YPK9_YEAST - dbPTM
YPK9_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YPK9_YEAST
UniProt AC Q12697
Protein Name Vacuolar cation-transporting ATPase YPK9
Gene Name YPK9
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1472
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description Vacuolar transporter which plays a role in sequestration of divalent heavy metal ions..
Protein Sequence MDIPSSNQIQHGQRSERNRRMPRASFSSTATTSTAATLTSAMVLDQNNSEPYAGATFEAVPSSIVSFHHPHSFQSSNLPSPHSSGNLEQRGRRLTESEPLVLSSAEQSRSSSRNPSHFRFFTQEQISNAEGASTLENTDYDMAWDATPAYEQDRIYGTGLSSRRSSIRSFSRASSLSNAKSYGSFSKRGRSGSRAPQRLGENSDTGFVYHSATHSSSSLSRYTTRERIPIELESQTDEILEDESSTHSLESSDSRRSASENNRGSFSGHDDVHNQHSEYLKPDYHEKFYPQYAPNLHYQRFYIAEEDLVIGIAAYQTSKFWYIIYNLCCFLTFGLVYLLTRWLPHLKVKLYGVKVPLAKAEWVVIENEFGEFVIQPIDRQWYNRPLSTVLPFENYPNPSYEPNDINLSHHHANEINPNVPILITFEYRYIKFIYSPLDDLFKTNNNWIDPDWVDLSTVSNGLTKGVQEDRELAFGKNQINLRMKTTSEILFNEVLHPFYVFQVFSIILWGIDEYYYYAACIFLISVLSIFDSLNEQKKVSRNLAEMSHFHCDVRVLRDKFWTTISSSELVPGDIYEVSDPNITILPCDSILLSSDCIVNESMLTGESVPVSKFPATEETMYQLCDDFQSTQISSFVSKSFLYNGTNIIRARIAPGQTAALAMVVRTGFSTTKGSLVRSMVFPKPTGFKFYRDSFKYIGFMSLIAIFGFCVSCVQFIKLGLDKKTMILRALDIITIVVPPALPATLTIGTNFALSRLKEKGIFCISPTRLNISGKIDVMCFDKTGTLTEDGLDVLGVQISEPNGVRGQKFGELLSDIRQVFPKFSLNDCSSPLDFKSRNFFMSLLTCHSLRSVDGNLLGDPLDFKMFQFTGWSFEEDFQKRAFHSLYEGRHEDDVFPENSEIIPAVVHPDSNNRENTFTDNDPHNFLGVVRSFEFLSELRRMSVIVKTNNDDVYWSFTKGAPEVISEICNKSTLPADFEEVLRCYTHNGYRVIACAGKTLPKRTWLYSQKVSREEVESNLEFLGFIIFQNKLKKETSETLKSLQDANIRTIMCTGDNILTAISVGREAGLIQCSRVYVPSINDTPLHGEPVIVWRDVNEPDKILDTKTLKPVKLGNNSVESLRECNYTLAVSGDVFRLLFRDENEIPEEYLNEILLNSSIYARMSPDEKHELMIQLQKLDYTVGFCGDGANDCGALKAADVGISLSEAEASVAAPFTSKIFNISCVLDVIREGRAALVTSFACFQYMSLYSAIQFITITILYSRGSNLGDFQFLYIDLLLIVPIAICMSWSKSYEKIDKKRPSANLVSPKILVPLLISVFLVFLFQFIPWIIVQKMSWYIKPIVGGDDAVQSSDNTVLFFVSNFQYILTAIVLSVGPPYREPMSKNFEFIVDITVSIGASLLLMTLDTESYLGKMLQLTPISNSFTMFIIVWVILNYYAQLYIPPSIKGWLKKKKSSKKYKLLIQEEMKLKEV
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
1Acetylation-------MDIPSSNQ
-------CCCCCCCC		44.9522814378
95PhosphorylationEQRGRRLTESEPLVL
HHHCCCCCCCCCEEC		35.3422369663
97PhosphorylationRGRRLTESEPLVLSS
HCCCCCCCCCEECCC		39.0028152593
103PhosphorylationESEPLVLSSAEQSRS
CCCCEECCCCCHHCC		21.7422369663
104PhosphorylationSEPLVLSSAEQSRSS
CCCEECCCCCHHCCC		31.5022369663
108PhosphorylationVLSSAEQSRSSSRNP
ECCCCCHHCCCCCCH		26.1523749301
110PhosphorylationSSAEQSRSSSRNPSH
CCCCHHCCCCCCHHH		37.6029136822
111PhosphorylationSAEQSRSSSRNPSHF
CCCHHCCCCCCHHHH		32.0129136822
112PhosphorylationAEQSRSSSRNPSHFR
CCHHCCCCCCHHHHE		37.0129136822
116PhosphorylationRSSSRNPSHFRFFTQ
CCCCCCHHHHEEECH		38.5128889911
156PhosphorylationAYEQDRIYGTGLSSR
CCCCCCCCCCCCCCC		14.9928889911
158PhosphorylationEQDRIYGTGLSSRRS
CCCCCCCCCCCCCHH		20.2728132839
161PhosphorylationRIYGTGLSSRRSSIR
CCCCCCCCCCHHHHH		24.1228889911
162PhosphorylationIYGTGLSSRRSSIRS
CCCCCCCCCHHHHHH		36.4328889911
165PhosphorylationTGLSSRRSSIRSFSR
CCCCCCHHHHHHHHC		29.0728889911
166PhosphorylationGLSSRRSSIRSFSRA
CCCCCHHHHHHHHCH		21.8728889911
169PhosphorylationSRRSSIRSFSRASSL
CCHHHHHHHHCHHCC		26.3821440633
171PhosphorylationRSSIRSFSRASSLSN
HHHHHHHHCHHCCCC		28.3421440633
174PhosphorylationIRSFSRASSLSNAKS
HHHHHCHHCCCCCCH		30.6022369663
175PhosphorylationRSFSRASSLSNAKSY
HHHHCHHCCCCCCHH		34.5322369663
177PhosphorylationFSRASSLSNAKSYGS
HHCHHCCCCCCHHCC		36.3722369663
181PhosphorylationSSLSNAKSYGSFSKR
HCCCCCCHHCCCCCC		32.1122369663
184PhosphorylationSNAKSYGSFSKRGRS
CCCCHHCCCCCCCCC		20.3622369663
186PhosphorylationAKSYGSFSKRGRSGS
CCHHCCCCCCCCCCC		24.1222369663
205PhosphorylationRLGENSDTGFVYHSA
CCCCCCCCCCEEEEC		32.1329688323
209PhosphorylationNSDTGFVYHSATHSS
CCCCCCEEEECCCCC		6.4429688323
211PhosphorylationDTGFVYHSATHSSSS
CCCCEEEECCCCCCC		19.7119684113
213PhosphorylationGFVYHSATHSSSSLS
CCEEEECCCCCCCCC		25.8819684113
215PhosphorylationVYHSATHSSSSLSRY
EEEECCCCCCCCCCC		27.7923749301
216PhosphorylationYHSATHSSSSLSRYT
EEECCCCCCCCCCCC		19.1523749301
217PhosphorylationHSATHSSSSLSRYTT
EECCCCCCCCCCCCC		38.0117330950
218PhosphorylationSATHSSSSLSRYTTR
ECCCCCCCCCCCCCC		32.1017330950
220PhosphorylationTHSSSSLSRYTTRER
CCCCCCCCCCCCCCC		25.7823749301
257PhosphorylationESSDSRRSASENNRG
CCCCCCCCCCCCCCC		34.7327214570
672UbiquitinationRTGFSTTKGSLVRSM
HCCCCCCCCCEEEEC		46.7423749301
1117PhosphorylationPVKLGNNSVESLREC
CEECCCCCHHHHHHC		31.1225752575
1120PhosphorylationLGNNSVESLRECNYT
CCCCCHHHHHHCCCE		30.4825752575
1126PhosphorylationESLRECNYTLAVSGD
HHHHHCCCEEEECCH		18.1319779198
1307PhosphorylationRPSANLVSPKILVPL
CCCCCCCCHHHHHHH		24.5229734811
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 YPK9_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YPK9_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 YPK9_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PMT3_YEASTPMT3genetic
16269340
SEC63_YEASTSEC63genetic
16269340
RIC1_YEASTRIC1genetic
16269340
SEC66_YEASTSEC66genetic
16269340
PLMT_YEASTOPI3genetic
16269340
COPE_YEASTSEC28genetic
16269340
SYUA_HUMANSNCAgenetic
19182805
FMT_YEASTFMT1genetic
20093466
GCS1_YEASTGCS1genetic
20093466
CHAC_YEASTGCG1genetic
20093466
RL2A_YEASTRPL2Agenetic
20093466
RL2B_YEASTRPL2Agenetic
20093466
YGY5_YEASTYGL235Wgenetic
20093466
FYV10_YEASTFYV10genetic
20093466
DCOR_YEASTSPE1genetic
20093466
RS21A_YEASTRPS21Agenetic
20093466
MUB1_YEASTMUB1genetic
20093466
SSO2_YEASTSSO2genetic
20093466
DCAM_YEASTSPE2genetic
20093466
MSA1_YEASTMSA1genetic
20093466
MDL2_YEASTMDL2genetic
20093466
ALG1_YEASTALG1genetic
22457822
CDK1_YEASTCDC28genetic
22457822
DPOD_YEASTPOL3genetic
22457822
CDC53_YEASTCDC53genetic
22457822
CDC12_YEASTCDC12genetic
22457822
CDC11_YEASTCDC11genetic
22457822
SFH1_YEASTSFH1genetic
22457822
CDC91_YEASTGAB1genetic
22457822
APC5_YEASTAPC5genetic
22457822
MYO2_YEASTMYO2genetic
22457822
DIM1_YEASTDIM1genetic
22457822
PGTB2_YEASTBET2genetic
22457822
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YPK9_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-218, 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 THR-95, AND MASSSPECTROMETRY.

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