Full text data of PURB
PURB
[Confidence: low (only semi-automatic identification from reviews)]
Transcriptional activator protein Pur-beta (Purine-rich element-binding protein B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transcriptional activator protein Pur-beta (Purine-rich element-binding protein B)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96QR8
ID PURB_HUMAN Reviewed; 312 AA.
AC Q96QR8; A4D2L7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Transcriptional activator protein Pur-beta;
DE AltName: Full=Purine-rich element-binding protein B;
GN Name=PURB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=1448097;
RA Bergemann A.D., Ma Z.-W., Johnson E.M.;
RT "Sequence of cDNA comprising the human pur gene and sequence-specific
RT single-stranded-DNA-binding properties of the encoded protein.";
RL Mol. Cell. Biol. 12:5673-5682(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INVOLVEMENT IN MDS.
RX PubMed=11417483; DOI=10.1038/sj.leu.2402108;
RA Lezon-Geyda K., Najfeld V., Johnson E.M.;
RT "Deletions of PURA, at 5q31, and PURB, at 7p13, in myelodysplastic
RT syndrome and progression to acute myelogenous leukemia.";
RL Leukemia 15:954-962(2001).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12933792; DOI=10.1074/jbc.M307696200;
RA Gupta M., Sueblinvong V., Raman J., Jeevanandam V., Gupta M.P.;
RT "Single-stranded DNA-binding proteins PURalpha and PURbeta bind to a
RT purine-rich negative regulatory element of the alpha-myosin heavy
RT chain gene and control transcriptional and translational regulation of
RT the gene expression. Implications in the repression of alpha-myosin
RT heavy chain during heart failure.";
RL J. Biol. Chem. 278:44935-44948(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASS
RP SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-298 AND
RP SER-304, AND MASS SPECTROMETRY.
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-6; SER-8 AND SER-304, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-298 AND SER-304, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Has capacity to bind repeated elements in single-
CC stranded DNA such as the purine-rich single strand of the PUR
CC element located upstream of the MYC gene. Plays a role in the
CC control of vascular smooth muscle (VSM) alpha-actin gene
CC transcription as repressor in myoblasts and fibroblasts.
CC Participates in transcriptional and translational regulation of
CC alpha-MHC expression in cardiac myocytes by binding to the purine-
CC rich negative regulatory (PNR) element. Modulates constitutive
CC liver galectin-3 gene transcription by binding to its promoter.
CC May play a role in the dendritic transport of a subset of mRNAs
CC (By similarity).
CC -!- SUBUNIT: Homodimer, heterodimer with PURA and heterotrimer with
CC PURA and YBX1/Y-box protein 1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in myocardium of heart failure
CC patients.
CC -!- MISCELLANEOUS: Defects in PURB may be a cause of progression of
CC myelodysplastic syndrome (MDS) towards acute myelogenous leukemia
CC (AML). MDS refers to a heterogeneous group of closely related
CC hematopoietic disorders. All are characterized by a cellular
CC marrow with impaired morphology and maturation (dysmyelopoiesis)
CC and peripheral blood cytopenias, resulting from ineffective blood
CC cell production. Some patients with MDS develop acute myelogenous
CC leukemia (AML), a malignant disease in which hematopoietic
CC precursors are arrested in an early stage of development.
CC -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
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DR EMBL; AY039216; AAK72462.1; -; mRNA.
DR EMBL; AC004854; AAS00366.1; -; Genomic_DNA.
DR EMBL; CH236960; EAL23749.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61073.1; -; Genomic_DNA.
DR EMBL; BC101735; AAI01736.1; -; mRNA.
DR EMBL; BC101737; AAI01738.1; -; mRNA.
DR PIR; B45036; B45036.
DR RefSeq; NP_150093.1; NM_033224.4.
DR UniGene; Hs.349150; -.
DR UniGene; Hs.596321; -.
DR ProteinModelPortal; Q96QR8; -.
DR SMR; Q96QR8; 32-278.
DR IntAct; Q96QR8; 3.
DR STRING; 9606.ENSP00000379051; -.
DR PhosphoSite; Q96QR8; -.
DR DMDM; 74732688; -.
DR PaxDb; Q96QR8; -.
DR PeptideAtlas; Q96QR8; -.
DR PRIDE; Q96QR8; -.
DR Ensembl; ENST00000395699; ENSP00000379051; ENSG00000146676.
DR GeneID; 5814; -.
DR KEGG; hsa:5814; -.
DR UCSC; uc003tme.3; human.
DR CTD; 5814; -.
DR GeneCards; GC07M044882; -.
DR H-InvDB; HIX0034001; -.
DR HGNC; HGNC:9702; PURB.
