VATE1_HUMAN - dbPTM
VATE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VATE1_HUMAN
UniProt AC P36543
Protein Name V-type proton ATPase subunit E 1
Gene Name ATP6V1E1
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..
Protein Sequence MALSDADVQKQIKHMMAFIEQEANEKAEEIDAKAEEEFNIEKGRLVQTQRLKIMEYYEKKEKQIEQQKKIQMSNLMNQARLKVLRARDDLITDLLNEAKQRLSKVVKDTTRYQVLLDGLVLQGLYQLLEPRMIVRCRKQDFPLVKAAVQKAIPMYKIATKNDVDVQIDQESYLPEDIAGGVEIYNGDRKIKVSNTLESRLDLIAQQMMPEVRGALFGANANRKFLD
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------MALSDADVQ
------CCCCHHHHH
18.7725944712
4Phosphorylation----MALSDADVQKQ
----CCCCHHHHHHH
22.6324719451
10AcetylationLSDADVQKQIKHMMA
CCHHHHHHHHHHHHH
54.5625953088
10UbiquitinationLSDADVQKQIKHMMA
CCHHHHHHHHHHHHH
54.56-
42UbiquitinationEEEFNIEKGRLVQTQ
HHHHCCCCCCCHHHH
45.6021906983
52MalonylationLVQTQRLKIMEYYEK
CHHHHHHHHHHHHHH
42.0432601280
52AcetylationLVQTQRLKIMEYYEK
CHHHHHHHHHHHHHH
42.0422424773
56PhosphorylationQRLKIMEYYEKKEKQ
HHHHHHHHHHHHHHH
10.2721082442
57PhosphorylationRLKIMEYYEKKEKQI
HHHHHHHHHHHHHHH
14.1525884760
59MalonylationKIMEYYEKKEKQIEQ
HHHHHHHHHHHHHHH
50.5426320211
59AcetylationKIMEYYEKKEKQIEQ
HHHHHHHHHHHHHHH
50.5425953088
59UbiquitinationKIMEYYEKKEKQIEQ
HHHHHHHHHHHHHHH
50.54-
69UbiquitinationKQIEQQKKIQMSNLM
HHHHHHHHHCHHHHH
33.56-
72SulfoxidationEQQKKIQMSNLMNQA
HHHHHHCHHHHHHHH
3.0621406390
76SulfoxidationKIQMSNLMNQARLKV
HHCHHHHHHHHHHHH
4.0130846556
99UbiquitinationTDLLNEAKQRLSKVV
HHHHHHHHHHHHHHH
29.76-
103PhosphorylationNEAKQRLSKVVKDTT
HHHHHHHHHHHCCCC
26.12-
138UbiquitinationRMIVRCRKQDFPLVK
CEEEEECCCCCHHHH
58.82-
138MalonylationRMIVRCRKQDFPLVK
CEEEEECCCCCHHHH
58.8226320211
145UbiquitinationKQDFPLVKAAVQKAI
CCCCHHHHHHHHHHC
38.01-
145MalonylationKQDFPLVKAAVQKAI
CCCCHHHHHHHHHHC
38.0126320211
156UbiquitinationQKAIPMYKIATKNDV
HHHCCHHHCCCCCCC
21.44-
156AcetylationQKAIPMYKIATKNDV
HHHCCHHHCCCCCCC
21.4425953088
191UbiquitinationYNGDRKIKVSNTLES
ECCCCEEEECCCHHH
42.52-
191AcetylationYNGDRKIKVSNTLES
ECCCCEEEECCCHHH
42.5223749302
193O-linked_GlycosylationGDRKIKVSNTLESRL
CCCEEEECCCHHHHH
21.0630379171
207SulfoxidationLDLIAQQMMPEVRGA
HHHHHHHHCHHHHHH
3.0021406390
208SulfoxidationDLIAQQMMPEVRGAL
HHHHHHHCHHHHHHH
1.9130846556

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 VATE1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VATE1_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 VATE1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC6_HUMANXRCC6physical
16169070
VATG1_HUMANATP6V1G1physical
16169070
ALDOA_HUMANALDOAphysical
11399750
ALDOB_HUMANALDOBphysical
11399750
ALDOC_HUMANALDOCphysical
11399750
A4_HUMANAPPphysical
21832049
VATG1_HUMANATP6V1G1physical
22939629
VATH_HUMANATP6V1Hphysical
22939629
VPP1_HUMANATP6V0A1physical
22939629
VATF_HUMANATP6V1Fphysical
22939629
VPP3_HUMANTCIRG1physical
22939629
YBOX1_HUMANYBX1physical
22939629
XPP1_HUMANXPNPEP1physical
22939629
ZFR_HUMANZFRphysical
22939629
ZN827_HUMANZNF827physical
22939629
ZNT5_HUMANSLC30A5physical
22939629
YES_HUMANYES1physical
22939629
SAMH1_HUMANSAMHD1physical
22863883
AT1B1_HUMANATP1B1physical
26344197
VATA_HUMANATP6V1Aphysical
26344197
VATB2_HUMANATP6V1B2physical
26344197
VATD_HUMANATP6V1Dphysical
26344197
VATF_HUMANATP6V1Fphysical
26344197
VATH_HUMANATP6V1Hphysical
26344197
COX41_HUMANCOX4I1physical
26344197
NDUS8_HUMANNDUFS8physical
26344197
TMOD2_HUMANTMOD2physical
26344197

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 VATE1_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, AND MASS SPECTROMETRY.
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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