HAP28_MOUSE - dbPTM
HAP28_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HAP28_MOUSE
UniProt AC Q3UHX2
Protein Name 28 kDa heat- and acid-stable phosphoprotein
Gene Name Pdap1
Organism Mus musculus (Mouse).
Sequence Length 181
Subcellular Localization
Protein Description
Protein Sequence MPKGGRKGGHKGRVRQYTSPEEIDAQLQAEKQKANEEDEQEEGGDGASGDPKKEKKSLDSDESEDEDDDYQQKRKGVEGLIDIENPNRVAQTTKKVTQLDLDGPKELSRREREEIEKQKAKERYMKMHLAGKTEQAKADLARLAIIRKQREEAARKKEEERKAKDDATLSGKRMQSLSLNK
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
17PhosphorylationHKGRVRQYTSPEEID
CCCCCCCCCCHHHHH
9.9123984901
18PhosphorylationKGRVRQYTSPEEIDA
CCCCCCCCCHHHHHH
29.4825521595
19PhosphorylationGRVRQYTSPEEIDAQ
CCCCCCCCHHHHHHH
25.9425521595
48PhosphorylationEEGGDGASGDPKKEK
HCCCCCCCCCCHHHH
49.6225521595
52AcetylationDGASGDPKKEKKSLD
CCCCCCCHHHHCCCC
77.6012563341
53AcetylationGASGDPKKEKKSLDS
CCCCCCHHHHCCCCC
78.9612649943
57PhosphorylationDPKKEKKSLDSDESE
CCHHHHCCCCCCCCC
48.7727087446
60PhosphorylationKEKKSLDSDESEDED
HHHCCCCCCCCCCCC
48.8727087446
63PhosphorylationKSLDSDESEDEDDDY
CCCCCCCCCCCCCHH
56.1727087446
70PhosphorylationSEDEDDDYQQKRKGV
CCCCCCHHHHHHHCC
21.6027149854
95MalonylationRVAQTTKKVTQLDLD
HHHHCCCEEEECCCC
48.7126320211
97PhosphorylationAQTTKKVTQLDLDGP
HHCCCEEEECCCCCH
32.0929514104
108PhosphorylationLDGPKELSRREREEI
CCCHHHHCHHHHHHH
30.31-
126MethylationKAKERYMKMHLAGKT
HHHHHHHHHHHCCCH
17.77-
132MalonylationMKMHLAGKTEQAKAD
HHHHHCCCHHHHHHH
43.1926320211
132AcetylationMKMHLAGKTEQAKAD
HHHHHCCCHHHHHHH
43.1923806337
137MalonylationAGKTEQAKADLARLA
CCCHHHHHHHHHHHH
41.9726320211
164AcetylationKEEERKAKDDATLSG
HHHHHHHHHHCCCCC
60.2123806337
168PhosphorylationRKAKDDATLSGKRMQ
HHHHHHCCCCCHHHH
28.5722817900
170PhosphorylationAKDDATLSGKRMQSL
HHHHCCCCCHHHHHH
37.6026824392
172AcetylationDDATLSGKRMQSLSL
HHCCCCCHHHHHHCC
41.1269133
176PhosphorylationLSGKRMQSLSLNK--
CCCHHHHHHCCCC--
15.5827087446
178PhosphorylationGKRMQSLSLNK----
CHHHHHHCCCC----
34.8328725479

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 HAP28_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HAP28_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 HAP28_MOUSE !!

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

Oops, there are no PPI records of HAP28_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HAP28_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-63 AND TYR-70,AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-63, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60 AND SER-63,AND MASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60 AND SER-63,AND MASS SPECTROMETRY.
"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-48 AND SER-63, AND MASSSPECTROMETRY.

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