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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
 
 
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