SSX1_HUMAN
ID SSX1_HUMAN Reviewed; 188 AA.
AC Q16384; A3KN76; Q08AJ2; Q5JQ64;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein SSX1;
DE AltName: Full=Cancer/testis antigen 5.1;
DE Short=CT5.1;
DE AltName: Full=Synovial sarcoma, X breakpoint 1;
GN Name=SSX1;
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], AND CHROMOSOMAL TRANSLOCATION WITH SS18.
RC TISSUE=Fibrosarcoma;
RX PubMed=7539744; DOI=10.1002/j.1460-2075.1995.tb07228.x;
RA Crew A.J., Clark J., Fisher C., Gill S., Grimer R., Chand A., Shipley J.,
RA Gusterson B.A., Cooper C.S.;
RT "Fusion of SYT to two genes, SSX1 and SSX2, encoding proteins with homology
RT to the Kruppel-associated box in human synovial sarcoma.";
RL EMBO J. 14:2333-2340(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Skin;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 111-188.
RC TISSUE=Synovial sarcoma;
RX PubMed=7655467; DOI=10.1093/hmg/4.6.1097;
RA de Leeuw B., Balemans M., Olde Weghuis D., Geurts van Kessel A.;
RT "Identification of two alternative fusion genes, SYT-SSX1 and SYT-SSX2, in
RT t(X;18)(p11.2;q11.2)-positive synovial sarcomas.";
RL Hum. Mol. Genet. 4:1097-1099(1995).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Could act as a modulator of transcription.
CC -!- INTERACTION:
CC Q16384; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-10237585, EBI-5278764;
CC Q16384; Q9UBF1: MAGEC2; NbExp=3; IntAct=EBI-10237585, EBI-5651487;
CC Q16384; Q8N3F0: MTURN; NbExp=3; IntAct=EBI-10237585, EBI-11980301;
CC -!- TISSUE SPECIFICITY: Expressed at high level in the testis. Expressed at
CC low level in thyroid. Not detected in tonsil, colon, lung, spleen,
CC prostate, kidney, striated and smooth muscles. Detected in
CC rhabdomyosarcoma and fibrosarcoma cell lines. Not detected in
CC mesenchymal and epithelial cell lines.
CC -!- DISEASE: Note=A chromosomal aberration involving SSX1 may be a cause of
CC synovial sarcoma. Translocation t(X;18)(p11.2;q11.2). The translocation
CC is specifically found in more than 80% of synovial sarcoma. The fusion
CC products SSXT-SSX1 or SSXT-SSX2 are probably responsible for
CC transforming activity. Heterogeneity in the position of the breakpoint
CC can occur (low frequency). {ECO:0000269|PubMed:7539744}.
CC -!- SIMILARITY: Belongs to the SSX family. {ECO:0000305}.
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DR EMBL; X86174; CAA60110.1; -; mRNA.
DR EMBL; AL683817; CAI41141.1; -; Genomic_DNA.
DR EMBL; BC001003; AAH01003.1; -; mRNA.
DR EMBL; BC125151; AAI25152.1; -; mRNA.
DR EMBL; BC128611; AAI28612.1; -; mRNA.
DR EMBL; BC133693; AAI33694.1; -; mRNA.
DR EMBL; BC150487; AAI50488.1; -; mRNA.
DR EMBL; S79325; AAB35378.1; -; mRNA.
DR CCDS; CCDS14290.1; -.
DR PIR; S55057; S55057.
DR RefSeq; NP_001265620.1; NM_001278691.1.
DR RefSeq; NP_005626.1; NM_005635.3.
DR AlphaFoldDB; Q16384; -.
DR BioGRID; 112634; 11.
DR IntAct; Q16384; 5.
DR STRING; 9606.ENSP00000366118; -.
DR iPTMnet; Q16384; -.
DR PhosphoSitePlus; Q16384; -.
DR BioMuta; SSX1; -.
