VNX1_YEAST - dbPTM
VNX1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VNX1_YEAST
UniProt AC P42839
Protein Name Low affinity vacuolar monovalent cation/H(+) antiporter
Gene Name VNX1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 908
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description Has a role in promoting intracellular monovalent cation sequestration via the exchange of monovalent cations and especially Na(+) for hydrogen ions across the vacuolar membrane..
Protein Sequence MAKNNHISASGNSTSGDHRLKEEVLTPTTSASTPHRIFSVDDDPKEIQNDIRYLEGLHEGLKFALHANKSKRSVSSQSPIVHSSNNTLHHHEHQQHLPPTLESLSSKSHSVPDLNTATPSSPKRMHSSIRELPHDDNDDEDANDDSRFIIHDSHGHDLLIDEINCQSPSHLENNDQASNASSTESFTLRERQDAINETHPFGIRIWKPALYKKHRSVQRTAAQDIHETQLKTITWEVTCSNVLWFILFGFPIAILFYSAAIVVFLLGGGGLVTNSAKEYSKCLYKLANYFLWPFGKMVYLLQDEQYLQEDKDEGISMQQFYNWVTSYSNRLVFHQSQAKFQQREDHPAPATESSSLMPPANTTATPLNSNHPSYNSIRHEIPHAAAQRRYFGRGKWSWGRVLFYTIFHLVLQPILAVLSLCLWLLVFTIPMSNVLWQIMYHCRRHPLALGFKYVENSSQSHENEITQQQLNKNILLCTFRAAGWHYYKYTVDGTNVIVVNLISIVFFTIFDFYVLKNFLHWKTWFTYESSIFILCLTSTIPLAFYIGQAVASISAQTSMGVGAVINAFFSTIVEIFLYCVALQQKKGLLVEGSMIGSILGAVLLLPGLSMCGGALNRKTQRYNPASAGVSSALLIFSMIVMFVPTVLYEIYGGYSVNCADGANDRDCTFSHPPLKFNRLFTHVIQPMSISCAIVLFCAYIIGLWFTLRTHAKMIWQLPIADPTSTAPEQQEQNSHDAPNWSRSKSTCILLMSTLLYAIIAEILVSCVDAVLEDIPSLNPKFLGLTIFALIPNTTEFLNAISFAIHGNVALSMEIGSAYALQVCLLQIPSLVIYSIFYTWNVKKSMINIRTQMFPLVFPRWDIFGAMTSVFMFTYLYAEGKSNYFKGSMLILLYIIIVVGFYFQGALSE
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
3Ubiquitination-----MAKNNHISAS
-----CCCCCCCCCC		57.9119722269
8PhosphorylationMAKNNHISASGNSTS
CCCCCCCCCCCCCCC		14.6119823750
10PhosphorylationKNNHISASGNSTSGD
CCCCCCCCCCCCCCC		31.5521440633
13PhosphorylationHISASGNSTSGDHRL
CCCCCCCCCCCCCCC		27.7223749301
14PhosphorylationISASGNSTSGDHRLK
CCCCCCCCCCCCCCC		40.5025005228
15PhosphorylationSASGNSTSGDHRLKE
CCCCCCCCCCCCCCC		41.8824961812
21AcetylationTSGDHRLKEEVLTPT
CCCCCCCCCCCCCCC		52.3524489116
21UbiquitinationTSGDHRLKEEVLTPT
CCCCCCCCCCCCCCC		52.3517644757
26PhosphorylationRLKEEVLTPTTSAST
CCCCCCCCCCCCCCC		24.6217330950
28PhosphorylationKEEVLTPTTSASTPH
CCCCCCCCCCCCCCC		28.3129136822
29PhosphorylationEEVLTPTTSASTPHR
CCCCCCCCCCCCCCE		24.4129136822
30PhosphorylationEVLTPTTSASTPHRI
CCCCCCCCCCCCCEE		23.7717330950
32PhosphorylationLTPTTSASTPHRIFS
CCCCCCCCCCCEEEE		42.0917330950
33PhosphorylationTPTTSASTPHRIFSV
CCCCCCCCCCEEEEC		23.8820377248
39PhosphorylationSTPHRIFSVDDDPKE
CCCCEEEECCCCHHH		23.4324961812
