TSSC4_HUMAN
ID TSSC4_HUMAN Reviewed; 329 AA.
AC Q9Y5U2; C9JS66; Q86VL2; Q9BRS6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein TSSC4;
DE AltName: Full=Tumor-suppressing STF cDNA 4 protein;
DE AltName: Full=Tumor-suppressing subchromosomal transferable fragment candidate gene 4 protein;
GN Name=TSSC4;
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 1), TISSUE SPECIFICITY, AND VARIANT
RP PRO-274.
RX PubMed=10072438; DOI=10.1093/hmg/8.4.683;
RA Lee M.P., Brandenburg S., Landes G.M., Adams M., Miller G., Feinberg A.P.;
RT "Two novel genes in the center of the 11p15 imprinted domain escape genomic
RT imprinting.";
RL Hum. Mol. Genet. 8:683-690(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP PRO-274.
RC TISSUE=Brain, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND SER-146, AND
RP 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-217, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143 AND SER-146, 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-132 AND SER-146, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- INTERACTION:
CC Q9Y5U2; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-717229, EBI-742887;
CC Q9Y5U2; Q53SE7: FLJ13057; NbExp=3; IntAct=EBI-717229, EBI-10172181;
CC Q9Y5U2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-717229, EBI-618309;
CC Q9Y5U2; O00505: KPNA3; NbExp=4; IntAct=EBI-717229, EBI-358297;
CC Q9Y5U2; Q04864: REL; NbExp=3; IntAct=EBI-717229, EBI-307352;
CC Q9Y5U2; Q96EP0-3: RNF31; NbExp=3; IntAct=EBI-717229, EBI-10225152;
CC Q9Y5U2; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-717229, EBI-750109;
CC Q9Y5U2; Q13077: TRAF1; NbExp=3; IntAct=EBI-717229, EBI-359224;
CC Q9Y5U2; Q12933: TRAF2; NbExp=3; IntAct=EBI-717229, EBI-355744;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y5U2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5U2-2; Sequence=VSP_016561;
CC -!- TISSUE SPECIFICITY: Expressed in fetal brain, lung, liver and kidney.
CC Widely expressed in adult tissues. {ECO:0000269|PubMed:10072438}.
CC -!- SIMILARITY: Belongs to the TSSC4 family. {ECO:0000305}.
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DR EMBL; AF125568; AAD23579.1; -; mRNA.
DR EMBL; AC124057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006091; AAH06091.1; -; mRNA.
DR EMBL; BC050616; AAH50616.1; -; mRNA.
DR CCDS; CCDS73241.1; -. [Q9Y5U2-2]
DR CCDS; CCDS7735.1; -. [Q9Y5U2-1]
DR RefSeq; NP_001284587.1; NM_001297658.1. [Q9Y5U2-1]
DR RefSeq; NP_001284588.1; NM_001297659.1. [Q9Y5U2-1]
DR RefSeq; NP_001284589.1; NM_001297660.1. [Q9Y5U2-1]
DR RefSeq; NP_001284590.1; NM_001297661.1. [Q9Y5U2-2]
DR RefSeq; NP_005697.2; NM_005706.3. [Q9Y5U2-1]
DR RefSeq; XP_006718181.1; XM_006718118.2. [Q9Y5U2-1]
DR RefSeq; XP_011518132.1; XM_011519830.2. [Q9Y5U2-1]
DR PDB; 7PX3; EM; 3.05 A; T=1-329.
DR PDBsum; 7PX3; -.
DR AlphaFoldDB; Q9Y5U2; -.
DR SMR; Q9Y5U2; -.
DR BioGRID; 115388; 112.
DR IntAct; Q9Y5U2; 70.
DR MINT; Q9Y5U2; -.
DR STRING; 9606.ENSP00000331087; -.
DR iPTMnet; Q9Y5U2; -.
DR PhosphoSitePlus; Q9Y5U2; -.
DR BioMuta; TSSC4; -.
DR DMDM; 296453006; -.
