VATE_YEAST - dbPTM
VATE_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VATE_YEAST
UniProt AC P22203
Protein Name V-type proton ATPase subunit E
Gene Name VMA4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 233
Subcellular Localization Vacuole membrane
Peripheral membrane protein .
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 MSSAITALTPNQVNDELNKMQAFIRKEAEEKAKEIQLKADQEYEIEKTNIVRNETNNIDGNFKSKLKKAMLSQQITKSTIANKMRLKVLSAREQSLDGIFEETKEKLSGIANNRDEYKPILQSLIVEALLKLLEPKAIVKALERDVDLIESMKDDIMREYGEKAQRAPLEEIVISNDYLNKDLVSGGVVVSNASDKIEINNTLEERLKLLSEEALPAIRLELYGPSKTRKFFD
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------MSSAITALT
------CCCCHHHCC		28.6022814378
2Phosphorylation------MSSAITALT
------CCCCHHHCC		28.6024909858
3Phosphorylation-----MSSAITALTP
-----CCCCHHHCCH		23.5328132839
6Phosphorylation--MSSAITALTPNQV
--CCCCHHHCCHHHH		18.4828132839
9PhosphorylationSSAITALTPNQVNDE
CCCHHHCCHHHHHHH		20.1024909858
38AcetylationKAKEIQLKADQEYEI
HHHHHCCCCCCCEEE		33.2824489116
47AcetylationDQEYEIEKTNIVRNE
CCCEEEHHHHCEECC		53.1624489116
47UbiquitinationDQEYEIEKTNIVRNE
CCCEEEHHHHCEECC		53.1623749301
55PhosphorylationTNIVRNETNNIDGNF
HHCEECCCCCCCCCH		36.7921440633
63AcetylationNNIDGNFKSKLKKAM
CCCCCCHHHHHHHHH		51.1624489116
63SuccinylationNNIDGNFKSKLKKAM
CCCCCCHHHHHHHHH		51.1623954790
63UbiquitinationNNIDGNFKSKLKKAM
CCCCCCHHHHHHHHH		51.1623749301
64PhosphorylationNIDGNFKSKLKKAML
CCCCCHHHHHHHHHH		38.8021440633
65UbiquitinationIDGNFKSKLKKAMLS
CCCCHHHHHHHHHHC		65.9922817900
67UbiquitinationGNFKSKLKKAMLSQQ
CCHHHHHHHHHHCCC		42.0722817900
68UbiquitinationNFKSKLKKAMLSQQI
CHHHHHHHHHHCCCC		49.8423749301
72PhosphorylationKLKKAMLSQQITKST
HHHHHHHCCCCCHHH		13.6222369663
76PhosphorylationAMLSQQITKSTIANK
HHHCCCCCHHHHHHH		18.0122369663
772-HydroxyisobutyrylationMLSQQITKSTIANKM
HHCCCCCHHHHHHHH		47.43-
77AcetylationMLSQQITKSTIANKM
HHCCCCCHHHHHHHH		47.4324489116
77UbiquitinationMLSQQITKSTIANKM
HHCCCCCHHHHHHHH		47.4323749301
83AcetylationTKSTIANKMRLKVLS
CHHHHHHHHHHHHHH		19.1725381059
832-HydroxyisobutyrylationTKSTIANKMRLKVLS
CHHHHHHHHHHHHHH		19.17-
87UbiquitinationIANKMRLKVLSAREQ
HHHHHHHHHHHHHHH		30.6623749301
872-HydroxyisobutyrylationIANKMRLKVLSAREQ
HHHHHHHHHHHHHHH		30.66-
95PhosphorylationVLSAREQSLDGIFEE
HHHHHHHHHHHHHHH		24.5528889911
104AcetylationDGIFEETKEKLSGIA
HHHHHHHHHHHHCCC		57.0124489116
104UbiquitinationDGIFEETKEKLSGIA
HHHHHHHHHHHHCCC		57.0122817900
106UbiquitinationIFEETKEKLSGIANN
HHHHHHHHHHCCCCC		49.8922817900
108PhosphorylationEETKEKLSGIANNRD
HHHHHHHHCCCCCHH		38.9428889911
118AcetylationANNRDEYKPILQSLI
CCCHHHCHHHHHHHH		24.4324489116
136AcetylationLLKLLEPKAIVKALE
HHHHHCHHHHHHHHH		41.1724489116
140UbiquitinationLEPKAIVKALERDVD
HCHHHHHHHHHHCHH		40.9323749301
140AcetylationLEPKAIVKALERDVD
HCHHHHHHHHHHCHH		40.9322865919
1402-HydroxyisobutyrylationLEPKAIVKALERDVD
HCHHHHHHHHHHCHH		40.93-
153SuccinylationVDLIESMKDDIMREY
