-value: 6.26e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPV 139
Cdd:cd16460     3 CVICHEAFSDGDRLLVLPCAHKFHTQCIGPWLDGQQTCPTCRLHV 47
COG5540 COG5540
RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, ...
94-139 7.17e-11

RING-finger-containing ubiquitin ligase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227827 [Multi-domain]  Cd Length: 374  Bit Score: 59.24  E-value: 7.17e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMK-SFTCPSCLEPV 139
Cdd:COG5540   325 ECAICMSNFIKNDRLRVLPCDHRFHVGCVDKWLLGySNKCPVCRTAI 371
RING-H2_RNF126-like cd16667
RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; ...
94-135 7.95e-11

RING finger, H2 subclass, found in RING finger proteins RNF126, RNF115, and similar proteins; This subfamily includes RING finger proteins RNF126, RNF115, and similar proteins. RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation; this inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a cofactor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. RNF115 and RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. Both of them contain an N-terminal BCA2 Zinc-finger domain (BZF), AKT-phosphorylation sites, and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438329 [Multi-domain]  Cd Length: 43  Bit Score: 54.23  E-value: 7.95e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16667     1 ECAVCKEDFEVGEEVRQLPCKHLFHPDCIVPWLELHNSCPVC 42
mRING-H2-C3H2C2D_ZSWM2 cd16486
Modified RING finger, H2 subclass (C3H2C2D-type), found in zinc finger SWIM domain-containing ...
94-146 9.78e-11

Modified RING finger, H2 subclass (C3H2C2D-type), found in zinc finger SWIM domain-containing protein 2 (ZSWIM2) and similar proteins; ZSWIM2, also known as MEKK1-related protein X (MEX) or ZZ-type zinc finger-containing protein 2, is a testis-specific E3 ubiquitin ligase that promotes death receptor-induced apoptosis through Fas, death receptor (DR) 3 and DR4 signaling. ZSWIM2 is self-ubiquitinated and targeted for degradation through the proteasome pathway. It acts as an E3 ubiquitin ligase, through the E2, Ub-conjugating enzymes UbcH5a, UbcH5c, or UbcH6. ZSWIM2 contains four putative zinc-binding domains including an N-terminal SWIM (SWI2/SNF2 and MuDR) domain critical for its ubiquitination, and two modified RING-H2 fingers separated by a ZZ zinc finger domain, which was required for interaction with UbcH5a and its self-association. This model corresponds to the second RING-H2 finger, which is not a canonical C3H2C3-type, but a modified C3H2C2D-type.


Pssm-ID: 438149 [Multi-domain]  Cd Length: 49  Bit Score: 54.30  E-value: 9.78e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSftCPSClePVDSTILSS 146
Cdd:cd16486     1 QCRICLKAFQLGQHVRTLPCRHKFHRDCIDNWLLHS--RNSC--PIDGQVVYN 49
RING-H2_RNF38 cd16679
RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins; RNF38 ...
76-135 1.03e-10

RING finger, H2 subclass, found in RING finger protein 38 (RNF38) and similar proteins; RNF38 is a nuclear E3 ubiquitin protein ligase that is widely expressed throughout the human body, and is especially highly expressed in the heart, brain, placenta and the testis. It recognizes p53 as a substrate for ubiquitination, and thus plays a role in regulating p53. The overexpression of RNF38 increases p53 ubiquitination and alters p53 localization. It is also capable of autoubiquitination. RNF38 expression is negatively regulated by the serotonergic system. Induction of RNF38 may be involved in the anxiety-like behavior or non-cell autonomy in Oryzias latipes by the decline of serotonin (5-HT) levels. RNF38 contains a coiled-coil motif, a KIL motif (Lys-X2-Ile/Leu-X2-Ile/Leu, X can be any amino acid), a C3H2C3-type RING-H2 finger, as well as two potential nuclear localization signals.


Pssm-ID: 438341 [Multi-domain]  Cd Length: 67  Bit Score: 54.68  E-value: 1.03e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972253235  76 GLLEQIPADVFRGDMTSNE---CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16679     1 ADIEQLPSYRFNPNNHQSEqtlCVVCMCDFESRQLLRVLPCNHEFHAKCVDKWLKANRTCPIC 63
RING-H2_RNF130 cd16803
RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; ...
93-135 1.12e-10

RING finger, H2 subclass, found in RING finger protein 130 (RNF130) and similar proteins; RNF130, also known as Goliath homolog (H-Goliath), is a paralog of RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL). It is a transmembrane E3 ubiquitin-protein ligase expressed in leukocytes. It has a self-ubiquitination property, and controls the development of T cell clonal anergy by ubiquitination. RNF130 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 319717 [Multi-domain]  Cd Length: 49  Bit Score: 54.21  E-value: 1.12e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  93 NECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16803     1 DHCAVCIEGYKQNDVVRILPCKHVFHKSCVDPWLNEHCTCPMC 43
RING-H2_PJA1_2 cd16465
RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and ...
95-135 1.37e-10

RING finger, H2 subclass, found in protein E3 ubiquitin-protein ligase Praja-1, Praja-2, and similar proteins; This family includes two highly similar E3 ubiquitin-protein ligases, Praja-1 and Praja-2. Praja-1, also known as RING finger protein 70, is a RING-H2 finger ubiquitin ligase encoded by gene PJA1, a novel human X chromosome gene abundantly expressed in the brain. It has been implicated in bone and liver development, as well as memory formation and X-linked mental retardation (MRX). Praja-1 interacts with and activates the ubiquitin-conjugating enzyme UbcH5B, and shows E2-dependent E3 ubiquitin ligase activity. It is a 3-deazaneplanocin A (DZNep)-induced ubiquitin ligase that directly ubiquitinates individual polycomb repressive complex 2 (PRC2) subunits in a cell free system, which leads to their proteasomal degradation. It also plays an important role in neuronal plasticity, which is the basis for learning and memory. Moreover, Praja-1 ubiquitinates embryonic liver fodrin (ELF) and Smad3, but not Smad4, in a transforming growth factor-beta (TGF-beta)-dependent manner. It controls ELF abundance through ubiquitin-mediated degradation, and further regulates TGF-beta signaling, which plays a key role in the suppression of gastric carcinoma. Praja-1 also regulates the transcription function of the homeodomain protein Dlx5 by controlling the stability of Dlxin-1, via a ubiquitin-dependent degradation pathway. Praja-2, also known as RING finger protein 131, NEURODAP1, or KIAA0438, is an E2-dependent E3 ubiquitin ligase that interacts with and activates the ubiquitin-conjugating enzyme UbcH5B. It functions as an A-kinase anchoring protein (AKAP)-like E3 ubiquitin ligase that plays a critical role in controlling cyclic AMP (cAMP)-dependent PKA activity and pro-survival signaling, and further promotes cell proliferation and growth. Praja-2 is also involved in protein sorting at the postsynaptic density region of axosomatic synapses and possibly plays a role in synaptic communication and plasticity. Together with the AMPK-related kinase SIK2 and the CDK5 activator CDK5R1/p35, it forms a SIK2-p35-PJA2 complex that plays an essential role for glucose homeostasis in pancreatic beta cell functional compensation. Praja-2 ubiquitylates and degrades Mob, a core component of NDR/LATS kinase and a positive regulator of the tumor-suppressor Hippo signaling. Both Praja-1 and Praja-2 contain a potential nuclear localization signal (NLS) and a C-terminal C3H2C3-type RING-H2 motif.


Pssm-ID: 438128 [Multi-domain]  Cd Length: 46  Bit Score: 53.61  E-value: 1.37e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16465     2 CPICCSEYVKDEIATELPCHHLFHKPCITAWLQKSGTCPVC 42
RING-H2_RNF24-like cd16469
RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; ...
95-139 2.40e-10

RING finger, H2 subclass, found in RING finger proteins RNF24, RNF122, and similar proteins; This subfamily includes RNF24, RNF122, and similar proteins. RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, -3, -4, -5, -6, and -7, and affects TRPC intracellular trafficking without affecting their activity. RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergo degradation through its RING finger in a proteasome-dependent manner. Both RNF24 and RNF122 contain an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438132 [Multi-domain]  Cd Length: 47  Bit Score: 53.16  E-value: 2.40e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPV 139
Cdd:cd16469     3 CAVCLEEFKLKEELGVCPCGHAFHTKCLKKWLEVRNSCPICKSPV 47
RING-H2_RNF12 cd16674
RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins; RNF12, ...
95-139 2.77e-10

RING finger, H2 subclass, found in RING finger protein 12 (RNF12) and similar proteins; RNF12, also known as LIM domain-interacting RING finger protein or RING finger LIM domain-binding protein (R-LIM), is an E3 ubiquitin-protein ligase encoded by gene RLIM that is crucial for normal embryonic development in some species and for normal X inactivation in mice. It thus functions as a major sex-specific epigenetic regulator of female mouse nurturing tissues. RNF12 is widely expressed during embryogenesis, and mainly localizes to the cell nucleus, where it regulates the levels of many proteins, including CLIM, LMO, HDAC2, TRF1, SMAD7, and REX1, by proteasomal degradation. Its functional activity is regulated by phosphorylation-dependent nucleocytoplasmic shuttling. It is negatively regulated by pluripotency factors in embryonic stem cells. p53 represses its transcription through Sp1. RNF12 is the primary factor responsible for X chromosome inactivation (XCI) in female placental mammals. It is an indispensable factor in up-regulation of Xist transcription, thereby leading to initiation of random XCI. It also targets REX1, an inhibitor of XCI, for proteasomal degradation. RNF12 also acts as a co-regulator for a range of transcription factors, particularly those containing a LIM homeodomain, and modulates the formation of transcriptional multiprotein complexes. It is a negative regulator of Smad7, which in turn negatively regulates the signaling of type I receptors from the transforming growth factor beta (TGF-beta) superfamily. In addition, paternal RNF12 is a critical survival factor for milk-producing alveolar cells. RNF12 contains an nuclear localization signal (NLS) and a C3H2C3-type RING-H2 finger.


