SSXT_PONAB
ID SSXT_PONAB Reviewed; 418 AA.
AC Q5RFQ1; Q5R5S5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Protein SSXT;
GN Name=SS18;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. 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. {ECO:0000250|UniProtKB:Q15532}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15532}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RFQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RFQ1-2; Sequence=VSP_035802;
CC -!- SIMILARITY: Belongs to the SS18 family. {ECO:0000305}.
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DR EMBL; CR857101; CAH89406.1; -; mRNA.
DR EMBL; CR860781; CAH92891.1; -; mRNA.
DR RefSeq; NP_001126694.1; NM_001133222.1. [Q5RFQ1-2]
DR RefSeq; NP_001128735.1; NM_001135263.1.
DR AlphaFoldDB; Q5RFQ1; -.
DR SMR; Q5RFQ1; -.
DR STRING; 9601.ENSPPYP00000010187; -.
DR Ensembl; ENSPPYT00000010592; ENSPPYP00000010188; ENSPPYG00000009075. [Q5RFQ1-1]
DR GeneID; 100173694; -.
DR GeneID; 100189625; -.
DR KEGG; pon:100189625; -.
DR CTD; 6760; -.
DR eggNOG; KOG3227; Eukaryota.
DR GeneTree; ENSGT00940000156352; -.
DR HOGENOM; CLU_054580_1_0_1; -.
DR InParanoid; Q5RFQ1; -.
DR OrthoDB; 1442230at2759; -.
DR Proteomes; UP000001595; Chromosome 18.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR InterPro; IPR044779; SS18.
DR InterPro; IPR007726; SS18_N.
DR PANTHER; PTHR23107; PTHR23107; 1.
DR Pfam; PF05030; SSXT; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Alternative splicing; Nucleus; Reference proteome;
KW Repeat; Transcription; 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_0000354680"
FT REPEAT 344..356
FT /note="1"
FT REPEAT 357..369
FT /note="2"
FT REGION 76..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..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 199..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 VAR_SEQ 1..23
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_035802"
FT CONFLICT 147
FT /note="N -> D (in Ref. 1; CAH89406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 418 AA; 45956 MW; 665F8824222A08C1 CRC64;
MSVAFAAPRQ RGKGEITPAA IQKMLDDNNH LIQCIMDSQN KGKTSECSQY QQMLHTNLVY
LATIADSNQN MQSLLPAPPT QNMPMGPGGM NQSGPPPPPR SHNMPSDGMV GGGPPAPHMQ
NQMNGQMPGP NHMPMQGPGP NQLNMTNSSM NMPSSSHGSM GGYNHSVPSS QSMPVQNQMT
MSQGQPMGNY GPRPNMNMQP NQGPMMHQQP PSQQYNMPQG GGQHYQGQQP PMGMMGQVNQ
GNHMMGQRQI PPYRPPQQGP PQQYSGQEDY YGDQYSHGGQ GPPEGMNQQY YPDGHNDYGY
QQPSYPEQGY DRPYEDSSQH YYEGGNSQYG QQQDAYQGPP PQQGYPPQQQ QYPGQQGYPG
QQQGYGPSQG GPGPQYPNYP QGQGQQYGGY RPTQPGPPQP PQQRPYGYDQ GQYGNYQQ
