TRI29_HUMAN
ID TRI29_HUMAN Reviewed; 588 AA.
AC Q14134; Q96AA9; Q9BZY7;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Tripartite motif-containing protein 29;
DE AltName: Full=Ataxia telangiectasia group D-associated protein;
GN Name=TRIM29; Synonyms=ATDC;
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 ALPHA).
RX PubMed=8188213; DOI=10.1006/geno.1994.1022;
RA Leonhardt E.A., Kapp L.N., Young B.R., Murnane J.P.;
RT "Nucleotide sequence analysis of a candidate gene for ataxia-telangiectasia
RT group D (ATDC).";
RL Genomics 19:130-136(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND TISSUE
RP SPECIFICITY.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Astrocytoma;
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 [4]
RP INTERACTION WITH VIM AND HINT1, AND SUBCELLULAR LOCATION.
RX PubMed=7644499; DOI=10.1073/pnas.92.17.7824;
RA Brzoska P.M., Chen H., Zhu Y., Levin N.A., Disatnik M.H., Mochly-Rosen D.,
RA Murnane J.P., Christman M.F.;
RT "The product of the ataxia-telangiectasia group D complementing gene, ATDC,
RT interacts with a protein kinase C substrate and inhibitor.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:7824-7828(1995).
RN [5]
RP PHOSPHORYLATION.
RX PubMed=8647648;
RX DOI=10.1002/(sici)1097-0215(19960611)66:6<772::aid-ijc11>3.0.co;2-5;
RA Laderoute K.R., Knapp A.M., Green C.J., Sutherland R.M., Kapp L.N.;
RT "Expression of the ATDC (ataxia telangiectasia group D-complementing) gene
RT in A431 human squamous carcinoma cells.";
RL Int. J. Cancer 66:772-778(1996).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, 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].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-104; THR-476 AND
RP SER-489, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-104, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-28; SER-58; SER-104
RP AND TYR-106, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [12]
RP STRUCTURE BY NMR OF 212-270.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZF-B_box type2 domain of human tripartite motif
RT protein TRIM29 isoform alpha.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-514.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [14]
RP FUNCTION, INTERACTION WITH IKBKG, AND SUBCELLULAR LOCATION.
RX PubMed=27695001; DOI=10.1038/ni.3580;
RA Xing J., Weng L., Yuan B., Wang Z., Jia L., Jin R., Lu H., Li X.C.,
RA Liu Y.J., Zhang Z.;
RT "Identification of a role for TRIM29 in the control of innate immunity in
RT the respiratory tract.";
RL Nat. Immunol. 17:1373-1380(2016).
RN [15]
RP FUNCTION, AND INTERACTION WITH STING1.
RX PubMed=29038422; DOI=10.1038/s41467-017-00101-w;
RA Xing J., Zhang A., Zhang H., Wang J., Li X.C., Zeng M.S., Zhang Z.;
RT "TRIM29 promotes DNA virus infections by inhibiting innate immune
RT response.";
RL Nat. Commun. 8:945-945(2017).
CC -!- FUNCTION: Plays a crucial role in the regulation of macrophage
CC activation in response to viral or bacterial infections within the
CC respiratory tract. Mechanistically, TRIM29 interacts with IKBKG/NEMO in
CC the lysosome where it induces its 'Lys-48' ubiquitination and
CC subsequent degradation. In turn, the expression of type I interferons
CC and the production of pro-inflammatory cytokines are inhibited.
CC Additionally, induces the 'Lys-48' ubiquitination of STING1 in a
CC similar way, leading to its degradation. {ECO:0000269|PubMed:27695001,
CC ECO:0000269|PubMed:29038422}.
CC -!- SUBUNIT: Interacts with VIM and HINT1 (PubMed:7644499). Interacts with
CC IKBKG/NEMO (PubMed:27695001). Interacts with STING1 (PubMed:29038422).
CC {ECO:0000269|PubMed:27695001, ECO:0000269|PubMed:29038422,
CC ECO:0000269|PubMed:7644499}.