HHHHHHCHHHHHHHH		62.6223954790
153AcetylationVDLIESMKDDIMREY
HHHHHHCHHHHHHHH		62.6224489116
153UbiquitinationVDLIESMKDDIMREY
HHHHHHCHHHHHHHH		62.6223749301
185PhosphorylationYLNKDLVSGGVVVSN
CCCCCCCCCCEEEEC		36.8119823750
191PhosphorylationVSGGVVVSNASDKIE
CCCCEEEECCCCCEE		18.3119823750
194PhosphorylationGVVVSNASDKIEINN
CEEEECCCCCEEECC		43.6219823750
208UbiquitinationNTLEERLKLLSEEAL
CCHHHHHHHHCCCCH		54.3123749301
208AcetylationNTLEERLKLLSEEAL
CCHHHHHHHHCCCCH		54.3124489116
226PhosphorylationRLELYGPSKTRKFFD
HHHHHCCCCCCCCCC		42.1521440633
227AcetylationLELYGPSKTRKFFD-
HHHHCCCCCCCCCC-		56.3225381059
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 VATE_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VATE_YEAST !!
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 VATE_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATG_YEASTVMA10physical
9334266
VATE_YEASTVMA4physical
8626613
VATB_YEASTVMA2physical
9195975
VATH_YEASTVMA13physical
9195975
VATD_YEASTVMA8physical
9195975
RAV1_YEASTRAV1physical
16429126
VATA_YEASTVMA1physical
16429126
VATB_YEASTVMA2physical
16429126
VATC_YEASTVMA5physical
16429126
RAV2_YEASTRAV2physical
16429126
VATH_YEASTVMA13physical
16429126
VATF_YEASTVMA7physical
16429126
VATD_YEASTVMA8physical
16429126
VATG_YEASTVMA10physical
20446876
VATC_YEASTVMA5physical
20446876
SNF7_YEASTSNF7genetic
20134403
VPS24_YEASTVPS24genetic
20134403
VPS25_YEASTVPS25genetic
20134403
VPS36_YEASTVPS36genetic
20134403
VATG_YEASTVMA10physical
16774922
VATE_YEASTVMA4physical
16774922
VATB_YEASTVMA2physical
16774922
VATD_YEASTVMA8physical
16774922
VATF_YEASTVMA7physical
16774922
VATA_YEASTVMA1physical
16774922
VATH_YEASTVMA13physical
16774922
VATC_YEASTVMA5physical
16774922
VATA_YEASTVMA1physical
12413952
VATB_YEASTVMA2physical
12413952
VATA_YEASTVMA1physical
22940862
VATD_YEASTVMA8physical
22940862
VATE_YEASTVMA4physical
22940862
VATB_YEASTVMA2physical
22940862
VATG_YEASTVMA10physical
23071676
VATH_YEASTVMA13physical
23071676
VATF_YEASTVMA7physical
23071676
VATD_YEASTVMA8physical
23071676
VATB_YEASTVMA2physical
23071676
VA0D_YEASTVMA6physical
23071676
VPH1_YEASTVPH1physical
23071676
VATB_YEASTVMA2physical
23142977
ARL1_YEASTARL1genetic
27708008
MTC4_YEASTMTC4genetic
27708008
ENT5_YEASTENT5genetic
27708008
ERD1_YEASTERD1genetic
27708008
ERV14_YEASTERV14genetic
27708008
PTPA1_YEASTRRD1genetic
27708008
SYS1_YEASTSYS1genetic
27708008
PEP8_YEASTPEP8genetic
27708008
PHO86_YEASTPHO86genetic
27708008
VPS35_YEASTVPS35genetic
27708008
VPS38_YEASTVPS38genetic
27708008
TSA1_YEASTTSA1genetic
27708008
DLT1_YEASTDLT1genetic
27708008
TRI1_YEASTTRI1genetic
27708008
VPS21_YEASTVPS21genetic
27708008
TRS33_YEASTTRS33genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VATE_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9 AND SER-95, AND MASSSPECTROMETRY.

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