DR EPD; Q9Y5U2; -.
DR jPOST; Q9Y5U2; -.
DR MassIVE; Q9Y5U2; -.
DR MaxQB; Q9Y5U2; -.
DR PaxDb; Q9Y5U2; -.
DR PeptideAtlas; Q9Y5U2; -.
DR PRIDE; Q9Y5U2; -.
DR ProteomicsDB; 86505; -. [Q9Y5U2-1]
DR ProteomicsDB; 86506; -. [Q9Y5U2-2]
DR Antibodypedia; 42107; 75 antibodies from 18 providers.
DR DNASU; 10078; -.
DR Ensembl; ENST00000333256.11; ENSP00000331087.6; ENSG00000184281.15. [Q9Y5U2-1]
DR Ensembl; ENST00000380996.9; ENSP00000370384.5; ENSG00000184281.15. [Q9Y5U2-2]
DR Ensembl; ENST00000451491.2; ENSP00000411224.2; ENSG00000184281.15. [Q9Y5U2-1]
DR GeneID; 10078; -.
DR KEGG; hsa:10078; -.
DR MANE-Select; ENST00000333256.11; ENSP00000331087.6; NM_005706.4; NP_005697.2.
DR UCSC; uc001lwi.4; human. [Q9Y5U2-1]
DR CTD; 10078; -.
DR DisGeNET; 10078; -.
DR GeneCards; TSSC4; -.
DR HGNC; HGNC:12386; TSSC4.
DR HPA; ENSG00000184281; Low tissue specificity.
DR MIM; 603852; gene.
DR neXtProt; NX_Q9Y5U2; -.
DR OpenTargets; ENSG00000184281; -.
DR PharmGKB; PA37054; -.
DR VEuPathDB; HostDB:ENSG00000184281; -.
DR eggNOG; ENOG502S07M; Eukaryota.
DR GeneTree; ENSGT00390000011846; -.
DR HOGENOM; CLU_077569_0_0_1; -.
DR InParanoid; Q9Y5U2; -.
DR OMA; HFRNKGS; -.
DR OrthoDB; 1538986at2759; -.
DR PhylomeDB; Q9Y5U2; -.
DR TreeFam; TF335741; -.
DR PathwayCommons; Q9Y5U2; -.
DR SignaLink; Q9Y5U2; -.
DR BioGRID-ORCS; 10078; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; TSSC4; human.
DR GenomeRNAi; 10078; -.
DR Pharos; Q9Y5U2; Tdark.
DR PRO; PR:Q9Y5U2; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y5U2; protein.
DR Bgee; ENSG00000184281; Expressed in left testis and 153 other tissues.
DR ExpressionAtlas; Q9Y5U2; baseline and differential.
DR Genevisible; Q9Y5U2; HS.
DR InterPro; IPR029338; TSSC4.
DR PANTHER; PTHR13445; PTHR13445; 1.
DR Pfam; PF15264; TSSC4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..329
FT /note="Protein TSSC4"
FT /id="PRO_0000076360"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHE7"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHE7"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 217
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 8..71
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016561"
FT VARIANT 17
FT /note="H -> P (in dbSNP:rs2234278)"
FT /id="VAR_057826"
FT VARIANT 124
FT /note="R -> Q (in dbSNP:rs1008265)"
FT /id="VAR_060194"
FT VARIANT 230
FT /note="R -> S (in dbSNP:rs2234280)"
FT /id="VAR_057827"
FT VARIANT 262
FT /note="G -> R (in dbSNP:rs2234281)"
FT /id="VAR_057828"
FT VARIANT 274
FT /note="H -> P (in dbSNP:rs2234283)"
FT /evidence="ECO:0000269|PubMed:10072438,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_063128"
FT CONFLICT 72
FT /note="L -> F (in Ref. 1; AAD23579)"
FT /evidence="ECO:0000305"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:7PX3"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:7PX3"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:7PX3"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:7PX3"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:7PX3"
SQ 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
