VATE2_HUMAN - dbPTM
VATE2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VATE2_HUMAN
UniProt AC Q96A05
Protein Name V-type proton ATPase subunit E 2
Gene Name ATP6V1E2
Organism Homo sapiens (Human).
Sequence Length 226
Subcellular Localization
Protein Description Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. This isoform is essential for energy coupling involved in acidification of acrosome (By similarity)..
Protein Sequence MALSDVDVKKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQTQRLKIMEYYEKKEKQIEQQKKILMSTMRNQARLKVLRARNDLISDLLSEAKLRLSRIVEDPEVYQGLLDKLVLQGLLRLLEPVMIVRCRPQDLLLVEAAVQKAIPEYMTISQKHVEVQIDKEAYLAVNAAGGVEVYSGNQRIKVSNTLESRLDLSAKQKMPEIRMALFGANTNRKFFI
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
4Phosphorylation----MALSDVDVKKQ
----CCCCHHHHHHH
26.5029255136
10UbiquitinationLSDVDVKKQIKHMMA
CCHHHHHHHHHHHHH
58.04-
332-HydroxyisobutyrylationKAEEIDAKAEEEFNI
HHHHHHHHHHHHHCC
53.21-
422-HydroxyisobutyrylationEEEFNIEKGRLVQTQ
HHHHCCCCCCCEEHH
45.60-
42UbiquitinationEEEFNIEKGRLVQTQ
HHHHCCCCCCCEEHH
45.6021906983
52AcetylationLVQTQRLKIMEYYEK
CEEHHHHHHHHHHHH
42.04178226061
56PhosphorylationQRLKIMEYYEKKEKQ
HHHHHHHHHHHHHHH
10.2724927040
57PhosphorylationRLKIMEYYEKKEKQI
HHHHHHHHHHHHHHH
14.1525884760
59UbiquitinationKIMEYYEKKEKQIEQ
HHHHHHHHHHHHHHH
50.54-
592-HydroxyisobutyrylationKIMEYYEKKEKQIEQ
HHHHHHHHHHHHHHH
50.54-
73PhosphorylationQQKKILMSTMRNQAR
HHHHHHHHHHHHHHH
18.66-
74PhosphorylationQKKILMSTMRNQARL
HHHHHHHHHHHHHHH
13.24-
96PhosphorylationDLISDLLSEAKLRLS
HHHHHHHHHHHHHHH
42.6923403867
191AcetylationYSGNQRIKVSNTLES
ECCCCEEEEECCHHH
41.63-
191UbiquitinationYSGNQRIKVSNTLES
ECCCCEEEEECCHHH
41.63-
195PhosphorylationQRIKVSNTLESRLDL
CEEEEECCHHHHHCC
25.1323403867
198PhosphorylationKVSNTLESRLDLSAK
EEECCHHHHHCCCHH
41.0523403867
203PhosphorylationLESRLDLSAKQKMPE
HHHHHCCCHHHHCHH
32.8423403867

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 VATE2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VATE2_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 VATE2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATG1_HUMANATP6V1G1physical
21516116

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 VATE2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-56, AND MASSSPECTROMETRY.

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