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Tripartite motif-containing protein 35 (Hemopoietic lineage switch protein 5)

 TRI35_HUMAN             Reviewed;         493 AA.
Q9UPQ4; Q86XQ0; Q8WVA4;
07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
07-DEC-2004, sequence version 2.
12-SEP-2018, entry version 151.
RecName: Full=Tripartite motif-containing protein 35;
AltName: Full=Hemopoietic lineage switch protein 5;
Name=TRIM35; Synonyms=HLS5, KIAA1098;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=14662771; DOI=10.1074/jbc.M306751200;
Lalonde J.-P., Lim R., Ingley E., Tilbrook P.A., Thompson M.J.,
McCulloch R., Beaumont J.G., Wicking C., Eyre H.J., Sutherland G.R.,
Howe K., Solomon E., Williams J.H., Klinken S.P.;
"HLS5, a novel RBCC (ring finger, B box, coiled-coil) family member
isolated from a hemopoietic lineage switch, is a candidate tumor
suppressor.";
J. Biol. Chem. 279:8181-8189(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-4 AND SER-8, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[6]
FUNCTION, INTERACTION WITH PKM, AND SUBCELLULAR LOCATION.
PubMed=25263439; DOI=10.1038/onc.2014.325;
Chen Z., Wang Z., Guo W., Zhang Z., Zhao F., Zhao Y., Jia D., Ding J.,
Wang H., Yao M., He X.;
"TRIM35 Interacts with pyruvate kinase isoform M2 to suppress the
Warburg effect and tumorigenicity in hepatocellular carcinoma.";
Oncogene 34:3946-3956(2015).
-!- FUNCTION: Reduces FGFR1-dependent tyrosine phosphorylation of PKM,
inhibiting PKM-dependent lactate production, glucose metabolism,
and cell growth (PubMed:25263439). Involved in the cell death
mechanism (By similarity). {ECO:0000250|UniProtKB:Q8C006,
ECO:0000269|PubMed:25263439}.
-!- SUBUNIT: Interacts with PKM isoform M2, but not isoform M1; this
interaction may compete with that between PKM and FGFR1, and hence
reduces FGFR1-dependent tyrosine phosphorylation of PKM.
{ECO:0000269|PubMed:25263439}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25263439}.
Nucleus {ECO:0000250}. Note=Found predominantly in cytoplasm with
a granular distribution. Found in punctuate nuclear bodies (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UPQ4-1; Sequence=Displayed;
Name=2;
IsoId=Q9UPQ4-2; Sequence=VSP_012061;
Note=No experimental confirmation available.;
-!- DOMAIN: The RING finger domain and the coiled-coil region are
required for the apoptosis-inducing activity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA83050.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF492463; AAO85480.1; -; mRNA.
EMBL; AB029021; BAA83050.1; ALT_INIT; mRNA.
EMBL; BC018337; AAH18337.1; -; mRNA.
EMBL; BC069226; AAH69226.1; -; mRNA.
CCDS; CCDS6056.2; -. [Q9UPQ4-1]
RefSeq; NP_741983.2; NM_171982.4. [Q9UPQ4-1]
UniGene; Hs.104223; -.
ProteinModelPortal; Q9UPQ4; -.
SMR; Q9UPQ4; -.
BioGrid; 116716; 35.
IntAct; Q9UPQ4; 36.
STRING; 9606.ENSP00000301924; -.
iPTMnet; Q9UPQ4; -.
PhosphoSitePlus; Q9UPQ4; -.
BioMuta; TRIM35; -.
DMDM; 56404980; -.
PaxDb; Q9UPQ4; -.
PeptideAtlas; Q9UPQ4; -.
PRIDE; Q9UPQ4; -.
ProteomicsDB; 85414; -.
ProteomicsDB; 85415; -. [Q9UPQ4-2]
DNASU; 23087; -.
Ensembl; ENST00000305364; ENSP00000301924; ENSG00000104228. [Q9UPQ4-1]
GeneID; 23087; -.
KEGG; hsa:23087; -.
UCSC; uc003xfl.2; human. [Q9UPQ4-1]
CTD; 23087; -.
DisGeNET; 23087; -.
EuPathDB; HostDB:ENSG00000104228.12; -.
GeneCards; TRIM35; -.
HGNC; HGNC:16285; TRIM35.
HPA; HPA019647; -.
MIM; 617007; gene.
neXtProt; NX_Q9UPQ4; -.
OpenTargets; ENSG00000104228; -.
PharmGKB; PA38115; -.
eggNOG; ENOG410ITFW; Eukaryota.
eggNOG; ENOG410YB4K; LUCA.
GeneTree; ENSGT00760000118838; -.
HOGENOM; HOG000124586; -.
HOVERGEN; HBG098569; -.
InParanoid; Q9UPQ4; -.
KO; K12012; -.
OMA; LRICPLR; -.
OrthoDB; EOG091G0AKN; -.
PhylomeDB; Q9UPQ4; -.
TreeFam; TF334286; -.
Reactome; R-HSA-877300; Interferon gamma signaling.
GenomeRNAi; 23087; -.
PRO; PR:Q9UPQ4; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104228; Expressed in 170 organ(s), highest expression level in skin of abdomen.
CleanEx; HS_TRIM35; -.
ExpressionAtlas; Q9UPQ4; baseline and differential.
Genevisible; Q9UPQ4; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB.
GO; GO:1902187; P:negative regulation of viral release from host cell; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
CDD; cd00021; BBOX; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR006574; PRY.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF13765; PRY; 1.
Pfam; PF00622; SPRY; 1.
Pfam; PF00643; zf-B_box; 1.
PRINTS; PR01407; BUTYPHLNCDUF.
SMART; SM00336; BBOX; 1.
SMART; SM00589; PRY; 1.
SMART; SM00184; RING; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; Coiled coil;
Complete proteome; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Zinc; Zinc-finger.
CHAIN 1 493 Tripartite motif-containing protein 35.
/FTId=PRO_0000056250.
DOMAIN 284 487 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 21 61 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 96 137 B box-type. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 210 251 {ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
VAR_SEQ 146 206 AKCRNMEHALREKAKAFWAMRRSYEAIAKHNQVEAAWLEGR
IRQEFDKLREFLRVEEQAIL -> VRSLIAEERRNFLPTHQ
WIVTKTRLQTSSPNLQSRRQGQVQEHGACTAGEGQGLLGHA
ALL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012061.
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


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