NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907073726|ref|XP_036011547|]
View 

rhotekin-2 isoform X2 [Mus musculus]

Protein Classification

RTKN2 family PH domain-containing protein( domain architecture ID 10192577)

RTKN2 family PH (pleckstrin homology) domain-containing protein similar to PH region of rhotekin-2 (RTKN2) that may play an important role in lymphopoiesis

CATH:  2.30.29.30
Gene Ontology:  GO:0005515
PubMed:  22728242|17233582|15766521
SCOP:  4002395

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 4-112 1.59e-50

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270069  Cd Length: 111  Bit Score: 163.32  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726   4 DAFAGFLNEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEIEAKVEPALVVPIDKETRIQAVEKDSK-KMHCFSVLSTAAG 82
Cdd:cd13249     2 EMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKgRASSLSIINPYSG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907073726  83 RAVSHIFAADSLADFQEWMGAFRQHFFDLS 112
Cdd:cd13249    82 EEVTHVLSADSREELQKWMEALWQHFYDMS 111
 
Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 4-112 1.59e-50

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270069  Cd Length: 111  Bit Score: 163.32  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726   4 DAFAGFLNEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEIEAKVEPALVVPIDKETRIQAVEKDSK-KMHCFSVLSTAAG 82
Cdd:cd13249     2 EMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKgRASSLSIINPYSG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907073726  83 RAVSHIFAADSLADFQEWMGAFRQHFFDLS 112
Cdd:cd13249    82 EEVTHVLSADSREELQKWMEALWQHFYDMS 111
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 8-107 2.58e-11

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 59.48  E-value: 2.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726    8 GFLnEQQTGKGLVGWRRLYCALRGGKLrCFYGPEEIEAKVEPALVVPIDKET-RIQAVEKDSKKMHCFsVLSTAAGRavS 86
Cdd:smart00233   5 GWL-YKKSGGGKKSWKKRYFVLFNSTL-LYYKSKKDKKSYKPKGSIDLSGCTvREAPDPDSSKKPHCF-EIKTSDRK--T 79

                           90       100
                   ....*....|....*....|.
gi 1907073726   87 HIFAADSLADFQEWMGAFRQH 107
Cdd:smart00233  80 LLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 8-106 1.37e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 57.57  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726   8 GFLNEQqTGKGLVGWRRLYCALRGGKLrCFYGPEEIEAKVEPALVVPIDKETRIQAVEKDS-KKMHCFSVLSTAAGRAVS 86
Cdd:pfam00169   5 GWLLKK-GGGKKKSWKKRYFVLFDGSL-LYYKDDKSGKSKEPKGSISLSGCEVVEVVASDSpKRKFCFELRTGERTGKRT 82

                          90       100
                  ....*....|....*....|
gi 1907073726  87 HIFAADSLADFQEWMGAFRQ 106
Cdd:pfam00169  83 YLLQAESEEERKDWIKAIQS 102
 
Name Accession Description Interval E-value
PH_rhotekin2 cd13249
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 4-112 1.59e-50

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270069  Cd Length: 111  Bit Score: 163.32  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726   4 DAFAGFLNEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEIEAKVEPALVVPIDKETRIQAVEKDSK-KMHCFSVLSTAAG 82
Cdd:cd13249     2 EMMSGYLSQQQSVEGLQSWTRLYCVLKGGNLLCYYSPEEIEAKVEPLLTIPINKETRIRAVEKDSKgRASSLSIINPYSG 81

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907073726  83 RAVSHIFAADSLADFQEWMGAFRQHFFDLS 112
Cdd:cd13249    82 EEVTHVLSADSREELQKWMEALWQHFYDMS 111
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
 8-107 2.58e-11

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 59.48  E-value: 2.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726    8 GFLnEQQTGKGLVGWRRLYCALRGGKLrCFYGPEEIEAKVEPALVVPIDKET-RIQAVEKDSKKMHCFsVLSTAAGRavS 86
Cdd:smart00233   5 GWL-YKKSGGGKKSWKKRYFVLFNSTL-LYYKSKKDKKSYKPKGSIDLSGCTvREAPDPDSSKKPHCF-EIKTSDRK--T 79

                           90       100
                   ....*....|....*....|.
gi 1907073726   87 HIFAADSLADFQEWMGAFRQH 107
Cdd:smart00233  80 LLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
 8-106 1.37e-10

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 57.57  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726   8 GFLNEQqTGKGLVGWRRLYCALRGGKLrCFYGPEEIEAKVEPALVVPIDKETRIQAVEKDS-KKMHCFSVLSTAAGRAVS 86
Cdd:pfam00169   5 GWLLKK-GGGKKKSWKKRYFVLFDGSL-LYYKDDKSGKSKEPKGSISLSGCEVVEVVASDSpKRKFCFELRTGERTGKRT 82

                          90       100
                  ....*....|....*....|
gi 1907073726  87 HIFAADSLADFQEWMGAFRQ 106
Cdd:pfam00169  83 YLLQAESEEERKDWIKAIQS 102
PH cd00821
Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...
 7-104 4.96e-10