Pssm-ID: 438336 [Multi-domain]  Cd Length: 51  Bit Score: 53.19  E-value: 2.77e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPV 139
Cdd:cd16674     3 CSVCITEYTEGNKLRKLPCSHEYHVHCIDRWLSENSTCPICRRAV 47
RING-H2_RNF126 cd16801
RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; ...
94-135 3.44e-10

RING finger, H2 subclass, found in RING finger protein 126 (RNF126) and similar proteins; RNF126 is a Bag6-dependent E3 ubiquitin ligase that is involved in the mislocalized protein (MLP) pathway of quality control. It regulates the retrograde sorting of the cation-independent mannose 6-phosphate receptor (CI-MPR). Moreover, RNF126 promotes cancer cell proliferation by targeting the tumor suppressor p21 for ubiquitin-mediated degradation, and could be a novel therapeutic target in breast and prostate cancers. It is also able to ubiquitylate cytidine deaminase (AID), a poorly soluble protein that is essential for antibody diversification. In addition, RNF126 and the related protein, RNF115 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF126 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438453 [Multi-domain]  Cd Length: 44  Bit Score: 52.68  E-value: 3.44e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16801     1 ECPVCKEDYTVGENVRQLPCNHLFHNDCIVPWLEQHDTCPVC 42
RING-H2_RNF128-like cd16802
RING finger, H2 subclass, found in RING finger protein 128 (RNF128) and similar proteins; This ...
95-135 4.09e-10

RING finger, H2 subclass, found in RING finger protein 128 (RNF128) and similar proteins; This subfamily includes RING finger proteins RNF128, RNF133, RNF148, and similar proteins, which belong to a larger PA-TM-RING ubiquitin ligase family that has been characterized by containing an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger followed by a putative PEST sequence. RNF128, also known as gene related to anergy in lymphocytes protein (GRAIL), is a type 1 transmembrane E3 ubiquitin-protein ligase that is a critical regulator of adaptive immunity and development. It inhibits cytokine gene transcription, is expressed in anergic CD4+ T cells, and has been implicated in primary T cell activation, survival, and differentiation, as well as in T cell anergy and oral tolerance. It induces T cell anergy through the ubiquitination activity of its cytosolic RING finger. It regulates expression of the costimulatory molecule CD40L on CD4 T cells, and ubiquitinates the costimulatory molecule CD40 ligand (CD40L) during the induction of T cell anergy. Moreover, RNF128 interacts with the luminal/extracellular portion of both CD151 and the related tetraspanin CD81 via its PA domain, which promoted ubiquitination of cytosolic lysine residues. It also down-modulates the expression of CD83 (previously described as a cell surface marker for mature dendritic cells) on CD4 T cells. Furthermore, Rho guanine dissociation inhibitor (RhoGDI) has been identified as a potential substrate of RNF128, suggesting a role for Rho effector molecules in T cell anergy. In addition, RNF128 plays a role in environmental stress responses. It promotes environmental salinity tolerance in euryhaline tilapia. RNF133 is a testis-specific endoplasmic reticulum-associated E3 ubiquitin ligase that is mainly present in the cytoplasm of elongated spermatids. It may play a role in sperm maturation through an ER-associated degradation (ERAD) pathway. RNF148 is a testis-specific E3 ubiquitin ligase that is abundantly expressed in testes and slightly expressed in pancreas. Its expression is regulated by histone deacetylases.


Pssm-ID: 438454 [Multi-domain]  Cd Length: 49  Bit Score: 52.43  E-value: 4.09e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16802     3 CAVCIEPYKPNDVVRILTCNHLFHKNCIDPWLLEHRTCPMC 43
zf-RING_11 pfam17123
RING-like zinc finger;
94-122 1.01e-09

RING-like zinc finger;


Pssm-ID: 465355 [Multi-domain]  Cd Length: 29  Bit Score: 51.00  E-value: 1.01e-09
                          10        20
                  ....*....|....*....|....*....
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECV 122
Cdd:pfam17123   1 ECSICLDEFKPGQALFVLPCSHVFHYKCI 29
RING-H2_RNF150 cd16805
RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins; ...
93-135 1.54e-09

RING finger, H2 subclass, found in RING finger protein 150 (RNF150) and similar proteins; RNF150 is a RING finger protein and its polymorphisms may be associated with chronic obstructive pulmonary disease (COPD) risk in the Chinese population. Further studies with larger numbers of participants worldwide are needed for validation of the relationships between RNF150 genetic variants and the pathogenesis of COPD. RNF150 contains an N-terminal signal peptide, a protease-associated (PA) domain, a transmembrane (TM) domain and a C-terminal C3H2C3-type RING-H2 finger domain followed by a putative PEST sequence.


Pssm-ID: 438456 [Multi-domain]  Cd Length: 55  Bit Score: 51.21  E-value: 1.54e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  93 NECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16805     7 DNCAVCIEGYKPNDVVRILPCRHLFHKSCVDPWLLDHRTCPMC 49
RING-H2_RHA1-like cd23121
RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) ...
93-135 1.64e-09

RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 finger A1a (RHA1A), A1b (RHA1B) and similar proteins; This subfamily includes Arabidopsis thaliana RHA1A, RHA1B and XERICO. RHA1A is a probable E3 ubiquitin-protein ligase that may possess E3 ubiquitin ligase activity in vitro. RHA1B possesses E3 ubiquitin-protein ligase activity when associated with the E2 enzyme UBC8 in vitro. XERICO functions on abscisic acid homeostasis at post-translational level, probably through ubiquitin/proteasome-dependent substrate-specific degradation. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438483 [Multi-domain]  Cd Length: 50  Bit Score: 50.95  E-value: 1.64e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972253235  93 NECAICMIDFEPGERIRFLP-CMHSFHQECVDEWL-MKSFTCPSC 135
Cdd:cd23121     2 DCCAICLSDFNSDEKLRQLPkCGHIFHHHCLDRWIrYNKITCPLC 46
RING-H2_RNF122 cd16676
RING finger, H2 subclass, found in RING finger protein 122 (RNF122) and similar proteins; ...
95-139 2.98e-09

RING finger, H2 subclass, found in RING finger protein 122 (RNF122) and similar proteins; RNF122 is a RING finger protein associated with HEK 293T cell viability. It is localized to the endoplasmic reticulum (ER) and the Golgi apparatus, and overexpressed in anaplastic thyroid cancer cells. RNF122 functions as an E3 ubiquitin ligase that can ubiquitinate itself and undergo degradation through its RING finger in a proteasome-dependent manner. It interacts with calcium-modulating cyclophilin ligand (CAML), which is not a substrate, but a stabilizer of RNF122. RNF122 contains an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438338 [Multi-domain]  Cd Length: 47  Bit Score: 50.34  E-value: 2.98e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPV 139
Cdd:cd16676     3 CAVCLEDFKTKDELGVLPCQHAFHRKCLVKWLEIRCVCPMCNKPI 47
RING-H2_RNF115 cd16800
RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; ...
94-135 3.11e-09

RING finger, H2 subclass, found in RING finger protein 115 (RNF115) and similar proteins; RNF115, also known as Rab7-interacting ring finger protein (Rabring 7), or zinc finger protein 364 (ZNF364), or breast cancer-associated gene 2 (BCA2), is an E3 ubiquitin-protein ligase that is an endogenous inhibitor of adenosine monophosphate-activated protein kinase (AMPK) activation and its inhibition increases the efficacy of metformin in breast cancer cells. It also functions as a co-factor in the restriction imposed by tetherin on HIV-1, and targets HIV-1 Gag for lysosomal degradation, impairing virus assembly and release, in a tetherin-independent manner. Moreover, RNF115 is a Rab7-binding protein that stimulates c-Myc degradation through mono-ubiquitination of MM-1. It also plays crucial roles as a Rab7 target protein in vesicle traffic to late endosome/lysosome and lysosome biogenesis. Furthermore, RNF115 and the related protein, RNF126 associate with the epidermal growth factor receptor (EGFR) and promote ubiquitylation of EGFR, suggesting they play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors. RNF115 contains an N-terminal BCA2 Zinc-finger domain (BZF), the AKT-phosphorylation sites, and the C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438452 [Multi-domain]  Cd Length: 50  Bit Score: 50.33  E-value: 3.11e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16800     2 ECPVCKEDYTVGEQVRQLPCNHFFHSDCIVPWLELHDTCPVC 43
RING-H2_RNF24 cd16675
RING finger, H2 subclass, found in RING finger protein 24 (RNF24) and similar proteins; RNF24 ...
95-139 6.50e-09

RING finger, H2 subclass, found in RING finger protein 24 (RNF24) and similar proteins; RNF24 is an intrinsic membrane protein localized in the Golgi apparatus. It specifically interacts with the ankyrin-repeats domains (ARDs) of TRPC1, -3, -4, -5, -6, and -7, and affects TRPC intracellular trafficking without affecting their activity. RNF24 contains an N-terminal transmembrane domain and a C-terminal C3H2C3-type RING-H2 finger.


