TRI31_HUMAN
ID TRI31_HUMAN Reviewed; 425 AA.
AC Q9BZY9; A6NLX6; A9R9Q4; Q53H52; Q5RI37; Q5SRJ7; Q5SRJ8; Q5SS28; Q96AK4;
AC Q96AP8; Q99579; Q9BZY8;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM31;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM31 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 31;
GN Name=TRIM31; Synonyms=C6orf13, RNF;
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] (ISOFORMS ALPHA AND BETA).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
RP LYS-421.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Colon;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS CYS-118;
RP ILE-232 AND LYS-421.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
RP LYS-421.
RC TISSUE=Colon;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-236.
RA Henry J., Ribouchon M.-T., Depetris D., Mattei M.-G., Offer C.,
RA Tazi-Ahnini R., Pantarotti P.;
RT "Cloning, structural analysis and mapping of B30 and B7 family members, to
RT the MHC and other chromosomal regions. Toward the identification of the
RT ancestral major histocompatibility complex.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [8]
RP FUNCTION, OLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP AUTOUBIQUITINATION.
RX PubMed=18773414; DOI=10.1002/jcb.21908;
RA Sugiura T., Miyamoto K.;
RT "Characterization of TRIM31, upregulated in gastric adenocarcinoma, as a
RT novel RBCC protein.";
RL J. Cell. Biochem. 105:1081-1091(2008).
RN [9]
RP STRUCTURE BY NMR OF 1-66.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RING domain (1-66) from tripartite motif-
RT containing protein 31.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Regulator of Src-induced anchorage independent cell growth
CC (By similarity). May have E3 ubiquitin-protein ligase activity.
CC {ECO:0000250, ECO:0000269|PubMed:18773414}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with isoform p52shc of SHC1 (By similarity). May
CC form oligomers. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BZY9; P40227: CCT6A; NbExp=3; IntAct=EBI-747544, EBI-356687;
CC Q9BZY9; P43355: MAGEA1; NbExp=4; IntAct=EBI-747544, EBI-740978;
CC Q9BZY9; P61086: UBE2K; NbExp=11; IntAct=EBI-747544, EBI-473850;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18773414}.
CC Mitochondrion {ECO:0000269|PubMed:18773414}. Note=Predominantly
CC expressed in the cytoplasm but a fraction is associated with the
CC mitochondria.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=Q9BZY9-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9BZY9-2; Sequence=VSP_005764, VSP_005765;
CC -!- TISSUE SPECIFICITY: Up-regulated in gastric adenocarcinomas.
CC {ECO:0000269|PubMed:18773414}.
CC -!- PTM: Auto-ubiquitinated (in vitro). {ECO:0000269|PubMed:18773414}.
CC -!- MISCELLANEOUS: [Isoform Beta]: May be produced at very low levels due
CC to a premature stop codon in the mRNA, leading to nonsense-mediated
CC mRNA decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16866.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF230386; AAG50165.1; -; mRNA.
DR EMBL; AF230387; AAG50166.1; -; mRNA.
DR EMBL; BT006675; AAP35321.1; -; mRNA.
DR EMBL; AK222729; BAD96449.1; -; mRNA.
DR EMBL; AL669914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX322644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016866; AAH16866.1; ALT_INIT; mRNA.
DR EMBL; BC017017; AAH17017.1; -; mRNA.
DR EMBL; Y07828; CAA69165.1; -; mRNA.
DR CCDS; CCDS34374.1; -. [Q9BZY9-1]
DR RefSeq; NP_008959.3; NM_007028.4. [Q9BZY9-1]
DR PDB; 2YSJ; NMR; -; A=1-56.
DR PDB; 2YSL; NMR; -; A=1-66.
DR PDBsum; 2YSJ; -.
DR PDBsum; 2YSL; -.
DR AlphaFoldDB; Q9BZY9; -.
DR BMRB; Q9BZY9; -.
DR SMR; Q9BZY9; -.
DR BioGRID; 116257; 34.
DR CORUM; Q9BZY9; -.
DR IntAct; Q9BZY9; 15.
DR STRING; 9606.ENSP00000365924; -.
DR GlyGen; Q9BZY9; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q9BZY9; -.
DR PhosphoSitePlus; Q9BZY9; -.
DR SwissPalm; Q9BZY9; -.
DR BioMuta; TRIM31; -.
DR DMDM; 68068082; -.
DR EPD; Q9BZY9; -.
DR MassIVE; Q9BZY9; -.
DR PaxDb; Q9BZY9; -.
DR PeptideAtlas; Q9BZY9; -.
DR PRIDE; Q9BZY9; -.
DR ProteomicsDB; 79921; -. [Q9BZY9-1]
DR ProteomicsDB; 79922; -. [Q9BZY9-2]
DR Antibodypedia; 11702; 199 antibodies from 26 providers.
DR DNASU; 11074; -.
DR Ensembl; ENST00000357569.5; ENSP00000350182.5; ENSG00000137397.18.
DR Ensembl; ENST00000376734.4; ENSP00000365924.3; ENSG00000204616.11. [Q9BZY9-1]
DR Ensembl; ENST00000433864.2; ENSP00000390551.2; ENSG00000233573.9.
