SSX2_HUMAN
ID SSX2_HUMAN Reviewed; 188 AA.
AC Q16385; Q16404; Q5JS26; Q96IP7; Q9BU88;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Protein SSX2;
DE AltName: Full=Cancer/testis antigen 5.2;
DE Short=CT5.2;
DE AltName: Full=Synovial sarcoma, X breakpoint 2;
DE AltName: Full=Tumor antigen HOM-MEL-40;
GN Name=SSX2; Synonyms=SSX2A;
GN and
GN Name=SSX2B;
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), AND CHROMOSOMAL TRANSLOCATION WITH
RP SS18.
RC TISSUE=Testis;
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] (ISOFORMS 1 AND 2).
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 (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 111-188 (SSXT-SSX2 FUSION PROTEIN), AND
RP CHROMOSOMAL TRANSLOCATION WITH SS18.
RC TISSUE=Synovial sarcoma;
RX PubMed=7951320; DOI=10.1038/ng0894-502;
RA Clark J., Rocques P.J., Crew A.J., Gill S., Shipley J., Chan A.M.-L.,
RA Gusterson B.A., Cooper C.S.;
RT "Identification of novel genes, SYT and SSX, involved in the
RT t(X;18)(p11.2;q11.2) translocation found in human synovial sarcoma.";
RL Nat. Genet. 7:502-508(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 68-116 (SSXT-SSX2 FUSION PROTEIN).
RX PubMed=7495284;
RA Fligman I., Lonardo F., Jhanwar S.C., Gerald W.L., Woodruff J., Ladanyi M.;
RT "Molecular diagnosis of synovial sarcoma and characterization of a variant
RT SYT-SSX2 fusion transcript.";
RL Am. J. Pathol. 147:1592-1599(1995).
RN [7]
RP INTERACTION WITH RAB3IP AND SSX2IP.
RX PubMed=12007189; DOI=10.1002/gcc.10073;
RA de Bruijn D.R.H., dos Santos N.R., Kater-Baats E., Thijssen J.,
RA van den Berk L., Stap J., Balemans M., Schepens M., Merkx G.,
RA van Kessel A.G.;
RT "The cancer-related protein SSX2 interacts with the human homologue of a
RT Ras-like GTPase interactor, RAB3IP, and a novel nuclear protein, SSX2IP.";
RL Genes Chromosomes Cancer 34:285-298(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-123, AND
RP IDENTIFICATION BY 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 -!- SUBUNIT: Interacts via its N-terminal region with RAB3IP and SSX2IP.
CC {ECO:0000269|PubMed:12007189}.
CC -!- INTERACTION:
CC Q16385; Q99996-2: AKAP9; NbExp=4; IntAct=EBI-2210673, EBI-9641546;
CC Q16385; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-2210673, EBI-2548012;
CC Q16385; Q6A162: KRT40; NbExp=3; IntAct=EBI-2210673, EBI-10171697;
CC Q16385; Q9UBF1: MAGEC2; NbExp=3; IntAct=EBI-2210673, EBI-5651487;
CC Q16385; Q96QF0: RAB3IP; NbExp=4; IntAct=EBI-2210673, EBI-747844;
CC Q16385; Q96QF0-2: RAB3IP; NbExp=4; IntAct=EBI-2210673, EBI-747865;
CC Q16385; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2210673, EBI-5235340;
CC Q16385; Q9Y2D8: SSX2IP; NbExp=8; IntAct=EBI-2210673, EBI-2212028;
CC Q16385; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-2210673, EBI-6872807;
CC Q16385; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-2210673, EBI-529518;
CC Q16385; O96006: ZBED1; NbExp=3; IntAct=EBI-2210673, EBI-740037;
CC Q16385; Q8NF64-2: ZMIZ2; NbExp=3; IntAct=EBI-2210673, EBI-10182121;
CC Q16385-2; Q96Q35-2: FLACC1; NbExp=3; IntAct=EBI-17564583, EBI-11533409;
CC Q16385-2; Q8IY81: FTSJ3; NbExp=3; IntAct=EBI-17564583, EBI-744088;
CC Q16385-2; Q96CN5: LRRC45; NbExp=3; IntAct=EBI-17564583, EBI-2805176;
CC Q16385-2; Q53GA4: PHLDA2; NbExp=3; IntAct=EBI-17564583, EBI-4402464;
CC Q16385-2; Q9Y5L0: TNPO3; NbExp=3; IntAct=EBI-17564583, EBI-1042571;
CC Q16385-2; Q9UL33-2: TRAPPC2L; NbExp=3; IntAct=EBI-17564583, EBI-11119202;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16385-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16385-2; Sequence=VSP_017595;
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 SSX2 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 ECO:0000269|PubMed:7951320}.
