Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Transcriptional activator protein Pur-beta  

UniProtKB / Swiss-Prot ID :  PURB_HUMAN

Gene Name (Synonyms) : 
PURB  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  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. 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 similarity). 

Protein Sequence MADGDSGSERGGGGGPCGFQPASRGGGEQETQELASKRLDIQNKRFYLDVKQNAKGRFLKIAEVGAGGSK...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHCCCCCCEEEEEEEECCCCCEEEEEEEECCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MADGDS
---CCCCCC
29.50UniProtKB
Link-
6PhosphoserineADGDSGSER
CCCCCCCCC
50.15HPRD
Link-
6PhosphoserineADGDSGSER
CCCCCCCCC
50.15Phosphositeplus
Link-
6PhosphoserineADGDSGSER
CCCCCCCCC
50.15SysPTM
Link-
6Phosphoserine.ADGDSGSER
CCCCCCCCC
50.15UniProtKB
Link-
8PhosphoserineGDSGSERGG
CCCCCCCCC
28.24HPRD
Link-
8PhosphoserineGDSGSERGG
CCCCCCCCC
28.24PhosphoELM
Link-
8PhosphoserineGDSGSERGG
CCCCCCCCC
28.24Phosphositeplus
Link-
8PhosphoserineGDSGSERGG
CCCCCCCCC
28.24SysPTM
Link-
8Phosphoserine.GDSGSERGG
CCCCCCCCC
28.24UniProtKB
Link-
100PhosphoserineQLGPSSPEQ
HCCCCCCHH
57.64HPRD
Link-
100PhosphoserineQLGPSSPEQ
HCCCCCCHH
57.64Phosphositeplus
Link-
100PhosphoserineQLGPSSPEQ
HCCCCCCHH
57.64SysPTM
Link-
101PhosphoserineLGPSSPEQL
CCCCCCHHH
35.27HPRD
Link-
101PhosphoserineLGPSSPEQL
CCCCCCHHH
35.27PhosphoELM
Link-
101PhosphoserineLGPSSPEQL
CCCCCCHHH
35.27Phosphositeplus
Link-
101PhosphoserineLGPSSPEQL
CCCCCCHHH
35.27SysPTM
Link-
101Phosphoserine.LGPSSPEQL
CCCCCCHHH
35.27UniProtKB
Link-
298PhosphoserineRGGGSGGGE
CCCCCCCCC
37.22HPRD
Link-
298PhosphoserineRGGGSGGGE
CCCCCCCCC
37.22PhosphoELM
Link-
298PhosphoserineRGGGSGGGE
CCCCCCCCC
37.22Phosphositeplus
Link-
298PhosphoserineRGGGSGGGE
CCCCCCCCC
37.22SysPTM
Link-
298Phosphoserine.RGGGSGGGE
CCCCCCCCC
37.22UniProtKB
Link-
304PhosphoserineGGEESEGEE
CCCCCCCCC
46.75HPRD
Link-
304PhosphoserineGGEESEGEE
CCCCCCCCC
46.75PhosphoELM
Link-
304PhosphoserineGGEESEGEE
CCCCCCCCC
46.75Phosphositeplus
Link-
304PhosphoserineGGEESEGEE
CCCCCCCCC
46.75SysPTM
Link-
304Phosphoserine.GGEESEGEE
CCCCCCCCC
46.75UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PURA_HUMANin vitro
in vivo
HPRD:12325HPRD10318844
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6 AND SER-8, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-298 ANDSER-304, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6 AND SER-8, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-298 ANDSER-304, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-8; SER-298 ANDSER-304, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures