PMA2_YEAST - dbPTM
PMA2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMA2_YEAST
UniProt AC P19657
Protein Name Plasma membrane ATPase 2
Gene Name PMA2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 947
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses..
Protein Sequence MSSTEAKQYKEKPSKEYLHASDGDDPANNSAASSSSSSSTSTSASSSAAAVPRKAAAASAADDSDSDEDIDQLIDELQSNYGEGDESGEEEVRTDGVHAGQRVVPEKDLSTDPAYGLTSDEVARRRKKYGLNQMAEENESLIVKFLMFFVGPIQFVMEAAAILAAGLSDWVDVGVICALLLLNASVGFIQEFQAGSIVDELKKTLANTATVIRDGQLIEIPANEVVPGEILQLESGTIAPADGRIVTEDCFLQIDQSAITGESLAAEKHYGDEVFSSSTVKTGEAFMVVTATGDNTFVGRAAALVGQASGVEGHFTEVLNGIGIILLVLVIATLLLVWTACFYRTVGIVSILRYTLGITIIGVPVGLPAVVTTTMAVGAAYLAKKQAIVQKLSAIESLAGVEILCSDKTGTLTKNKLSLHEPYTVEGVSPDDLMLTACLAASRKKKGLDAIDKAFLKSLIEYPKAKDALTKYKVLEFHPFDPVSKKVTAVVESPEGERIVCVKGAPLFVLKTVEEDHPIPEDVHENYENKVAELASRGFRALGVARKRGEGHWEILGVMPCMDPPRDDTAQTINEARNLGLRIKMLTGDAVGIAKETCRQLGLGTNIYNAERLGLGGGGDMPGSELADFVENADGFAEVFPQHKYRVVEILQNRGYLVAMTGDGVNDAPSLKKADTGIAVEGATDAARSAADIVFLAPGLSAIIDALKTSRQIFHRMYSYVVYRIALSLHLEIFLGLWIAILNNSLDINLIVFIAIFADVATLTIAYDNAPYAPEPVKWNLPRLWGMSIILGIVLAIGSWITLTTMFLPNGGIIQNFGAMNGVMFLQISLTENWLIFVTRAAGPFWSSIPSWQLAGAVFAVDIIATMFTLFGWWSENWTDIVSVVRVWIWSIGIFCVLGGFYYIMSTSQAFDRLMNGKSLKEKKSTRSVEDFMAAMQRVSTQHEKSS
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
296PhosphorylationVTATGDNTFVGRAAA
EEECCCCCCHHHHHH		25.1628889911
391UbiquitinationKKQAIVQKLSAIESL
HHHHHHHHHHHHHHH		33.2517644757
408UbiquitinationVEILCSDKTGTLTKN
CEEEECCCCCCCCCC		32.3417644757
409PhosphorylationEILCSDKTGTLTKNK
EEEECCCCCCCCCCC		40.1519823750
411PhosphorylationLCSDKTGTLTKNKLS
EECCCCCCCCCCCEE		36.1619823750
413PhosphorylationSDKTGTLTKNKLSLH
CCCCCCCCCCCEECC		32.2019795423
414UbiquitinationDKTGTLTKNKLSLHE
CCCCCCCCCCEECCC		56.0217644757
416UbiquitinationTGTLTKNKLSLHEPY
CCCCCCCCEECCCCC		40.8017644757
418PhosphorylationTLTKNKLSLHEPYTV
CCCCCCEECCCCCEE		29.3221440633
429PhosphorylationPYTVEGVSPDDLMLT
CCEECCCCHHHHHHH		33.2121440633
444UbiquitinationACLAASRKKKGLDAI
HHHHHHHHHCCHHHH		57.2322817900
445UbiquitinationCLAASRKKKGLDAID
HHHHHHHHCCHHHHH		51.4622817900
446UbiquitinationLAASRKKKGLDAIDK
HHHHHHHCCHHHHHH		68.6823749301
453UbiquitinationKGLDAIDKAFLKSLI
CCHHHHHHHHHHHHH		34.6223749301
466UbiquitinationLIEYPKAKDALTKYK
HHHCHHHHHHHHHCC		50.0522817900
466AcetylationLIEYPKAKDALTKYK
HHHCHHHHHHHHHCC		50.0525381059
471UbiquitinationKAKDALTKYKVLEFH
HHHHHHHHCCEEEEC		43.8823749301
473UbiquitinationKDALTKYKVLEFHPF
HHHHHHCCEEEECCC		41.7323749301
484PhosphorylationFHPFDPVSKKVTAVV
ECCCCCCCCCEEEEE		31.9521440633
485UbiquitinationHPFDPVSKKVTAVVE
CCCCCCCCCEEEEEE		52.0423749301
486UbiquitinationPFDPVSKKVTAVVES
CCCCCCCCEEEEEEC		36.9923749301
488PhosphorylationDPVSKKVTAVVESPE
CCCCCCEEEEEECCC		23.7120377248
493PhosphorylationKVTAVVESPEGERIV
CEEEEEECCCCCEEE		19.3523749301
503UbiquitinationGERIVCVKGAPLFVL
CCEEEEECCCEEEEE		44.2023749301
511UbiquitinationGAPLFVLKTVEEDHP
CCEEEEEEECCCCCC		45.2624961812
530UbiquitinationVHENYENKVAELASR