CC -!- SIMILARITY: Belongs to the SSX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB35674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SSX2ID42406chXp11.html";
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DR EMBL; X86175; CAA60111.1; -; mRNA.
DR EMBL; AL445236; CAI41623.1; -; Genomic_DNA.
DR EMBL; AL450023; CAI41623.1; JOINED; Genomic_DNA.
DR EMBL; AL445236; CAI41624.1; -; Genomic_DNA.
DR EMBL; AL450023; CAI41624.1; JOINED; Genomic_DNA.
DR EMBL; BC002818; AAH02818.1; -; mRNA.
DR EMBL; BC007343; AAH07343.1; -; mRNA.
DR EMBL; BC016957; AAH16957.1; -; mRNA.
DR EMBL; BC069313; AAH69313.1; -; mRNA.
DR EMBL; BC071827; AAH71827.1; -; mRNA.
DR EMBL; BC103863; AAI03864.1; -; mRNA.
DR EMBL; S79332; AAB35379.1; -; mRNA.
DR EMBL; X79200; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; S79894; AAB35674.1; ALT_INIT; mRNA.
DR CCDS; CCDS14344.2; -. [Q16385-1]
DR CCDS; CCDS14345.2; -. [Q16385-2]
DR CCDS; CCDS48129.1; -. [Q16385-1]
DR CCDS; CCDS65267.1; -. [Q16385-2]
DR PIR; S55058; S55058.
DR RefSeq; NP_001157889.1; NM_001164417.2. [Q16385-1]
DR RefSeq; NP_001265626.1; NM_001278697.1.
DR RefSeq; NP_001265630.1; NM_001278701.1. [Q16385-2]
DR RefSeq; NP_001265631.1; NM_001278702.1.
DR RefSeq; NP_003138.3; NM_003147.5. [Q16385-2]
DR RefSeq; NP_783629.1; NM_175698.2. [Q16385-1]
DR AlphaFoldDB; Q16385; -.
DR BioGRID; 112635; 43.
DR BioGRID; 608281; 9.
DR IntAct; Q16385; 30.
DR iPTMnet; Q16385; -.
DR PhosphoSitePlus; Q16385; -.
DR BioMuta; SSX2; -.
DR DMDM; 3915028; -.
DR MassIVE; Q16385; -.
DR MaxQB; Q16385; -.
DR PaxDb; Q16385; -.
DR PeptideAtlas; Q16385; -.
DR PRIDE; Q16385; -.
DR ProteomicsDB; 60867; -. [Q16385-1]
DR ProteomicsDB; 60868; -. [Q16385-2]
DR Antibodypedia; 43485; 279 antibodies from 22 providers.
DR Antibodypedia; 73920; 15 antibodies from 6 providers.
DR DNASU; 6757; -.
DR Ensembl; ENST00000336777.9; ENSP00000338796.5; ENSG00000241476.9. [Q16385-2]
DR Ensembl; ENST00000337502.6; ENSP00000338561.5; ENSG00000241476.9. [Q16385-1]
DR Ensembl; ENST00000596480.6; ENSP00000470740.2; ENSG00000268447.6. [Q16385-1]
DR Ensembl; ENST00000612490.1; ENSP00000477922.1; ENSG00000268447.6. [Q16385-2]
DR Ensembl; ENST00000616191.4; ENSP00000478714.1; ENSG00000268447.6. [Q16385-1]
DR GeneID; 6757; -.
