ID TRI47_HUMAN Reviewed; 638 AA. AC Q96LD4; Q96AD0; Q96GU5; Q9BRN7; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 27-MAR-2024, entry version 185. DE RecName: Full=E3 ubiquitin-protein ligase TRIM47 {ECO:0000305}; DE EC=2.3.2.27 {ECO:0000269|PubMed:29291351}; DE AltName: Full=Gene overexpressed in astrocytoma protein; DE AltName: Full=RING finger protein 100; DE AltName: Full=Tripartite motif-containing protein 47 {ECO:0000305}; GN Name=TRIM47 {ECO:0000312|HGNC:HGNC:19020}; Synonyms=GOA, RNF100; 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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND CHROMOSOMAL LOCATION. RC TISSUE=Astrocytoma; RX PubMed=11511098; DOI=10.1006/bbrc.2001.5431; RA Vandeputte D.A.A., Meije C.B., van Dartel M., Leenstra S., RA Ijlst-Keizers H., Das P.K., Troost D., Bosch D.A., Baas F., RA Hulsebos T.J.M.; RT "GOA, a novel gene encoding a ring finger B-box coiled-coil protein, is RT overexpressed in astrocytoma."; RL Biochem. Biophys. Res. Commun. 286:574-579(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 236-638 (ISOFORM 1). RC TISSUE=Lung, and Pancreas; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-582, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [12] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=29291351; DOI=10.1038/nm.4461; RA Ji Y.X., Huang Z., Yang X., Wang X., Zhao L.P., Wang P.X., Zhang X.J., RA Alves-Bezerra M., Cai L., Zhang P., Lu Y.X., Bai L., Gao M.M., Zhao H., RA Tian S., Wang Y., Huang Z.X., Zhu X.Y., Zhang Y., Gong J., She Z.G., Li F., RA Cohen D.E., Li H.; RT "The deubiquitinating enzyme cylindromatosis mitigates nonalcoholic RT steatohepatitis."; RL Nat. Med. 24:213-223(2018). CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates the ubiquitination CC and proteasomal degradation of CYLD. {ECO:0000269|PubMed:29291351}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:29291351}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:29291351}. CC -!- INTERACTION: CC Q96LD4-2; Q13867: BLMH; NbExp=3; IntAct=EBI-12371725, EBI-718504; CC Q96LD4-2; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-12371725, EBI-995714; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11511098}. Nucleus CC {ECO:0000269|PubMed:11511098}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96LD4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96LD4-2; Sequence=VSP_055440; CC -!- TISSUE SPECIFICITY: Low expression in most tissues. Higher expression CC in kidney tubular cells. Overexpressed in astrocytoma tumor cells. CC {ECO:0000269|PubMed:11511098}. CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY026763; AAK07687.1; -; mRNA. DR EMBL; AC087289; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471099; EAW89332.1; -; Genomic_DNA. DR EMBL; BC006153; AAH06153.1; -; mRNA. DR EMBL; BC009225; AAH09225.2; -; mRNA. DR EMBL; BC017299; AAH17299.1; -; mRNA. DR CCDS; CCDS32737.1; -. [Q96LD4-1] DR PIR; JC7753; JC7753. DR RefSeq; NP_258411.2; NM_033452.2. [Q96LD4-1] DR RefSeq; XP_005257844.1; XM_005257787.4. [Q96LD4-2] DR RefSeq; XP_005257845.1; XM_005257788.4. [Q96LD4-2] DR AlphaFoldDB; Q96LD4; -. DR SMR; Q96LD4; -. DR BioGRID; 124794; 61. DR IntAct; Q96LD4; 16. DR MINT; Q96LD4; -. DR STRING; 9606.ENSP00000254816; -. DR iPTMnet; Q96LD4; -. DR PhosphoSitePlus; Q96LD4; -. DR BioMuta; TRIM47; -. DR DMDM; 313104035; -. DR EPD; Q96LD4; -. DR jPOST; Q96LD4; -. DR MassIVE; Q96LD4; -. DR MaxQB; Q96LD4; -. DR PaxDb; 9606-ENSP00000254816; -. DR PeptideAtlas; Q96LD4; -. DR ProteomicsDB; 77206; -. [Q96LD4-1] DR Pumba; Q96LD4; -. DR Antibodypedia; 32298; 122 antibodies from 22 providers. DR DNASU; 91107; -. DR Ensembl; ENST00000254816.6; ENSP00000254816.1; ENSG00000132481.7. [Q96LD4-1] DR GeneID; 91107; -. DR KEGG; hsa:91107; -. DR MANE-Select; ENST00000254816.6; ENSP00000254816.1; NM_033452.3; NP_258411.2. DR UCSC; uc002jpv.4; human. [Q96LD4-1] DR AGR; HGNC:19020; -. DR CTD; 91107; -. DR DisGeNET; 91107; -. DR GeneCards; TRIM47; -. DR HGNC; HGNC:19020; TRIM47. DR HPA; ENSG00000132481; Low tissue specificity. DR MIM; 611041; gene. DR