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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};
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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
 
 
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