DR DMDM; 3915027; -.
DR MassIVE; Q16384; -.
DR PaxDb; Q16384; -.
DR PeptideAtlas; Q16384; -.
DR PRIDE; Q16384; -.
DR ProteomicsDB; 60866; -.
DR Antibodypedia; 25598; 227 antibodies from 22 providers.
DR DNASU; 6756; -.
DR Ensembl; ENST00000376919.4; ENSP00000366118.3; ENSG00000126752.8.
DR GeneID; 6756; -.
DR KEGG; hsa:6756; -.
DR MANE-Select; ENST00000376919.4; ENSP00000366118.3; NM_005635.4; NP_005626.1.
DR UCSC; uc004djb.2; human.
DR CTD; 6756; -.
DR DisGeNET; 6756; -.
DR GeneCards; SSX1; -.
DR HGNC; HGNC:11335; SSX1.
DR HPA; ENSG00000126752; Tissue enriched (testis).
DR MalaCards; SSX1; -.
DR MIM; 312820; gene+phenotype.
DR neXtProt; NX_Q16384; -.
DR OpenTargets; ENSG00000126752; -.
DR Orphanet; 3273; Synovial sarcoma.
DR PharmGKB; PA36159; -.
DR VEuPathDB; HostDB:ENSG00000126752; -.
DR eggNOG; ENOG502RU1A; Eukaryota.
DR GeneTree; ENSGT00390000012484; -.
DR HOGENOM; CLU_097196_1_0_1; -.
DR InParanoid; Q16384; -.
DR OMA; CPPGNAN; -.
DR OrthoDB; 1270676at2759; -.
DR PhylomeDB; Q16384; -.
DR TreeFam; TF338517; -.
DR PathwayCommons; Q16384; -.
DR SignaLink; Q16384; -.
DR BioGRID-ORCS; 6756; 48 hits in 635 CRISPR screens.
DR ChiTaRS; SSX1; human.
DR GeneWiki; SSX1; -.
DR GenomeRNAi; 6756; -.
DR Pharos; Q16384; Tbio.
DR PRO; PR:Q16384; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q16384; protein.
DR Bgee; ENSG00000126752; Expressed in buccal mucosa cell and 40 other tissues.
DR Genevisible; Q16384; HS.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR InterPro; IPR003655; aKRAB.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR028804; SSX.
DR InterPro; IPR019041; SSXRD_motif.
DR PANTHER; PTHR14112; PTHR14112; 1.
DR Pfam; PF09514; SSXRD; 1.
DR SMART; SM00349; KRAB; 1.
DR SUPFAM; SSF109640; SSF109640; 1.
DR PROSITE; PS50806; KRAB_RELATED; 1.
PE 1: Evidence at protein level;
KW Chromosomal rearrangement; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..188
FT /note="Protein SSX1"
FT /id="PRO_0000181828"
FT DOMAIN 20..83
FT /note="KRAB-related"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00120"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 62..63
FT /note="Breakpoint for translocation to form the SSXT-SSX1
FT fusion protein (rare)"
FT /evidence="ECO:0000269|PubMed:7539744"
FT SITE 110..111
FT /note="Breakpoint for translocation to form the SSXT-SSX1
FT fusion protein"
FT /evidence="ECO:0000269|PubMed:7539744"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
SQ SEQUENCE 188 AA; 21931 MW; E440D1B2AE3AE9F7 CRC64;
MNGDDTFAKR PRDDAKASEK RSKAFDDIAT YFSKKEWKKM KYSEKISYVY MKRNYKAMTK
LGFKVTLPPF MCNKQATDFQ GNDFDNDHNR RIQVEHPQMT FGRLHRIIPK IMPKKPAEDE
NDSKGVSEAS GPQNDGKQLH PPGKANISEK INKRSGPKRG KHAWTHRLRE RKQLVIYEEI
SDPEEDDE