DR HPA; HPA048766; -.
DR MIM; 608887; gene.
DR neXtProt; NX_Q96QR8; -.
DR PharmGKB; PA34046; -.
DR eggNOG; NOG312871; -.
DR HOGENOM; HOG000232132; -.
DR HOVERGEN; HBG006888; -.
DR InParanoid; Q96QR8; -.
DR OMA; KENVRGR; -.
DR OrthoDB; EOG78D7M4; -.
DR PhylomeDB; Q96QR8; -.
DR ChiTaRS; PURB; human.
DR GeneWiki; PURB; -.
DR GenomeRNAi; 5814; -.
DR NextBio; 22646; -.
DR PRO; PR:Q96QR8; -.
DR Bgee; Q96QR8; -.
DR CleanEx; HS_PURB; -.
DR Genevestigator; Q96QR8; -.
DR GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; NAS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR006628; PUR_DNA_RNA-bd.
DR PANTHER; PTHR12611; PTHR12611; 1.
DR Pfam; PF04845; PurA; 1.
DR SMART; SM00712; PUR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 312 Transcriptional activator protein Pur-
FT beta.
FT /FTId=PRO_0000225615.
FT DNA_BIND 28 254 By similarity.
FT COMPBIAS 153 222 Gly-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 6 6 Phosphoserine.
FT MOD_RES 8 8 Phosphoserine.
FT MOD_RES 31 31 Phosphothreonine (By similarity).
FT MOD_RES 101 101 Phosphoserine.
FT MOD_RES 298 298 Phosphoserine.
FT MOD_RES 304 304 Phosphoserine.
SQ SEQUENCE 312 AA; 33241 MW; E39E84E8D2957A18 CRC64;
MADGDSGSER GGGGGPCGFQ PASRGGGEQE TQELASKRLD IQNKRFYLDV KQNAKGRFLK
IAEVGAGGSK SRLTLSMAVA AEFRDSLGDF IEHYAQLGPS SPEQLAAGAE EGGGPRRALK
SEFLVRENRK YYLDLKENQR GRFLRIRQTV NRGGGGFGAG PGPGGLQSGQ TIALPAQGLI
EFRDALAKLI DDYGGEDDEL AGGPGGGAGG PGGGLYGELP EGTSITVDSK RFFFDVGCNK
YGVFLRVSEV KPSYRNAITV PFKAWGKFGG AFCRYADEMK EIQERQRDKL YERRGGGSGG
GEESEGEEVD ED
//
ID PURB_HUMAN Reviewed; 312 AA.
AC Q96QR8; A4D2L7;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 101.
DE RecName: Full=Transcriptional activator protein Pur-beta;
DE AltName: Full=Purine-rich element-binding protein B;
GN Name=PURB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=1448097;
RA Bergemann A.D., Ma Z.-W., Johnson E.M.;
RT "Sequence of cDNA comprising the human pur gene and sequence-specific
RT single-stranded-DNA-binding properties of the encoded protein.";
RL Mol. Cell. Biol. 12:5673-5682(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INVOLVEMENT IN MDS.
RX PubMed=11417483; DOI=10.1038/sj.leu.2402108;
RA Lezon-Geyda K., Najfeld V., Johnson E.M.;
RT "Deletions of PURA, at 5q31, and PURB, at 7p13, in myelodysplastic
RT syndrome and progression to acute myelogenous leukemia.";
RL Leukemia 15:954-962(2001).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12933792; DOI=10.1074/jbc.M307696200;
RA Gupta M., Sueblinvong V., Raman J., Jeevanandam V., Gupta M.P.;
RT "Single-stranded DNA-binding proteins PURalpha and PURbeta bind to a
RT purine-rich negative regulatory element of the alpha-myosin heavy
RT chain gene and control transcriptional and translational regulation of
RT the gene expression. Implications in the repression of alpha-myosin
RT heavy chain during heart failure.";
RL J. Biol. Chem. 278:44935-44948(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASS
RP SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-298 AND
RP SER-304, AND MASS SPECTROMETRY.
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-6; SER-8 AND SER-304, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-298 AND SER-304, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Has capacity to bind repeated elements in single-
CC stranded DNA such as the purine-rich single strand of the PUR
CC element located upstream of the MYC gene. Plays a role in the
CC control of vascular smooth muscle (VSM) alpha-actin gene
CC transcription as repressor in myoblasts and fibroblasts.
CC Participates in transcriptional and translational regulation of
CC alpha-MHC expression in cardiac myocytes by binding to the purine-
CC rich negative regulatory (PNR) element. Modulates constitutive
CC liver galectin-3 gene transcription by binding to its promoter.
