zinc finger protein-like 1 isoform X1 [Danio rerio]
Protein Classification
zinc finger protein-like 1( domain architecture ID 11613437)
zinc finger protein-like 1 (ZFPL1) 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
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| mRING-H2-C3DHC3_ZFPL1 | cd16487 | Modified RING finger, H2 subclass (C3DHC3-type), found in zinc finger protein-like 1 (ZFPL1) ... |
50-106 | 3.36e-30 | ||
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: 108.93 E-value: 3.36e-30
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| Name | Accession | Description | Interval | E-value | ||
| mRING-H2-C3DHC3_ZFPL1 | cd16487 | Modified RING finger, H2 subclass (C3DHC3-type), found in zinc finger protein-like 1 (ZFPL1) ... |
50-106 | 3.36e-30 | ||
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: 108.93 E-value: 3.36e-30
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| Name | Accession | Description | Interval | E-value | ||
| mRING-H2-C3DHC3_ZFPL1 | cd16487 | Modified RING finger, H2 subclass (C3DHC3-type), found in zinc finger protein-like 1 (ZFPL1) ... |
50-106 | 3.36e-30 | ||
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: 108.93 E-value: 3.36e-30
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| RING-H2 | cd16448 | H2 subclass of RING (RING-H2) fingers and its variants; The RING finger is a specialized type ... |
53-101 | 9.04e-05 | ||
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: 39.31 E-value: 9.04e-05
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| RING-HC_RNF5 | cd16743 | RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, ... |
53-104 | 2.67e-04 | ||
RING finger, HC subclass, found in RING finger protein 5 (RNF5) and similar proteins; RNF5, also known as protein G16 or Ram1, is an E3 ubiquitin-protein ligase anchored to the outer membrane of the endoplasmic reticulum (ER). It acts at early stages of cystic fibrosis (CF) transmembrane conductance regulator (CFTR) biosynthesis and functions as a target for therapeutic modalities to antagonize mutant CFTR proteins in CF patients carrying the F508del allele. It also regulates the turnover of specific G protein-coupled receptors by ubiquitinating JNK-associated membrane protein (JAMP) and preventing proteasome recruitment. RNF5 limits basal levels of autophagy and influences susceptibility to bacterial infection through the regulation of ATG4B stability. It is also involved in the degradation of Pendrin, a transmembrane chloride/anion exchanger highly expressed in thyroid, kidney, and inner ear. RNF5 plays an important role in cell adhesion and migration. It can modulate cell migration by ubiquitinating paxillin. Furthermore, RNF5 interacts with virus-induced signaling adaptor (VISA) at mitochondria in a viral infection-dependent manner, and further targets VISA at K362 and K461 for K48-linked ubiquitination and degradation after viral infection. It also negatively regulates virus-triggered signaling by targeting MITA, also known as STING, for ubiquitination and degradation at the mitochondria. In addition, RNF5 determines breast cancer response to ER stress-inducing chemotherapies through the regulation of the L-glutamine carrier proteins SLC1A5 and SLC38A2 (SLC1A5/38A2). It also has been implicated in muscle organization and in recognition and processing of misfolded proteins. RNF5 contains a C3HC4-type RING-HC finger. Pssm-ID: 438401 [Multi-domain] Cd Length: 54 Bit Score: 38.33 E-value: 2.67e-04
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| RING-HC_RNF185 | cd16744 | RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; ... |
53-104 | 5.74e-03 | ||
RING finger, HC subclass, found in RING finger protein 185 (RNF185) and similar proteins; RNF185 is an E3 ubiquitin-protein ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR). It controls the degradation of CFTR and CFTR F508del allele in a RING- and proteasome-dependent manner, but does not control that of other classical ERAD model substrates. It also negatively regulates osteogenic differentiation by targeting dishevelled2 (Dvl2), a key mediator of the Wnt signaling pathway, for degradation. Moreover, RNF185 regulates selective mitochondrial autophagy through interaction with the Bcl-2 family protein BNIP1. It also plays an important role in cell adhesion and migration through the modulation of cell migration by ubiquitinating paxillin. RNF185 contains a C3HC4-type RING-HC finger. Pssm-ID: 438402 [Multi-domain] Cd Length: 57 Bit Score: 34.51 E-value: 5.74e-03
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