VATB_YEAST - dbPTM
VATB_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VATB_YEAST
UniProt AC P16140
Protein Name V-type proton ATPase subunit B
Gene Name VMA2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 517
Subcellular Localization
Protein Description Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mv, inside positive and acidic, in the vacuolar membrane vesicles..
Protein Sequence MVLSDKELFAINKKAVEQGFNVKPRLNYNTVSGVNGPLVILEKVKFPRYNEIVNLTLPDGTVRQGQVLEIRGDRAIVQVFEGTSGIDVKKTTVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRQAGLVRPTKDVHDGHEENFSIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIFVDRQLHNKGIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYAKYAIGKDAAAMKAVVGEEALSIEDKLSLEFLEKFEKTFITQGAYEDRTVFESLDQAWSLLRIYPKEMLNRISPKILDEFYDRARDDADEDEEDPDTRSSGKKKDASQEESLI
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----MVLSDKELFAI
----CCCCHHHHEEE		34.9121082442
6Ubiquitination--MVLSDKELFAINK
--CCCCHHHHEEECH		53.6024961812
132-HydroxyisobutyrylationKELFAINKKAVEQGF
HHHEEECHHHHHCCC		35.68-
13UbiquitinationKELFAINKKAVEQGF
HHHEEECHHHHHCCC		35.6822817900
13SuccinylationKELFAINKKAVEQGF
HHHEEECHHHHHCCC		35.6823954790
13AcetylationKELFAINKKAVEQGF
HHHEEECHHHHHCCC		35.6822865919
14AcetylationELFAINKKAVEQGFN
HHEEECHHHHHCCCC		53.8524489116
14UbiquitinationELFAINKKAVEQGFN
HHEEECHHHHHCCCC		53.8523749301
23AcetylationVEQGFNVKPRLNYNT
HHCCCCCCCCCCCCC		26.0624489116
23UbiquitinationVEQGFNVKPRLNYNT
HHCCCCCCCCCCCCC		26.0623749301
43AcetylationGPLVILEKVKFPRYN
CCEEEEEEECCCCCC		47.4824489116
43UbiquitinationGPLVILEKVKFPRYN
CCEEEEEEECCCCCC		47.4817644757
83PhosphorylationIVQVFEGTSGIDVKK
EEEEEECCCCCEEEE		19.3128889911
84PhosphorylationVQVFEGTSGIDVKKT
EEEEECCCCCEEEEE		44.6125752575
89AcetylationGTSGIDVKKTTVEFT
CCCCCEEEEEEEEEC		40.4324489116
90UbiquitinationTSGIDVKKTTVEFTG
CCCCEEEEEEEEECC		49.6423749301
902-HydroxyisobutyrylationTSGIDVKKTTVEFTG
CCCCEEEEEEEEECC		49.64-
92PhosphorylationGIDVKKTTVEFTGES
CCEEEEEEEEECCCC		27.2428889911
125UbiquitinationRPIDNGPKVFAEDYL
CCCCCCCCEEEECCC		51.9223749301
131PhosphorylationPKVFAEDYLDINGSP
CCEEEECCCCCCCCC		9.5929136822
137PhosphorylationDYLDINGSPINPYAR
CCCCCCCCCCCCCCC		20.3722369663
169UbiquitinationNSIARGQKIPIFSAS
HHHHCCCCCCEEECC		53.9623749301
226SuccinylationLETARFFKQDFEENG
HHHHHHHHHHHHHCC		46.3623954790
226AcetylationLETARFFKQDFEENG
HHHHHHHHHHHHHCC		46.3624489116
226UbiquitinationLETARFFKQDFEENG
HHHHHHHHHHHHHCC		46.3623749301
268PhosphorylationTTAEYLAYQTERHVL
HHHHHHHHHCHHHHH		17.2424909858
270PhosphorylationAEYLAYQTERHVLTI
HHHHHHHCHHHHHHH		23.4724909858
328PhosphorylationRVEGRNGSITQIPIL
CCCCCCCCCCEEEEE		26.4730377154
330PhosphorylationEGRNGSITQIPILTM
CCCCCCCCEEEEEEC		23.3423749301
367UbiquitinationVDRQLHNKGIYPPIN
ECCHHCCCCCCCCHH		35.6222817900
367AcetylationVDRQLHNKGIYPPIN
ECCHHCCCCCCCCHH		35.6224489116
370PhosphorylationQLHNKGIYPPINVLP
HHCCCCCCCCHHHHH		16.1819684113
378PhosphorylationPPINVLPSLSRLMKS