Pssm-ID: 438337 [Multi-domain]  Cd Length: 54  Bit Score: 49.63  E-value: 6.50e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPV 139
Cdd:cd16675     3 CAVCLEEFKPKDELGICPCKHAFHRKCLIKWLEVRKVCPLCNMPV 47
RING-H2_TTC3 cd16481
RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar ...
95-139 2.24e-08

RING finger, H2 subclass, found in Tetratricopeptide repeat protein 3 (TTC3) and similar proteins; TTC3, also known as protein DCRR1, TPR repeat protein D, TPR repeat protein 3, or RING finger protein 105 (RNF105), is an E3 ubiquitin-protein ligase encoded by a gene within the Down syndrome (DS) critical region on chromosome 21. It affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. It inhibits the neuronal-like differentiation of pheocromocytoma cells by activating RhoA and by binding to Citron proteins. TTC3 is an Akt-specific E3 ligase that binds to phosphorylated Akt and facilitates its ubiquitination and degradation within the nucleus. It contains four N-terminal TPR motifs, a potential coiled-coil region and a Citron binding region in the central part, and a C-terminal C3H2C2-type RING-H2 finger.


Pssm-ID: 438144 [Multi-domain]  Cd Length: 45  Bit Score: 48.11  E-value: 2.24e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972253235  95 CAICMIDFEPGERiRFLPCMHSFHQECVDEWLMKSFTCPSCLEPV 139
Cdd:cd16481     2 CIICHDDLKPDQL-AKLECGHIFHKECIKQWLKEQSTCPTCRVHV 45
RING-H2_NIPL1-like cd23119
RING finger, H2 subclass, found in Arabidopsis thaliana NEP1-interacting protein-like 1 (NIPL1) ...
94-135 2.47e-08

RING finger, H2 subclass, found in Arabidopsis thaliana NEP1-interacting protein-like 1 (NIPL1) and similar proteins; This subfamily includes Arabidopsis thaliana NIPL1 and MISFOLDED PROTEIN SENSING RING E3 LIGASE 1 (MPSR1). NIPL1, also called RING-H2 finger protein ATL27, may be involved in the early steps of the plant defense signaling pathway. MPSR1 is a cytoplasmic E3 ubiquitin-protein ligase involved in protein quality control (PQC) under proteotoxic stress. It is essential for plant survival under proteotoxic stress. It functions by removing damaged proteins before they form cytotoxic aggregates. It recognizes misfolded proteins selectively and tethers polyubiquitin chains to the proteins directly for subsequent degradation by the 26S proteasome pathway. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438481 [Multi-domain]  Cd Length: 44  Bit Score: 47.88  E-value: 2.47e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  94 ECAICMIDFEPGERIRFLP-CMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd23119     1 CCTICLQDLQVGEIARSLPhCHHTFHLGCVDKWLGRHGSCPVC 43
RING-HC_EHV1-like cd23130
RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) ...
93-145 1.99e-07

RING finger, HC subclass, found in Equid alphaherpesvirus 1 (Equine herpesvirus 1/EHV-1) regulatory protein and similar proteins; EHV-1 regulatory protein belongs to the Vmw110 (IPC0) protein family. It contains a typical C3HC4-type RING-HC finger and binds zinc stably.


Pssm-ID: 438492 [Multi-domain]  Cd Length: 51  Bit Score: 45.42  E-value: 1.99e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972253235  93 NECAICMIDfePGERIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPVDSTILS 145
Cdd:cd23130     1 DVCPICLDD--PEDEAITLPCLHQFCYTCILRWLQTSPTCPLCKTPVTSIIHS 51
RING smart00184
Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and ...
95-135 2.16e-07

Ring finger; E3 ubiquitin-protein ligase activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain; Various RING fingers exhibit binding activity towards E2 ubiquitin-conjugating enzymes (Ubc' s)


Pssm-ID: 214546 [Multi-domain]  Cd Length: 40  Bit Score: 45.19  E-value: 2.16e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1972253235   95 CAICMIDFEpgERIRFLPCMHSFHQECVDEWLM-KSFTCPSC 135
Cdd:smart00184   1 CPICLEEYL--KDPVILPCGHTFCRSCIRKWLEsGNNTCPIC 40
RING-H2_RHA2B cd23123
RING finger, H2 subclass, found in Saccharomyces cerevisiae RING-H2 zinc finger protein RHA2B ...
93-138 3.44e-07

RING finger, H2 subclass, found in Saccharomyces cerevisiae RING-H2 zinc finger protein RHA2B and similar proteins; RHA2B is an E3 ubiquitin-protein ligase involved in the positive regulation of abscisic acid (ABA) signaling and responses to salt and osmotic stresses during seed germination and early seedling development. It acts additively with RHA2A in regulating ABA signaling and drought response. RHA2B contains a C3H2C3-type RING-H2 finger.


Pssm-ID: 438485 [Multi-domain]  Cd Length: 47  Bit Score: 44.88  E-value: 3.44e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1972253235  93 NECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMK-SFTCPSCLEP 138
Cdd:cd23123     1 SDCCICLDKLKTGEEVKKLDCRHKFHKQCIEGWLKHlNFNCPLCRSP 47
RING-H2_MBR cd23113
RING finger, H2 subclass, found in Arabidopsis thaliana MED25-binding RING-H2 protein (MBR) ...
95-135 4.47e-07

RING finger, H2 subclass, found in Arabidopsis thaliana MED25-binding RING-H2 protein (MBR) and similar proteins; This subfamily includes MBR1 and MBR2 (also called HAL3-interacting protein 1 or AtHIP1). They are E3 ubiquitin-protein ligases that function as regulators of MED25 stability by targeting MED25 for degradation in a RING-H2-dependent manner. Proteasome-dependent degradation of MED25 seems to activate its function as a positive regulator of FLOWERING LOCUS T (FT) and is important to induce the expression of FT, and consequently to promote flowering. MBR2 may also function downstream of HAL3 and be required for HAL3-regulated plant growth. Activation of MBR2 by HAL3 may lead to the degradation of cell cycle suppressors, resulting in enhancement of cell division and plant growth. Both MBR1 and MBR2 contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438475 [Multi-domain]  Cd Length: 50  Bit Score: 44.48  E-value: 4.47e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd23113     5 CCICQEEYEEGDELGTIECGHEYHSDCIKQWLVQKNLCPIC 45
mRING-CH-C4HC2H_ZNRF2 cd16695
Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 2 (ZNRF2) ...
92-133 4.47e-07

Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 2 (ZNRF2) and similar proteins; ZNRF2, also known as protein Ells2 or RING finger protein 202 (RNF202), is an E3 ubiquitin-protein ligase that is highly expressed in the nervous system during development and is present in presynaptic plasma membranes. It is N-myrisotoylated and is also located in the endosome-lysosome compartment in fibroblasts. It contains an N-terminal MAGE domain, and a special C-terminal domain that combines a zinc finger and a modified C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of RING-H2 finger. Only the RING finger of the zinc finger-RING finger motif is required for its E3 ubiquitin ligase activity. Together with its sister protein ZNRF1, ZNRF2 regulates the ubiquitous Na+/K+ pump (Na+/K+ATPase).


Pssm-ID: 438356 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 4.47e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  92 SNECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCP 133
Cdd:cd16695    10 AGECAICLEELQQGDTIARLPCLCIYHKGCIDEWFEVNRSCP 51
mRING-CH-C4HC2H_ZNRF1 cd16694
Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 1 (ZNRF1) ...
94-133 5.55e-07

Modified RING-CH finger, H2 subclass (C4HC2H-type), found in zinc/RING finger protein 1 (ZNRF1) and similar proteins; ZNRF1, also known as Nerve injury-induced gene 283 protein (nin283), or peripheral nerve injury protein (PNIP), is an E3 ubiquitin-protein ligase that is highly expressed in the nervous system during development and is associated with synaptic vesicle membranes. It is N-myrisotoylated and is also located in the endosome-lysosome compartment in fibroblasts, suggesting it may participate in ubiquitin-mediated protein modification. It contains an N-terminal MAGE domain, and a special C-terminal domain that combines a zinc finger and a modified C4HC2H-type RING-CH finger, rather than the typical C4HC3-type RING-CH finger, which is a variant of the RING-H2 finger. Only the RING finger of the zinc finger-RING finger motif is required for its E3 ubiquitin ligase activity. ZNRF1 regulates Schwann cell differentiation by proteasomal degradation of glutamine synthetase (GS). It also mediates regulation of neuritogenesis via interaction with beta-tubulin type 2 (Tubb2). Moreover, ZNRF1 promotes Wallerian degeneration by degrading AKT to induce glycogen synthase kinase-3beta (GSK3B)-dependent CRMP2 phosphorylation. Furthermore, ZNRF1 and its sister protein ZNRF2 regulate the ubiquitous Na+/K+ pump (Na+/K+ATPase). In addition, ZNRF1 may be associated with leukemogenesis of acute lymphoblastic leukemia (ALL) with paired box domain gene 5 (PAX5) alteration.


Pssm-ID: 438355 [Multi-domain]  Cd Length: 45  Bit Score: 44.25  E-value: 5.55e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCP 133
Cdd:cd16694     1 ECVICLEELLQGDTIARLPCLCIYHKSCIDSWFEVNRSCP 40
RING-H2_AMFR cd16455
RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar ...
93-139 1.15e-06

RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar proteins; AMFR, also known as AMF receptor, or RING finger protein 45, or ER-protein gp78, is an internalizing cell surface glycoprotein localized in both plasma membrane caveolae and the endoplasmic reticulum (ER). It is involved in the regulation of cellular adhesion, proliferation, motility and apoptosis, as well as in the process of learning and memory. AMFR also functions as a RING finger-dependent ubiquitin protein ligase (E3) implicated in the degradation from the ER. AMFR contains an N-terminal RING-H2 finger and a C-terminal ubiquitin-associated (UBA)-like CUE domain.


