SSBP3_RAT
ID SSBP3_RAT Reviewed; 361 AA.
AC Q9R050;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Single-stranded DNA-binding protein 3;
DE AltName: Full=Sequence-specific single-stranded-DNA-binding protein;
GN Name=Ssbp3; Synonyms=Ssdp, Ssdp1, Ssdp3;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
RX PubMed=10524251; DOI=10.1016/s0378-1119(99)00289-9;
RA Raval-Fernandes S., Kickhoefer V.A., Rome L.H.;
RT "Cloning of a cDNA encoding a sequence-specific single-stranded-DNA-binding
RT protein from Rattus norvegicus.";
RL Gene 237:201-207(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; THR-333 AND SER-360, AND
RP IDENTIFICATION BY 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: May be involved in transcription regulation of the alpha 2(I)
CC collagen gene where it binds to the single-stranded polypyrimidine
CC sequences in the promoter region. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AF121893; AAD52710.1; -; mRNA.
DR RefSeq; NP_445810.1; NM_053358.1.
DR AlphaFoldDB; Q9R050; -.
DR SMR; Q9R050; -.
DR STRING; 10116.ENSRNOP00000011408; -.
DR iPTMnet; Q9R050; -.
DR PhosphoSitePlus; Q9R050; -.
DR PaxDb; Q9R050; -.
DR PRIDE; Q9R050; -.
DR GeneID; 84354; -.
DR KEGG; rno:84354; -.
DR UCSC; RGD:621502; rat.
DR CTD; 23648; -.
DR RGD; 621502; Ssbp3.
DR eggNOG; KOG4594; Eukaryota.
DR InParanoid; Q9R050; -.
DR OrthoDB; 907486at2759; -.
DR PhylomeDB; Q9R050; -.
DR PRO; PR:Q9R050; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; TAS:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0060322; P:head development; ISO:RGD.
DR GO; GO:0060323; P:head morphogenesis; ISO:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0048382; P:mesendoderm development; ISO:RGD.
DR GO; GO:0021547; P:midbrain-hindbrain boundary initiation; ISO:RGD.
DR GO; GO:2000744; P:positive regulation of anterior head development; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0021501; P:prechordal plate formation; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR008116; SSDP_DNA-bd.
DR PRINTS; PR01743; SSDNABINDING.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..361
FT /note="Single-stranded DNA-binding protein 3"
FT /id="PRO_0000123830"
FT DOMAIN 16..48
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REGION 140..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWW4"
FT MOD_RES 128
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWW4"
FT MOD_RES 134
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWW4"
FT MOD_RES 138
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWW4"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWW4"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D032"
FT MOD_RES 333
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWW4"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 361 AA; 37714 MW; 7E1AA48EC355B161 CRC64;
MFAKGKGSAV PSDGQAREKL ALYVYEYLLH VGAQKSAQTF LSEIRWEKNI TLGEPPGFLH
SWWCVFWDLY CAAPERRDTC EHSSEAKAFH DYSAAAAPSP VLGNIPPNDG MPGGPIPPGF
FQPFMSPRYA GGPRPPIRMG NQPPGGVPGT QPLMPNSMDP TRQQGHPNMG GSMQRMNPPR
GMGPMGPGPQ NYGSGMRPPP NSLGPAMPGI NMGPGAGRPW PNPNSANSIP YSSSSPGTYV
GPPGGGGPPG TPIMPSPADS TNSSDNIYTM INPVPPGGSR SNFPMGPGSD GPMGGMGGME
PHHMNGSLGS GDINGLPKNS PNNISGISNP PGTPRDDGEL GGNFLHSFQN DNYSPSMTMS
V
