PURB_RAT - dbPTM
PURB_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PURB_RAT
UniProt AC Q68A21
Protein Name Transcriptional activator protein Pur-beta
Gene Name Purb
Organism Rattus norvegicus (Rat).
Sequence Length 315
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 (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..
Protein Sequence MADGDSGSERGGGGPGSFQPAPRGGGGPGGEQETQELASKRLDIQNKRFYLDVKQNAKGRFLKIAEVGAGGSKSRLTLSMAVAAEFRDSLGDFIEHYAQLGPSSPEQLAAGAEEGGGPRRALKSEFLVRENRKYYLDLKENQRGRFLRIRQTVNRGGGGFGGGPGPGGLQSGQTIALPAQGLIEFRDALAKLIDDYGGEDDELAGGPGGGAGGPGGGLYGELPEGTSITVDSKRFFFDVGCNKYGVFLRVSEVKPSYRNAITVPFKAWGKFGGAFCRYADEMKEIQERQRDKLYERRGGGSGGGDESEGEEVDED
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
29.50-
6Phosphorylation--MADGDSGSERGGG
--CCCCCCCCCCCCC
50.1527097102
8PhosphorylationMADGDSGSERGGGGP
CCCCCCCCCCCCCCC
28.2427097102
17PhosphorylationRGGGGPGSFQPAPRG
CCCCCCCCCCCCCCC
24.6827097102
23MethylationGSFQPAPRGGGGPGG
CCCCCCCCCCCCCCC
59.50-
34PhosphorylationGPGGEQETQELASKR
CCCCHHHHHHHHHHH
27.34-
54AcetylationKRFYLDVKQNAKGRF
CEEEEECHHHCCCCE
37.1922902405
63AcetylationNAKGRFLKIAEVGAG
HCCCCEEEEEEECCC
36.8422902405
89PhosphorylationVAAEFRDSLGDFIEH
HHHHHHHHHHHHHHH
29.9628689409
103PhosphorylationHYAQLGPSSPEQLAA
HHHHHCCCCHHHHHH
57.6427097102
104PhosphorylationYAQLGPSSPEQLAAG
HHHHCCCCHHHHHHH
35.2723712012
124PhosphorylationGPRRALKSEFLVREN
CHHHHHHHHEEEECC
34.1425575281
133AcetylationFLVRENRKYYLDLKE
EEEECCCEEEEECCC
50.2472589035
139AcetylationRKYYLDLKENQRGRF
CEEEEECCCCCCCCE
55.0422902405
155MethylationRIRQTVNRGGGGFGG
EEEEEECCCCCCCCC
40.5716185873
266AcetylationNAITVPFKAWGKFGG
CCEEECCCHHHHCCH
36.8422902405
270AcetylationVPFKAWGKFGGAFCR
ECCCHHHHCCHHHHH
30.0922902405
283AcetylationCRYADEMKEIQERQR
HHHHHHHHHHHHHHH
50.0122902405
292AcetylationIQERQRDKLYERRGG
HHHHHHHHHHHCCCC
55.9822902405
297MethylationRDKLYERRGGGSGGG
HHHHHHCCCCCCCCC
35.85-
301PhosphorylationYERRGGGSGGGDESE
HHCCCCCCCCCCHHC
37.2229779826
307PhosphorylationGSGGGDESEGEEVDE
CCCCCCHHCCCCCCC
56.4923712012

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_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PURB_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PURB_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PURB_RAT

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Related Literatures of Post-Translational Modification

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