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275388 [Multi-domain]  Cd Length: 92  Bit Score: 55.63  E-value: 4.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726   7 AGFLnEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEieAKVEPALVVPIDKETRIQAVEKDSKKmHCFSvLSTAAGRavS 86
Cdd:cd00821     2 EGYL-LKRGGGGLKSWKKRWFVLFEGVLLYYKSKKD--SSYKPKGSIPLSGILEVEEVSPKERP-HCFE-LVTPDGR--T 74

                          90
                  ....*....|....*...
gi 1907073726  87 HIFAADSLADFQEWMGAF 104
Cdd:cd00821    75 YYLQADSEEERQEWLKAL 92
PH_anillin cd01263
Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin ...
 6-111 6.23e-10

Anillin Pleckstrin homology (PH) domain; Anillin (Rhotekin/RTKN; also called PLEKHK/Pleckstrin homology domain-containing family K) is an actin binding protein involved in cytokinesis. It interacts with GTP-bound Rho proteins and results in the inhibition of their GTPase activity. Dysregulation of the Rho signal transduction pathway has been implicated in many forms of cancer. Anillin proteins have a N-terminal HRI domain/ACC (anti-parallel coiled-coil) finger domain or Rho-binding domain binds small GTPases from the Rho family. The C-terminal PH domain helps target anillin to ectopic septin containing foci. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 269964  Cd Length: 121  Bit Score: 56.13  E-value: 6.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726   6 FAGFLNEQQTGKGLVGWRRLYCALRGGKLRCFYGPEEiEAKVEPALVVPIDKET--RIQAVEKD-SKKMHCFSVLSTAAG 82
Cdd:cd01263     4 YRGFLTVFEDVSGLGAWHRRWCVLRGGYLSFWKYPDD-EEKKKPIGSIDLTKCIteKVEPAPRElCARPNTFLLETLRPA 82

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907073726  83 RAVS---------HIFAADSLADFQEWMGAFRQHFFDL 111
Cdd:cd01263    83 EDDDrddtnekirVLLSADTKEERIEWLSALNQTLADL 120
PH_RASA1 cd13260
RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 ...
 5-106 2.97e-06

RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 (also called RasGap1 or p120) is a member of the RasGAP family of GTPase-activating proteins. RASA1 contains N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Splice variants lack the N-terminal domains. It is a cytosolic vertebrate protein that acts as a suppressor of RAS via its C-terminal GAP domain function, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. Additionally, it is involved in mitogenic signal transmission towards downstream interacting partners through its N-terminal SH2-SH3-SH2 domains. RASA1 interacts with a number of proteins including: G3BP1, SOCS3, ANXA6, Huntingtin, KHDRBS1, Src, EPHB3, EPH receptor B2, Insulin-like growth factor 1 receptor, PTK2B, DOK1, PDGFRB, HCK, Caveolin 2, DNAJA3, HRAS, GNB2L1 and NCK1. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270080  Cd Length: 103  Bit Score: 45.03  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726   5 AFAGFLNEQqtGKGLVGWRRLYCALRGGKLR-CFYgpeEIEAKVEPALVvpID-KETRIQAVEkDS--KKMHCFSVLSTA 80
Cdd:cd13260     4 DKKGYLLKK--GGKNKKWKNLYFVLEGKEQHlYFF---DNEKRTKPKGL--IDlSYCSLYPVH-DSlfGRPNCFQIVVRA 75

                          90       100
                  ....*....|....*....|....*.
gi 1907073726  81 AGRAVSHIFAADSLADFQEWMGAFRQ 106
Cdd:cd13260    76 LNESTITYLCADTAELAQEWMRALRA 101
BAR-PH_APPL cd13247
Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif Bin1/amphiphysin ...
 7-103 8.07e-05

Adaptor protein containing PH domain, PTB domain, and Leucine zipper motif Bin1/amphiphysin/Rvs167 (BAR)-Pleckstrin homology (PH) domain; APPL (also called DCC-interacting protein (DIP)-13alpha) interacts with oncoprotein serine/threonine kinase AKT2, tumor suppressor protein DCC (deleted in colorectal cancer), Rab5, GIPC (GAIP-interacting protein, C terminus), human follicle-stimulating hormone receptor (FSHR), and the adiponectin receptors AdipoR1 and AdipoR2. There are two isoforms of human APPL: APPL1 and APPL2, which share about 50% sequence identity. APPL has a BAR and a PH domain near its N terminus, and the two domains are thought to function as a unit (BAR-PH domain). C-terminal to this is a PTB domain. Lipid binding assays show that the BAR, PH, and PTB domains can bind phospholipids. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270067  Cd Length: 125  Bit Score: 41.59  E-value: 8.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726   7 AGFLNEQQTGKGLV-GWRRLYCALRGGKLRCfygpeeiEAKVEPA--LVVPIDKeTRIQAVEKDSKKmHCFSVLSTAAGR 83
Cdd:cd13247    30 AGYLFIRSKTGLVTnKWDRTYFFTQGGNLMS-------QPRDEVAgsLVLDLDN-CSVQAADCEDRR-NVFQITSPDGKK 100

