PURB_RAT
ID PURB_RAT Reviewed; 315 AA.
AC Q68A21;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Transcriptional activator protein Pur-beta;
DE AltName: Full=Purine-rich element-binding protein B;
GN Name=Purb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=16309856; DOI=10.1016/j.gene.2005.09.006;
RA Li F., Kato I., Kawaguchi H., Takasawa K., Hibino Y., Hiraga K.;
RT "The galectin-3 gene promoter binding proteins in the liver of rats 48-h
RT post-treatment with CCl(4).";
RL Gene 367:46-55(2006).
RN [2]
RP PROTEIN SEQUENCE OF 49-54; 76-87; 124-129; 235-249; 259-266 AND 271-288,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP FUNCTION.
RX PubMed=11032866; DOI=10.1046/j.1471-4159.2000.0751781.x;
RA Ohashi S., Kobayashi S., Omori A., Ohara S., Omae A., Muramatsu T., Li Y.,
RA Anzai K.;
RT "The single-stranded DNA- and RNA-binding proteins pur alpha and pur beta
RT link BC1 RNA to microtubules through binding to the dendrite-targeting RNA
RT motifs.";
RL J. Neurochem. 75:1781-1790(2000).
RN [4]
RP FUNCTION, AND 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 chain
RT gene and control transcriptional and translational regulation of the gene
RT expression. Implications in the repression of alpha-myosin heavy chain
RT during heart failure.";
RL J. Biol. Chem. 278:44935-44948(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-301 AND SER-307, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Plays a role in the control of vascular
CC smooth muscle (VSM) alpha-actin gene transcription as repressor in
CC myoblasts and fibroblasts (By similarity). Participates in
CC transcriptional and translational regulation of alpha-MHC expression in
CC cardiac myocytes by binding to the purine-rich negative regulatory
CC (PNR) element. Modulates constitutive liver galectin-3 gene
CC transcription by binding to its promoter. May play a role in the
CC dendritic transport of a subset of mRNAs. {ECO:0000250,
CC ECO:0000269|PubMed:11032866, ECO:0000269|PubMed:12933792,
CC ECO:0000269|PubMed:16309856}.
CC -!- SUBUNIT: Homodimer, heterodimer with PURA and heterotrimer with PURA
CC and YBX1/Y-box protein 1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in muscle cells and in the liver.
CC {ECO:0000269|PubMed:12933792, ECO:0000269|PubMed:16309856}.
CC -!- INDUCTION: Induced in the liver 48 hours after tetrachloromethane
CC (CCL4) administration. {ECO:0000269|PubMed:16309856}.
CC -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
CC {ECO:0000305}.
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DR EMBL; AB182574; BAD38899.1; -; mRNA.
DR RefSeq; NP_001017503.1; NM_001017503.1.
DR AlphaFoldDB; Q68A21; -.
DR SMR; Q68A21; -.
DR BioGRID; 269717; 5.
DR IntAct; Q68A21; 1.
DR MINT; Q68A21; -.
DR STRING; 10116.ENSRNOP00000009214; -.
DR iPTMnet; Q68A21; -.
DR PhosphoSitePlus; Q68A21; -.
DR jPOST; Q68A21; -.
DR PaxDb; Q68A21; -.
DR PeptideAtlas; Q68A21; -.
DR PRIDE; Q68A21; -.
DR GeneID; 498407; -.
DR KEGG; rno:498407; -.
DR UCSC; RGD:1559465; rat.
DR CTD; 5814; -.
DR RGD; 1559465; Purb.
DR eggNOG; KOG3074; Eukaryota.
DR InParanoid; Q68A21; -.
DR OrthoDB; 1248813at2759; -.
DR PhylomeDB; Q68A21; -.
DR PRO; PR:Q68A21; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IDA:HGNC-UCL.
DR GO; GO:0032422; F:purine-rich negative regulatory element binding; IDA:HGNC-UCL.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:HGNC-UCL.
DR GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:HGNC-UCL.
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:0000250|UniProtKB:Q96QR8"
FT CHAIN 2..315
FT /note="Transcriptional activator protein Pur-beta"
FT /id="PRO_0000225617"
FT DNA_BIND 28..254
FT /evidence="ECO:0000250"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q96QR8"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QR8"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QR8"
FT MOD_RES 23
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35295"
FT MOD_RES 34
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O35295"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 155
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35295"
FT MOD_RES 270
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35295"
FT MOD_RES 297
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35295"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 315 AA; 33418 MW; 0EC268D1EC3E513B CRC64;
MADGDSGSER GGGGPGSFQP APRGGGGPGG EQETQELASK RLDIQNKRFY LDVKQNAKGR
FLKIAEVGAG GSKSRLTLSM AVAAEFRDSL GDFIEHYAQL GPSSPEQLAA GAEEGGGPRR
ALKSEFLVRE NRKYYLDLKE NQRGRFLRIR QTVNRGGGGF GGGPGPGGLQ SGQTIALPAQ
GLIEFRDALA KLIDDYGGED DELAGGPGGG AGGPGGGLYG ELPEGTSITV DSKRFFFDVG
CNKYGVFLRV SEVKPSYRNA ITVPFKAWGK FGGAFCRYAD EMKEIQERQR DKLYERRGGG
SGGGDESEGE EVDED