neXtProt; NX_Q96LD4; -. DR OpenTargets; ENSG00000132481; -. DR PharmGKB; PA134883590; -. DR VEuPathDB; HostDB:ENSG00000132481; -. DR eggNOG; KOG2177; Eukaryota. DR GeneTree; ENSGT00940000154334; -. DR HOGENOM; CLU_013137_0_2_1; -. DR InParanoid; Q96LD4; -. DR OMA; CLESRDY; -. DR OrthoDB; 5322335at2759; -. DR PhylomeDB; Q96LD4; -. DR TreeFam; TF351086; -. DR PathwayCommons; Q96LD4; -. DR SignaLink; Q96LD4; -. DR SIGNOR; Q96LD4; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 91107; 22 hits in 1201 CRISPR screens. DR ChiTaRS; TRIM47; human. DR GenomeRNAi; 91107; -. DR Pharos; Q96LD4; Tbio. DR PRO; PR:Q96LD4; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q96LD4; Protein. DR Bgee; ENSG00000132481; Expressed in apex of heart and 151 other cell types or tissues. DR ExpressionAtlas; Q96LD4; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProt. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR CDD; cd19842; Bbox1_TRIM25-like_C-IV; 1. DR CDD; cd19769; Bbox2_TRIM16-like; 1. DR CDD; cd16604; RING-HC_TRIM47-like_C-IV; 1. DR CDD; cd15808; SPRY_PRY_TRIM47; 1. DR Gene3D; 2.60.120.920; -; 1. DR Gene3D; 4.10.830.40; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR001870; B30.2/SPRY. DR InterPro; IPR043136; B30.2/SPRY_sf. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR042780; TRIM47_SPRY_PRY. DR InterPro; IPR027370; Znf-RING_euk. DR InterPro; IPR000315; Znf_B-box. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR25465; B-BOX DOMAIN CONTAINING; 1. DR PANTHER; PTHR25465:SF21; E3 UBIQUITIN-PROTEIN LIGASE TRIM47; 1. DR Pfam; PF00643; zf-B_box; 1. DR Pfam; PF13445; zf-RING_UBOX; 1. DR SMART; SM00336; BBOX; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF57845; B-box zinc-binding domain; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50188; B302_SPRY; 1. DR PROSITE; PS50119; ZF_BBOX; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q96LD4; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Transferase; KW Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..638 FT /note="E3 ubiquitin-protein ligase TRIM47" FT /id="PRO_0000056270" FT DOMAIN 410..631 FT /note="B30.2/SPRY" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548" FT ZN_FING 9..58 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 177..217 FT /note="B box-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT REGION 79..119 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 300..322 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 384..411 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 296..324 FT /evidence="ECO:0000255" FT COMPBIAS 90..119 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 182 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 204 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 209 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT MOD_RES 72 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q8C0E3" FT MOD_RES 461 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243" FT MOD_RES 582 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 588 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..238 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055440" FT VARIANT 500 FT /note="E -> A (in dbSNP:rs1047043)" FT /id="VAR_057223" FT MOD_RES Q96LD4-2:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 638 AA; 69532 MW; F524910DFC5CDF28 CRC64; MDGSGPFSCP ICLEPLREPV TLPCGHNFCL ACLGALWPHR GASGAGGPGG AARCPLCQEP FPDGLQLRKN HTLSELLQLR QGSGPGSGPG PAPALAPEPS APSALPSVPE PSAPCAPEPW PAGEEPVRCD ACPEGAALPA ALSCLSCLAS FCPAHLGPHE RSPALRGHRL VPPLRRLEES LCPRHLRPLE RYCRAERVCL CEACAAQEHR GHELVPLEQE RALQEAEQSK VLSAVEDRMD ELGAGIAQSR RTVALIKSAA VAERERVSRL FADAAAALQG FQTQVLGFIE EGEAAMLGRS QGDLRRQEEQ RSRLSRARQN LSQVPEADSV SFLQELLALR LALEDGCGPG PGPPRELSFT KSSQAVRAVR DMLAVACVNQ WEQLRGPGGN EDGPQKLDSE ADAEPQDLES TNLLESEAPR DYFLKFAYIV DLDSDTADKF LQLFGTKGVK RVLCPINYPL SPTRFTHCEQ VLGEGALDRG TYYWEVEIIE GWVSMGVMAE DFSPQEPYDR GRLGRNAHSC CLQWNGRSFS VWFHGLEAPL PHPFSPTVGV CLEYADRALA FYAVRDGKMS LLRRLKASRP RRGGIPASPI DPFQSRLDSH FAGLFTHRLK PAFFLESVDA HLQIGPLKKS CISVLKRR //