CC -!- INTERACTION:
CC Q14134; Q08043: ACTN3; NbExp=3; IntAct=EBI-702370, EBI-2880652;
CC Q14134; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-702370, EBI-11954519;
CC Q14134; O15169: AXIN1; NbExp=2; IntAct=EBI-702370, EBI-710484;
CC Q14134; Q9H257: CARD9; NbExp=3; IntAct=EBI-702370, EBI-751319;
CC Q14134; Q2TAC2-2: CCDC57; NbExp=6; IntAct=EBI-702370, EBI-10961624;
CC Q14134; Q8NHQ1: CEP70; NbExp=5; IntAct=EBI-702370, EBI-739624;
CC Q14134; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-702370, EBI-11988027;
CC Q14134; O14641: DVL2; NbExp=5; IntAct=EBI-702370, EBI-740850;
CC Q14134; Q96CN9: GCC1; NbExp=2; IntAct=EBI-702370, EBI-746252;
CC Q14134; Q08379: GOLGA2; NbExp=5; IntAct=EBI-702370, EBI-618309;
CC Q14134; P49841: GSK3B; NbExp=2; IntAct=EBI-702370, EBI-373586;
CC Q14134; Q92764: KRT35; NbExp=3; IntAct=EBI-702370, EBI-1058674;
CC Q14134; Q9BRK4: LZTS2; NbExp=4; IntAct=EBI-702370, EBI-741037;
CC Q14134; Q9Y6D9: MAD1L1; NbExp=7; IntAct=EBI-702370, EBI-742610;
CC Q14134; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-702370, EBI-11522433;
CC Q14134; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-702370, EBI-10271199;
CC Q14134; P36406: TRIM23; NbExp=4; IntAct=EBI-702370, EBI-740098;
CC Q14134; Q14134: TRIM29; NbExp=5; IntAct=EBI-702370, EBI-702370;
CC Q14134; Q15654: TRIP6; NbExp=3; IntAct=EBI-702370, EBI-742327;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7644499}. Lysosome
CC {ECO:0000269|PubMed:27695001}. Note=Colocalizes with intermediate
CC filaments.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=Q14134-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q14134-2; Sequence=VSP_011999;
CC -!- TISSUE SPECIFICITY: Expressed in placenta, prostate and thymus.
CC {ECO:0000269|PubMed:11331580}.
CC -!- PTM: Constitutively phosphorylated by PKC on serine/threonine in A431
CC cells. {ECO:0000269|PubMed:8647648}.
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DR EMBL; L24203; AAA35762.1; -; mRNA.
DR EMBL; AF230388; AAG50167.1; -; mRNA.
DR EMBL; AF230389; AAG50168.1; -; mRNA.
DR EMBL; BC017352; AAH17352.1; -; mRNA.
DR CCDS; CCDS8428.1; -. [Q14134-1]
DR PIR; A49618; A49618.
DR RefSeq; NP_036233.2; NM_012101.3. [Q14134-1]
DR PDB; 2CSV; NMR; -; A=212-270.
DR PDBsum; 2CSV; -.
DR AlphaFoldDB; Q14134; -.
DR SMR; Q14134; -.
DR BioGRID; 117177; 246.
DR IntAct; Q14134; 85.
DR MINT; Q14134; -.
DR STRING; 9606.ENSP00000343129; -.
DR GlyGen; Q14134; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14134; -.
DR PhosphoSitePlus; Q14134; -.
DR BioMuta; TRIM29; -.
DR DMDM; 116242825; -.
DR EPD; Q14134; -.
DR jPOST; Q14134; -.
DR MassIVE; Q14134; -.
DR MaxQB; Q14134; -.
DR PaxDb; Q14134; -.
DR PeptideAtlas; Q14134; -.
DR PRIDE; Q14134; -.
DR ProteomicsDB; 59831; -. [Q14134-1]
DR ProteomicsDB; 59832; -. [Q14134-2]
DR Antibodypedia; 18856; 607 antibodies from 40 providers.
DR DNASU; 23650; -.
DR Ensembl; ENST00000341846.10; ENSP00000343129.5; ENSG00000137699.17. [Q14134-1]
DR GeneID; 23650; -.
DR KEGG; hsa:23650; -.