Pssm-ID: 438119 [Multi-domain]  Cd Length: 44  Bit Score: 43.21  E-value: 1.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1972253235  93 NECAICmidFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPV 139
Cdd:cd16455     1 DDCAIC---WESMQSARKLPCGHLFHNSCLRSWLEQDTSCPTCRMSL 44
RING-H2_TRAIP cd16480
RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; ...
95-135 1.79e-06

RING finger, H2 subclass, found in TRAF-interacting protein (TRAIP) and similar proteins; TRAIP, also known as RING finger protein 206 (RNF206) or TRIP, is a ubiquitously expressed nucleolar E3 ubiquitin ligase important for cellular proliferation and differentiation. It is found near mitotic chromosomes and functions as a regulator of the spindle assembly checkpoint. TRAIP interacts with tumor necrosis factor (TNF)-receptor-associated factor (TRAF) proteins and inhibits TNF-alpha-mediated nuclear factor (NF)-kappaB activation. It also interacts with two tumor suppressors CYLD and spleen tyrosine kinase (Syk), and DNA polymerase eta, which facilitates translesional synthesis after DNA damage. TRAIP contains an N-terminal C3H2C2-type RING-H2 finger and an extended coiled-coil domain.


Pssm-ID: 438143 [Multi-domain]  Cd Length: 43  Bit Score: 42.80  E-value: 1.79e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16480     2 CTICSDFFDNSRDVAAIHCGHTFHYDCLLQWFDTSRTCPQC 42
RING-H2_RNF139 cd16683
RING finger, H2 subclass, found in RING finger protein 139 (RNF139) and similar proteins; ...
95-139 4.07e-06

RING finger, H2 subclass, found in RING finger protein 139 (RNF139) and similar proteins; RNF139, also known as translocation in renal carcinoma on chromosome 8 protein (TRC8), is an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. It is a tumor suppressor that has been implicated in a novel regulatory relationship linking the cholesterol/lipid biosynthetic pathway with cellular growth control. A mutation in RNF139 has been identified in families with hereditary renal (RCC) and thyroid cancers. RNF139 physically and functionally interacts with von Hippel-Lindau (VHL), which is part of an SCF related E3-ubiquitin ligase complex with "gatekeeper" function in renal carcinoma and is defective in most sporadic clear-cell renal cell carcinomas (ccRCC). It suppresses growth and functions with VHL in a common pathway. RNF139 also suppresses tumorigenesis by targeting heme oxygenase-1 for ubiquitination and degradation. Moreover, RNF139 is a target of Translin (TSN), a posttranscriptional regulator of genes transcribed by the transcription factor CREM-tau in postmeiotic male germ cells, suggesting a role of RNF139 in dysgerminoma. In addition, RNF139 forms an integral part of a novel multi-protein ER complex, containing MHC I, US2, and signal peptide peptidase, which is associated with the ER-associated degradation (ERAD) pathway. It is required for the ubiquitination of MHC class I molecules before dislocation from the ER. As a novel sterol-sensing ER membrane protein, RNF139 hinders sterol regulatory element-binding protein-2 (SREBP-2) processing through interaction with SREBP-2 and SREBP cleavage-activated protein (SCAP), regulating its own turnover rate via its E3 ubiquitin ligase activity. RNF139 shows two regions of similarity with the receptor for sonic hedgehog (SHH), Patched. The first region corresponds to the second extracellular domain of Patched, which is involved in binding SHH. The second region is a putative sterol-sensing domain (SSD). The C-terminal half of RNF139 contains a C3H2C3-type RING-H2 finger with E3-ubiquitin ligase activity in vitro.


Pssm-ID: 438345 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 4.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972253235  95 CAICMIDFEPGERIRflPCMHSFHQECVDEWLMKSFTCPSCLEPV 139
Cdd:cd16683     7 CAICYQEFTTSARIT--PCNHYFHALCLRKWLYIQDTCPMCHQKV 49
RING-H2_synoviolin cd16479
RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as ...
93-135 4.48e-06

RING finger, H2 subclass, found in synoviolin and similar proteins; Synoviolin, also known as synovial apoptosis inhibitor 1 (Syvn1), Hrd1, or Der3, is an endoplasmic reticulum (ER)-anchoring E3 ubiquitin ligase that functions as a suppressor of ER stress-induced apoptosis and plays a role in homeostasis maintenance. It also targets tumor suppressor gene p53 for proteasomal degradation, suggesting crosstalk between ER associated degradation (ERAD) and p53 mediated apoptotic pathway under ER stress. Moreover, synoviolin controls body weight and mitochondrial biogenesis through negative regulation of the thermogenic coactivator peroxisome proliferator-activated receptor coactivator (PGC)-1beta. It upregulates amyloid beta production by targeting a negative regulator of gamma-secretase, Retention in endoplasmic reticulum 1 (Rer1), for degradation. It is also involved in the degradation of endogenous immature nicastrin, and affects amyloid beta-protein generation. Moreover, synoviolin is highly expressed in rheumatoid synovial cells and may be involved in the pathogenesis of rheumatoid arthritis (RA). It functions as an anti-apoptotic factor that is responsible for the outgrowth of synovial cells during the development of RA. It promotes inositol-requiring enzyme 1 (IRE1) ubiquitination and degradation in synovial fibroblasts with collagen-induced arthritis. Furthermore, the upregulation of synoviolin may represent a protective response against neurodegeneration in Parkinson's disease (PD). In addition, synoviolin is involved in liver fibrogenesis. Synoviolin contains a C3H2C2-type RING-H2 finger.


Pssm-ID: 438142 [Multi-domain]  Cd Length: 43  Bit Score: 41.57  E-value: 4.48e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  93 NECAICMIDFEPGERIrfLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16479     2 NTCIICREEMTVGAKK--LPCGHIFHLSCLRSWLQRQQTCPTC 42
RING-HC_RNF141 cd16545
RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; ...
93-135 6.00e-06

RING finger, HC subclass, found in RING finger protein 141 (RNF141) and similar proteins; RNF141, also known as zinc finger protein 230 (ZNF230), is a RING finger protein present primarily in the nuclei of spermatogonia, the acrosome, and the tail of spermatozoa. It may have a broad function during early development of vertebrates. It plays an important role in spermatogenesis, including spermatogenic cell proliferation and sperm maturation, as well as motility and fertilization. It also exhibits DNA binding activity. RNF141/ZNF230 gene mutations may be associated with azoospermia. RNF141 contains a C3HC4-type RING finger domain that may function as an activator module in transcription.


Pssm-ID: 438207 [Multi-domain]  Cd Length: 40  Bit Score: 41.31  E-value: 6.00e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  93 NECAICMiDFEPGeriRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16545     1 EECCICM-DRKAD---LILPCAHSYCQKCIDKWSDRHRTCPIC 39
HRD1 COG5243
HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein ...
93-170 6.99e-06

HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227568 [Multi-domain]  Cd Length: 491  Bit Score: 44.96  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972253235  93 NECAICMID-FEPGE---------RIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPV-----DSTILSSLTAHNMQSLQQ 157
Cdd:COG5243   288 RTCTICMDEmFHPDHeplprgldmTPKRLPCGHILHLHCLKNWLERQQTCPICRRPVifdqsSPTPASPNVRNTQIATQV 367
                          90
                  ....*....|...
gi 1972253235 158 IVCSPTSSSTAKP 170
Cdd:COG5243   368 PNPDNTPTTTAVP 380
zf-C3HC4_2 pfam13923
Zinc finger, C3HC4 type (RING finger);
94-135 2.83e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 404756 [Multi-domain]  Cd Length: 40  Bit Score: 39.73  E-value: 2.83e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  94 ECAICMIDFEPGERIRflPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:pfam13923   1 MCPICMDMLKDPSTTT--PCGHVFCQDCILRALRAGNECPLC 40
RING-H2_RNF139-like cd16476
RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; ...
95-135 3.26e-05

RING finger, H2 subclass, found in RING finger proteins RNF139, RNF145, and similar proteins; RNF139, also known as translocation in renal carcinoma on chromosome 8 protein (TRC8), is an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. It is a tumor suppressor that has been implicated in a novel regulatory relationship linking the cholesterol/lipid biosynthetic pathway with cellular growth control. A mutation in RNF139 has been identified in families with hereditary renal (RCC) and thyroid cancers. RNF145 is an uncharacterized RING finger protein encoded by the RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139. Both RNF139 and RNF145 contain a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity.


Pssm-ID: 438139 [Multi-domain]  Cd Length: 41  Bit Score: 39.36  E-value: 3.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEpgeRIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16476     3 CAICYQEMK---EARITPCNHFFHGLCLRKWLYVQDTCPLC 40
RING-H2_RHF2A cd23122
RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 zinc finger protein RHF2A and ...
89-139 3.73e-05

RING finger, H2 subclass, found in Arabidopsis thaliana RING-H2 zinc finger protein RHF2A and similar proteins; RHF2A is an E3 ubiquitin-protein ligase involved in the positive regulation of the gametogenesis progression. It is required for the degradation of KRP6, a cyclin-dependent kinase inhibitor which accumulates during meiosis and blocks the progression of subsequent mitoses during gametophytes development. It functions in association with RHF1A. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438484 [Multi-domain]  Cd Length: 63  Bit Score: 39.96  E-value: 3.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1972253235  89 DMTSNECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPV 139
Cdd:cd23122     8 DACEDACSICLESFCEADPATVTSCKHEYHLQCILEWSQRSKECPMCWQAL 58
RING-H2_TUL1-like cd23117
RING finger, H2 subclass, found in Saccharomyces cerevisiae transmembrane E3 ubiquitin-protein ...
89-138 3.85e-05

