PRVA_MOUSE - dbPTM
PRVA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRVA_MOUSE
UniProt AC P32848
Protein Name Parvalbumin alpha
Gene Name Pvalb
Organism Mus musculus (Mouse).
Sequence Length 110
Subcellular Localization
Protein Description In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions..
Protein Sequence MSMTDVLSAEDIKKAIGAFAAADSFDHKKFFQMVGLKKKNPDEVKKVFHILDKDKSGFIEEDELGSILKGFSSDARDLSAKETKTLLAAGDKDGDGKIGVEEFSTLVAES
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------MSMTDVLSA
------CCHHHCCCH
30.3210036163
2Phosphorylation------MSMTDVLSA
------CCHHHCCCH
30.3222210690
4Phosphorylation----MSMTDVLSAED
----CCHHHCCCHHH
18.6922210690
8PhosphorylationMSMTDVLSAEDIKKA
CCHHHCCCHHHHHHH
29.4722817900
14UbiquitinationLSAEDIKKAIGAFAA
CCHHHHHHHHHHHHH
45.6422790023
24PhosphorylationGAFAAADSFDHKKFF
HHHHHCCCCCHHHHH
28.0428464351
28UbiquitinationAADSFDHKKFFQMVG
HCCCCCHHHHHHHHC
53.7922790023
28AcetylationAADSFDHKKFFQMVG
HCCCCCHHHHHHHHC
53.7921728379
29AcetylationADSFDHKKFFQMVGL
CCCCCHHHHHHHHCC
48.2521728379
29UbiquitinationADSFDHKKFFQMVGL
CCCCCHHHHHHHHCC
48.2522790023
37AcetylationFFQMVGLKKKNPDEV
HHHHHCCCCCCHHHH
56.6321728379
37UbiquitinationFFQMVGLKKKNPDEV
HHHHHCCCCCCHHHH
56.6322790023
39UbiquitinationQMVGLKKKNPDEVKK
HHHCCCCCCHHHHHH
72.61-
46UbiquitinationKNPDEVKKVFHILDK
CCHHHHHHHHHHHCC
56.1422790023
53UbiquitinationKVFHILDKDKSGFIE
HHHHHHCCCCCCCCC
64.7122790023
53AcetylationKVFHILDKDKSGFIE
HHHHHHCCCCCCCCC
64.7121728379
55UbiquitinationFHILDKDKSGFIEED
HHHHCCCCCCCCCHH
59.2122790023
55AcetylationFHILDKDKSGFIEED
HHHHCCCCCCCCCHH
59.2121728379
56PhosphorylationHILDKDKSGFIEEDE
HHHCCCCCCCCCHHH
49.4122210690
66PhosphorylationIEEDELGSILKGFSS
CCHHHHHHHHHHCCC
37.0522210690
69UbiquitinationDELGSILKGFSSDAR
HHHHHHHHHCCCCHH
57.1322790023
69AcetylationDELGSILKGFSSDAR
HHHHHHHHHCCCCHH
57.1321728379
72PhosphorylationGSILKGFSSDARDLS
HHHHHHCCCCHHHCC
35.6622817900
73PhosphorylationSILKGFSSDARDLSA
HHHHHCCCCHHHCCH
32.7817203969
79PhosphorylationSSDARDLSAKETKTL
CCCHHHCCHHHHHHH
41.4017203969
81UbiquitinationDARDLSAKETKTLLA
CHHHCCHHHHHHHHH
63.6422790023
83PhosphorylationRDLSAKETKTLLAAG
HHCCHHHHHHHHHCC
28.7317203969
84UbiquitinationDLSAKETKTLLAAGD
HCCHHHHHHHHHCCC
37.9622790023
85PhosphorylationLSAKETKTLLAAGDK
CCHHHHHHHHHCCCC
34.1322210690
92UbiquitinationTLLAAGDKDGDGKIG
HHHHCCCCCCCCCCC
63.7922790023
97UbiquitinationGDKDGDGKIGVEEFS
CCCCCCCCCCHHHHH
40.8122790023
105PhosphorylationIGVEEFSTLVAES--
CCHHHHHHHHCCC--
30.49-
110PhosphorylationFSTLVAES-------
HHHHHCCC-------
35.4722210690

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 PRVA_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 PRVA_MOUSE !!

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

Oops, there are no PPI records of PRVA_MOUSE !!

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

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Electrospray ionization mass spectrometry: analysis of the Ca2+-binding properties of human recombinant alpha-parvalbumin and ninemutant proteins.";
Troxler H., Kuster T., Rhyner J.A., Gehrig P., Heizmann C.W.;
Anal. Biochem. 268:64-71(1999).
Cited for: SEQUENCE REVISION TO 110, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-79 AND THR-83,AND MASS SPECTROMETRY.

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