DR MANE-Select; ENST00000341846.10; ENSP00000343129.5; NM_012101.4; NP_036233.2.
DR UCSC; uc001pwz.4; human. [Q14134-1]
DR CTD; 23650; -.
DR DisGeNET; 23650; -.
DR GeneCards; TRIM29; -.
DR HGNC; HGNC:17274; TRIM29.
DR HPA; ENSG00000137699; Tissue enhanced (esophagus, skin, vagina).
DR MIM; 610658; gene.
DR neXtProt; NX_Q14134; -.
DR OpenTargets; ENSG00000137699; -.
DR PharmGKB; PA38218; -.
DR VEuPathDB; HostDB:ENSG00000137699; -.
DR eggNOG; ENOG502QWDV; Eukaryota.
DR GeneTree; ENSGT00940000161416; -.
DR HOGENOM; CLU_039304_0_0_1; -.
DR InParanoid; Q14134; -.
DR OMA; TNGHSGE; -.
DR OrthoDB; 619794at2759; -.
DR PhylomeDB; Q14134; -.
DR TreeFam; TF351086; -.
DR PathwayCommons; Q14134; -.
DR Reactome; R-HSA-877300; Interferon gamma signaling.
DR SignaLink; Q14134; -.
DR BioGRID-ORCS; 23650; 15 hits in 1105 CRISPR screens.
DR ChiTaRS; TRIM29; human.
DR EvolutionaryTrace; Q14134; -.
DR GeneWiki; TRIM29; -.
DR GenomeRNAi; 23650; -.
DR Pharos; Q14134; Tbio.
DR PRO; PR:Q14134; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q14134; protein.
DR Bgee; ENSG00000137699; Expressed in lower esophagus mucosa and 148 other tissues.
DR ExpressionAtlas; Q14134; baseline and differential.
DR Genevisible; Q14134; HS.
DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR InterPro; IPR000315; Znf_B-box.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Immunity;
KW Innate immunity; Lysosome; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..588
FT /note="Tripartite motif-containing protein 29"
FT /id="PRO_0000056242"
FT ZN_FING 220..260
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 259..352
FT /evidence="ECO:0000255"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 228
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 106
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 476
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 569..588
FT /note="SHYRPFYVNKGNGIGSNEAP -> VV (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_011999"
FT VARIANT 514
FT /note="S -> F (in a breast cancer sample; somatic mutation;
FT dbSNP:rs112973609)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035962"
FT CONFLICT 126..127
FT /note="EL -> DV (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:2CSV"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:2CSV"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2CSV"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:2CSV"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:2CSV"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2CSV"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:2CSV"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:2CSV"
SQ SEQUENCE 588 AA; 65835 MW; 7CBAD7A4C43A311C CRC64;
MEAADASRSN GSSPEARDAR SPSGPSGSLE NGTKADGKDA KTTNGHGGEA AEGKSLGSAL
KPGEGRSALF AGNEWRRPII QFVESGDDKN SNYFSMDSME GKRSPYAGLQ LGAAKKPPVT
FAEKGELRKS IFSESRKPTV SIMEPGETRR NSYPRADTGL FSRSKSGSEE VLCDSCIGNK
QKAVKSCLVC QASFCELHLK PHLEGAAFRD HQLLEPIRDF EARKCPVHGK TMELFCQTDQ
TCICYLCMFQ EHKNHSTVTV EEAKAEKETE LSLQKEQLQL KIIEIEDEAE KWQKEKDRIK
SFTTNEKAIL EQNFRDLVRD LEKQKEEVRA ALEQREQDAV DQVKVIMDAL DERAKVLHED
KQTREQLHSI SDSVLFLQEF GALMSNYSLP PPLPTYHVLL EGEGLGQSLG NFKDDLLNVC
MRHVEKMCKA DLSRNFIERN HMENGGDHRY VNNYTNSFGG EWSAPDTMKR YSMYLTPKGG
VRTSYQPSSP GRFTKETTQK NFNNLYGTKG NYTSRVWEYS SSIQNSDNDL PVVQGSSSFS
LKGYPSLMRS QSPKAQPQTW KSGKQTMLSH YRPFYVNKGN GIGSNEAP
