ID R144A_HUMAN Reviewed; 292 AA.
AC P50876; D6W4Y6; Q585H5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 18-JUN-2025, entry version 194.
DE RecName: Full=E3 ubiquitin-protein ligase RNF144A;
DE EC=2.3.2.31 {ECO:0000269|PubMed:26216882};
DE AltName: Full=RING finger protein 144A;
DE AltName: Full=UbcM4-interacting protein 4;
DE AltName: Full=Ubiquitin-conjugating enzyme 7-interacting protein 4;
GN Name=RNF144A; Synonyms=KIAA0161, RNF144, UBCE7IP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-4.
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-4.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-4.
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH UBE2L3.
RX PubMed=10431818; DOI=10.1016/s0014-5793(99)00823-6;
RA Martinez-Noel G., Niedenthal R., Tamura T., Harbers K.;
RT "A family of structurally related RING finger proteins interacts
RT specifically with the ubiquitin-conjugating enzyme UbcM4.";
RL FEBS Lett. 454:257-261(1999).
RN [6]
RP FUNCTION, AUTOUBIQUITINATION, AND SUBCELLULAR LOCATION.
RX PubMed=24979766; DOI=10.1073/pnas.1323107111;
RA Ho S.R., Mahanic C.S., Lee Y.J., Lin W.C.;
RT "RNF144A, an E3 ubiquitin ligase for DNA-PKcs, promotes apoptosis during
RT DNA damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E2646-E2655(2014).
RN [7]
RP FUNCTION, MUTAGENESIS OF CYS-20; CYS-23; GLY-252 AND GLY-256, SUBUNIT,
RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND UBIQUITINATION.
RX PubMed=26216882; DOI=10.1074/jbc.m115.645499;
RA Ho S.R., Lee Y.J., Lin W.C.;
RT "Regulation of RNF144A E3 Ubiquitin Ligase Activity by Self-association
RT through Its Transmembrane Domain.";
RL J. Biol. Chem. 290:23026-23038(2015).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-20 AND CYS-23.
RX PubMed=30171075; DOI=10.1074/jbc.ra118.002887;
RA Ho S.R., Lin W.C.;
RT "RNF144A sustains EGFR signaling to promote EGF-dependent cell
RT proliferation.";
RL J. Biol. Chem. 293:16307-16323(2018).
RN [9]
RP FUNCTION.
RX PubMed=33067254; DOI=10.1242/jcs.247304;
RA Han S.H., Kim K.T.;
RT "RNF144a induces ERK-dependent cell death under oxidative stress via
RT downregulation of vaccinia-related kinase 3.";
RL J. Cell Sci. 133:0-0(2020).
RN [10]
RP FUNCTION, MUTAGENESIS OF CYS-20; CYS-23; CYS-198 AND GLY-252, AND
RP SUBCELLULAR LOCATION.
RX PubMed=37955227; DOI=10.15252/embr.202357528;
RA Yang B., Pei J., Lu C., Wang Y., Shen M., Qin X., Huang Y., Yang X.,
RA Zhao X., Ma S., Song Z., Liang Y., Wang H., Wang J.;
RT "RNF144A promotes antiviral responses by modulating STING ubiquitination.";
RL EMBO Rep. 0:0-0(2023).
RN [11]
RP STRUCTURE BY NMR OF 20-100.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RING finger domain of the human UbcM4-
RT interacting protein 4.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2
CC ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a
CC thioester and then directly transfers the ubiquitin to targeted
CC substrates (PubMed:26216882). Mediates the ubiquitination and
CC degradation of the DNA damage kinase PRKDC during DNA damage
CC (PubMed:24979766). Positively regulates DNA virus or exogenous
CC cytosolic DNA-triggered innate immune response by mediating STING1
CC ubiquitination and increasing its 'Lys-6'-linked ubiquitination and
CC translocation from the endoplasmic reticulum to the Golgi leading to
CC downstream signaling pathways (PubMed:37955227). Plays a positive role
CC in EGF-dependent cell proliferation by prolonging EGF/EGFR signaling
CC during EGF stimulation through EGFR ubiquitination (PubMed:30171075).
CC Increases ERK activity independently of EGFR signaling by promoting
CC polyubiquitination and subsequent degradation of VRK3 in the cytosol
CC (PubMed:33067254). {ECO:0000250, ECO:0000269|PubMed:24979766,
CC ECO:0000269|PubMed:26216882, ECO:0000269|PubMed:30171075,
CC ECO:0000269|PubMed:33067254, ECO:0000269|PubMed:37955227}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:O60260};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Self-associates (PubMed:26216882). Interacts with UBE2L3
CC (PubMed:10431818). {ECO:0000269|PubMed:10431818,
CC ECO:0000269|PubMed:26216882}.
