PURB_MOUSE
ID PURB_MOUSE Reviewed; 324 AA.
AC O35295;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Transcriptional activator protein Pur-beta;
DE AltName: Full=Purine-rich element-binding protein B;
DE AltName: Full=Vascular actin single-stranded DNA-binding factor 2 p44 component;
GN Name=Purb;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX PubMed=9334258; DOI=10.1074/jbc.272.42.26727;
RA Kelm R.J. Jr., Elder P.K., Strauch A.R., Getz M.J.;
RT "Sequence of cDNAs encoding components of vascular actin single-stranded
RT DNA-binding factor 2 establish identity to Puralpha and Purbeta.";
RL J. Biol. Chem. 272:26727-26733(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PROTEIN SEQUENCE OF 68-82, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP SUBUNIT.
RX PubMed=10318844; DOI=10.1074/jbc.274.20.14238;
RA Kelm R.J. Jr., Cogan J.G., Elder P.K., Strauch A.R., Getz M.J.;
RT "Molecular interactions between single-stranded DNA-binding proteins
RT associated with an essential MCAT element in the mouse smooth muscle alpha-
RT actin promoter.";
RL J. Biol. Chem. 274:14238-14245(1999).
RN [5]
RP FUNCTION.
RX PubMed=11751932; DOI=10.1074/jbc.m109754200;
RA Carlini L.E., Getz M.J., Strauch A.R., Kelm R.J. Jr.;
RT "Cryptic MCAT enhancer regulation in fibroblasts and smooth muscle cells.
RT Suppression of TEF-1 mediated activation by the single-stranded DNA-binding
RT proteins, Pur alpha, Pur beta, and MSY1.";
RL J. Biol. Chem. 277:8682-8692(2002).
RN [6]
RP REGION.
RX PubMed=12874279; DOI=10.1074/jbc.m306163200;
RA Kelm R.J. Jr., Wang S.X., Polikandriotis J.A., Strauch A.R.;
RT "Structure/function analysis of mouse Purbeta, a single-stranded DNA-
RT binding repressor of vascular smooth muscle alpha-actin gene
RT transcription.";
RL J. Biol. Chem. 278:38749-38757(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-8 AND SER-316, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6; SER-310 AND SER-316, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-6; SER-8 AND SER-316, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-310 AND SER-316, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-279, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-28; ARG-164 AND ARG-306, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Has capacity to bind repeated elements in single-stranded DNA
CC such as the purine-rich single strand of the PUR element located
CC upstream of the MYC gene. Participates in transcriptional and
CC translational regulation of alpha-MHC expression in cardiac myocytes by
CC binding to the purine-rich negative regulatory (PNR) element. Modulates
CC constitutive liver galectin-3 gene transcription by binding to its
CC promoter. May play a role in the dendritic transport of a subset of
CC mRNAs (By similarity). Plays a role in the control of vascular smooth
CC muscle (VSM) alpha-actin gene transcription as repressor in myoblasts
CC and fibroblasts. {ECO:0000250, ECO:0000269|PubMed:11751932,
CC ECO:0000269|PubMed:9334258}.
CC -!- SUBUNIT: Homodimer, heterodimer with PURA and heterotrimer with PURA
CC and YBX1/Y-box protein 1. {ECO:0000269|PubMed:10318844}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
CC {ECO:0000305}.
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DR EMBL; AF017630; AAB71859.1; -; mRNA.
DR EMBL; AL646020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24420.1; -.
DR RefSeq; NP_035351.1; NM_011221.3.
DR AlphaFoldDB; O35295; -.
DR SMR; O35295; -.
DR BioGRID; 202516; 12.
DR IntAct; O35295; 9.
DR MINT; O35295; -.
DR STRING; 10090.ENSMUSP00000136957; -.
DR iPTMnet; O35295; -.
DR PhosphoSitePlus; O35295; -.
DR SwissPalm; O35295; -.
DR EPD; O35295; -.
DR jPOST; O35295; -.
DR MaxQB; O35295; -.
DR PaxDb; O35295; -.
DR PeptideAtlas; O35295; -.
DR PRIDE; O35295; -.
DR ProteomicsDB; 301982; -.
DR Antibodypedia; 44598; 98 antibodies from 19 providers.
DR DNASU; 19291; -.
DR Ensembl; ENSMUST00000179343; ENSMUSP00000136957; ENSMUSG00000094483.
DR GeneID; 19291; -.
DR KEGG; mmu:19291; -.
DR UCSC; uc007hyr.3; mouse.
DR CTD; 5814; -.
DR MGI; MGI:1338779; Purb.
DR VEuPathDB; HostDB:ENSMUSG00000094483; -.
DR eggNOG; KOG3074; Eukaryota.
DR GeneTree; ENSGT00950000183162; -.
DR HOGENOM; CLU_057873_1_1_1; -.
DR InParanoid; O35295; -.
DR OMA; RFIRVEN; -.
DR OrthoDB; 1248813at2759; -.
DR PhylomeDB; O35295; -.
DR TreeFam; TF313701; -.
DR BioGRID-ORCS; 19291; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Purb; mouse.
DR PRO; PR:O35295; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O35295; protein.
DR Bgee; ENSMUSG00000094483; Expressed in lateral septal nucleus and 240 other tissues.
DR Genevisible; O35295; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; ISO:MGI.
DR GO; GO:0032422; F:purine-rich negative regulatory element binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR006628; PUR-bd_fam.
DR InterPro; IPR030499; PURbeta.
DR PANTHER; PTHR12611; PTHR12611; 1.
DR PANTHER; PTHR12611:SF4; PTHR12611:SF4; 1.
DR Pfam; PF04845; PurA; 1.
DR SMART; SM00712; PUR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; DNA-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326"
FT CHAIN 2..324
FT /note="Transcriptional activator protein Pur-beta"
FT /id="PRO_0000225616"
FT DNA_BIND 37..263
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:19131326"
FT MOD_RES 28
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 164
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 279
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 306
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 324 AA; 33901 MW; 5CB70CCE3FDB7913 CRC64;
MADGDSGSER GGGGGGGGGP GGFQPAPRGG GGGGGGPGGE QETQELASKR LDIQNKRFYL
DVKQNAKGRF LKIAEVGAGG SKSRLTLSMA VAAEFRDSLG DFIEHYAQLG PSSPEQLAAG
AEEGGGPRRA LKSEFLVREN RKYYLDLKEN QRGRFLRIRQ TVNRGGGGFG GGPGPGGLQS
GQTIALPAQG LIEFRDALAK LIDDYGGDED ELAGGPGGGA GGPGGGLYGE LPEGTSITVD
SKRFFFDVGC NKYGVFLRVS EVKPSYRNAI TVPFKAWGKF GGAFCRYADE MKEIQERQRD
KLYERRGGGS GGGDESEGEE VDED
