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Protein TSSC4 (Tumor-suppressing STF cDNA 4 protein) (Tumor-suppressing subchromosomal transferable fragment candidate gene 4 protein)

 TSSC4_HUMAN             Reviewed;         329 AA.
Q9Y5U2; C9JS66; Q86VL2; Q9BRS6;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
05-DEC-2018, entry version 123.
RecName: Full=Protein TSSC4;
AltName: Full=Tumor-suppressing STF cDNA 4 protein;
AltName: Full=Tumor-suppressing subchromosomal transferable fragment candidate gene 4 protein;
Name=TSSC4;
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 SPECIFICITY, AND
VARIANT PRO-274.
PubMed=10072438; DOI=10.1093/hmg/8.4.683;
Lee M.P., Brandenburg S., Landes G.M., Adams M., Miller G.,
Feinberg A.P.;
"Two novel genes in the center of the 11p15 imprinted domain escape
genomic imprinting.";
Hum. Mol. Genet. 8:683-690(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
PRO-274.
TISSUE=Brain, and Lymph;
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND SER-146, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-217, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND SER-146, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-132 AND SER-146,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- INTERACTION:
Q8TAP6:CEP76; NbExp=3; IntAct=EBI-717229, EBI-742887;
Q53SE7:FLJ13057; NbExp=3; IntAct=EBI-717229, EBI-10172181;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-717229, EBI-618309;
O00505:KPNA3; NbExp=4; IntAct=EBI-717229, EBI-358297;
Q04864:REL; NbExp=3; IntAct=EBI-717229, EBI-307352;
Q96EP0-3:RNF31; NbExp=3; IntAct=EBI-717229, EBI-10225152;
Q9NYB0:TERF2IP; NbExp=2; IntAct=EBI-717229, EBI-750109;
Q13077:TRAF1; NbExp=3; IntAct=EBI-717229, EBI-359224;
Q12933:TRAF2; NbExp=3; IntAct=EBI-717229, EBI-355744;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y5U2-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y5U2-2; Sequence=VSP_016561;
-!- TISSUE SPECIFICITY: Expressed in fetal brain, lung, liver and
kidney. Widely expressed in adult tissues.
{ECO:0000269|PubMed:10072438}.
-!- SIMILARITY: Belongs to the TSSC4 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF125568; AAD23579.1; -; mRNA.
EMBL; AC124057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006091; AAH06091.1; -; mRNA.
EMBL; BC050616; AAH50616.1; -; mRNA.
CCDS; CCDS73241.1; -. [Q9Y5U2-2]
CCDS; CCDS7735.1; -. [Q9Y5U2-1]
RefSeq; NP_001284587.1; NM_001297658.1. [Q9Y5U2-1]
RefSeq; NP_001284588.1; NM_001297659.1. [Q9Y5U2-1]
RefSeq; NP_001284589.1; NM_001297660.1. [Q9Y5U2-1]
RefSeq; NP_001284590.1; NM_001297661.1. [Q9Y5U2-2]
RefSeq; NP_005697.2; NM_005706.3. [Q9Y5U2-1]
RefSeq; XP_006718181.1; XM_006718118.2. [Q9Y5U2-1]
RefSeq; XP_011518132.1; XM_011519830.2. [Q9Y5U2-1]
UniGene; Hs.523424; -.
UniGene; Hs.732116; -.
ProteinModelPortal; Q9Y5U2; -.
BioGrid; 115388; 98.
IntAct; Q9Y5U2; 23.
MINT; Q9Y5U2; -.
STRING; 9606.ENSP00000331087; -.
iPTMnet; Q9Y5U2; -.
PhosphoSitePlus; Q9Y5U2; -.
BioMuta; TSSC4; -.
DMDM; 296453006; -.
EPD; Q9Y5U2; -.
PaxDb; Q9Y5U2; -.
PeptideAtlas; Q9Y5U2; -.
