SSRP1_RAT
ID SSRP1_RAT Reviewed; 709 AA.
AC Q04931; Q5XIT2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=FACT complex subunit SSRP1;
DE AltName: Full=Facilitates chromatin transcription complex subunit SSRP1;
DE AltName: Full=Recombination signal sequence recognition protein 1;
DE AltName: Full=Structure-specific recognition protein 1;
DE AltName: Full=T160;
GN Name=Ssrp1; Synonyms=Ciidbp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 149-709.
RC TISSUE=Chondrosarcoma;
RX PubMed=8464746; DOI=10.1093/nar/21.6.1493;
RA Wang L., Precht P., Balakir R., Horton W.E. Jr.;
RT "Rat and chick cDNA clones encoding HMG-like proteins.";
RL Nucleic Acids Res. 21:1493-1493(1993).
RN [3]
RP INTERACTION WITH SRF.
RX PubMed=10336466; DOI=10.1074/jbc.274.22.15686;
RA Spencer J.A., Baron M.H., Olson E.N.;
RT "Cooperative transcriptional activation by serum response factor and the
RT high mobility group protein SSRP1.";
RL J. Biol. Chem. 274:15686-15693(1999).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the FACT complex, a general chromatin factor
CC that acts to reorganize nucleosomes. The FACT complex is involved in
CC multiple processes that require DNA as a template such as mRNA
CC elongation, DNA replication and DNA repair. During transcription
CC elongation the FACT complex acts as a histone chaperone that both
CC destabilizes and restores nucleosomal structure. It facilitates the
CC passage of RNA polymerase II and transcription by promoting the
CC dissociation of one histone H2A-H2B dimer from the nucleosome, then
CC subsequently promotes the reestablishment of the nucleosome following
CC the passage of RNA polymerase II. The FACT complex is probably also
CC involved in phosphorylation of 'Ser-392' of p53/TP53 via its
CC association with CK2 (casein kinase II). Binds specifically to double-
CC stranded DNA and at low levels to DNA modified by the antitumor agent
CC cisplatin. May potentiate cisplatin-induced cell death by blocking
CC replication and repair of modified DNA. Also acts as a transcriptional
CC coactivator for p63/TP63. {ECO:0000250|UniProtKB:Q08943,
CC ECO:0000250|UniProtKB:Q08945}.
CC -!- SUBUNIT: Interacts with MYOG (via C-terminal region) (By similarity).
CC Component of the FACT complex, a stable heterodimer of SSRP1 and
CC SUPT16H. Also a component of a CK2-SPT16-SSRP1 complex which forms
CC following UV irradiation, composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2
CC and CSNK2B. Binds to histone H3-H4 tetramers, but not to intact
CC nucleosomes. Identified in a centromere complex containing histones
CC H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP,
CC SUPT16H, SSRP1 and RSF1. Interacts with isoform gamma of TP63.
CC Interacts with FYTTD1/UIF (By similarity). Interacts with SRF
CC (PubMed:10336466). Interacts with NEK9 (By similarity).
CC {ECO:0000250|UniProtKB:Q08943, ECO:0000250|UniProtKB:Q08945,
CC ECO:0000269|PubMed:10336466}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q05344}.
CC Chromosome {ECO:0000250|UniProtKB:Q05344}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q05344}. Note=Colocalizes with RNA polymerase II
CC on chromatin. Recruited to actively transcribed loci.
CC {ECO:0000250|UniProtKB:Q05344}.
CC -!- PTM: Phosphorylated by CK2 following UV but not gamma irradiation.
CC Phosphorylation inhibits its DNA-binding activity (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Polyubiquitinated following caspase cleavage
CC resulting in degradation of the N-terminal ubiquitinated part of the
CC cleaved protein (By similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SSRP1 family. {ECO:0000305}.
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DR EMBL; BC083588; AAH83588.1; -; mRNA.
DR EMBL; L08814; AAA40927.1; -; mRNA.
DR PIR; S35637; S35637.
DR RefSeq; NP_112383.1; NM_031121.1.
DR RefSeq; XP_006234539.2; XM_006234477.2.
DR RefSeq; XP_008760215.2; XM_008761993.2.
DR RefSeq; XP_008760216.1; XM_008761994.1.
DR RefSeq; XP_017447548.1; XM_017592059.1.
DR RefSeq; XP_017447549.1; XM_017592060.1.
