TRI15_HUMAN
ID TRI15_HUMAN Reviewed; 465 AA.
AC Q9C019; A2BEC9; O95604; Q8IUX9; Q9C018;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Tripartite motif-containing protein 15;
DE AltName: Full=RING finger protein 93;
DE AltName: Full=Zinc finger protein 178;
DE AltName: Full=Zinc finger protein B7;
GN Name=TRIM15; Synonyms=RNF93, ZNF178, ZNFB7;
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 1 AND 2), AND VARIANT VAL-29.
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 [MRNA] (ISOFORM 1), AND VARIANT VAL-29.
RX PubMed=8304341;
RA Goei V.L., Parimoo S., Capossela A., Chu T.W., Gruen J.R.;
RT "Isolation of novel non-HLA gene fragments from the hemochromatosis region
RT (6p21.3) by cDNA hybridization selection.";
RL Am. J. Hum. Genet. 54:244-251(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina S., Tamiya G., Oka A., Inoko H.;
RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-29.
RA Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.;
RT "Genome diversity in HLA: a new strategy for detection of genetic
RT polymorphisms in expressed genes within the HLA class III and class I
RT regions.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-324.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-324.
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).
CC -!- INTERACTION:
CC Q9C019; O15169: AXIN1; NbExp=3; IntAct=EBI-2342111, EBI-710484;
CC Q9C019; Q00534: CDK6; NbExp=3; IntAct=EBI-2342111, EBI-295663;
CC Q9C019; Q6UXP7: FAM151B; NbExp=3; IntAct=EBI-2342111, EBI-8456391;
CC Q9C019; Q3B820: FAM161A; NbExp=3; IntAct=EBI-2342111, EBI-719941;
CC Q9C019; Q96MY7: FAM161B; NbExp=3; IntAct=EBI-2342111, EBI-7225287;
CC Q9C019; Q9UJ41: RABGEF1; NbExp=3; IntAct=EBI-2342111, EBI-913954;
CC Q9C019; Q9BW85: YJU2; NbExp=3; IntAct=EBI-2342111, EBI-10300345;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q9C019-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q9C019-2; Sequence=VSP_005760, VSP_005761;
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF220132; AAG53505.1; -; mRNA.
DR EMBL; AF220133; AAG53506.1; -; mRNA.
DR EMBL; U34249; AAD03787.1; -; mRNA.
DR EMBL; BA000025; BAB63331.1; -; Genomic_DNA.
DR EMBL; AB088089; BAC54922.1; -; Genomic_DNA.
DR EMBL; BX248419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038585; AAH38585.1; -; mRNA.
DR CCDS; CCDS4677.1; -. [Q9C019-1]
DR RefSeq; NP_150232.2; NM_033229.2. [Q9C019-1]
DR AlphaFoldDB; Q9C019; -.
DR SMR; Q9C019; -.
DR BioGRID; 124626; 49.
DR IntAct; Q9C019; 18.
DR STRING; 9606.ENSP00000365884; -.
DR MoonDB; Q9C019; Predicted.
DR iPTMnet; Q9C019; -.
DR PhosphoSitePlus; Q9C019; -.
DR BioMuta; TRIM15; -.
DR DMDM; 25009482; -.
DR MassIVE; Q9C019; -.
DR MaxQB; Q9C019; -.
DR PaxDb; Q9C019; -.
DR PeptideAtlas; Q9C019; -.
DR PRIDE; Q9C019; -.
DR ProteomicsDB; 79941; -. [Q9C019-1]
DR ProteomicsDB; 79942; -. [Q9C019-2]
DR Antibodypedia; 26243; 179 antibodies from 21 providers.
DR DNASU; 89870; -.
DR Ensembl; ENST00000259930.10; ENSP00000259930.6; ENSG00000137384.12. [Q9C019-1]
DR Ensembl; ENST00000376694.9; ENSP00000365884.4; ENSG00000204610.14. [Q9C019-1]
DR Ensembl; ENST00000414873.6; ENSP00000415480.2; ENSG00000235259.8. [Q9C019-1]
DR Ensembl; ENST00000421984.6; ENSP00000413961.2; ENSG00000227147.9. [Q9C019-1]
DR Ensembl; ENST00000427091.6; ENSP00000411683.2; ENSG00000235960.9. [Q9C019-1]
DR Ensembl; ENST00000431059.6; ENSP00000403221.2; ENSG00000233599.8. [Q9C019-1]
DR Ensembl; ENST00000550400.2; ENSP00000447500.2; ENSG00000233599.8. [Q9C019-2]
DR Ensembl; ENST00000552676.2; ENSP00000449686.2; ENSG00000235905.8. [Q9C019-2]
DR Ensembl; ENST00000552836.2; ENSP00000449617.2; ENSG00000224145.8. [Q9C019-2]
DR GeneID; 89870; -.