PRIDE; Q9Y5U2; -.
ProteomicsDB; 86505; -.
ProteomicsDB; 86506; -. [Q9Y5U2-2]
DNASU; 10078; -.
Ensembl; ENST00000333256; ENSP00000331087; ENSG00000184281. [Q9Y5U2-1]
Ensembl; ENST00000380996; ENSP00000370384; ENSG00000184281. [Q9Y5U2-2]
Ensembl; ENST00000451491; ENSP00000411224; ENSG00000184281. [Q9Y5U2-1]
GeneID; 10078; -.
KEGG; hsa:10078; -.
UCSC; uc001lwi.4; human. [Q9Y5U2-1]
CTD; 10078; -.
EuPathDB; HostDB:ENSG00000184281.14; -.
GeneCards; TSSC4; -.
H-InvDB; HIX0009365; -.
HGNC; HGNC:12386; TSSC4.
HPA; HPA041801; -.
HPA; HPA058763; -.
MIM; 603852; gene.
neXtProt; NX_Q9Y5U2; -.
OpenTargets; ENSG00000184281; -.
PharmGKB; PA37054; -.
eggNOG; ENOG410IIC0; Eukaryota.
eggNOG; ENOG41120VA; LUCA.
GeneTree; ENSGT00390000011846; -.
HOGENOM; HOG000154697; -.
HOVERGEN; HBG059835; -.
InParanoid; Q9Y5U2; -.
OMA; PEAEEWS; -.
OrthoDB; EOG091G0SVE; -.
PhylomeDB; Q9Y5U2; -.
TreeFam; TF335741; -.
ChiTaRS; TSSC4; human.
GenomeRNAi; 10078; -.
PRO; PR:Q9Y5U2; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000184281; Expressed in 187 organ(s), highest expression level in left testis.
CleanEx; HS_TSSC4; -.
ExpressionAtlas; Q9Y5U2; baseline and differential.
Genevisible; Q9Y5U2; HS.
InterPro; IPR029338; TSSC4.
PANTHER; PTHR13445; PTHR13445; 1.
Pfam; PF15264; TSSC4; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 329 Protein TSSC4.
/FTId=PRO_0000076360.
MOD_RES 60 60 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JHE7}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JHE7}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 146 146 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 217 217 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
VAR_SEQ 8 71 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_016561.
VARIANT 17 17 H -> P (in dbSNP:rs2234278).
/FTId=VAR_057826.
VARIANT 124 124 R -> Q (in dbSNP:rs1008265).
/FTId=VAR_060194.
VARIANT 230 230 R -> S (in dbSNP:rs2234280).
/FTId=VAR_057827.
VARIANT 262 262 G -> R (in dbSNP:rs2234281).
/FTId=VAR_057828.
VARIANT 274 274 H -> P (in dbSNP:rs2234283).
{ECO:0000269|PubMed:10072438,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_063128.
CONFLICT 72 72 L -> F (in Ref. 1; AAD23579).
{ECO:0000305}.
SEQUENCE 329 AA; 34326 MW; AFC2D5CBD93844F0 CRC64;
MAEAGTGEPS PSVEGEHGTE YDTLPSDTVS LSDSDSDLSL PGGAEVEALS PMGLPGEEDS
GPDEPPSPPS GLLPATVQPF HLRGMSSTFS QRSRDIFDCL EGAARRAPSS VAHTSMSDNG
GFKRPLAPSG RSPVEGLGRA HRSPASPRVP PVPDYVAHPE RWTKYSLEDV TEVSEQSNQA
TALAFLGSQS LAAPTDCVSS FNQDPSSCGE GRVIFTKPVR GVEARHERKR VLGKVGEPGR
GGLGNPATDR GEGPVELAHL AGPGSPEAEE WGSHHGGLQE VEALSGSVHS GSVPGLPPVE
TVGFHGSRKR SRDHFRNKSS SPEDPGAEV


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