                          90       100
                  ....*....|....*....|
gi 1907073726  84 AVshIFAADSLADFQEWMGA 103
Cdd:cd13247   101 AI--VLQAESKKDYEEWIAT 118
PH_AtPH1 cd13276
Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all ...
 6-103 2.76e-04

Arabidopsis thaliana Pleckstrin homolog (PH) 1 (AtPH1) PH domain; AtPH1 is expressed in all plant tissue and is proposed to be the plant homolog of human pleckstrin. Pleckstrin consists of two PH domains separated by a linker region, while AtPH has a single PH domain with a short N-terminal extension. AtPH1 binds PtdIns3P specifically and is thought to be an adaptor molecule since it has no obvious catalytic functions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270095  Cd Length: 106  Bit Score: 39.61  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726   6 FAGFLNEQqtGKGLVGWRRLYCALRGGKLRCFYGPEEIEAKVePALVVPIDKETRIQAVEKDSKKMHCFSvLSTAAGrav 85
Cdd:cd13276     1 KAGWLEKQ--GEFIKTWRRRWFVLKQGKLFWFKEPDVTPYSK-PRGVIDLSKCLTVKSAEDATNKENAFE-LSTPEE--- 73

                          90
                  ....*....|....*...
gi 1907073726  86 SHIFAADSLADFQEWMGA 103
Cdd:cd13276    74 TFYFIADNEKEKEEWIGA 91
PH_CNK_insect-like cd13326
Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; ...
 16-104 3.01e-04

Connector enhancer of KSR (Kinase suppressor of ras) (CNK) pleckstrin homology (PH) domain; CNK family members function as protein scaffolds, regulating the activity and the subcellular localization of RAS activated RAF. There is a single CNK protein present in Drosophila and Caenorhabditis elegans in contrast to mammals which have 3 CNK proteins (CNK1, CNK2, and CNK3). All of the CNK members contain a sterile a motif (SAM), a conserved region in CNK (CRIC) domain, and a PSD-95/DLG-1/ZO-1 (PDZ) domain, and a PH domain. A CNK2 splice variant CNK2A also has a PDZ domain-binding motif at its C terminus and Drosophila CNK (D-CNK) also has a domain known as the Raf-interacting region (RIR) that mediates binding of the Drosophila Raf kinase. This cd contains CNKs from insects, spiders, mollusks, and nematodes. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270135  Cd Length: 91  Bit Score: 39.25  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726  16 GKGLVGWRRLYCALRGGKLRCFYGPEEIEAkvepALVVPIDKETRIQAVEKDSKKmHCFSVLSTAagraVSHIFAADSLA 95
Cdd:cd13326    12 GKGGGKWAKRWFVLKGSNLYGFRSQESTKA----DCVIFLPGFTVSPAPEVKSRK-YAFKVYHTG----TVFYFAAESQE 82


                  ....*....
gi 1907073726  96 DFQEWMGAF 104
Cdd:cd13326    83 DMKKWLDLL 91
PH_PLEKHJ1 cd13258
Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; ...
 21-107 1.90e-03

Pleckstrin homology domain containing, family J member 1 Pleckstrin homology (PH) domain; PLEKHJ1 (also called GNRPX2/Guanine nucleotide-releasing protein x ). It contains a single PH domain. Very little information is known about PLEKHJ1. PLEKHJ1 has been shown to interact with IKBKG (inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase gamma) and KRT33B (keratin 33B). PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270078  Cd Length: 123  Bit Score: 37.69  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726  21 GWRRLYCALRGGKLrcFY-GPEEIEAKVEPALVVpIDKETRIQaVEKDSKKMHCFS-VLSTAAGRavSHIFAADSLADFQ 98
Cdd:cd13258    35 VFKERWFKLKGNLL--FYfRTNEFGDCSEPIGAI-VLENCRVQ-MEEITEKPFAFSiVFNDEPEK--KYIFSCRSEEQCE 108


                  ....*....
gi 1907073726  99 EWMGAFRQH 107
Cdd:cd13258   109 QWIEALRQA 117
PH_PEPP1_2_3 cd13248
Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; ...
 6-106 3.56e-03

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270068  Cd Length: 104  Bit Score: 36.48  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073726   6 FAGFLNeQQTGKGLVGWRRLYCALRGGKLrcFYGPEEIEAKVEPALVVPIDKETRIQAvEKDSKKMHCFSVLSTAAgRav 85
Cdd:cd13248     9 MSGWLH-KQGGSGLKNWRKRWFVLKDNCL--YYYKDPEEEKALGSILLPSYTISPAPP-SDEISRKFAFKAEHANM-R-- 81

                          90       100
                  ....*....|....*....|.
gi 1907073726  86 SHIFAADSLADFQEWMGAFRQ 106
Cdd:cd13248    82 TYYFAADTAEEMEQWMNAMSL 102
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH