TRI47_HUMAN
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 03-AUG-2022, entry version 177.
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}.
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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; 56.
DR IntAct; Q96LD4; 17.
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; Q96LD4; -.
DR PeptideAtlas; Q96LD4; -.
DR PRIDE; Q96LD4; -.
DR ProteomicsDB; 77206; -. [Q96LD4-1]
DR Antibodypedia; 32298; 109 antibodies from 21 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 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; 440803at2759; -.
DR PhylomeDB; Q96LD4; -.
DR TreeFam; TF351086; -.
DR PathwayCommons; Q96LD4; -.
DR SignaLink; Q96LD4; -.
DR SIGNOR; Q96LD4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 91107; 21 hits in 1123 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 149 other tissues.
DR ExpressionAtlas; Q96LD4; baseline and differential.
DR Genevisible; Q96LD4; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; cd15808; SPRY_PRY_TRIM47; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 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_LisH.
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 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; SSF49899; SSF49899; 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.
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
