SRFB1_HUMAN
ID SRFB1_HUMAN Reviewed; 429 AA.
AC Q8NEF9; Q5QFI2; Q96AH4; Q96DK2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 143.
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|EMBL:AAH31222.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAU25829.2}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Heart {ECO:0000312|EMBL:AAU25829.2};
RX PubMed=15492011; DOI=10.1074/jbc.m405945200;
RA Zhang X., Azhar G., Zhong Y., Wei J.Y.;
RT "Identification of a novel serum response factor cofactor in cardiac gene
RT regulation.";
RL J. Biol. Chem. 279:55626-55632(2004).
RN [2] {ECO:0000312|EMBL:BAB71631.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastric mucosa {ECO:0000312|EMBL:BAB71631.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3] {ECO:0000312|EMBL:EAW48900.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH31222.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retinoblastoma {ECO:0000312|EMBL:AAH17102.1}, and
RC Testis {ECO:0000312|EMBL:AAH31222.1};
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND SER-281, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-264, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-205 AND SER-264, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-264; SER-349;
RP SER-351 AND SER-367, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-190 AND LYS-316, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in heart and skeletal muscle,
CC and at much lower levels in brain and lung.
CC {ECO:0000269|PubMed:15492011}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in adult heart (at protein level).
CC {ECO:0000269|PubMed:15492011}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71631.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY611630; AAU25829.2; -; mRNA.
DR EMBL; AK058015; BAB71631.1; ALT_FRAME; mRNA.
DR EMBL; CH471086; EAW48900.1; -; Genomic_DNA.
DR EMBL; BC017102; AAH17102.1; -; mRNA.
DR EMBL; BC031222; AAH31222.1; -; mRNA.
DR CCDS; CCDS43354.1; -.
DR RefSeq; NP_689759.2; NM_152546.2.
DR AlphaFoldDB; Q8NEF9; -.
DR SMR; Q8NEF9; -.
DR BioGRID; 127495; 58.
DR IntAct; Q8NEF9; 26.
DR MINT; Q8NEF9; -.
DR STRING; 9606.ENSP00000341324; -.
DR GlyGen; Q8NEF9; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8NEF9; -.
DR PhosphoSitePlus; Q8NEF9; -.
DR BioMuta; SRFBP1; -.
DR DMDM; 74751249; -.
DR EPD; Q8NEF9; -.
DR jPOST; Q8NEF9; -.
DR MassIVE; Q8NEF9; -.
DR MaxQB; Q8NEF9; -.
DR PaxDb; Q8NEF9; -.
DR PeptideAtlas; Q8NEF9; -.
DR PRIDE; Q8NEF9; -.
DR ProteomicsDB; 73159; -.
DR TopDownProteomics; Q8NEF9; -.
DR Antibodypedia; 25600; 143 antibodies from 23 providers.
DR DNASU; 153443; -.
DR Ensembl; ENST00000339397.5; ENSP00000341324.4; ENSG00000151304.6.
DR GeneID; 153443; -.
DR KEGG; hsa:153443; -.
DR MANE-Select; ENST00000339397.5; ENSP00000341324.4; NM_152546.3; NP_689759.2.
DR UCSC; uc003kst.2; human.
DR CTD; 153443; -.
DR DisGeNET; 153443; -.
DR GeneCards; SRFBP1; -.
DR HGNC; HGNC:26333; SRFBP1.
DR HPA; ENSG00000151304; Low tissue specificity.
DR MalaCards; SRFBP1; -.
DR MIM; 610479; gene.
DR neXtProt; NX_Q8NEF9; -.
DR OpenTargets; ENSG00000151304; -.
DR PharmGKB; PA142670870; -.
DR VEuPathDB; HostDB:ENSG00000151304; -.
DR eggNOG; ENOG502QV1I; Eukaryota.
DR GeneTree; ENSGT00390000006478; -.
DR HOGENOM; CLU_054142_0_0_1; -.
DR InParanoid; Q8NEF9; -.
DR OMA; QFSKKID; -.
DR OrthoDB; 1397283at2759; -.
DR PhylomeDB; Q8NEF9; -.
DR TreeFam; TF328596; -.
DR PathwayCommons; Q8NEF9; -.
DR SignaLink; Q8NEF9; -.
DR BioGRID-ORCS; 153443; 613 hits in 1078 CRISPR screens.
DR ChiTaRS; SRFBP1; human.
DR GenomeRNAi; 153443; -.
DR Pharos; Q8NEF9; Tbio.
DR PRO; PR:Q8NEF9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8NEF9; protein.
DR Bgee; ENSG00000151304; Expressed in calcaneal tendon and 171 other tissues.
DR Genevisible; Q8NEF9; HS.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
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 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:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..429
FT /note="Serum response factor-binding protein 1"
FT /id="PRO_0000320006"
FT REGION 131..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..67
FT /evidence="ECO:0000255"
FT COILED 108..146
FT /evidence="ECO:0000255"
FT COMPBIAS 132..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..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..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 190
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 316
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 345
FT /note="F -> S (in Ref. 2; BAB71631)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 48634 MW; 6046C3E73C87BCF0 CRC64;
MAQPGTLNLN NEVVKMRKEV KRIRVLVIRK LVRSVGRLKS KKGTEDALLK NQRRAQRLLE
EIHAMKELKP DIVTKSALGD DINFEKIFKK PDSTATERAI ARLAVHPLLK KKIDVLKAAV
QAFKEARQNV AEVESSKNAS EDNHSENTLY SNDNGSNLQR EATVISEQKV KETKILAKKP
IHNSKEKIAK MEHGPKAVTI ANSPSKPSEK DSVVSLESQK TPADPKLKTL SQTKKNKGSD
SSLSGNSDGG EEFCEEEKEY FDDSTEERFY KQSSMSEDSD SGDDFFIGKV RRTRKKESSC
HSSVKEQKPL EKVFLKEDTG ETHGDTRNDK IKPSTETRKL ESVFFHSLSG SKSSRRNFKE
QAPKTRSLDF PQNEPQIKNQ FNKKLSGRLE NTKQQLQLPL HPSWEASRRR KEQQSNIAVF
QGKKITFDD