CC -!- INTERACTION:
CC P50876; Q07065: CKAP4; NbExp=2; IntAct=EBI-2340657, EBI-702400;
CC P50876; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-2340657, EBI-12831978;
CC P50876; Q6N075: MFSD5; NbExp=3; IntAct=EBI-2340657, EBI-3920969;
CC P50876; Q6TCH4: PAQR6; NbExp=3; IntAct=EBI-2340657, EBI-17265310;
CC P50876; Q96AA3: RFT1; NbExp=3; IntAct=EBI-2340657, EBI-6269616;
CC P50876; Q96IW7: SEC22A; NbExp=3; IntAct=EBI-2340657, EBI-8652744;
CC P50876; O43765: SGTA; NbExp=3; IntAct=EBI-2340657, EBI-347996;
CC P50876; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-2340657, EBI-744081;
CC P50876; P30825: SLC7A1; NbExp=3; IntAct=EBI-2340657, EBI-4289564;
CC P50876; P68036: UBE2L3; NbExp=4; IntAct=EBI-2340657, EBI-711173;
CC P50876; O95070: YIF1A; NbExp=3; IntAct=EBI-2340657, EBI-2799703;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24979766,
CC ECO:0000269|PubMed:30171075}; Single-pass membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:24979766, ECO:0000269|PubMed:37955227}. Endosome
CC membrane {ECO:0000269|PubMed:30171075}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:37955227}.
CC -!- DOMAIN: Members of the RBR family are atypical E3 ligases. They
CC interact with the E2 conjugating enzyme UBE2L3 and function like HECT-
CC type E3 enzymes: they bind E2s via the first RING domain, but require
CC an obligate trans-thiolation step during the ubiquitin transfer,
CC requiring a conserved cysteine residue in the second RING domain.
CC {ECO:0000250|UniProtKB:O60260}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:24979766,
CC ECO:0000269|PubMed:26216882}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF144 subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks the His residue in the RING-type domain 2 that is one of
CC the conserved features of the family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11478.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D79983; BAA11478.2; ALT_INIT; mRNA.
DR EMBL; AC068481; AAX82010.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01030.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01031.1; -; Genomic_DNA.
DR EMBL; BC050373; AAH50373.1; -; mRNA.
DR CCDS; CCDS1657.1; -.
DR RefSeq; NP_001336111.1; NM_001349182.2.
DR RefSeq; NP_001336112.1; NM_001349183.2.
DR RefSeq; NP_001336113.1; NM_001349184.2.
DR RefSeq; NP_055561.2; NM_014746.4.
DR RefSeq; XP_005246257.1; XM_005246200.3.
DR RefSeq; XP_005246259.1; XM_005246202.4.
DR RefSeq; XP_016860885.1; XM_017005396.1.
DR RefSeq; XP_016860886.1; XM_017005397.1.
DR PDB; 1WIM; NMR; -; A=20-100.
DR PDB; 6L99; NMR; -; A=13-87.
DR PDBsum; 1WIM; -.
DR PDBsum; 6L99; -.
DR AlphaFoldDB; P50876; -.
DR BMRB; P50876; -.
DR SMR; P50876; -.
DR BioGRID; 115125; 96.
DR FunCoup; P50876; 477.
DR IntAct; P50876; 23.
DR MINT; P50876; -.
DR STRING; 9606.ENSP00000321330; -.
DR GlyGen; P50876; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P50876; -.
DR PhosphoSitePlus; P50876; -.
DR BioMuta; RNF144A; -.
DR DMDM; 160358924; -.
DR jPOST; P50876; -.
DR MassIVE; P50876; -.
DR PaxDb; 9606-ENSP00000321330; -.
DR PeptideAtlas; P50876; -.
DR ProteomicsDB; 56267; -.
DR Antibodypedia; 26428; 180 antibodies from 29 providers.
DR DNASU; 9781; -.
DR Ensembl; ENST00000320892.11; ENSP00000321330.6; ENSG00000151692.15.
DR GeneID; 9781; -.
DR KEGG; hsa:9781; -.
DR MANE-Select; ENST00000320892.11; ENSP00000321330.6; NM_014746.6; NP_055561.2.
DR UCSC; uc002qys.4; human.
DR AGR; HGNC:20457; -.
DR CTD; 9781; -.
