ID   TRI35_HUMAN             Reviewed;         493 AA.
AC   Q9UPQ4; Q86XQ0; Q8WVA4;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   14-DEC-2011, entry version 89.
DE   RecName: Full=Tripartite motif-containing protein 35;
DE   AltName: Full=Hemopoietic lineage switch protein 5;
GN   Name=TRIM35; Synonyms=HLS5, KIAA1098;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=14662771; DOI=10.1074/jbc.M306751200;
RA   Lalonde J.-P., Lim R., Ingley E., Tilbrook P.A., Thompson M.J.,
RA   McCulloch R., Beaumont J.G., Wicking C., Eyre H.J., Sutherland G.R.,
RA   Howe K., Solomon E., Williams J.H., Klinken S.P.;
RT   "HLS5, a novel RBCC (ring finger, B box, coiled-coil) family member
RT   isolated from a hemopoietic lineage switch, is a candidate tumor
RT   suppressor.";
RL   J. Biol. Chem. 279:8181-8189(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=99397452; PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA   Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 6:197-205(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Lung;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-8, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=19007248; DOI=10.1021/ac801708p;
RA   Wang B., Malik R., Nigg E.A., Korner R.;
RT   "Evaluation of the low-specificity protease elastase for large-scale
RT   phosphoproteome analysis.";
RL   Anal. Chem. 80:9526-9533(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASS
RP   SPECTROMETRY.
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
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
CC   -!- FUNCTION: May play a role as a tumor suppressor. Implicated in the
CC       cell death mechanism (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Found predominantly in cytoplasm with a granular
CC       distribution. Found in punctuate nuclear bodies (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UPQ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UPQ4-2; Sequence=VSP_012061;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The RING finger domain and the coiled-coil region are
CC       required for the apoptosis-inducing activity (By similarity).
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC   -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA83050.1; Type=Erroneous initiation;
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DR   EMBL; AF492463; AAO85480.1; -; mRNA.
DR   EMBL; AB029021; BAA83050.1; ALT_INIT; mRNA.
DR   EMBL; BC018337; AAH18337.1; -; mRNA.
DR   EMBL; BC069226; AAH69226.1; -; mRNA.
DR   IPI; IPI00012331; -.
DR   IPI; IPI00746107; -.
DR   RefSeq; NP_741983.2; NM_171982.3.
DR   UniGene; Hs.104223; -.
DR   ProteinModelPortal; Q9UPQ4; -.
DR   SMR; Q9UPQ4; 8-86, 95-142, 299-483.
DR   IntAct; Q9UPQ4; 8.
DR   STRING; Q9UPQ4; -.
DR   PhosphoSite; Q9UPQ4; -.
DR   DMDM; 56404980; -.
DR   PRIDE; Q9UPQ4; -.
DR   Ensembl; ENST00000305364; ENSP00000301924; ENSG00000104228.
DR   GeneID; 23087; -.
DR   KEGG; hsa:23087; -.
DR   UCSC; uc003xfl.1; human.
DR   CTD; 23087; -.
DR   GeneCards; GC08M025687; -.
DR   H-InvDB; HIX0007406; -.
DR   HGNC; HGNC:16285; TRIM35.
DR   HPA; HPA019647; -.
DR   neXtProt; NX_Q9UPQ4; -.
DR   PharmGKB; PA38115; -.
DR   eggNOG; prNOG16628; -.
DR   GeneTree; ENSGT00570000078805; -.
DR   HOGENOM; HBG755403; -.
DR   HOVERGEN; HBG098569; -.
DR   InParanoid; Q9UPQ4; -.
DR   OMA; FRAKCRN; -.
DR   OrthoDB; EOG4QNMW8; -.
DR   NextBio; 44229; -.
DR   ArrayExpress; Q9UPQ4; -.
DR   Bgee; Q9UPQ4; -.
DR   CleanEx; HS_TRIM35; -.
DR   Genevestigator; Q9UPQ4; -.
DR   GermOnline; ENSG00000104228; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006917; P:induction of apoptosis; ISS:UniProtKB.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR003879; Butyrophylin.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_rcpt.
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   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   KO; K12012; -.
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; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 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; Apoptosis; Coiled coil; Complete proteome;
KW   Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    493       Tripartite motif-containing protein 35.
FT                                /FTId=PRO_0000056250.
FT   DOMAIN      284    487       B30.2/SPRY.
FT   ZN_FING      21     61       RING-type.
FT   ZN_FING      96    137       B box-type.
FT   COILED      210    251       Potential.
FT   MOD_RES       4      4       Phosphoserine.
FT   MOD_RES       8      8       Phosphoserine.
FT   MOD_RES      65     65       Phosphoserine.
FT   VAR_SEQ     146    206       AKCRNMEHALREKAKAFWAMRRSYEAIAKHNQVEAAWLEGR
FT                                IRQEFDKLREFLRVEEQAIL -> VRSLIAEERRNFLPTHQ
FT                                WIVTKTRLQTSSPNLQSRRQGQVQEHGACTAGEGQGLLGHA
FT                                ALL (in isoform 2).
FT                                /FTId=VSP_012061.
SQ   SEQUENCE   493 AA;  56540 MW;  BFB7E5BFD3AD7E2D CRC64;
     MERSPDVSPG PSRSFKEELL CAVCYDPFRD AVTLRCGHNF CRGCVSRCWE VQVSPTCPVC
     KDRASPADLR TNHTLNNLVE KLLREEAEGA RWTSYRFSRV CRLHRGQLSL FCLEDKELLC
     CSCQADPRHQ GHRVQPVKDT AHDFRAKCRN MEHALREKAK AFWAMRRSYE AIAKHNQVEA
     AWLEGRIRQE FDKLREFLRV EEQAILDAMA EETRQKQLLA DEKMKQLTEE TEVLAHEIER
     LQMEMKEDDV SFLMKHKSRK RRLFCTMEPE PVQPGMLIDV CKYLGSLQYR VWKKMLASVE
     SVPFSFDPNT AAGWLSVSDD LTSVTNHGYR VQVENPERFS SAPCLLGSRV FSQGSHAWEV
     ALGGLQSWRV GVVRVRQDSG AEGHSHSCYH DTRSGFWYVC RTQGVEGDHC VTSDPATSPL
     VLAIPRRLRV ELECEEGELS FYDAERHCHL YTFHARFGEV RPYFYLGGAR GAGPPEPLRI
     CPLHISVKEE LDG
//