RING finger, H2 subclass, found in Saccharomyces cerevisiae transmembrane E3 ubiquitin-protein ligase 1 (TUL1) and similar proteins; This subfamily includes Saccharomyces cerevisiae TUL1, Schizosaccharomyces pombe DSC E3 ubiquitin ligase complex subunit 1 (DSC1), and Arabidopsis thaliana protein FLYING SAUCER 2 (FLY2). TUL1 is the catalytic component of DSC E3 ubiquitin ligase complexes that tag proteins present in Golgi, endosome and vacuole membranes and function in protein homeostasis under non-stress conditions, and support a role in protein quality control. It mediates ubiquitination of vacuolar proteins such as CPS1, PPN1, PEP12 and other proteins containing exposed hydrophilic residues within their transmembrane domains, leading to their sorting into internal vesicles in late endosomes. TUL1 also targets the unpalmitoylated endosomal SNARE TLG1 to the multivesicular body (MVB) pathway. DSC1, also known as defective for SREBP cleavage protein 1, is the catalytic component of the DSC E3 ubiquitin ligase complex required for the sre1 transcriptional activator proteolytic cleavage to release the soluble transcription factor from the membrane in low oxygen or sterol conditions. FLY2 acts as an E3 ubiquitin-protein ligase that may be involved in xylem development. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438479 [Multi-domain]  Cd Length: 59  Bit Score: 39.69  E-value: 3.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972253235  89 DMTSNECAICMIDFEPGERIRFL------PCMHSFHQECVDEWLMKSFTCPSCLEP 138
Cdd:cd23117     1 ENGSVDCVICMSDIELPSTNSVRrdymvtPCNHIFHTNCLERWMDIKLECPTCRRP 56
zf-C3HC4 pfam00097
Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a ...
95-135 5.73e-05

Zinc finger, C3HC4 type (RING finger); The C3HC4 type zinc-finger (RING finger) is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C where X is any amino acid. Many proteins containing a RING finger play a key role in the ubiquitination pathway.


Pssm-ID: 395049 [Multi-domain]  Cd Length: 40  Bit Score: 38.88  E-value: 5.73e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  95 CAICMIDFEPGerIRFLPCMHSFHQECVDEWLM-KSFTCPSC 135
Cdd:pfam00097   1 CPICLEEPKDP--VTLLPCGHLFCSKCIRSWLEsGNVTCPLC 40
RING-H2_RNF121-like cd16475
RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins; ...
93-137 6.07e-05

RING finger, H2 subclass, found in RING finger proteins RNF121, RNF175 and similar proteins; This subfamily includes RNF121, RNF175 and similar proteins. RNF121 is an E3-ubiquitin ligase present in the endoplasmic reticulum (ER) and cis-Golgi compartments. It is a novel regulator of apoptosis. It also facilitates the degradation and membrane localization of voltage-gated sodium (NaV) channels, and thus plays a role in the quality control of NaV channels during their synthesis and subsequent transport to the membrane. Moreover, RNF121 acts as a broad regulator of nuclear factor kappaB (NF-kappaB) signaling since its silencing also dampens NF-kappaB activation following stimulation of toll-like receptors (TLRs), nod-like receptors (NLRs), RIG-I-like Receptors (RLRs) or after DNA damage. RNF121 contains five conserved transmembrane (TM) domains and a C3H2C2-type RING-H2 finger. RNF175 is an uncharacterized RING finger protein that shows high sequence similarity with RNF121. This family also includes Arabidopsis RING finger E3 ligase RHA2A, RHA2B, and their homologs. RHA2A is a positive regulator of abscisic acid (ABA) signaling during seed germination and early seedling development. RHA2B may play a role in the ubiquitin-dependent proteolysis pathway that respond to proteasome inhibition. All subfamily members contain a C3H2C3-type RING-H2 finger, which is responsible for E3-ubiquitin ligase activity.


Pssm-ID: 438138 [Multi-domain]  Cd Length: 55  Bit Score: 38.81  E-value: 6.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972253235  93 NECAICMIDFEP-------GERIRFLPCMHSFHQECVDEWLM--KSFTCPSCLE 137
Cdd:cd16475     1 NVCAVCGQKLDVddneegiIEKTYKLSCNHVFHEFCIRGWCIvgKKQTCPYCKE 54
mRING-H2-C3DHC3_ZFPL1 cd16487
Modified RING finger, H2 subclass (C3DHC3-type), found in zinc finger protein-like 1 (ZFPL1) ...
95-139 1.28e-04

Modified RING finger, H2 subclass (C3DHC3-type), found in zinc finger protein-like 1 (ZFPL1) and similar proteins; ZFPL1, also known as zinc finger protein MCG4, is a novel mitotic Golgi phosphoprotein required for cis-Golgi integrity and efficient endoplasmic reticulum (ER)-to-Golgi transport via directly interacting with the cis-Golgi matrix protein GM130. ZFPL1 is a widely expressed integral membrane protein with two predicted zinc fingers at its N-terminus. One is a novel type of zinc finger, and the other is a modified RING-H2 finger that lacks the fourth zinc-binding residue of the consensus C3H2C3-type RING-H2 finger. It also contains a bipartite nuclear localization signal (NLS), and a leucine zipper at the C-terminus.


Pssm-ID: 438150 [Multi-domain]  Cd Length: 57  Bit Score: 38.05  E-value: 1.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972253235  95 CAICMIDFEPGERIRfLPCMHSFHQECVDEWLMK--------SFTCPSCLEPV 139
Cdd:cd16487     4 CTLCNTSLANGDVVR-LVCYDLFHWSCLNEYAAQlpantapaGYTCPQCKGPI 55
RING-H2_Vps11 cd16688
RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog ...
108-137 1.49e-04

RING finger, H2 subclass, found in vacuolar protein sorting-associated protein 11 homolog (Vps11) and similar proteins; Vps11, also known as RING finger protein 108 (RNF108), is a soluble protein involved in regulation of glycolipid degradation and retrograde toxin transport. It is highly expressed in heart and pancreas. Vps11 associates with Vps16, Vps18, and Vps33 to form a Class C Vps core complex that is required for soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE)-mediated membrane fusion at the lysosome-like yeast vacuole. The core complex, together with two additional compartment-specific subunits, forms the tethering complexes HOPS (homotypic vacuole fusion and protein sorting) and CORVET (class C core vacuole/endosome transport). CORVET contains the additional Vps3 and Vps8 subunits. It operates at endosomes, controls traffic into late endosomes and interacts with the Rab5/Vps21-GTP form. HOPS contains the additional Vps39 and Vps41 subunits. It operates at the lysosomal vacuole, controls all traffic from late endosomes into the vacuole and interacts with the Rab7/Ypt7-GTP form. Vps11 is a central scaffold protein upon which both HOPS and CORVET assemble. The HOPS and CORVET complexes disassemble in the absence of Vps11, resulting in massive fragmentation of vacuoles. Vps11 contains a clathrin repeat domain and a C-terminal C3H2C3-type RING-H2 finger. This subfamily also includes Vps11 homologs found in fungi, such as Saccharomyces cerevisiae vacuolar membrane protein Pep5p, also known as carboxypeptidase Y-deficient protein 5, vacuolar morphogenesis protein 1, or vacuolar biogenesis protein END1. Pep5p is essential for vacuolar biogenesis. It associates with Pep3p to form a core Pep3p/Pep5p complex that promotes vesicular docking/fusion reactions in conjunction with SNARE proteins at multiple steps in transport routes to the vacuole.


Pssm-ID: 438349 [Multi-domain]  Cd Length: 44  Bit Score: 37.71  E-value: 1.49e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1972253235 108 IRFLpCMHSFHQECVDEWLMKSFTCPSCLE 137
Cdd:cd16688    15 VHFL-CGHSFHQHCLEDYEENDRECPLCAP 43
RING-HC_CHFR cd16503
RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein ...
95-141 1.64e-04

RING finger, HC subclass, found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also known as RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22, and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression, and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated (FHA) domain and a C3HC4-type RING-HC finger.


Pssm-ID: 438166 [Multi-domain]  Cd Length: 55  Bit Score: 37.73  E-value: 1.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1972253235  95 CAICM-IDFEPgerIRFLPCMHSFHQECVDEWLMKS-FTCPSCLEPVDS 141
Cdd:cd16503     5 CSICQdLLHDC---VSLQPCMHNFCAACYSDWMERSnTECPTCRATVQR 50
zf-RING_5 pfam14634
zinc-RING finger domain;
94-135 1.77e-04

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 37.41  E-value: 1.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEwLMKSFTCPSC 135
Cdd:pfam14634   1 HCNKCFKELSKTRPFYLTSCGHIFCEECLTR-LLQERQCPIC 41
RING-HC_RNF213 cd16561
RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; ...
94-139 3.27e-04

RING finger, HC subclass, found in RING finger protein 213 (RNF213) and similar proteins; RNF213, also known as ALK lymphoma oligomerization partner on chromosome 17 or Moyamoya steno-occlusive disease-associated AAA+ and RING finger protein (mysterin), is an intracellular soluble protein that functions as an E3 ubiquitin-protein ligase and AAA+ ATPase, which possibly contributes to vascular development through mechanical processes in the cell. It plays a unique role in endothelial cells for proper gene expression in response to inflammatory signals from the environment. Mutations in RNF213 may be associated with Moyamoya disease (MMD), an idiopathic cerebrovascular occlusive disorder prevalent in East Asia. It also acts as a nuclear marker for acanthomorph phylogeny. RNF213 contains two tandem enzymatically active AAA+ ATPase modules and a C3HC4-type RING-HC finger. It can form a huge ring-shaped oligomeric complex.


