TRI65_HUMAN
ID TRI65_HUMAN Reviewed; 517 AA.
AC Q6PJ69; Q4G0F0; Q6DKJ6; Q9BRP6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Tripartite motif-containing protein 65;
GN Name=TRIM65;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-222 AND PRO-509.
RC TISSUE=Brain, Liver, and Lymph;
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 [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH73831.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC087289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006138; AAH06138.1; -; mRNA.
DR EMBL; BC021259; AAH21259.2; -; mRNA.
DR EMBL; BC073831; AAH73831.1; ALT_INIT; mRNA.
DR EMBL; BC098412; AAH98412.1; -; mRNA.
DR CCDS; CCDS11732.1; -.
DR RefSeq; NP_001243053.1; NM_001256124.1.
DR RefSeq; NP_775818.2; NM_173547.3.
DR PDB; 7JL0; EM; 4.30 A; B=312-502.
DR PDB; 7JL2; EM; 4.30 A; B/D/F=312-502.
DR PDB; 7JL4; X-ray; 1.92 A; A/B/C=312-502.
DR PDBsum; 7JL0; -.
DR PDBsum; 7JL2; -.
DR PDBsum; 7JL4; -.
DR AlphaFoldDB; Q6PJ69; -.
DR SMR; Q6PJ69; -.
DR BioGRID; 128382; 77.
DR IntAct; Q6PJ69; 18.
DR MINT; Q6PJ69; -.
DR STRING; 9606.ENSP00000269383; -.
DR iPTMnet; Q6PJ69; -.
DR PhosphoSitePlus; Q6PJ69; -.
DR BioMuta; TRIM65; -.
DR DMDM; 296453004; -.
DR EPD; Q6PJ69; -.
DR jPOST; Q6PJ69; -.
DR MassIVE; Q6PJ69; -.
DR MaxQB; Q6PJ69; -.
DR PaxDb; Q6PJ69; -.
DR PeptideAtlas; Q6PJ69; -.
DR PRIDE; Q6PJ69; -.
DR ProteomicsDB; 67192; -.
DR Antibodypedia; 19643; 98 antibodies from 16 providers.
DR DNASU; 201292; -.
DR Ensembl; ENST00000269383.8; ENSP00000269383.3; ENSG00000141569.12.
DR GeneID; 201292; -.
DR KEGG; hsa:201292; -.
DR MANE-Select; ENST00000269383.8; ENSP00000269383.3; NM_173547.4; NP_775818.2.
DR UCSC; uc002jpx.4; human.
DR CTD; 201292; -.
DR DisGeNET; 201292; -.
DR GeneCards; TRIM65; -.
DR HGNC; HGNC:27316; TRIM65.
DR HPA; ENSG00000141569; Low tissue specificity.
DR MIM; 619408; gene.
DR neXtProt; NX_Q6PJ69; -.
DR OpenTargets; ENSG00000141569; -.
DR PharmGKB; PA134877726; -.
DR VEuPathDB; HostDB:ENSG00000141569; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000161851; -.
DR HOGENOM; CLU_013137_0_2_1; -.
DR InParanoid; Q6PJ69; -.
DR OMA; CTVHECR; -.
DR OrthoDB; 368202at2759; -.
DR PhylomeDB; Q6PJ69; -.
DR TreeFam; TF351090; -.
DR PathwayCommons; Q6PJ69; -.
DR SignaLink; Q6PJ69; -.
DR BioGRID-ORCS; 201292; 15 hits in 1112 CRISPR screens.
DR ChiTaRS; TRIM65; human.
DR GenomeRNAi; 201292; -.
DR Pharos; Q6PJ69; Tbio.
DR PRO; PR:Q6PJ69; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6PJ69; protein.
DR Bgee; ENSG00000141569; Expressed in buccal mucosa cell and 107 other tissues.
DR ExpressionAtlas; Q6PJ69; baseline and differential.
DR Genevisible; Q6PJ69; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP: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; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 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 3D-structure; Acetylation; Coiled coil; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..517
FT /note="Tripartite motif-containing protein 65"
FT /id="PRO_0000249191"
FT DOMAIN 313..506
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 12..51
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 90..137
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 75..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..227
FT /evidence="ECO:0000255"
FT COMPBIAS 80..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BFW4"
FT VARIANT 222
FT /note="V -> G (in dbSNP:rs7222757)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060245"
FT VARIANT 364
FT /note="G -> R (in dbSNP:rs34593741)"
FT /id="VAR_057224"
FT VARIANT 366
FT /note="G -> S (in dbSNP:rs9892938)"
FT /id="VAR_057225"
FT VARIANT 509
FT /note="L -> P (in dbSNP:rs3760128)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060246"
FT HELIX 321..326
FT /evidence="ECO:0007829|PDB:7JL4"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:7JL4"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:7JL4"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 381..400
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 429..436
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 439..444
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 450..456
FT /evidence="ECO:0007829|PDB:7JL4"
FT TURN 457..460
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 472..478
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 485..491
FT /evidence="ECO:0007829|PDB:7JL4"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:7JL4"
SQ SEQUENCE 517 AA; 57353 MW; 1382A178CB99BBBA CRC64;
MAAQLLEEKL TCAICLGLYQ DPVTLPCGHN FCGACIRDWW DRCGKACPEC REPFPDGAEL
RRNVALSGVL EVVRAGPARD PGPDPGPGPD PAARCPRHGR PLELFCRTEG RCVCSVCTVR
ECRLHERALL DAERLKREAQ LRASLEVTQQ QATQAEGQLL ELRKQSSQIQ NSACILASWV
SGKFSSLLQA LEIQHTTALR SIEVAKTQAL AQARDEEQRL RVHLEAVARH GCRIRELLEQ
VDEQTFLQES QLLQPPGPLG PLTPLQWDED QQLGDLKQLL SRLCGLLLEE GSHPGAPAKP
VDLAPVEAPG PLAPVPSTVC PLRRKLWQNY RNLTFDPVSA NRHFYLSRQD QQVKHCRQSR
GPGGPGSFEL WQVQCAQSFQ AGHHYWEVRA SDHSVTLGVS YPQLPRCRLG PHTDNIGRGP
CSWGLCVQED SLQAWHNGEA QRLPGVSGRL LGMDLDLASG CLTFYSLEPQ TQPLYTFHAL
FNQPLTPVFW LLEGRTLTLC HQPGAVFPLG PQEEVLS
