PURB_HUMAN - dbPTM
PURB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PURB_HUMAN
UniProt AC Q96QR8
Protein Name Transcriptional activator protein Pur-beta
Gene Name PURB
Organism Homo sapiens (Human).
Sequence Length 312
Subcellular Localization Nucleus .
Protein Description 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 MADGDSGSERGGGGGPCGFQPASRGGGEQETQELASKRLDIQNKRFYLDVKQNAKGRFLKIAEVGAGGSKSRLTLSMAVAAEFRDSLGDFIEHYAQLGPSSPEQLAAGAEEGGGPRRALKSEFLVRENRKYYLDLKENQRGRFLRIRQTVNRGGGGFGAGPGPGGLQSGQTIALPAQGLIEFRDALAKLIDDYGGEDDELAGGPGGGAGGPGGGLYGELPEGTSITVDSKRFFFDVGCNKYGVFLRVSEVKPSYRNAITVPFKAWGKFGGAFCRYADEMKEIQERQRDKLYERRGGGSGGGEESEGEEVDED
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MADGDSGSE
------CCCCCCCCC		29.5021406692
6Phosphorylation--MADGDSGSERGGG
--CCCCCCCCCCCCC		50.1529255136
8PhosphorylationMADGDSGSERGGGGG
CCCCCCCCCCCCCCC		28.2429255136
23PhosphorylationPCGFQPASRGGGEQE
CCCCCCCCCCCCHHH		37.8329255136
24MethylationCGFQPASRGGGEQET
CCCCCCCCCCCHHHH		50.29-
31PhosphorylationRGGGEQETQELASKR
CCCCHHHHHHHHHHH		27.3423403867
36PhosphorylationQETQELASKRLDIQN
HHHHHHHHHHHCCCC		30.8221406692
37UbiquitinationETQELASKRLDIQNK
HHHHHHHHHHCCCCC		51.9124816145
47PhosphorylationDIQNKRFYLDVKQNA
CCCCCEEEEECHHHC		13.16-
60UbiquitinationNAKGRFLKIAEVGAG
HCCCCEEEEEEECCC		36.8429967540
60MalonylationNAKGRFLKIAEVGAG
HCCCCEEEEEEECCC		36.8426320211
69PhosphorylationAEVGAGGSKSRLTLS
EEECCCCCHHHHHHH		26.92-
70UbiquitinationEVGAGGSKSRLTLSM
EECCCCCHHHHHHHH		42.76-
86PhosphorylationVAAEFRDSLGDFIEH
HHHHHHHHHHHHHHH		29.9622167270
94PhosphorylationLGDFIEHYAQLGPSS
HHHHHHHHHHHCCCC		5.3522167270
100PhosphorylationHYAQLGPSSPEQLAA
HHHHHCCCCHHHHHH		57.6422167270
101PhosphorylationYAQLGPSSPEQLAAG
HHHHCCCCHHHHHHH		35.2722167270
120UbiquitinationGGPRRALKSEFLVRE
CCHHHHHHHHEEEEC		47.13-
121PhosphorylationGPRRALKSEFLVREN
CHHHHHHHHEEEECC		34.1428857561
130UbiquitinationFLVRENRKYYLDLKE
EEEECCCEEEEECCC		50.2423000965
136UbiquitinationRKYYLDLKENQRGRF
CEEEEECCCCCCCCE		55.0423000965
136MethylationRKYYLDLKENQRGRF
CEEEEECCCCCCCCE		55.0466700475
152MethylationRIRQTVNRGGGGFGA
EEEEEECCCCCCCCC		40.5716185871
168PhosphorylationPGPGGLQSGQTIALP
CCCCCCCCCCEEEEE		37.6028857561
171PhosphorylationGGLQSGQTIALPAQG
CCCCCCCEEEEECCC		16.2528857561
241PhosphorylationFDVGCNKYGVFLRVS
EECCCCEEEEEEEEE		12.44-
251UbiquitinationFLRVSEVKPSYRNAI
EEEEEECCCCCCCCE		24.9724816145
253PhosphorylationRVSEVKPSYRNAITV
EEEECCCCCCCCEEE		30.8924719451
254NitrationVSEVKPSYRNAITVP
EEECCCCCCCCEEEC		19.20-
254PhosphorylationVSEVKPSYRNAITVP
EEECCCCCCCCEEEC		19.2028102081
263AcetylationNAITVPFKAWGKFGG
CCEEECCCHHHHCCH		36.8425953088
263UbiquitinationNAITVPFKAWGKFGG
CCEEECCCHHHHCCH		36.8423000965
267UbiquitinationVPFKAWGKFGGAFCR
ECCCHHHHCCHHHHH		30.0923000965
267AcetylationVPFKAWGKFGGAFCR
ECCCHHHHCCHHHHH		30.0925953088
280UbiquitinationCRYADEMKEIQERQR
HHHHHHHHHHHHHHH		50.0124816145
280AcetylationCRYADEMKEIQERQR
HHHHHHHHHHHHHHH		50.0123236377
291PhosphorylationERQRDKLYERRGGGS
HHHHHHHHHCCCCCC		17.0925849741
294MethylationRDKLYERRGGGSGGG
HHHHHHCCCCCCCCC		35.85-
298PhosphorylationYERRGGGSGGGEESE
HHCCCCCCCCCCCCC		37.2229255136
304PhosphorylationGSGGGEESEGEEVDE
CCCCCCCCCCCCCCC		46.7529255136
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PURB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PURB_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PURB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFC3_HUMANRFC3physical
22939629
IL7RA_HUMANIL7Rphysical
23151878
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PURB_HUMAN

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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
"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.
"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.
"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.
"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.
"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.
"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.
"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.

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