Pssm-ID: 438223 [Multi-domain]  Cd Length: 50  Bit Score: 36.87  E-value: 3.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1972253235  94 ECAICMIDFEpgeRIRFLPCMHSFHQECVDEWLMKSFTCPSCLEPV 139
Cdd:cd16561     4 ECSICLEDLN---DPVKLPCDHVFCEECIRQWLPGQMSCPLCRTEL 46
RING-H2_Dmap-like cd16458
RING finger, H2 subclass, found in defective in mitotic arrest proteins (Dmap) and similar ...
94-135 3.45e-04

RING finger, H2 subclass, found in defective in mitotic arrest proteins (Dmap) and similar proteins; This subfamily includes Schizosaccharomyces pombe protein Dma1 (SpDma1p), Saccharomyces cerevisiae proteins Dma1 (ScDma1p) and Dma2 (ScDma2p), and their homologs from fungi. SpDma1p was originally isolated as a multicopy suppressor of the temperature-sensitive growth phenotype caused by cdc16 mutations. It functions to prevent mitotic exit and cytokinesis during spindle checkpoint arrest by inhibiting septation initiation network (SIN) signaling. ScDma1p and ScDma2p, also known as checkpoint forkhead associated with RING domains-containing protein 1 and 2 respectively, seem to be functionally redundant. They are involved in proper septin ring positioning and cytokinesis. The simultaneous lack of Dma1 and Dma2 leads to spindle mispositioning and defects in the spindle position checkpoint. All members of this family contain a forkhead-associated (FHA) domain and a C3H2C3-type RING-H2 finger, the latter suggesting they may possess E3 ubiquitin-ligase activities.


Pssm-ID: 319372 [Multi-domain]  Cd Length: 47  Bit Score: 36.70  E-value: 3.45e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECVDEWLMKS---FTCPSC 135
Cdd:cd16458     2 DCSICLFPVLPCQALFVSPCAHSWHFKCIRPLLEASypqFSCPNC 46
zf-rbx1 pfam12678
RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be ...
95-135 3.79e-04

RING-H2 zinc finger domain; There are 8 cysteine/ histidine residues which are proposed to be the conserved residues involved in zinc binding. The protein, of which this domain is the conserved region, participates in diverse functions relevant to chromosome metabolism and cell cycle control.


Pssm-ID: 463669 [Multi-domain]  Cd Length: 55  Bit Score: 36.92  E-value: 3.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1972253235  95 CAICMIDFE--------PGE---RIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:pfam12678   3 CAICRNPFMepcpecqaPGDdecPVVWGECGHAFHLHCISRWLKTNNTCPLC 54
RING-HC_RNFT1-like cd16532
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein ...
95-135 5.03e-04

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein RNFT1, RNFT2, and similar proteins; Both RNFT1 and RNFT2 are multi-pass membrane proteins containing a C3HC4-type RING-HC finger. Their biological roles remain unclear.


Pssm-ID: 438194 [Multi-domain]  Cd Length: 41  Bit Score: 36.13  E-value: 5.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMidfEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16532     3 CPICQ---DEFKDPVVLRCKHIFCEDCVSEWFERERTCPLC 40
RING-HC cd16449
HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type ...
94-135 5.05e-04

HC subclass of RING (RING-HC) finger and its variants; The RING finger is a specialized type of Zn-finger of 40 to 60 residues that binds two atoms of zinc. It is defined by the "cross-brace" motif that chelates zinc atoms by eight amino acid residues, typically Cys or His, arranged in a characteristic spacing. Canonical RING motifs have been categorized into two major subclasses, RING-HC (C3HC4-type) and RING-H2 (C3H2C3-type), according to their Cys/His content. There are also many variants of RING fingers. Some have a different Cys/His pattern. Some lack a single Cys or His residue at typical Zn ligand positions, especially, the fourth or eighth zinc ligand is prevalently exchanged for an Asp, which can chelate Zn in a RING finger as well. This family corresponds to the HC subclass of RING (RING-HC) fingers that are characterized by containing C3HC4-type canonical RING-HC fingers or noncanonical RING-HC finger variants, including C4C4-, C3HC3D-, C2H2C4-, and C3HC5-type modified RING-HC fingers. The canonical RING-HC finger has been defined as C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C. It binds two Zn ions in a unique "cross-brace" arrangement, which distinguishes it from tandem zinc fingers and other similar motifs. RING-HC fingers can be found in a group of diverse proteins with a variety of cellular functions, including oncogenesis, development, viral replication, signal transduction, the cell cycle, and apoptosis. Many of them are ubiquitin-protein ligases (E3s) that serve as scaffolds for binding to ubiquitin-conjugating enzymes (E2s, also referred to as ubiquitin carrier proteins or UBCs) in close proximity to substrate proteins, which enables efficient transfer of ubiquitin from E2 to the substrates.


Pssm-ID: 438113 [Multi-domain]  Cd Length: 41  Bit Score: 36.31  E-value: 5.05e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  94 ECAICMidfEPGERIRFLPCMHSFHQECVDEWLM-KSFTCPSC 135
Cdd:cd16449     2 ECPICL---ERLKDPVLLPCGHVFCRECIRRLLEsGSIKCPIC 41
RING-HC_RNF8 cd16535
RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is ...
111-141 8.07e-04

RING finger, HC subclass, found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal forkhead-associated (FHA) domain and a C-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438197 [Multi-domain]  Cd Length: 64  Bit Score: 36.22  E-value: 8.07e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1972253235 111 LPCMHSFHQECVDEWLMKSFTCPSCLEPVDS 141
Cdd:cd16535    17 LNCSHSFCSYCITEWMKRKKECPICRKPITS 47
PHA02929 PHA02929
N1R/p28-like protein; Provisional
94-145 8.30e-04

N1R/p28-like protein; Provisional


Pssm-ID: 222944 [Multi-domain]  Cd Length: 238  Bit Score: 38.61  E-value: 8.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972253235  94 ECAICM-IDFEPGERIRF---LP-CMHSFHQECVDEWLMKSFTCPSCLEPVDSTILS 145
Cdd:PHA02929  176 ECAICMeKVYDKEIKNMYfgiLSnCNHVFCIECIDIWKKEKNTCPVCRTPFISVIKS 232
mRING-C3HGC3_RFWD3 cd16450
Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing ...
92-135 8.74e-04

Modified RING finger, C3HGC3-type, found in RING finger and WD repeat domain-containing protein 3 (RFWD3) and similar proteins; RFWD3, also known as RING finger protein 201 (RNF201) or FLJ10520, is an E3 ubiquitin-protein ligase that forms a complex with Mdm2 and p53 to synergistically ubiquitinate p53 and acts as a positive regulator of p53 stability in response to DNA damage. It is phosphorylated by checkpoint kinase ATM/ATR and the phosphorylation mutant fails to stimulate p53 ubiquitination. RFWD3 also functions as a novel replication protein A (RPA)-associated protein involved in DNA replication checkpoint control. RFWD3 contains an N-terminal SQ-rich region followed by a RING finger domain that exhibits robust E3 ubiquitin ligase activity toward p53, a coiled-coil domain and three WD40 repeats in the C-terminus, the latter two of which may be responsible for protein-protein interaction. The RING finger in this family is a modified C3HGC3-type RING finger, but not a canonical C3H2C3-type RING-H2 finger or C3HC4-type RING-HC finger.


Pssm-ID: 438114 [Multi-domain]  Cd Length: 61  Bit Score: 36.05  E-value: 8.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1972253235  92 SNECAICmidFEP----GE-RIRFLPCMHSFHQECVDEWLMKSF-TCPSC 135
Cdd:cd16450     2 GNTCPIC---FEPwtssGEhRLVSLKCGHLFGYSCIEKWLKGKGkKCPQC 48
RING-H2_Pirh2-like cd16464
RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; ...
95-135 8.97e-04

RING finger, H2 subclass, found in p53-induced RING-H2 protein (Pirh2) and similar proteins; Pirh2, also known as RING finger and CHY zinc finger domain-containing protein 1 (Rchy1), androgen receptor N-terminal-interacting protein, CH-rich-interacting match with PLAG1, RING finger protein 199 (RNF199), or zinc finger protein 363 (ZNF363), is a p53 inducible E3 ubiquitin-protein ligase that functions as a negative regulator of p53. It preferably ubiquitylates the tetrameric form of p53 in vitro and in vivo, suggesting a role of Pirh2 in downregulating the transcriptionally active form of p53 in the cell. Moreover, Pirh2 inhibits the transcriptional activity of p73, a homolog of the tumor suppressor p53, by promoting its ubiquitination. It also monoubiquitinates DNA polymerase eta (PolH) to suppress translesion DNA synthesis. Furthermore, Pirh2 functions as a negative regulator of the cyclin-dependent kinase inhibitor p27(Kip1) function by promoting ubiquitin-dependent proteasomal degradation. Pirh2 enhances androgen receptor (AR) signaling through inhibition of histone deacetylase 1 (HDAC1) and is overexpressed in prostate cancer. It interacts with TIP60 and this association may regulate Pirh2 stability. In addition, the oncoprotein pleomorphic adenoma gene like 2 (PLAGL2) can bind to the Pirh2 dimer and therefore control the stability of Pirh2. Pirh2 contains a total of nine zinc-binding sites with six located at the N-terminal region, two in the C3H2C3-type RING-H2 domain, and one in the C-terminal region. Nine zinc binding sites comprise three different zinc coordination schemes, including RING type cross-brace zinc coordination, C4 zinc finger, and a novel left-handed beta-spiral zinc-binding motif formed by three recurrent CCHC sequence motifs. This subfamily also includes Drosophila melanogaster Deltex, a ubiquitously expressed cytoplasmic ubiquitin E3 ligase that mediates Notch activation in Drosophila. It selectively suppresses T-cell activation through degradation of a key signaling molecule, MAP kinase kinase kinase 1 (MEKK1). It also inhibits Jun-mediated transcription at the stage of Ras-dependent Jun N-terminal protein kinase (JNK) activation. Deltex contains N-terminal two Notch-binding WWE domains that physically interact with the Notch ankyrin domains, a proline-rich motif that shares homology with SH3-binding domains, and a RING finger at the C-terminus.