DR RefSeq; XP_017447550.1; XM_017592061.1.
DR AlphaFoldDB; Q04931; -.
DR SMR; Q04931; -.
DR BioGRID; 249657; 1.
DR STRING; 10116.ENSRNOP00000012022; -.
DR iPTMnet; Q04931; -.
DR PhosphoSitePlus; Q04931; -.
DR jPOST; Q04931; -.
DR PaxDb; Q04931; -.
DR PRIDE; Q04931; -.
DR GeneID; 81785; -.
DR KEGG; rno:81785; -.
DR UCSC; RGD:621143; rat.
DR CTD; 6749; -.
DR RGD; 621143; Ssrp1.
DR VEuPathDB; HostDB:ENSRNOG00000008825; -.
DR eggNOG; KOG0526; Eukaryota.
DR InParanoid; Q04931; -.
DR OMA; SKQPGKC; -.
DR OrthoDB; 915055at2759; -.
DR Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-RNO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q04931; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000008825; Expressed in thymus and 20 other tissues.
DR Genevisible; Q04931; RN.
DR GO; GO:0035101; C:FACT complex; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006337; P:nucleosome disassembly; ISO:RGD.
DR GO; GO:1902275; P:regulation of chromatin organization; ISO:RGD.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 2.30.29.220; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR013719; DUF1747.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR035417; POB3_N.
DR InterPro; IPR000969; SSrcognition.
DR InterPro; IPR024954; SSRP1_dom.
DR InterPro; IPR038167; SSRP1_sf.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF17292; POB3_N; 1.
DR Pfam; PF08512; Rtt106; 1.
DR Pfam; PF03531; SSrecog; 1.
DR PRINTS; PR00887; SSRCOGNITION.
DR SMART; SM00398; HMG; 1.
DR SMART; SM01287; Rtt106; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT CHAIN 2..709
FT /note="FACT complex subunit SSRP1"
FT /id="PRO_0000048608"
FT DNA_BIND 547..615
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 458..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..536
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..638
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 450..451
FT /note="Cleavage; by caspase-3 and/or caspase-7"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 413
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 441
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q08943"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 452
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q08943"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 510
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 542
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q08943"
FT MOD_RES 657
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT MOD_RES 688
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT CROSSLNK 296
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT CROSSLNK 364
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08945"
FT CONFLICT 382
FT /note="G -> A (in Ref. 2; AAA40927)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="F -> S (in Ref. 2; AAA40927)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="A -> G (in Ref. 2; AAA40927)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="K -> E (in Ref. 2; AAA40927)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="S -> A (in Ref. 2; AAA40927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 709 AA; 80914 MW; 3A2FFC192820882F CRC64;
MAETLEFNDI FQEVKGSMND GRLRLSRQGI IFKNSKTGKV DNIQAGELTE GIWRRVALGH
GLKLLTKNGH VYKYDGFRES EFEKLSDFFK THYRLELMEK DLCVKGWNWG TVKFGGQLLS
FDIGDQPVFE IPLSNVSQCT TGKNEVTLEF HQNDDAEVSL MEVRFYVPPT QEDGVDPVEA
FAQNVLSKAD VIQATGDAIC IFRELQCLTP RGRYDIRIYP TFLHLHGKTF DYKIPYTTVL
RLFLLPHKDQ RQMFFVISLD PPIKQGQTRY HFLILLFSKD EDISLTLNMN EEEVEKRFEG
RLTKNMSGSL YEMVSRVMKA LVNRKITVPG NFQGHSGAQC ITCSYKASSG LLYPLERGFI
YVHKPPVHIR FDEISFVNFA RGTTTTRSFD FEIETKQGTQ YTFSSIEREE YGKLFDFVNA
KKLNIKNRGL KEGINPGYDD YADSDEDQHD AYLERMKEEG KIREENANDS SDDSGEETDE
SFNPGEEEED VAEEFDSNAS ASSSSNEGDS DREEKKRKQL KRAKMAKDRK SRKKSSEGKK
GKDPNAPKRP MSAYMLWLNA SREKIKSDHP GISITDLSKK AGEIWKGMSK EKKEEWDRKA
EDARREYEKA MKEYEGGRGD SSKRDKSKKK KKVKAKLEKK STPSRGSSSK SSSRQLSDSF
KSKEFVSSDE SSSGENKSKK KRRRSEDSDE EELASTPPSS EDSASGSDE
