SRFB1_PONAB
ID SRFB1_PONAB Reviewed; 429 AA.
AC Q5NVE2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Serum response factor-binding protein 1;
DE AltName: Full=SRF-dependent transcription regulation-associated protein;
GN Name=SRFBP1 {ECO:0000250|UniProtKB:Q8NEF9};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAI29721.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex {ECO:0000312|EMBL:CAI29721.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR926095; CAI29721.1; -; mRNA.
DR RefSeq; NP_001127116.1; NM_001133644.1.
DR AlphaFoldDB; Q5NVE2; -.
DR SMR; Q5NVE2; -.
DR STRING; 9601.ENSPPYP00000017575; -.
DR GeneID; 100174161; -.
DR KEGG; pon:100174161; -.
DR CTD; 153443; -.
DR eggNOG; ENOG502QV1I; Eukaryota.
DR InParanoid; Q5NVE2; -.
DR OrthoDB; 1397283at2759; -.
DR Proteomes; UP000001595; 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..429
FT /note="Serum response factor-binding protein 1"
FT /id="PRO_0000320008"
FT REGION 128..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..67
FT /evidence="ECO:0000255"
FT COILED 108..144
FT /evidence="ECO:0000255"
FT COMPBIAS 128..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
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 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 367
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"
FT CROSSLNK 316
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
SQ SEQUENCE 429 AA; 48856 MW; CFEA88BA68329FE8 CRC64;
MAQPGTLNLN NEVVKMRKEV KRIRVLVIRK LVRSVGRLKS KKGTEDALLK NQRRAQRLLE
EIHAMKELKP DMVTKSALGD DINFEKICKK PDSTATERAI ARLAVHPLLK KKIDVLKAAV
QAFKEARQNV TEVESSKNAS EDNHSKNTLY SNDNGSNLQR EGTVISEQEV KETKILAKKP
IHNSKEKIAK MEHGPKAVTI ANSPSKPSEK DSVISLESQK TPADPKLKTL SQTKKNKESD
SSLSGNSDGG EELCEEEKEY FDDSTEERFY KQSSMSEDSD SGDDFFIGKV RRTRKKESSC
HSSVKEQKRL EKVFLKEDTG ETHGDTRNDK TKPSTETRKL ESVFFHSLSG SKSSRRNFKE
QAPKTRSLDF PQNEPQFKNQ FNKKLSRRLE NTKQQLQLPL HPSWEASRRR KEQQSNIAVF
QGKKITFDD