Pssm-ID: 438127 [Multi-domain]  Cd Length: 45  Bit Score: 35.71  E-value: 8.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  95 CAICMID-FEPGERIRFLPCMHSFHQECVDEWLMK-SFTCPSC 135
Cdd:cd16464     2 CPVCLEDlFTSREPVHVLPCGHLMHSTCFEEYLKSgNYRCPLC 44
RING-H2_ASR1 cd23120
RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger ...
92-144 9.60e-04

RING finger, H2 subclass, found in Saccharomyces cerevisiae alcohol-sensitive RING finger protein 1 (ASR1) and similar proteins; ASR1 is required for tolerance to alcohol. It signals alcohol stress to the nucleus. ASR1 contains a C3H2C3-type RING-H2 finger.


Pssm-ID: 438482 [Multi-domain]  Cd Length: 54  Bit Score: 35.59  E-value: 9.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972253235  92 SNECAICMIDFEPGERiRFLPCMHSFHQECVDEWLMKS--FTCPSClePVDSTIL 144
Cdd:cd23120     1 IEECPICLEEMNSGTG-YLADCGHEFHLTCIREWHNKSgnLDCPIC--RVESLLL 52
RING-H2_RNF145 cd16684
RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; ...
97-135 1.26e-03

RING finger, H2 subclass, found in RING finger protein 145 (RNF145) and similar proteins; RNF145 is an uncharacterized RING finger protein encoded by the RNF145 gene, which is expressed in T lymphocytes, and its expression is altered in acute myelomonocytic and acute promyelocytic leukemias. Although its biological function remains unclear, RNF145 shows high sequence similarity with RNF139, an endoplasmic reticulum (ER)-resident multi-transmembrane protein that functions as a potent growth suppressor in mammalian cells, inducing G2/M arrest, decreased DNA synthesis and increased apoptosis. Like RNF139, RNF145 contains a C3H2C3-type RING-H2 finger with possible E3-ubiquitin ligase activity.


Pssm-ID: 319598 [Multi-domain]  Cd Length: 43  Bit Score: 35.03  E-value: 1.26e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1972253235  97 ICMIDFEPGERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16684     4 ICSICYQDMKSAVITPCSHFFHAGCLKKWLYVQETCPLC 42
RING-H2_AIRP1-like cd23116
RING finger, H2 subclass, found in Arabidopsis thaliana protein ABA INSENSITIVE RING PROTEIN 1 ...
93-139 1.49e-03

RING finger, H2 subclass, found in Arabidopsis thaliana protein ABA INSENSITIVE RING PROTEIN 1 (AIRP1) and similar proteins; This subfamily includes Arabidopsis thaliana AIRP1 and RING-H2 finger B1a (RHB1A). AIRP1, also known as RING-type E3 ubiquitin transferase AIRP1, possesses E3 ubiquitin-protein ligase activity in vitro when associated with the E2 enzyme UBC8. It plays combinatory roles with AIRP2 in the positive regulation of the abscisic acid-mediated drought stress response. RHB1A is a probable E3 ubiquitin-protein ligase. Members of this subfamily contain a C3H2C3-type RING-H2 finger.


Pssm-ID: 438478 [Multi-domain]  Cd Length: 49  Bit Score: 35.14  E-value: 1.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1972253235  93 NECAICMIDFEPgERIRFLP-CMHSFHQECVDEWLMKSFTCPSCLEPV 139
Cdd:cd23116     3 DVCPTCLEGYTE-ENPKLLTkCGHHFHLACIYEWMERSERCPVCDKEM 49
RING-HC_TRIM13_like_C-V cd16581
RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and ...
95-135 1.67e-03

RING finger, HC subclass, found in tripartite motif-containing proteins TRIM13, TRIM59 and similar proteins; TRIM13 and TRIM59, two closely related tripartite motif-containing proteins, belong to the C-V subclass of the TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domain, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, followed by a C-terminal transmembrane domain. TRIM13, also known as B-cell chronic lymphocytic leukemia tumor suppressor Leu5, leukemia-associated protein 5, putative tumor suppressor RFP2, RING finger protein 77 (RNF77), or Ret finger protein 2, is an endoplasmic reticulum (ER) membrane anchored E3 ubiquitin-protein ligase that interacts with proteins localized to the ER, including valosin-containing protein (VCP), a protein indispensable for ER-associated degradation (ERAD). TRIM59, also known as RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis.


Pssm-ID: 438243 [Multi-domain]  Cd Length: 50  Bit Score: 35.18  E-value: 1.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1972253235  95 CAICMIDFEPGeriRFLPCMHSFHQECVD-------EWLMKSFTCPSC 135
Cdd:cd16581     5 CSICYNIFDDP---KILPCSHTFCKNCLEkllaasgYYLLASLKCPTC 49
RING-HC_RNFT2 cd16742
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2 ...
95-143 1.84e-03

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 2(RNFT2); RNFT2, also known as transmembrane protein 118 (TMEM118), is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 438400 [Multi-domain]  Cd Length: 67  Bit Score: 35.24  E-value: 1.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1972253235  95 CAICMIDF-EPgeriRFLPCMHSFHQECVDEWLMKSFTCPSCLEPVDSTI 143
Cdd:cd16742    16 CAICQAEFrEP----LILICQHVFCEECLCLWFDRERTCPLCRSVVVETL 61
RING-HC_TRIM32_C-VII cd16587
RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar ...
94-135 2.32e-03

RING finger, HC subclass, found in tripartite motif-containing protein 32 (TRIM32) and similar proteins; TRIM32, also known as 72 kDa Tat-interacting protein, zinc finger protein HT2A, or BBS11, is an E3 ubiquitin-protein ligase that promotes degradation of several targets, including actin, PIASgamma, Abl interactor 2, dysbindin, X-linked inhibitor of apoptosis (XIAP), p73 transcription factor, thin filaments and Z-bands during fasting. It plays important roles in neuronal differentiation of neural progenitor cells, as well as in controlling cell fate in skeletal muscle progenitor cells. It reduces PI3K-Akt-FoxO signaling in muscle atrophy by promoting plakoglobin-PI3K dissociation. It also functions as a pluripotency-reprogramming roadblock that facilitates cellular transition towards differentiation by modulating the levels of Oct4 and cMyc. Moreover, TRIM32 is an intrinsic influenza A virus (IAV) restriction factor which senses and targets the polymerase basic protein 1 (PB1) for ubiquitination and protein degradation. It also plays a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo, binds specifically to the activation domain of HIV-1 Tat, and can also interact with the HIV-2 and EIAV Tat proteins in vivo. Furthermore, TRIM32 regulates myoblast proliferation by controlling turnover of NDRG2 (N-myc downstream-regulated gene). It negatively regulates tumor suppressor p53 to promote tumorigenesis. It also facilitates degradation of MYCN on spindle poles and induces asymmetric cell division in human neuroblastoma cells. In addition, TRIM32 plays important roles in regulation of hyperactivities and positively regulates the development of anxiety and depression disorders induced by chronic stress. It also plays a role in regeneration by affecting satellite cell cycle progression via modulation of the SUMO ligase PIASy (PIAS4). Defects in TRIM32 leads to limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathies (STM) and Bardet-Biedl syndrome. TRIM32 belongs to the C-VII subclass of the TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The NHL domain mediates the interaction with Argonaute proteins and consequently allows TRIM32 to modulate the activity of certain miRNAs.


Pssm-ID: 438249 [Multi-domain]  Cd Length: 51  Bit Score: 34.69  E-value: 2.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1972253235  94 ECAICMIDFEPGERI-RFLPCMHSFHQECVDEWLMKS----FTCPSC 135
Cdd:cd16587     2 ECPICLESFDEGQLRpKLLHCGHTICEQCLEKLLASLsingVRCPFC 48
RING-HC_Topors cd16574
RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein ...
93-135 2.41e-03

RING finger, HC subclass, found in topoisomerase I-binding arginine/serine-rich protein (Topors) and similar proteins; Topors, also known as topoisomerase I-binding RING finger protein, tumor suppressor p53- binding protein 3, or p53-binding protein 3 (p53BP3), is a ubiquitously expressed nuclear E3 ubiquitin-protein ligase that can ligate both ubiquitin and small ubiquitin-like modifier (SUMO) to substrate proteins in the nucleus. It contains an N-terminal C3HC4-type RING-HC finger which ligates ubiquitin to its target proteins including DNA topoisomerase I, p53, NKX3.1, H2AX, and the AAV-2 Rep78/68 proteins. As a RING-dependent E3 ubiquitin ligase, Topors works with the E2 enzymes UbcH5a, UbcH5c, and UbcH6, but not with UbcH7, CDC34, or UbcH2b. Topors acts as a tumor suppressor in various malignancies. It regulates p53 modification, suggesting it may be responsible for astrocyte elevated gene-1 (AEG-1, also known as metadherin, or LYRIC) ubiquitin modification. Plk1-mediated phosphorylation of Topors inhibits Topors-mediated sumoylation of p53, whereas p53 ubiquitination is enhanced, leading to p53 degradation. It also functions as a negative regulator of the prostate tumor suppressor NKX3.1. Moreover, Topors is associated with promyelocytic leukemia nuclear bodies, and may be involved in the cellular response to camptothecin. It also plays a key role in the turnover of H2AX protein, discriminating the type of DNA damaging stress. Furthermore, Topors is a cilia-centrosomal protein associated with autosomal dominant retinal degeneration. Mutations in TOPORS cause autosomal dominant retinitis pigmentosa (adRP).