DR GeneID; 727837; -.
DR KEGG; hsa:6757; -.
DR KEGG; hsa:727837; -.
DR MANE-Select; ENST00000337502.6; ENSP00000338561.5; NM_175698.4; NP_783629.1.
DR MANE-Select; ENST00000596480.6; ENSP00000470740.2; NM_001164417.3; NP_001157889.1.
DR UCSC; uc004dqy.3; human. [Q16385-1]
DR CTD; 6757; -.
DR CTD; 727837; -.
DR DisGeNET; 6757; -.
DR DisGeNET; 727837; -.
DR GeneCards; SSX2; -.
DR GeneCards; SSX2B; -.
DR HGNC; HGNC:11336; SSX2.
DR HGNC; HGNC:22263; SSX2B.
DR HPA; ENSG00000241476; Tissue enriched (testis).
DR HPA; ENSG00000268447; Tissue enriched (testis).
DR MalaCards; SSX2; -.
DR MIM; 300192; gene.
DR neXtProt; NX_Q16385; -.
DR OpenTargets; ENSG00000241476; -.
DR Orphanet; 3273; Synovial sarcoma.
DR PharmGKB; PA162404839; -.
DR VEuPathDB; HostDB:ENSG00000241476; -.
DR VEuPathDB; HostDB:ENSG00000268447; -.
DR GeneTree; ENSGT00390000012484; -.
DR HOGENOM; CLU_097196_0_0_1; -.
DR InParanoid; Q16385; -.
DR OMA; FMCPKKR; -.
DR OrthoDB; 1270676at2759; -.
DR PhylomeDB; Q16385; -.
DR TreeFam; TF338517; -.
DR PathwayCommons; Q16385; -.
DR SignaLink; Q16385; -.
DR BioGRID-ORCS; 6757; 193 hits in 580 CRISPR screens.
DR BioGRID-ORCS; 727837; 5 hits in 246 CRISPR screens.
DR ChiTaRS; SSX2; human.
DR ChiTaRS; SSX2B; human.
DR GeneWiki; SSX2; -.
DR Pharos; Q16385; Tbio.
DR PRO; PR:Q16385; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q16385; protein.
DR Bgee; ENSG00000241476; Expressed in right testis and 10 other tissues.
DR Genevisible; Q16385; HS.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR CDD; cd07765; KRAB_A-box; 1.
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; PF01352; KRAB; 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 Alternative splicing; Chromosomal rearrangement; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..188
FT /note="Protein SSX2"
FT /id="PRO_0000181829"
FT DOMAIN 20..83
FT /note="KRAB-related"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00120"
FT REGION 1..80
FT /note="Interaction with SSX2IP"
FT /evidence="ECO:0000269|PubMed:12007189"
FT REGION 25..80
FT /note="Interaction with RAB3IP"
FT /evidence="ECO:0000269|PubMed:12007189"
FT REGION 76..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 68..69
FT /note="Breakpoint for translocation to form the SSXT-SSX2
FT fusion protein (rare)"
FT SITE 110..111
FT /note="Breakpoint for translocation to form the SSXT-SSX2
FT fusion protein"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 157..188
FT /note="PKRGEHAWTHRLRERKQLVIYEEISDPEEDDE -> NREAQEKEERRGTAHR
FT WSSQNTHNIGRFSLSTSMGAVHGTPKTITHNRDPKGGNMPGPTDCVRENSW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017595"
FT CONFLICT 169
FT /note="R -> P (in Ref. 3; AAH07343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21620 MW; BF5D18AA5F45B1B1 CRC64;
MNGDDAFARR PTVGAQIPEK IQKAFDDIAK YFSKEEWEKM KASEKIFYVY MKRKYEAMTK
LGFKATLPPF MCNKRAEDFQ GNDLDNDPNR GNQVERPQMT FGRLQGISPK IMPKKPAEEG
NDSEEVPEAS GPQNDGKELC PPGKPTTSEK IHERSGPKRG EHAWTHRLRE RKQLVIYEEI
SDPEEDDE