CC May play a role in the dendritic transport of a subset of mRNAs
CC (By similarity).
CC -!- SUBUNIT: Homodimer, heterodimer with PURA and heterotrimer with
CC PURA and YBX1/Y-box protein 1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in myocardium of heart failure
CC patients.
CC -!- MISCELLANEOUS: Defects in PURB may be a cause of progression of
CC myelodysplastic syndrome (MDS) towards acute myelogenous leukemia
CC (AML). MDS refers to a heterogeneous group of closely related
CC hematopoietic disorders. All are characterized by a cellular
CC marrow with impaired morphology and maturation (dysmyelopoiesis)
CC and peripheral blood cytopenias, resulting from ineffective blood
CC cell production. Some patients with MDS develop acute myelogenous
CC leukemia (AML), a malignant disease in which hematopoietic
CC precursors are arrested in an early stage of development.
CC -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
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DR EMBL; AY039216; AAK72462.1; -; mRNA.
DR EMBL; AC004854; AAS00366.1; -; Genomic_DNA.
DR EMBL; CH236960; EAL23749.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61073.1; -; Genomic_DNA.
DR EMBL; BC101735; AAI01736.1; -; mRNA.
DR EMBL; BC101737; AAI01738.1; -; mRNA.
DR PIR; B45036; B45036.
DR RefSeq; NP_150093.1; NM_033224.4.
DR UniGene; Hs.349150; -.
DR UniGene; Hs.596321; -.
DR ProteinModelPortal; Q96QR8; -.
DR SMR; Q96QR8; 32-278.
DR IntAct; Q96QR8; 3.
DR STRING; 9606.ENSP00000379051; -.
DR PhosphoSite; Q96QR8; -.
DR DMDM; 74732688; -.
DR PaxDb; Q96QR8; -.
DR PeptideAtlas; Q96QR8; -.
DR PRIDE; Q96QR8; -.
DR Ensembl; ENST00000395699; ENSP00000379051; ENSG00000146676.
DR GeneID; 5814; -.
DR KEGG; hsa:5814; -.
DR UCSC; uc003tme.3; human.
DR CTD; 5814; -.
DR GeneCards; GC07M044882; -.
DR H-InvDB; HIX0034001; -.
DR HGNC; HGNC:9702; PURB.
DR HPA; HPA048766; -.
DR MIM; 608887; gene.
DR neXtProt; NX_Q96QR8; -.
DR PharmGKB; PA34046; -.
DR eggNOG; NOG312871; -.
DR HOGENOM; HOG000232132; -.
DR HOVERGEN; HBG006888; -.
DR InParanoid; Q96QR8; -.
DR OMA; KENVRGR; -.
DR OrthoDB; EOG78D7M4; -.
DR PhylomeDB; Q96QR8; -.
DR ChiTaRS; PURB; human.
DR GeneWiki; PURB; -.
DR GenomeRNAi; 5814; -.
DR NextBio; 22646; -.
DR PRO; PR:Q96QR8; -.
DR Bgee; Q96QR8; -.
DR CleanEx; HS_PURB; -.
DR Genevestigator; Q96QR8; -.
DR GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; NAS:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR006628; PUR_DNA_RNA-bd.
DR PANTHER; PTHR12611; PTHR12611; 1.
DR Pfam; PF04845; PurA; 1.
DR SMART; SM00712; PUR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 312 Transcriptional activator protein Pur-
FT beta.
FT /FTId=PRO_0000225615.
FT DNA_BIND 28 254 By similarity.
FT COMPBIAS 153 222 Gly-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 6 6 Phosphoserine.
FT MOD_RES 8 8 Phosphoserine.
FT MOD_RES 31 31 Phosphothreonine (By similarity).
FT MOD_RES 101 101 Phosphoserine.
FT MOD_RES 298 298 Phosphoserine.
FT MOD_RES 304 304 Phosphoserine.
SQ SEQUENCE 312 AA; 33241 MW; E39E84E8D2957A18 CRC64;
MADGDSGSER GGGGGPCGFQ PASRGGGEQE TQELASKRLD IQNKRFYLDV KQNAKGRFLK
IAEVGAGGSK SRLTLSMAVA AEFRDSLGDF IEHYAQLGPS SPEQLAAGAE EGGGPRRALK
SEFLVRENRK YYLDLKENQR GRFLRIRQTV NRGGGGFGAG PGPGGLQSGQ TIALPAQGLI
EFRDALAKLI DDYGGEDDEL AGGPGGGAGG PGGGLYGELP EGTSITVDSK RFFFDVGCNK
YGVFLRVSEV KPSYRNAITV PFKAWGKFGG AFCRYADEMK EIQERQRDKL YERRGGGSGG
GEESEGEEVD ED
//
MIM
608887
*RECORD*
*FIELD* NO
608887
*FIELD* TI
*608887 PURINE-RICH ELEMENT-BINDING PROTEIN B; PURB
;;PUR-BETA
*FIELD* TX
CLONING
read more
By probing a HeLa cell cDNA library with a fragment of the PURA (600473)
sequence, Bergemann et al. (1992) identified a partial sequence of a
homologous cDNA, designated PURB, encoding a protein with a 23-amino
acid class I motif and an amphipathic helix similar to those found in
PURA.