DR KEGG; hsa:89870; -.
DR MANE-Select; ENST00000376694.9; ENSP00000365884.4; NM_033229.3; NP_150232.2.
DR UCSC; uc010jrx.4; human. [Q9C019-1]
DR CTD; 89870; -.
DR DisGeNET; 89870; -.
DR GeneCards; TRIM15; -.
DR HGNC; HGNC:16284; TRIM15.
DR HPA; ENSG00000204610; Group enriched (intestine, kidney, liver).
DR neXtProt; NX_Q9C019; -.
DR OpenTargets; ENSG00000204610; -.
DR PharmGKB; PA38114; -.
DR VEuPathDB; HostDB:ENSG00000204610; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162589; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q9C019; -.
DR OMA; EDTKCRE; -.
DR PhylomeDB; Q9C019; -.
DR TreeFam; TF342569; -.
DR PathwayCommons; Q9C019; -.
DR SignaLink; Q9C019; -.
DR BioGRID-ORCS; 89870; 13 hits in 1104 CRISPR screens.
DR ChiTaRS; TRIM15; human.
DR GeneWiki; TRIM15; -.
DR GenomeRNAi; 89870; -.
DR Pharos; Q9C019; Tbio.
DR PRO; PR:Q9C019; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9C019; protein.
DR ExpressionAtlas; Q9C019; baseline and differential.
DR Genevisible; Q9C019; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0007500; P:mesodermal cell fate determination; TAS:ProtInc.
DR GO; GO:1901253; P:negative regulation of intracellular transport of viral material; IMP:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IMP:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; 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:0044790; P:suppression of viral release by host; IDA:UniProtKB.
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; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
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; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 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 Alternative splicing; Coiled coil; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..465
FT /note="Tripartite motif-containing protein 15"
FT /id="PRO_0000056218"
FT DOMAIN 276..465
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..61
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 78..119
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 126..229
FT /evidence="ECO:0000255"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 103..115
FT /note="VFCREGPTHQAHT -> TSECRTTDGFGCA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_005760"
FT VAR_SEQ 116..465
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_005761"
FT VARIANT 29
FT /note="I -> V (in dbSNP:rs17194460)"
FT /evidence="ECO:0000269|PubMed:11331580,
FT ECO:0000269|PubMed:8304341, ECO:0000269|Ref.4"
FT /id="VAR_014228"
FT VARIANT 42
FT /note="A -> T (in dbSNP:rs17194467)"
FT /id="VAR_052129"
FT VARIANT 84
FT /note="E -> Q (in dbSNP:rs17194474)"
FT /id="VAR_052130"
FT VARIANT 235
FT /note="L -> V (in dbSNP:rs34823152)"
FT /id="VAR_052131"
FT VARIANT 324
FT /note="S -> N (in dbSNP:rs929156)"
FT /evidence="ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_052132"
SQ SEQUENCE 465 AA; 52113 MW; 303B8BF8623CB00A CRC64;
MPATPSLKVV HELPACTLCA GPLEDAVTIP CGHTFCRLCL PALSQMGAQS SGKILLCPLC
QEEEQAETPM APVPLGPLGE TYCEEHGEKI YFFCENDAEF LCVFCREGPT HQAHTVGFLD
EAIQPYRDRL RSRLEALSTE RDEIEDVKCQ EDQKLQVLLT QIESKKHQVE TAFERLQQEL
EQQRCLLLAR LRELEQQIWK ERDEYITKVS EEVTRLGAQV KELEEKCQQP ASELLQDVRV
NQSRCEMKTF VSPEAISPDL VKKIRDFHRK ILTLPEMMRM FSENLAHHLE IDSGVITLDP
QTASRSLVLS EDRKSVRYTR QKKSLPDSPL RFDGLPAVLG FPGFSSGRHR WQVDLQLGDG
GGCTVGVAGE GVRRKGEMGL SAEDGVWAVI ISHQQCWAST SPGTDLPLSE IPRGVRVALD
YEAGQVTLHN AQTQEPIFTF TASFSGKVFP FFAVWKKGSC LTLKG