HHHHHHHHHHHHHHH		30.7723749301
536PhosphorylationNKVAELASRGFRALG
HHHHHHHHHHHHHHH		45.638943257
584UbiquitinationRNLGLRIKMLTGDAV
HHHCCCEEEHHCCHH		22.7917644757
587PhosphorylationGLRIKMLTGDAVGIA
CCCEEEHHCCHHHHH		29.5321551504
595UbiquitinationGDAVGIAKETCRQLG
CCHHHHHHHHHHHCC		52.1923749301
605PhosphorylationCRQLGLGTNIYNAER
HHHCCCCCCCCCHHH		24.4024909858
644UbiquitinationAEVFPQHKYRVVEIL
HHHCHHHCEEEEHHH		29.5123749301
670PhosphorylationDGVNDAPSLKKADTG
CCCCCCCHHCCCCCC		55.3223749301
672UbiquitinationVNDAPSLKKADTGIA
CCCCCHHCCCCCCCC		50.7022817900
673UbiquitinationNDAPSLKKADTGIAV
CCCCHHCCCCCCCCC		57.7123749301
676PhosphorylationPSLKKADTGIAVEGA
CHHCCCCCCCCCCCH		35.0325752575
708UbiquitinationSAIIDALKTSRQIFH
HHHHHHHHHHHHHHH		46.2923749301
925PhosphorylationKSLKEKKSTRSVEDF
CCCCHHHCCCCHHHH		39.8719823750
926PhosphorylationSLKEKKSTRSVEDFM
CCCHHHCCCCHHHHH		35.5217287358
928PhosphorylationKEKKSTRSVEDFMAA
CHHHCCCCHHHHHHH		29.9122369663
940PhosphorylationMAAMQRVSTQHEKSS
HHHHHHHHHHHHHCC		25.2522369663
941PhosphorylationAAMQRVSTQHEKSS-
HHHHHHHHHHHHCC-		30.9625521595
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 PMA2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMA2_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 PMA2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP73_YEASTSSA3genetic
20093466
ACH1_YEASTACH1genetic
20093466
EDS1_YEASTEDS1genetic
20093466
ATG14_YEASTATG14genetic
20093466
SEC66_YEASTSEC66genetic
20093466
SNF11_YEASTSNF11genetic
20093466
DFM1_YEASTDFM1genetic
20093466
VPS72_YEASTVPS72genetic
20093466
DBP3_YEASTDBP3genetic
20093466
PUR4_YEASTADE6genetic
20093466
TRS65_YEASTTRS65genetic
20093466
SLT2_YEASTSLT2genetic
20093466
RPI1_YEASTRPI1genetic
20093466
XBP1_YEASTXBP1genetic
20093466
SDS3_YEASTSDS3genetic
20093466
PHO90_YEASTPHO90genetic
20093466
UBI4P_YEASTUBI4genetic
20093466
ARP6_YEASTARP6genetic
20093466
TMA7_YEASTTMA7genetic
20093466
ECM38_YEASTECM38genetic
20093466
RSC2_YEASTRSC2genetic
20093466
LEUR_YEASTLEU3genetic
20093466
COG8_YEASTCOG8genetic
20093466
STV1_YEASTSTV1genetic
20093466
TMA23_YEASTTMA23genetic
20093466
GAS1_YEASTGAS1genetic
20093466
MAS5_YEASTYDJ1genetic
20093466
HRB1_YEASTHRB1genetic
20093466
AHC1_YEASTAHC1genetic
20093466
RUD3_YEASTRUD3genetic
20093466
YO223_YEASTDSC3genetic
20093466
ATG13_YEASTATG13genetic
20093466
VPS27_YEASTVPS27genetic
20526336
RIC1_YEASTRIC1genetic
20526336
YAJ9_YEASTYAR029Wgenetic
27708008
DUG2_YEASTDUG2genetic
27708008
UME6_YEASTUME6genetic
27708008
LEUR_YEASTLEU3genetic
27708008
SAP30_YEASTSAP30genetic
27708008
YME2_YEASTYME2genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
PP2A4_YEASTPPG1genetic
27708008
HAL9_YEASTHAL9genetic
27708008
RUD3_YEASTRUD3genetic
27708008
YO223_YEASTDSC3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMA2_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-536; THR-926 ANDTHR-941, AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-941, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory