SRFB1_BOVIN
ID SRFB1_BOVIN Reviewed; 428 AA.
AC Q05B65;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Serum response factor-binding protein 1;
DE AltName: Full=SRF-dependent transcription regulation-associated protein;
GN Name=SRFBP1 {ECO:0000312|EMBL:AAI22715.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI22715.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI22715.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAI22715.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; BC122714; AAI22715.1; -; mRNA.
DR RefSeq; NP_001098919.1; NM_001105449.1.
DR AlphaFoldDB; Q05B65; -.
DR SMR; Q05B65; -.
DR STRING; 9913.ENSBTAP00000049639; -.
DR PaxDb; Q05B65; -.
DR PRIDE; Q05B65; -.
DR GeneID; 617136; -.
DR KEGG; bta:617136; -.
DR CTD; 153443; -.
DR eggNOG; ENOG502QV1I; Eukaryota.
DR InParanoid; Q05B65; -.
DR OrthoDB; 1397283at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR InterPro; IPR037393; Bud22/SRFB1.
DR InterPro; IPR015158; Bud22_dom.
DR PANTHER; PTHR23325; PTHR23325; 1.
DR Pfam; PF09073; BUD22; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT CHAIN 2..428
FT /note="Serum response factor-binding protein 1"
FT /id="PRO_0000320005"
FT REGION 132..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 45..72
FT /evidence="ECO:0000255"
FT COILED 109..130
FT /evidence="ECO:0000255"
FT COMPBIAS 175..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..261
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT CROSSLNK 190
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
SQ SEQUENCE 428 AA; 48938 MW; 245EC6FF5DD831CE CRC64;
MAEPETLNLN NEVVKMRKEV KRIRVLVIRK LVRSVGRLKS KKGREDALLK NQRRAQRLLE
EIRAMKELKP DVVTKSALGE DINFEKICKK PDSTAAERAI ARLAVHPLLK KKIDVLKAAV
KSFKDARQNV VEVKSSNSAS EENHSKDTLC SNDDASKLQH EGTIIREQKE KEAKILAKKP
INNSKEKIAK MDHGPKAMDV PNSLSKPSGK DSPASSASQK TPSDPKMKAL SKTKKMKESS
SSLDVDSDGE ELYEEEKEYF DDSTEERFYK QSSMSEDSDS GDDFFIGKVK RARKKESSCR
FSDKEQNPPK NLLLEEGILE THQNLQNDKN KPRTEARRFE SVFFQSLSGS KSLERNHREQ
VPRSKTMDFQ HIEPQNKNQF NKKAQRGFEN TKQKSQLPLH PSWEASRRRK EQQSKIAVFQ
GKKITFDD