CCHHHHHHHHHHHHH		34.5119684113
380PhosphorylationINVLPSLSRLMKSAI
HHHHHHHHHHHHHHH		27.9219684113
384UbiquitinationPSLSRLMKSAIGEGM
HHHHHHHHHHHCCCC		41.1323749301
384AcetylationPSLSRLMKSAIGEGM
HHHHHHHHHHHCCCC		41.1324489116
385PhosphorylationSLSRLMKSAIGEGMT
HHHHHHHHHHCCCCC		15.9128889911
394UbiquitinationIGEGMTRKDHGDVSN
HCCCCCCCCCCCHHH		44.9323749301
400PhosphorylationRKDHGDVSNQLYAKY
CCCCCCHHHHHHHHH		24.4921440633
406AcetylationVSNQLYAKYAIGKDA
HHHHHHHHHHHCCCH		22.9724489116
406UbiquitinationVSNQLYAKYAIGKDA
HHHHHHHHHHHCCCH		22.9724961812
407PhosphorylationSNQLYAKYAIGKDAA
HHHHHHHHHHCCCHH		8.6928889911
4112-HydroxyisobutyrylationYAKYAIGKDAAAMKA
HHHHHHCCCHHHHHH		37.77-
411AcetylationYAKYAIGKDAAAMKA
HHHHHHCCCHHHHHH		37.7724489116
411SuccinylationYAKYAIGKDAAAMKA
HHHHHHCCCHHHHHH		37.7723954790
411UbiquitinationYAKYAIGKDAAAMKA
HHHHHHCCCHHHHHH		37.7723749301
417UbiquitinationGKDAAAMKAVVGEEA
CCCHHHHHHHHCCHH		33.0517644757
426PhosphorylationVVGEEALSIEDKLSL
HHCCHHCCCCHHHHH		30.8622369663
430UbiquitinationEALSIEDKLSLEFLE
HHCCCCHHHHHHHHH		27.4717644757
438AcetylationLSLEFLEKFEKTFIT
HHHHHHHHHHHHHCC		62.0524489116
438UbiquitinationLSLEFLEKFEKTFIT
HHHHHHHHHHHHHCC		62.0522817900
441UbiquitinationEFLEKFEKTFITQGA
HHHHHHHHHHCCCCC		52.4423749301
441AcetylationEFLEKFEKTFITQGA
HHHHHHHHHHCCCCC		52.4422865919
442PhosphorylationFLEKFEKTFITQGAY
HHHHHHHHHCCCCCC		17.0522369663
445PhosphorylationKFEKTFITQGAYEDR
HHHHHHCCCCCCCCC		19.4322369663
449PhosphorylationTFITQGAYEDRTVFE
HHCCCCCCCCCCHHH		25.7822369663
453PhosphorylationQGAYEDRTVFESLDQ
CCCCCCCCHHHCHHH		41.7022369663
457PhosphorylationEDRTVFESLDQAWSL
CCCCHHHCHHHHHHH		26.2722369663
463PhosphorylationESLDQAWSLLRIYPK
HCHHHHHHHHHHCCH		22.1222369663
470AcetylationSLLRIYPKEMLNRIS
HHHHHCCHHHHHHHC		38.4924489116
470UbiquitinationSLLRIYPKEMLNRIS
HHHHHCCHHHHHHHC		38.4923749301
477PhosphorylationKEMLNRISPKILDEF
HHHHHHHCHHHHHHH		19.5322369663
479AcetylationMLNRISPKILDEFYD
HHHHHCHHHHHHHHH		49.4624489116
479UbiquitinationMLNRISPKILDEFYD
HHHHHCHHHHHHHHH		49.4623749301
485PhosphorylationPKILDEFYDRARDDA
HHHHHHHHHHHHCCC		11.5019795423
501PhosphorylationEDEEDPDTRSSGKKK
CCCCCCCCCCCCCCC		37.5322369663
503PhosphorylationEEDPDTRSSGKKKDA
CCCCCCCCCCCCCCC		45.6022369663
504PhosphorylationEDPDTRSSGKKKDAS
CCCCCCCCCCCCCCC		51.8722369663
506UbiquitinationPDTRSSGKKKDASQE
CCCCCCCCCCCCCHH		59.6122817900
507UbiquitinationDTRSSGKKKDASQEE
CCCCCCCCCCCCHHH		60.4522817900
508UbiquitinationTRSSGKKKDASQEES
CCCCCCCCCCCHHHH		63.1123749301
511PhosphorylationSGKKKDASQEESLI-
CCCCCCCCHHHHCC-		48.5422369663
515PhosphorylationKDASQEESLI-----
CCCCHHHHCC-----		30.5222369663
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
511SPhosphorylationKinaseATMP38110
Uniprot
511SPhosphorylationKinaseATRP38111
Uniprot
511SPhosphorylationKinaseATM/ATR-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VATB_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 VATB_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAV1_YEASTRAV1physical