Kelm et al. (1997) cloned mouse Purb (p44) and Pura (p46) and identified
them as the 2 components of the previously designated vascular actin
single-stranded DNA-binding factor-2, which specifically bound to
purine-rich regions within an enhancer and an exon of vascular actin
(Kelm et al., 1996). Like Pura, the deduced 324-amino acid Purb protein
contains class I and class II repeats and a 23-amino acid PSYC motif
that is homologous to the Rb-binding region of SV-40 large T antigen.
Purb differs from Pura in that the second class II repeat is interrupted
by a glycine-rich region, the N-terminal glycine-rich region is
interrupted by a 6-amino acid region, and there is no glutamine-rich
C-terminal region.
*FIELD* RF
1. Bergemann, A. D.; Ma, Z.-W.; Johnson, E. M.: Sequence of cDNA
comprising the human PUR gene and sequence-specific single-stranded-DNA-binding
properties of the encoded protein. Molec. Cell. Biol. 12: 5673-5682,
1992.
2. Kelm, R. J., Jr.; Elder, P. K.; Strauch, A. R.; Getz, M. J.: Sequence
of cDNAs encoding components of vascular actin single-stranded DNA-binding
factor 2 establish identity to Pur-alpha and Pur-beta. J. Biol. Chem. 272:
26727-26733, 1997.
3. Kelm, R. J., Jr.; Sun, S.; Strauch, A. R.; Getz, M. J.: Repression
of transcriptional enhancer factor-1 and activator protein-1-dependent
enhancer activity by vascular actin single-stranded DNA binding factor
2. J. Biol. Chem. 271: 24278-24285, 1996.
*FIELD* CD
Laura L. Baxter: 8/30/2004
*FIELD* ED
carol: 09/01/2004
carol: 8/31/2004
*RECORD*
*FIELD* NO
608887
*FIELD* TI
*608887 PURINE-RICH ELEMENT-BINDING PROTEIN B; PURB
;;PUR-BETA
*FIELD* TX
CLONING
read more
By probing a HeLa cell cDNA library with a fragment of the PURA (600473)
sequence, Bergemann et al. (1992) identified a partial sequence of a
homologous cDNA, designated PURB, encoding a protein with a 23-amino
acid class I motif and an amphipathic helix similar to those found in
PURA.
Kelm et al. (1997) cloned mouse Purb (p44) and Pura (p46) and identified
them as the 2 components of the previously designated vascular actin
single-stranded DNA-binding factor-2, which specifically bound to
purine-rich regions within an enhancer and an exon of vascular actin
(Kelm et al., 1996). Like Pura, the deduced 324-amino acid Purb protein
contains class I and class II repeats and a 23-amino acid PSYC motif
that is homologous to the Rb-binding region of SV-40 large T antigen.
Purb differs from Pura in that the second class II repeat is interrupted
by a glycine-rich region, the N-terminal glycine-rich region is
interrupted by a 6-amino acid region, and there is no glutamine-rich
C-terminal region.
*FIELD* RF
1. Bergemann, A. D.; Ma, Z.-W.; Johnson, E. M.: Sequence of cDNA
comprising the human PUR gene and sequence-specific single-stranded-DNA-binding
properties of the encoded protein. Molec. Cell. Biol. 12: 5673-5682,
1992.
2. Kelm, R. J., Jr.; Elder, P. K.; Strauch, A. R.; Getz, M. J.: Sequence
of cDNAs encoding components of vascular actin single-stranded DNA-binding
factor 2 establish identity to Pur-alpha and Pur-beta. J. Biol. Chem. 272:
26727-26733, 1997.
3. Kelm, R. J., Jr.; Sun, S.; Strauch, A. R.; Getz, M. J.: Repression
of transcriptional enhancer factor-1 and activator protein-1-dependent
enhancer activity by vascular actin single-stranded DNA binding factor
2. J. Biol. Chem. 271: 24278-24285, 1996.
*FIELD* CD
Laura L. Baxter: 8/30/2004
*FIELD* ED
carol: 09/01/2004
carol: 8/31/2004