SSXT_HUMAN
ID SSXT_HUMAN Reviewed; 418 AA.
AC Q15532; B0YJ95; Q16404; Q4VAX1; Q9BXC6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Protein SSXT;
DE AltName: Full=Protein SYT;
DE AltName: Full=Synovial sarcoma translocated to X chromosome protein;
GN Name=SS18; Synonyms=SSXT, SYT;
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 2), AND SSXT-SSX2 FUSION PROTEIN.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11368913; DOI=10.1016/s0378-1119(01)00412-7;
RA Brodin B., Haslam K., Yang K., Bartolazzi A., Xie Y., Starborg M.,
RA Lundeberg J., Larsson O.;
RT "Cloning and characterization of spliced fusion transcript variants of
RT synovial sarcoma: SYT/SSX4, SYT/SSX4v, and SYT/SSX2v. Possible regulatory
RT role of the fusion gene product in wild type SYT expression.";
RL Gene 268:173-182(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 405-410 (SSXT-SSX2 FUSION PROTEIN), AND
RP CHROMOSOMAL TRANSLOCATION WITH SSX2.
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 CHROMOSOMAL TRANSLOCATION WITH SSX1, AND CHROMOSOMAL TRANSLOCATION WITH
RP SSX2.
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 [8]
RP INTERACTION WITH MLLT10.
RX PubMed=11423977; DOI=10.1038/sj.onc.1204419;
RA de Bruijn D.R., dos Santos N.R., Thijssen J., Balemans M., Debernardi S.,
RA Linder B., Young B.D., Geurts van Kessel A.;
RT "The synovial sarcoma associated protein SYT interacts with the acute
RT leukemia associated protein AF10.";
RL Oncogene 20:3281-3289(2001).
RN [9]
RP FUNCTION, ALTERNATIVE SPLICING, AND INTERACTION WITH RBM14.
RX PubMed=15919756; DOI=10.1210/en.2004-1513;
RA Iwasaki T., Koibuchi N., Chin W.W.;
RT "Synovial sarcoma translocation (SYT) encodes a nuclear receptor
RT coactivator.";
RL Endocrinology 146:3892-3899(2005).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE GBAF COMPLEX.
RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065;
RA Alpsoy A., Dykhuizen E.C.;
RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog
RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
RL J. Biol. Chem. 293:3892-3903(2018).
CC -!- FUNCTION: Appears to function synergistically with RBM14 as a
CC transcriptional coactivator. Isoform 1 and isoform 2 function in
CC nuclear receptor coactivation. Isoform 1 and isoform 2 function in
CC general transcriptional coactivation. Component of SWI/SNF chromatin
CC remodeling subcomplex GBAF that carries out key enzymatic activities,
CC changing chromatin structure by altering DNA-histone contacts within a
CC nucleosome in an ATP-dependent manner (PubMed:29374058).
CC {ECO:0000269|PubMed:15919756, ECO:0000269|PubMed:29374058}.
CC -!- SUBUNIT: Interacts with MLLT10. Isoform 1 interacts with RBM14 isoform
CC 1. Isoform 2 interacts with RBM14 isoform 1. Component of the
CC multiprotein chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF),
CC SWI/SNF-B (PBAF) and related complexes. The canonical complex contains
CC a catalytic subunit (either SMARCA4/BRG1/BAF190A or
CC SMARCA2/BRM/BAF190B) and at least SMARCE1, ACTL6A/BAF53,
CC SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. Other subunits
CC specific to each of the complexes may also be present permitting
CC several possible combinations developmentally and tissue specific.
CC Component of the SWI/SNF (GBAF) subcomplex, which includes at least
CC BICRA or BICRAL (mutually exclusive), BRD9, SS18, the core BAF
CC subunits, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53,
CC SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058).
CC {ECO:0000269|PubMed:11423977, ECO:0000269|PubMed:15919756,
CC ECO:0000269|PubMed:29374058}.
CC -!- INTERACTION:
CC Q15532; P15336: ATF2; NbExp=2; IntAct=EBI-2560599, EBI-1170906;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SYTins, SYT-L;
CC IsoId=Q15532-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15532-2; Sequence=VSP_006258;
CC -!- TISSUE SPECIFICITY: Fairly ubiquitously expressed. Expressed in
CC synovial sarcomas and in other human cell lines. The fusion genes SSXT-
CC SSX1 and SSXT-SSX2 are expressed only in synovial sarcomas.
CC -!- DISEASE: Note=A chromosomal aberration involving SS18 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:7495284,
CC ECO:0000269|PubMed:7539744}.
CC -!- SIMILARITY: Belongs to the SS18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK21314.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA55792.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SS18ID84ch18q11.html";
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DR EMBL; X79201; CAA55792.1; ALT_INIT; mRNA.
DR EMBL; X79200; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF343880; AAK21314.1; ALT_INIT; mRNA.
DR EMBL; EF445031; ACA06073.1; -; Genomic_DNA.
DR EMBL; CH471088; EAX01210.1; -; Genomic_DNA.
DR EMBL; BC096223; AAH96223.1; -; mRNA.
DR EMBL; S79894; AAB35674.1; ALT_TERM; mRNA.
DR CCDS; CCDS32807.1; -. [Q15532-1]
DR CCDS; CCDS54183.1; -. [Q15532-2]
DR PIR; S46269; S46269.
DR RefSeq; NP_001007560.1; NM_001007559.2. [Q15532-1]
DR RefSeq; NP_001295130.1; NM_001308201.1.