DR DisGeNET; 9781; -.
DR GeneCards; RNF144A; -.
DR HGNC; HGNC:20457; RNF144A.
DR HPA; ENSG00000151692; Tissue enhanced (brain).
DR MIM; 619454; gene.
DR neXtProt; NX_P50876; -.
DR OpenTargets; ENSG00000151692; -.
DR PharmGKB; PA162401542; -.
DR VEuPathDB; HostDB:ENSG00000151692; -.
DR eggNOG; KOG1815; Eukaryota.
DR GeneTree; ENSGT00940000157701; -.
DR HOGENOM; CLU_053598_1_0_1; -.
DR InParanoid; P50876; -.
DR OMA; CMVAAEM; -.
DR OrthoDB; 10009520at2759; -.
DR PAN-GO; P50876; 8 GO annotations based on evolutionary models.
DR PhylomeDB; P50876; -.
DR TreeFam; TF324777; -.
DR BRENDA; 2.3.2.31; 2681.
DR PathwayCommons; P50876; -.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR SignaLink; P50876; -.
DR SIGNOR; P50876; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 9781; 13 hits in 1201 CRISPR screens.
DR ChiTaRS; RNF144A; human.
DR EvolutionaryTrace; P50876; -.
DR GenomeRNAi; 9781; -.
DR Pharos; P50876; Tbio.
DR PRO; PR:P50876; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P50876; protein.
DR Bgee; ENSG00000151692; Expressed in cerebellar hemisphere and 181 other cell types or tissues.
DR ExpressionAtlas; P50876; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProt.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IDA:UniProt.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd20366; BRcat_RBR_RNF144A; 1.
DR CDD; cd16777; mRING-HC-C4C4_RBR_RNF144A; 1.
DR CDD; cd20352; Rcat_RBR_RNF144; 1.
DR FunFam; 1.20.120.1750:FF:000006; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000051; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Endosome; Membrane; Metal-binding; Proteomics identification;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..292
FT /note="E3 ubiquitin-protein ligase RNF144A"
FT /id="PRO_0000056298"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 20..70
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 91..156
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 185..214
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 16..236
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ACT_SITE 198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT VARIANT 4
FT /note="T -> A (in dbSNP:rs364891)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8724849, ECO:0000269|Ref.3"
FT /id="VAR_035375"
FT MUTAGEN 20
FT /note="C->A: Complete loss of ubiquitin ligase activity and
FT auto-ubiquitination; when associated with A-23."
FT /evidence="ECO:0000269|PubMed:26216882,
FT ECO:0000269|PubMed:30171075, ECO:0000269|PubMed:37955227"
FT MUTAGEN 23
FT /note="C->A: Complete loss of ubiquitin ligase activity and
FT auto-ubiquitination; when associated with A-20."
FT /evidence="ECO:0000269|PubMed:26216882,
FT ECO:0000269|PubMed:30171075, ECO:0000269|PubMed:37955227"
FT MUTAGEN 252
FT /note="G->D: Preserves membrane localization but is
FT defective ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:37955227"
FT MUTAGEN 252
FT /note="G->L: Preserves membrane localization but is
FT defective in self-association and ubiquitin ligase
FT activity; when associated with L-256."
FT /evidence="ECO:0000269|PubMed:37955227"
FT MUTAGEN 256
FT /note="G->L: Preserves membrane localization but is
FT defective in self-association and ubiquitin ligase
FT activity; when associated with L-252."
FT /evidence="ECO:0000269|PubMed:37955227"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1WIM"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1WIM"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:1WIM"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:1WIM"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1WIM"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:1WIM"
FT HELIX 78..84
FT /evidence="ECO:0007829|PDB:1WIM"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:1WIM"
SQ SEQUENCE 292 AA; 32890 MW; E5BE7BC9560DCF93 CRC64;
MTTTRYRPTW DLALDPLVSC KLCLGEYPVE QMTTIAQCQC IFCTLCLKQY VELLIKEGLE
TAISCPDAAC PKQGHLQENE IECMVAAEIM QRYKKLQFER EVLFDPCRTW CPASTCQAVC
QLQDVGLQTP QPVQCKACRM EFCSTCKASW HPGQGCPETM PITFLPGETS AAFKMEEDDA
PIKRCPKCKV YIERDEGCAQ MMCKNCKHAF CWYCLESLDD DFLLIHYDKG PCRNKLGHSR
ASVIWHRTQV VGIFAGFGLL LLVASPFLLL ATPFVLCCKC KCSKGDDDPL PT
//
