SSXT_MOUSE
ID SSXT_MOUSE Reviewed; 418 AA.
AC Q62280; Q3TM96;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein SSXT;
DE AltName: Full=Protein SYT;
DE AltName: Full=Synovial sarcoma-associated Ss18-alpha;
GN Name=Ss18; Synonyms=Ssxt, Syt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129; TISSUE=Fetal brain;
RX PubMed=8760306;
RA de Bruijn D.R.H., Baats E., Zechner U., de Leeuw B., Balemans M.,
RA Olde Weghuis D., Hirning-Folz U., Geurts van Kessel A.G.;
RT "Isolation and characterization of the mouse homolog of SYT, a gene
RT implicated in the development of human synovial sarcomas.";
RL Oncogene 13:643-648(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=11435705; DOI=10.1159/000056920;
RA de Bruijn D.R., Kater-Baats E., Eleveld M., Merkx G., Geurts Van Kessel A.;
RT "Mapping and characterization of the mouse and human SS18 genes, two human
RT SS18-like genes and a mouse Ss18 pseudogene.";
RL Cytogenet. Cell Genet. 92:310-319(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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. Component of SWI/SNF chromatin remodeling
CC subcomplex GBAF that carries out key enzymatic activities, changing
CC chromatin structure by altering DNA-histone contacts within a
CC nucleosome in an ATP-dependent manner. {ECO:0000250|UniProtKB:Q15532}.
CC -!- SUBUNIT: Interacts with MLLT10 (By similarity). 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:0000250|UniProtKB:Q15532, ECO:0000269|PubMed:29374058}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15532}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in early embryogenesis
CC (12.5 days). In later stages (14.5 days), the expression is restricted
CC to cartilage forming cells, to specific neuronal cells and some
CC epithelial derived tissues. In adults, SSXT is expressed in heart,
CC kidney, testis and also in muscle, brain and liver. In mature testis,
CC expression is specifically observed in primary spermatocytes.
CC -!- SIMILARITY: Belongs to the SS18 family. {ECO:0000305}.
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DR EMBL; X93357; CAA63733.1; -; mRNA.
DR EMBL; AY055726; AAL17746.1; -; Genomic_DNA.
DR EMBL; AK166053; BAE38546.1; -; mRNA.
DR CCDS; CCDS29070.1; -.
DR RefSeq; NP_033306.2; NM_009280.2.
DR AlphaFoldDB; Q62280; -.
DR SMR; Q62280; -.
DR BioGRID; 234592; 4.
DR ComplexPortal; CPX-4202; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4204; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4221; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4222; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4227; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4228; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4229; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4230; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR DIP; DIP-60230N; -.
DR IntAct; Q62280; 4.
DR MINT; Q62280; -.
DR STRING; 10090.ENSMUSP00000046320; -.
DR iPTMnet; Q62280; -.
DR PhosphoSitePlus; Q62280; -.
DR MaxQB; Q62280; -.
DR PaxDb; Q62280; -.
DR PeptideAtlas; Q62280; -.
DR PRIDE; Q62280; -.
DR ProteomicsDB; 257424; -.
DR Antibodypedia; 22102; 170 antibodies from 29 providers.
DR DNASU; 268996; -.
DR Ensembl; ENSMUST00000040924; ENSMUSP00000046320; ENSMUSG00000037013.
DR GeneID; 268996; -.
DR KEGG; mmu:268996; -.
DR UCSC; uc008ede.1; mouse.
DR CTD; 6760; -.
DR MGI; MGI:107708; Ss18.
DR VEuPathDB; HostDB:ENSMUSG00000037013; -.
DR eggNOG; KOG3227; Eukaryota.
DR GeneTree; ENSGT00940000156352; -.
DR InParanoid; Q62280; -.
DR OMA; MLDENAH; -.
DR OrthoDB; 1442230at2759; -.
DR PhylomeDB; Q62280; -.
DR TreeFam; TF330999; -.
DR BioGRID-ORCS; 268996; 9 hits in 75 CRISPR screens.
DR ChiTaRS; Ss18; mouse.
DR PRO; PR:Q62280; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q62280; protein.
DR Bgee; ENSMUSG00000037013; Expressed in animal zygote and 180 other tissues.
DR ExpressionAtlas; Q62280; baseline and differential.
DR Genevisible; Q62280; MM.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0071564; C:npBAF complex; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IDA:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:MGI.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:MGI.
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; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:MGI.
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; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15532"
FT CHAIN 2..418
FT /note="Protein SSXT"
FT /id="PRO_0000181824"
FT REPEAT 344..356
FT /note="1"
FT REPEAT 357..369
FT /note="2"
FT REGION 77..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..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 193..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q15532"
FT CONFLICT 156
FT /note="S -> N (in Ref. 1; CAA63733 and 2; AAL17746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 45864 MW; FE2BE95EA7396888 CRC64;
MSVAFAAPRQ RGKGEITPAA IQKMLDENNH LIQCIMDYQN KGKASECSQY QQILHTNLVY
LATIADSNQN MQSLLPAPPT QTMPMGPGGM SQSGPPPPPR SHNMPSDGMV GGGPPAPHMQ
NQMNGQMPGP NHMPMQGPGP SQLSMTNSSM NMPSSSHGSM GGYNHSVPSS QSMPVQNQMT
MSQGQPMGNY GPRPNMNMQP NQGPMMHQQP PSQQYNMPPG GAQHYQGQQA PMGLMGQVNQ
GSHMMGQRQM PPYRPPQQGP PQQYSGQEDY YGDQYSHGGQ GPPEGMNQQY YPDGHNDYGY
QQPSYPEQGY DRPYEDSSQH YYEGGNSQYG QQQDAYQGPP PQQGYPPQQQ QYPGQQGYPG
QQQSYGPSQG GPGPQYPNYP QGQGQQYGGY RPTQPGPPQP PQQRPYGYDQ GQYGNYQQ
