SRFB1_MOUSE
ID SRFB1_MOUSE Reviewed; 441 AA.
AC Q9CZ91; Q3UGY0; Q3UMK2; Q3UR20; Q8R3W6; Q9CRL0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
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|MGI:MGI:1914472};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAU25828.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SRF, SUBUNIT, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAU25828.1};
RC TISSUE=Heart {ECO:0000312|EMBL:AAU25828.1};
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:BAB28520.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB28520.1, ECO:0000312|EMBL:BAE28077.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAE28077.1},
RC Embryo {ECO:0000312|EMBL:BAB28520.1},
RC Embryonic spinal ganglion {ECO:0000312|EMBL:BAE24868.1}, and
RC Lung {ECO:0000312|EMBL:BAE26096.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:AAH24338.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3 {ECO:0000312|EMBL:AAH24338.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH24338.1};
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 [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SLC2A4, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16647043; DOI=10.1016/j.bbrc.2006.04.017;
RA Lisinski I., Matsumoto H., Yver D.R., Schuermann A., Cushman S.W.,
RA Al-Hasani H.;
RT "Identification and characterization of p49/STRAP as a novel GLUT4-binding
RT protein.";
RL Biochem. Biophys. Res. Commun. 344:1179-1185(2006).
RN [5] {ECO:0000305}
RP SUBUNIT.
RX PubMed=16782067; DOI=10.1016/j.bbrc.2006.05.211;
RA Zhang X., Azhar G., Zhong Y., Wei J.Y.;
RT "Zipzap/p200 is a novel zinc finger protein contributing to cardiac gene
RT regulation.";
RL Biochem. Biophys. Res. Commun. 346:794-801(2006).
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.
CC {ECO:0000269|PubMed:15492011, ECO:0000269|PubMed:16647043}.
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.
CC {ECO:0000269|PubMed:15492011, ECO:0000269|PubMed:16647043,
CC ECO:0000269|PubMed:16782067}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16647043}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, liver,
CC kidney, testis and brain. Also expressed in white adipose tissue.
CC Expression is up-regulated in cardiomyopathic heart.
CC {ECO:0000269|PubMed:15492011, ECO:0000269|PubMed:16647043}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated in adult heart (at protein level).
CC {ECO:0000269|PubMed:15492011}.
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DR EMBL; AY611629; AAU25828.1; -; mRNA.
DR EMBL; AK012865; BAB28520.1; -; mRNA.
DR EMBL; AK020469; BAB32112.1; -; mRNA.
DR EMBL; AK141882; BAE24868.1; -; mRNA.
DR EMBL; AK144845; BAE26096.1; -; mRNA.
DR EMBL; AK147692; BAE28077.1; -; mRNA.
DR EMBL; BC024338; AAH24338.1; -; mRNA.
DR CCDS; CCDS37819.1; -.
DR RefSeq; NP_080316.3; NM_026040.3.
DR AlphaFoldDB; Q9CZ91; -.
DR SMR; Q9CZ91; -.
DR BioGRID; 212027; 1.
DR CORUM; Q9CZ91; -.
DR STRING; 10090.ENSMUSP00000025406; -.
DR iPTMnet; Q9CZ91; -.
DR PhosphoSitePlus; Q9CZ91; -.
DR EPD; Q9CZ91; -.
DR jPOST; Q9CZ91; -.
DR MaxQB; Q9CZ91; -.
DR PaxDb; Q9CZ91; -.
DR PeptideAtlas; Q9CZ91; -.
DR PRIDE; Q9CZ91; -.
DR ProteomicsDB; 257067; -.
DR Antibodypedia; 25600; 143 antibodies from 23 providers.
DR DNASU; 67222; -.
DR Ensembl; ENSMUST00000025406; ENSMUSP00000025406; ENSMUSG00000024528.
DR GeneID; 67222; -.
DR KEGG; mmu:67222; -.
DR UCSC; uc008exd.1; mouse.
DR CTD; 153443; -.
DR MGI; MGI:1914472; Srfbp1.
DR VEuPathDB; HostDB:ENSMUSG00000024528; -.
DR eggNOG; ENOG502QV1I; Eukaryota.
DR GeneTree; ENSGT00390000006478; -.
DR HOGENOM; CLU_054142_0_0_1; -.
DR InParanoid; Q9CZ91; -.
DR OMA; QFSKKID; -.
DR OrthoDB; 1397283at2759; -.
DR PhylomeDB; Q9CZ91; -.
DR TreeFam; TF328596; -.
DR BioGRID-ORCS; 67222; 20 hits in 72 CRISPR screens.
DR PRO; PR:Q9CZ91; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9CZ91; protein.
DR Bgee; ENSMUSG00000024528; Expressed in undifferentiated genital tubercle and 247 other tissues.
DR ExpressionAtlas; Q9CZ91; baseline and differential.
DR Genevisible; Q9CZ91; MM.
DR GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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..441
FT /note="Serum response factor-binding protein 1"
FT /id="PRO_0000320007"
FT REGION 137..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 52..77
FT /evidence="ECO:0000255"
FT COILED 118..140
FT /evidence="ECO:0000255"
FT COMPBIAS 150..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NEF9"
FT CONFLICT 67
FT /note="R -> G (in Ref. 2; BAE26096)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="D -> A (in Ref. 3; AAH24338)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="A -> V (in Ref. 2; BAE26096)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="A -> V (in Ref. 2; BAE24868)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="C -> Y (in Ref. 3; AAH24338)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="R -> S (in Ref. 3; AAH24338)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="R -> S (in Ref. 3; AAH24338)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> G (in Ref. 3; AAH24338)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="R -> K (in Ref. 3; AAH24338)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="E -> A (in Ref. 3; AAH24338)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="S -> C (in Ref. 3; AAH24338)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="R -> S (in Ref. 2; BAE28077)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="Y -> H (in Ref. 3; AAH24338)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="T -> P (in Ref. 3; AAH24338)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 48746 MW; 28BD129ABADAE30E CRC64;
MAADPLPPSA MVQPGTLNLN NEVVKMRKEV KRIRVLVIRK LVRSVGRLKS KKGTEDALLK
NQRRAQRLLE EIHAMKELKP DVVTKSALSD DINFEKTCKK PDSTATDRAV ARLAGHPLLK
KKIDVLKDAV QAFKDARQSA PAAESSESTS GEGRCKDIAR SKDDARESQH PERTVVREQK
AKDTNTAAKN AASGSKEKLA KTEQAPRAGT TPGSQGRPSG KGAGVNSEHQ GAPAPGDSNQ
GKASTKTPED SVCEPANNGV SEEEESEGEK EYFDDSTEER FYKQSSASED SDSGDDFFIG
KVRRTRKKES GVHSSAKELK PLPKVPSKTS TLETPWDVRN DKHRPIPEAR KFESVFFHSL
AGPKSSRRDP REQAPKNKAP DFPENEPPVK KQFTKSAYRG FESVKQTMQA PLHPSWEASR
RRKEQQSKIA VFQGKKITFD D
