SRFB1_RAT
ID SRFB1_RAT Reviewed; 442 AA.
AC Q66H19;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Serum response factor-binding protein 1;
DE AltName: Full=SRF-dependent transcription regulation-associated protein;
DE AltName: Full=p49/STRAP;
GN Name=Srfbp1 {ECO:0000312|RGD:1359398};
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] {ECO:0000312|EMBL:AAH82077.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH82077.1};
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-294, 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 regulating transcriptional activation of
CC cardiac genes during the aging process. May play a role in biosynthesis
CC and/or processing of SLC2A4 in adipose cells (By similarity).
CC {ECO:0000250|UniProtKB:Q9CZ91}.
CC -!- SUBUNIT: Interacts with SRF. Forms complexes with SRF and SRF cofactors
CC ARID2, MYOCD and NKX2-5. Interacts with the N-terminus of SLC2A4 (By
CC similarity). {ECO:0000250|UniProtKB:Q9CZ91}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9CZ91}.
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DR EMBL; BC082077; AAH82077.1; -; mRNA.
DR RefSeq; NP_001005536.1; NM_001005536.1.
DR AlphaFoldDB; Q66H19; -.
DR SMR; Q66H19; -.
DR STRING; 10116.ENSRNOP00000020030; -.
DR iPTMnet; Q66H19; -.
DR PhosphoSitePlus; Q66H19; -.
DR PaxDb; Q66H19; -.
DR PRIDE; Q66H19; -.
DR Ensembl; ENSRNOT00000020030; ENSRNOP00000020030; ENSRNOG00000014808.
DR GeneID; 291469; -.
DR KEGG; rno:291469; -.
DR UCSC; RGD:1359398; rat.
DR CTD; 153443; -.
DR RGD; 1359398; Srfbp1.
DR eggNOG; ENOG502QV1I; Eukaryota.
DR GeneTree; ENSGT00390000006478; -.
DR HOGENOM; CLU_054142_0_0_1; -.
DR InParanoid; Q66H19; -.
DR OMA; QFSKKID; -.
DR OrthoDB; 1397283at2759; -.
DR PhylomeDB; Q66H19; -.
DR TreeFam; TF328596; -.
DR PRO; PR:Q66H19; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000014808; Expressed in ovary and 19 other tissues.
DR Genevisible; Q66H19; RN.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR InterPro; IPR037393; Bud22/SRFB1.
DR InterPro; IPR015158; Bud22_dom.
DR PANTHER; PTHR23325; PTHR23325; 1.
DR Pfam; PF09073; BUD22; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..442
FT /note="Serum response factor-binding protein 1"
FT /id="PRO_0000320009"
FT REGION 137..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 55..77
FT /evidence="ECO:0000255"
FT COILED 118..140
FT /evidence="ECO:0000255"
FT COMPBIAS 171..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT CROSSLNK 202
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT CROSSLNK 329
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
SQ SEQUENCE 442 AA; 49195 MW; AF481615F212818C CRC64;
MAADPSPPSA MAQPRPLNLN NEVVKMRKEV KRIRVLVIRK LVRSVSRLKS KKGSEDALLK
NQRRAQRLLQ EIHAMKELKP DVITKSALND DINFEKTCKK PDSTATERAI ARLAVHPLLK
RKVDALKAAI QAFKDARQNA PEAESSKSAS KESQCEDIPR SQAEASESQH PERTVVGEQK
GKDKDPTTAK KAGSGSKEKL AKGKQGPKAV ATPHSPGKPS EKGAGINSER QGAPTPGNHS
QGKASTRTTE DSVCEPDDNS ISKEEVSEEE KEYFDDSTEE RFYKQSSASE DSDSGDDFFI
GKVRRTRKKE CAVPSSAKEQ KPLPKVSSKT NTLETHWDIR NDKHKLIPEA RKLESVFFHS
LSGPKSSRRD PREQAPKNKA PDIPENEPPI QNKFTKSARR GFESAKQPSY APLHPSWEAS
RRRKEQQSKI AVFQGKKITF DD