DR Ensembl; ENST00000445679.2; ENSP00000409501.2; ENSG00000224168.9. [Q9BZY9-1]
DR Ensembl; ENST00000449412.2; ENSP00000398677.2; ENSG00000223531.9. [Q9BZY9-1]
DR Ensembl; ENST00000453266.2; ENSP00000391685.2; ENSG00000225130.9. [Q9BZY9-1]
DR GeneID; 11074; -.
DR KEGG; hsa:11074; -.
DR MANE-Select; ENST00000376734.4; ENSP00000365924.3; NM_007028.5; NP_008959.3.
DR UCSC; uc003npg.2; human. [Q9BZY9-1]
DR CTD; 11074; -.
DR DisGeNET; 11074; -.
DR GeneCards; TRIM31; -.
DR HGNC; HGNC:16289; TRIM31.
DR HPA; ENSG00000204616; Tissue enhanced (intestine, stomach, urinary bladder).
DR MIM; 609316; gene.
DR neXtProt; NX_Q9BZY9; -.
DR OpenTargets; ENSG00000204616; -.
DR PharmGKB; PA38117; -.
DR VEuPathDB; HostDB:ENSG00000204616; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000163585; -.
DR HOGENOM; CLU_013137_6_1_1; -.
DR InParanoid; Q9BZY9; -.
DR OMA; FWALRIA; -.
DR PhylomeDB; Q9BZY9; -.
DR TreeFam; TF338674; -.
DR PathwayCommons; Q9BZY9; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q9BZY9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 11074; 9 hits in 1110 CRISPR screens.
DR ChiTaRS; TRIM31; human.
DR EvolutionaryTrace; Q9BZY9; -.
DR GeneWiki; TRIM31; -.
DR GenomeRNAi; 11074; -.
DR Pharos; Q9BZY9; Tbio.
DR PRO; PR:Q9BZY9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9BZY9; protein.
DR Bgee; ENSG00000204616; Expressed in mucosa of transverse colon and 92 other tissues.
DR ExpressionAtlas; Q9BZY9; baseline and differential.
DR Genevisible; Q9BZY9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IMP:UniProtKB.
DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0019076; P:viral release from host cell; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR020457; Znf_B-box_chordata.
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 PRINTS; PR01406; BBOXZNFINGER.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 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 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Metal-binding;
KW Mitochondrion; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..425
FT /note="E3 ubiquitin-protein ligase TRIM31"
FT /id="PRO_0000056245"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 90..131
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 328..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 126..162
FT /evidence="ECO:0000255"
FT COILED 270..307
FT /evidence="ECO:0000255"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 249..267
FT /note="DIKVVLCRSEEFQFLNPTP -> NWRKNSVKQNQDTTPSQGA (in
FT isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_005764"
FT VAR_SEQ 268..425
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_005765"
FT VARIANT 17
FT /note="P -> R (in dbSNP:rs36063651)"
FT /id="VAR_052139"
FT VARIANT 118
FT /note="R -> C (in dbSNP:rs3734838)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_022728"
FT VARIANT 232
FT /note="V -> I (in dbSNP:rs2523989)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_022729"
FT VARIANT 235
FT /note="L -> P (in dbSNP:rs35775852)"
FT /id="VAR_052140"
FT VARIANT 421
FT /note="E -> K (in dbSNP:rs1116221)"
FT /evidence="ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_019962"
FT CONFLICT 37..38
FT /note="LK -> PQ (in Ref. 1; AAG50165/AAG50166 and 6;
FT CAA69165)"
FT /evidence="ECO:0000305"
FT CONFLICT 62..63
FT /note="KN -> RD (in Ref. 1; AAG50165/AAG50166 and 6;
FT CAA69165)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="D -> G (in Ref. 3; BAD96449)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..236
FT /note="ASTEPQLNDLKKLVDSLK -> EIPLMPTVERSQEARCYP (in Ref. 6;
FT CAA69165)"
FT /evidence="ECO:0000305"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2YSJ"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:2YSL"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2YSJ"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:2YSJ"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2YSL"
SQ SEQUENCE 425 AA; 48244 MW; 8CCC0D07F2DBB52D CRC64;
MASGQFVNKL QEEVICPICL DILQKPVTID CGHNFCLKCI TQIGETSCGF FKCPLCKTSV
RKNAIRFNSL LRNLVEKIQA LQASEVQSKR KEATCPRHQE MFHYFCEDDG KFLCFVCRES
KDHKSHNVSL IEEAAQNYQG QIQEQIQVLQ QKEKETVQVK AQGVHRVDVF TDQVEHEKQR
ILTEFELLHQ VLEEEKNFLL SRIYWLGHEG TEAGKHYVAS TEPQLNDLKK LVDSLKTKQN
MPPRQLLEDI KVVLCRSEEF QFLNPTPVPL ELEKKLSEAK SRHDSITGSL KKFKDQLQAD
RKKDENRFFK SMNKNDMKSW GLLQKNNHKM NKTSEPGSSS AGGRTTSGPP NHHSSAPSHS
LFRASSAGKV TFPVCLLASY DEISGQGASS QDTKTFDVAL SEELHAALSE WLTAIRAWFC
EVPSS
