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Protein

Transcriptional activator protein Pur-beta

Gene

Purb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has capacity to bind repeated elements in single-stranded DNA such as the purine-rich single strand of the PUR element located upstream of the MYC gene. Plays a role in the control of vascular smooth muscle (VSM) alpha-actin gene transcription as repressor in myoblasts and fibroblasts (By similarity). Participates in transcriptional and translational regulation of alpha-MHC expression in cardiac myocytes by binding to the purine-rich negative regulatory (PNR) element. Modulates constitutive liver galectin-3 gene transcription by binding to its promoter. May play a role in the dendritic transport of a subset of mRNAs.By similarity3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi28 – 254227By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional activator protein Pur-beta
Alternative name(s):
Purine-rich element-binding protein B
Gene namesi
Name:Purb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1559465. Purb.

Subcellular locationi

GO - Cellular componenti

  • DNA replication factor A complex Source: UniProtKB
  • nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 315314Transcriptional activator protein Pur-betaPRO_0000225617Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei8 – 81PhosphoserineBy similarity
Modified residuei34 – 341PhosphothreonineBy similarity
Modified residuei104 – 1041PhosphoserineCombined sources
Modified residuei270 – 2701N6-acetyllysineBy similarity
Modified residuei301 – 3011PhosphoserineCombined sources
Modified residuei307 – 3071PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ68A21.
PRIDEiQ68A21.

PTM databases

iPTMnetiQ68A21.
PhosphoSiteiQ68A21.

Expressioni

Tissue specificityi

Expressed in muscle cells and in the liver.2 Publications

Inductioni

Induced in the liver 48 hours after tetrachloromethane (CCL4) administration.1 Publication

Interactioni

Subunit structurei

Homodimer, heterodimer with PURA and heterotrimer with PURA and YBX1/Y-box protein 1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi269717. 2 interactions.
STRINGi10116.ENSRNOP00000009214.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi24 – 307Poly-Gly
Compositional biasi156 – 22570Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the PUR DNA-binding protein family.Curated

Phylogenomic databases

eggNOGiKOG3074. Eukaryota.
ENOG410ZKKR. LUCA.
HOGENOMiHOG000232132.
HOVERGENiHBG006888.
InParanoidiQ68A21.
PhylomeDBiQ68A21.

Family and domain databases

InterProiIPR006628. PUR-bd_fam.
IPR030499. PURbeta.
[Graphical view]
PANTHERiPTHR12611. PTHR12611. 1 hit.
PTHR12611:SF4. PTHR12611:SF4. 1 hit.
PfamiPF04845. PurA. 1 hit.
[Graphical view]
SMARTiSM00712. PUR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q68A21-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADGDSGSER GGGGPGSFQP APRGGGGPGG EQETQELASK RLDIQNKRFY
60 70 80 90 100
LDVKQNAKGR FLKIAEVGAG GSKSRLTLSM AVAAEFRDSL GDFIEHYAQL
110 120 130 140 150
GPSSPEQLAA GAEEGGGPRR ALKSEFLVRE NRKYYLDLKE NQRGRFLRIR
160 170 180 190 200
QTVNRGGGGF GGGPGPGGLQ SGQTIALPAQ GLIEFRDALA KLIDDYGGED
210 220 230 240 250
DELAGGPGGG AGGPGGGLYG ELPEGTSITV DSKRFFFDVG CNKYGVFLRV
260 270 280 290 300
SEVKPSYRNA ITVPFKAWGK FGGAFCRYAD EMKEIQERQR DKLYERRGGG
310
SGGGDESEGE EVDED
Length:315
Mass (Da):33,418
Last modified:January 23, 2007 - v3
Checksum:i0EC268D1EC3E513B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB182574 mRNA. Translation: BAD38899.1.
RefSeqiNP_001017503.1. NM_001017503.1.
UniGeneiRn.156213.

Genome annotation databases

GeneIDi498407.
KEGGirno:498407.
UCSCiRGD:1559465. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB182574 mRNA. Translation: BAD38899.1.
RefSeqiNP_001017503.1. NM_001017503.1.
UniGeneiRn.156213.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi269717. 2 interactions.
STRINGi10116.ENSRNOP00000009214.

PTM databases

iPTMnetiQ68A21.
PhosphoSiteiQ68A21.

Proteomic databases

PaxDbiQ68A21.
PRIDEiQ68A21.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi498407.
KEGGirno:498407.
UCSCiRGD:1559465. rat.

Organism-specific databases

CTDi5814.
RGDi1559465. Purb.

Phylogenomic databases

eggNOGiKOG3074. Eukaryota.
ENOG410ZKKR. LUCA.
HOGENOMiHOG000232132.
HOVERGENiHBG006888.
InParanoidiQ68A21.
PhylomeDBiQ68A21.

Miscellaneous databases

NextBioi699705.
PROiQ68A21.

Family and domain databases

InterProiIPR006628. PUR-bd_fam.
IPR030499. PURbeta.
[Graphical view]
PANTHERiPTHR12611. PTHR12611. 1 hit.
PTHR12611:SF4. PTHR12611:SF4. 1 hit.
PfamiPF04845. PurA. 1 hit.
[Graphical view]
SMARTiSM00712. PUR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The galectin-3 gene promoter binding proteins in the liver of rats 48-h post-treatment with CCl(4)."
    Li F., Kato I., Kawaguchi H., Takasawa K., Hibino Y., Hiraga K.
    Gene 367:46-55(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY.
  2. Lubec G., Diao W., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 49-54; 76-87; 124-129; 235-249; 259-266 AND 271-288, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  3. "The single-stranded DNA- and RNA-binding proteins pur alpha and pur beta link BC1 RNA to microtubules through binding to the dendrite-targeting RNA motifs."
    Ohashi S., Kobayashi S., Omori A., Ohara S., Omae A., Muramatsu T., Li Y., Anzai K.
    J. Neurochem. 75:1781-1790(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. "Single-stranded DNA-binding proteins PURalpha and PURbeta bind to a purine-rich negative regulatory element of the alpha-myosin heavy chain gene and control transcriptional and translational regulation of the gene expression. Implications in the repression of alpha-myosin heavy chain during heart failure."
    Gupta M., Sueblinvong V., Raman J., Jeevanandam V., Gupta M.P.
    J. Biol. Chem. 278:44935-44948(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-301 AND SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPURB_RAT
AccessioniPrimary (citable) accession number: Q68A21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 85 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.