Pssm-ID: 438236 [Multi-domain]  Cd Length: 47  Bit Score: 34.57  E-value: 2.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1972253235  93 NECAICMIDFEPgERIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16574     2 SSCPICLDRFEN-EKAFLDGCFHAFCFTCILEWSKVKNECPLC 43
RING-HC_IRC20-like cd23135
RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers ...
95-135 2.41e-03

RING finger, HC subclass, found in Saccharomyces cerevisiae increased recombination centers protein 20 (IRC20) and similar proteins; IRC20 is an uncharacterized ATP-dependent helicase that is probably involved in a pathway contributing to genomic integrity. IRC20 contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438497 [Multi-domain]  Cd Length: 44  Bit Score: 34.41  E-value: 2.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEPGErirFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd23135     6 CSICFSEIRSGA---ILKCGHFFCLSCIASWLREKSTCPLC 43
RING-HC_RNFT1 cd16741
RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 ...
95-135 3.92e-03

RING finger, HC subclass, found in RING finger and transmembrane domain-containing protein 1 (RNFT1); RNFT1, also known as protein PTD016, is a multi-pass membrane protein containing a C3HC4-type RING-HC finger. Its biological role remains unclear.


Pssm-ID: 438399 [Multi-domain]  Cd Length: 58  Bit Score: 34.09  E-value: 3.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1972253235  95 CAICMIDFEpgeRIRFLPCMHSFHQECVDEWLMKSFTCPSC 135
Cdd:cd16741    17 CAICQAEFR---KPILLICQHVFCEECISLWFNREKTCPLC 54
RING-HC_TRIM36_C-I cd16756
RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar ...
111-140 4.47e-03

RING finger, HC subclass, found in tripartite motif-containing protein 36 (TRIM36) and similar proteins; TRIM36, the human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequently dorsal axis formation. It is also potentially associated with chromosome segregation by interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, a PRY domain and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438414 [Multi-domain]  Cd Length: 49  Bit Score: 33.73  E-value: 4.47e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1972253235 111 LPCMHSFHQECVDEwLMKSFTCPSCLEPVD 140
Cdd:cd16756    19 LPCQHSVCHKCVKE-LLTTFPCPGCQHDVD 47
zf-RING_UBOX pfam13445
RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.
95-133 4.81e-03

RING-type zinc-finger; This zinc-finger is a typical RING-type of plant ubiquitin ligases.


Pssm-ID: 463881 [Multi-domain]  Cd Length: 38  Bit Score: 33.53  E-value: 4.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  95 CAICMIDFEPgeriRFLPCMHSFHQECVDEWLM---KSFTCP 133
Cdd:pfam13445   1 CPICLELFTD----PVLPCGHTFCRECLEEMSQkkgGKFKCP 38
RING-H2_RNF25 cd16470
RING finger, H2 subclass, found in RING finger protein 25 (RNF25) and similar proteins; RNF25, ...
94-139 4.94e-03

RING finger, H2 subclass, found in RING finger protein 25 (RNF25) and similar proteins; RNF25, also known as AO7, is a putative E3 ubiquitin-protein ligase that was initially identified as an interacting protein of the E2 ubiquitin-conjugating enzyme, Ubc5B. It is ubiquitously expressed in various tissues and predominantly localized in the nucleus. RNF25 activates the nuclear factor (NF)-kappaB-dependent gene expression upon stimulation with Interleukin-1 beta (IL-1beta), or tumor necrosis factor (TNF), or overexpression of NF-kappaB-inducing kinase. It interacts with the p65 transactivation domain (TAD) and modulates its transcriptional activity. RNF25 contains an N-terminal RWD domain, a C3H2C3-type RING-H2 finger, and a C-terminal Pro-rich region. Both the RING-H2 finger and the C-terminal regions of RNF25 are necessary for transcriptional activation.


Pssm-ID: 438133 [Multi-domain]  Cd Length: 74  Bit Score: 34.30  E-value: 4.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQECV--------DEWLM-----------------KSFTCPSCLEPV 139
Cdd:cd16470     4 QCVICLYGFQEGDAFTKTPCYHYFHSHCLaryiqhmeENLKEeqeeqeerpraqteqeqFQVLCPVCREPL 74
mRING-HC-C3HC3D_RBR_HOIL1 cd16633
Modified RING finger, HC subclass (C3HC3D-type), found in heme-oxidized IRP2 ubiquitin ligase ...
94-121 5.02e-03

Modified RING finger, HC subclass (C3HC3D-type), found in heme-oxidized IRP2 ubiquitin ligase 1 (HOIL-1) and similar proteins; HOIL-1, also known as RBCK1, HOIL-1L, RanBP-type and C3HC4-type zinc finger-containing protein 1, HBV-associated factor 4, Hepatitis B virus X-associated protein 4, RING finger protein 54 (RNF54), ubiquitin-conjugating enzyme 7-interacting protein 3, or UbcM4-interacting protein 28 (UIP28), together with E3 ubiquitin-protein ligase RNF31 (also known as HOIP) and SHANK-associated RH domain interacting protein (SHARPIN), form the E3-ligase complex (also known as linear-ubiquitin-chain assembly complex LUBAC) that regulates NF-kappaB activity and apoptosis through conjugation of linear polyubiquitin chains to NF-kappaB essential modulator (also known as NEMO or IKBKG). HOIL-1 plays a crucial role in TNF-alpha-mediated NF-kappaB activation. It also functions as an ubiquitin-protein ligase E3 that interacts with not only PKCbeta, but also PKCzeta. It can recognize heme-oxidized IRP2 (iron regulatory protein2) and is thought to affect the turnover of oxidatively damaged proteins. HOIL-1 contains an N-terminal ubiqutin-like (UBL) domain and an Npl4 zinc-finger (NZF) domain, which regulate the interaction with the LUBAC subunit RNF31 and ubiquitin, respectively. The NZF domain belongs to the RanBP2-type zinc finger (zf-RanBP2) domain superfamily. In addition, HOIL-1 has an RBR domain that was previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been corrected as RING-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR (RING1-BRcat-Rcat) domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase function to facilitate the ubiquitination reaction. This model corresponds to the RING domain, a modified C3HC3D-type RING-HC finger required for RBR-mediated ubiquitination.


Pssm-ID: 438295 [Multi-domain]  Cd Length: 56  Bit Score: 33.77  E-value: 5.02e-03
                          10        20
                  ....*....|....*....|....*...
gi 1972253235  94 ECAICMIDFEPGERIRFLPCMHSFHQEC 121
Cdd:cd16633     9 ECPICFDDVPPGEGVVLRECLHSFCREC 36
RING-H2_BRAP2 cd16457
RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; ...
95-135 8.34e-03

RING finger, H2 subclass, found in BRCA1-associated protein (BRAP2) and similar proteins; BRAP2, also known as impedes mitogenic signal propagation (IMP), RING finger protein 52, or renal carcinoma antigen NY-REN-63, is a novel cytoplasmic protein interacting with the two functional nuclear localization signal (NLS) motifs of BRCA1, a nuclear protein linked to breast cancer. It also binds to the SV40 large T antigen NLS motif and the bipartite NLS motif found in mitosin. BRAP2 serves as a cytoplasmic retention protein and plays a role in the regulation of nuclear protein transport. It contains an N-terminal RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), followed by a C3H2C3-type RING-H2 finger and a UBP-type zinc finger.


Pssm-ID: 438121 [Multi-domain]  Cd Length: 44  Bit Score: 33.03  E-value: 8.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1972253235  95 CAICMIDF-EPGERIRFLPCMHSFHQECVDEWlmKSFTCPSC 135
Cdd:cd16457     3 CPVCLERMdESVSGILTILCNHSFHCSCLSKW--GDSSCPVC 42
RING-HC_RNF151 cd16547
RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; ...
111-140 8.72e-03

RING finger, HC subclass, found in RING finger protein 151 (RNF151) and similar proteins; RNF151 is a testis-specific RING finger protein that interacts with dysbindin, a synaptic and microtubular protein that binds brain snapin, a SNARE-binding protein that mediates intracellular membrane fusion in both neuronal and non-neuronal cells. Thus, it may be involved in acrosome formation of spermatids by interacting with multiple proteins participating in membrane biogenesis and microtubule organization. RNF151 contains a C3HC4-type RING finger domain, a putative nuclear localization signal (NLS), and a TNF receptor associated factor (TRAF)-type zinc finger domain.


Pssm-ID: 438209 [Multi-domain]  Cd Length: 49  Bit Score: 32.82  E-value: 8.72e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1972253235 111 LPCMHSFHQECVDEWLMKSFTCPSCLEPVD 140
Cdd:cd16547    19 LSCSHIFCKKCILQWLKRQETCPCCRKEVK 48
RING-HC_TRIM65_C-IV cd16609
RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar ...
95-142 9.54e-03

RING finger, HC subclass, found in tripartite motif-containing protein TRIM65 and similar proteins; TRIM65 is an E3 ubiquitin-protein ligase that interacts with the innate immune receptor MDA5, enhancing its ability to stimulate interferon-beta signaling. It functions as a potential oncogenic protein that negatively regulates p53 through ubiquitination, providing insight into the development of novel approaches targeting TRIM65 for non-small cell lung carcinoma (NSCLC) treatment, and also overcoming chemotherapy resistance. Moreover, TRIM65 negatively regulates microRNA-driven suppression of mRNA translation by targeting TNRC6 proteins for ubiquitination and degradation. TRIM65 belongs to the C-IV subclass of the TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a C3HC4-type RING-HC finger, Bbox1 and Bbox2, and a coiled coil region, as well as a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain.


Pssm-ID: 438271 [Multi-domain]  Cd Length: 58  Bit Score: 33.11  E-value: 9.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972253235  95 CAICM-IDFEPgeriRFLPCMHSFHQECVDEWL----MKSFTCPSCLEPVDST 142
Cdd:cd16609     6 CSICLgLYQDP----VTLPCQHSFCRACIEDHWrqkdEGSFSCPECRAPFPEG 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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