DR RefSeq; NP_005628.2; NM_005637.3. [Q15532-2]
DR AlphaFoldDB; Q15532; -.
DR SMR; Q15532; -.
DR BioGRID; 112638; 82.
DR ComplexPortal; CPX-4084; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4203; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4206; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4207; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4223; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4224; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4225; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4226; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR IntAct; Q15532; 62.
DR MINT; Q15532; -.
DR STRING; 9606.ENSP00000414516; -.
DR iPTMnet; Q15532; -.
DR PhosphoSitePlus; Q15532; -.
DR BioMuta; SS18; -.
DR EPD; Q15532; -.
DR jPOST; Q15532; -.
DR MassIVE; Q15532; -.
DR MaxQB; Q15532; -.
DR PaxDb; Q15532; -.
DR PeptideAtlas; Q15532; -.
DR PRIDE; Q15532; -.
DR ProteomicsDB; 60621; -. [Q15532-1]
DR ProteomicsDB; 60622; -. [Q15532-2]
DR Antibodypedia; 22102; 170 antibodies from 29 providers.
DR DNASU; 6760; -.
DR Ensembl; ENST00000269137.11; ENSP00000269137.7; ENSG00000141380.14. [Q15532-2]
DR Ensembl; ENST00000415083.7; ENSP00000414516.2; ENSG00000141380.14. [Q15532-1]
DR GeneID; 6760; -.
DR KEGG; hsa:6760; -.
DR MANE-Select; ENST00000415083.7; ENSP00000414516.2; NM_001007559.3; NP_001007560.1.
DR UCSC; uc002kvm.4; human. [Q15532-1]
DR CTD; 6760; -.
DR DisGeNET; 6760; -.
DR GeneCards; SS18; -.
DR HGNC; HGNC:11340; SS18.
DR HPA; ENSG00000141380; Low tissue specificity.
DR MalaCards; SS18; -.
DR MIM; 600192; gene.
DR neXtProt; NX_Q15532; -.
DR OpenTargets; ENSG00000141380; -.
DR Orphanet; 3273; Synovial sarcoma.
DR PharmGKB; PA36164; -.
DR VEuPathDB; HostDB:ENSG00000141380; -.
DR eggNOG; KOG3227; Eukaryota.
DR GeneTree; ENSGT00940000156352; -.
DR InParanoid; Q15532; -.
DR OMA; MLDENAH; -.
DR OrthoDB; 715844at2759; -.
DR PhylomeDB; Q15532; -.
DR TreeFam; TF330999; -.
DR PathwayCommons; Q15532; -.
DR SignaLink; Q15532; -.
DR SIGNOR; Q15532; -.
DR BioGRID-ORCS; 6760; 27 hits in 1094 CRISPR screens.
DR ChiTaRS; SS18; human.
DR GeneWiki; SS18; -.
DR GenomeRNAi; 6760; -.
DR Pharos; Q15532; Tbio.
DR PRO; PR:Q15532; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q15532; protein.
DR Bgee; ENSG00000141380; Expressed in adrenal tissue and 203 other tissues.
DR ExpressionAtlas; Q15532; baseline and differential.
DR Genevisible; Q15532; HS.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:Ensembl.
DR GO; GO:0071564; C:npBAF complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR InterPro; IPR044779; SS18.
DR InterPro; IPR007726; SS18_N.
DR PANTHER; PTHR23107; PTHR23107; 1.
DR Pfam; PF05030; SSXT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Chromosomal rearrangement;
KW Nucleus; Proto-oncogene; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..418
FT /note="Protein SSXT"
FT /id="PRO_0000181823"
FT REPEAT 344..356
FT /note="1"
FT REPEAT 357..369
FT /note="2"
FT REGION 2..186
FT /note="Transcriptional activation"
FT REGION 77..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..369
FT /note="2 X 13 AA imperfect tandem repeats"
FT MOTIF 50..53
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 374..377
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 392..401
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 413..416
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 188..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 366..367
FT /note="Breakpoint for translocation to form the SSXT-SSX1
FT fusion protein (rare)"
FT /evidence="ECO:0000269|PubMed:7539744"
FT SITE 410..411
FT /note="Breakpoint for translocation to form the SSXT-SSX1
FT or SSXT-SSX2 fusion proteins"
FT /evidence="ECO:0000269|PubMed:7539744"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 295..325
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7951320"
FT /id="VSP_006258"
SQ SEQUENCE 418 AA; 45929 MW; 7E089D557538252F CRC64;
MSVAFAAPRQ RGKGEITPAA IQKMLDDNNH LIQCIMDSQN KGKTSECSQY QQMLHTNLVY
LATIADSNQN MQSLLPAPPT QNMPMGPGGM NQSGPPPPPR SHNMPSDGMV GGGPPAPHMQ
NQMNGQMPGP NHMPMQGPGP NQLNMTNSSM NMPSSSHGSM GGYNHSVPSS QSMPVQNQMT
MSQGQPMGNY GPRPNMSMQP NQGPMMHQQP PSQQYNMPQG GGQHYQGQQP PMGMMGQVNQ
GNHMMGQRQI PPYRPPQQGP PQQYSGQEDY YGDQYSHGGQ GPPEGMNQQY YPDGHNDYGY
QQPSYPEQGY DRPYEDSSQH YYEGGNSQYG QQQDAYQGPP PQQGYPPQQQ QYPGQQGYPG
QQQGYGPSQG GPGPQYPNYP QGQGQQYGGY RPTQPGPPQP PQQRPYGYDQ GQYGNYQQ