11805826
VATA_YEASTVMA1physical
11805826
VATG_YEASTVMA10physical
11805826
VATC_YEASTVMA5physical
11805826
VA0D_YEASTVMA6physical
11805826
LCB1_YEASTLCB1genetic
7929582
ARPC2_YEASTARC35genetic
7929582
ERG2_YEASTERG2genetic
7929582
VPS34_YEASTVPS34genetic
7929582
VPS4_YEASTVPS4genetic
7929582
END3_YEASTEND3genetic
7929582
SLA2_YEASTSLA2genetic
7929582
VATA_YEASTVMA1physical
16554755
SKP1_YEASTSKP1physical
16554755
VATD_YEASTVMA8physical
16554755
VATF_YEASTVMA7physical
16554755
VATG_YEASTVMA10physical
16554755
RAV1_YEASTRAV1physical
16554755
VATH_YEASTVMA13physical
16554755
RAV1_YEASTRAV1physical
16429126
VATA_YEASTVMA1physical
16429126
VATG_YEASTVMA10physical
16429126
VATC_YEASTVMA5physical
16429126
VA0D_YEASTVMA6physical
16429126
VATA_YEASTVMA1physical
16926153
VPH1_YEASTVPH1physical
16926153
TRX2_YEASTTRX2genetic
17215245
RBG2_YEASTRBG2genetic
17215245
SODM_YEASTSOD2genetic
17215245
SODC_YEASTSOD1genetic
17215245
GSH1_YEASTGSH1genetic
17215245
VATA_YEASTVMA1physical
18344484
RAV1_YEASTRAV1physical
17623654
VATG_YEASTVMA10physical
20446876
VATE_YEASTVMA4physical
20446876
FOLE_YEASTMET7genetic
21623372
INP53_YEASTINP53genetic
21623372
ACON2_YEASTACO2genetic
21623372
ELO3_YEASTELO3genetic
21623372
THDH_YEASTILV1genetic
21623372
ELO2_YEASTELO2genetic
21623372
SDHX_YEASTYJL045Wgenetic
21623372
COQ4_YEASTCOQ4genetic
21623372
6PGD1_YEASTGND1genetic
21623372
ATPO_YEASTATP5genetic
21623372
DCOR_YEASTSPE1genetic
21623372
TGL2_YEASTTGL2genetic
21623372
PYRX_YEASTURA10genetic
21623372
ADH3_YEASTADH3genetic
21623372
GGPPS_YEASTBTS1genetic
21623372
GPX1_YEASTGPX1genetic
21623372
VATE_YEASTVMA4physical
12220197
VATD_YEASTVMA8physical
12220197
VATG_YEASTVMA10physical
12220197
HOG1_YEASTHOG1genetic
22210831
VATB_YEASTVMA2physical
22940862
VATA_YEASTVMA1physical
22940862
VATC_YEASTVMA5physical
24805887
VPH1_YEASTVPH1physical
24805887
VPS25_YEASTVPS25genetic
25239548
SNF7_YEASTSNF7genetic
25239548
VPS28_YEASTVPS28genetic
25239548
FRA1_YEASTFRA1genetic
23457300
TSA1_YEASTTSA1genetic
23457300
TSA2_YEASTTSA2genetic
23457300
ARF1_YEASTARF1genetic
25002144
GTR1_YEASTGTR1genetic
25002144
SUR2_YEASTSUR2genetic
26404656
SUR1_YEASTSUR1genetic
26404656
CSH1_YEASTCSH1genetic
26404656
SCS7_YEASTSCS7genetic
26404656
RAV1_YEASTRAV1physical
26405040
PALF_YEASTRIM8genetic
25271159
RSP5_YEASTRSP5genetic
25271159
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VATB_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 SER-4; THR-83; SER-84;SER-137; SER-378; THR-501; SER-503; SER-504; SER-511 AND SER-515, ANDMASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-501; SER-503; SER-504;SER-511 AND SER-515, AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511 AND SER-515, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASSSPECTROMETRY.

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