45UbiquitinationFSVDDDPKEIQNDIR
EECCCCHHHHHHHHH		74.5617644757
70PhosphorylationFALHANKSKRSVSSQ
HHHHCCCCCCCCCCC		32.8624961812
73PhosphorylationHANKSKRSVSSQSPI
HCCCCCCCCCCCCCE		30.0424961812
75PhosphorylationNKSKRSVSSQSPIVH
CCCCCCCCCCCCEEE		24.7324961812
76PhosphorylationKSKRSVSSQSPIVHS
CCCCCCCCCCCEEEC		32.3024961812
78PhosphorylationKRSVSSQSPIVHSSN
CCCCCCCCCEEECCC		20.6724961812
107UbiquitinationTLESLSSKSHSVPDL
CHHHHHCCCCCCCCC		49.1417644757
108PhosphorylationLESLSSKSHSVPDLN
HHHHHCCCCCCCCCC		23.9622890988
110PhosphorylationSLSSKSHSVPDLNTA
HHHCCCCCCCCCCCC		42.3022369663
116PhosphorylationHSVPDLNTATPSSPK
CCCCCCCCCCCCCCC		38.9225521595
118PhosphorylationVPDLNTATPSSPKRM
CCCCCCCCCCCCCCC		22.9722369663
120PhosphorylationDLNTATPSSPKRMHS
CCCCCCCCCCCCCCH		55.7225521595
121PhosphorylationLNTATPSSPKRMHSS
CCCCCCCCCCCCCHH		35.3322369663
123UbiquitinationTATPSSPKRMHSSIR
CCCCCCCCCCCHHHH		65.3923749301
128PhosphorylationSPKRMHSSIRELPHD
CCCCCCHHHHCCCCC		15.8119779198
336PhosphorylationNRLVFHQSQAKFQQR
CCEEEEHHHHHHHCC		24.4422369663
339UbiquitinationVFHQSQAKFQQREDH
EEEHHHHHHHCCCCC		35.7517644757
361N-linked_GlycosylationSSLMPPANTTATPLN
CCCCCCCCCCCCCCC		43.68-
453PhosphorylationPLALGFKYVENSSQS
CHHHCEEECCCCCCC		15.6724930733
458PhosphorylationFKYVENSSQSHENEI
EEECCCCCCCCCCHH		47.4824930733
460PhosphorylationYVENSSQSHENEITQ
ECCCCCCCCCCHHHH		34.4124930733
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 VNX1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VNX1_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 VNX1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NHX1_YEASTNHX1genetic
17588950
PHO88_YEASTPHO88physical
16093310
NSG1_YEASTNSG1physical
16093310
NHX1_YEASTNHX1genetic
20578725
ATC1_YEASTPMR1genetic
20578725
DPM1_YEASTDPM1physical
20578725
RPC6_YEASTRPC34genetic
27708008
CDC24_YEASTCDC24genetic
27708008
CDC1_YEASTCDC1genetic
27708008
PRP18_YEASTPRP18genetic
27708008
BET3_YEASTBET3genetic
27708008
RSC9_YEASTRSC9genetic
27708008
DBP6_YEASTDBP6genetic
27708008
VPS41_YEASTVPS41genetic
27708008
TFS2_YEASTDST1genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
PET8_YEASTPET8genetic
27708008
NEW1_YEASTNEW1genetic
27708008
ESS1_YEASTESS1genetic
29674565
TYW4_YEASTPPM2genetic
29674565
VPS51_YEASTVPS51genetic
29674565
ACT_YEASTACT1genetic
29674565
RS21B_YEASTRPS21Bgenetic
29674565
RL14A_YEASTRPL14Agenetic
29674565
VPS24_YEASTVPS24genetic
29674565
ELM1_YEASTELM1genetic
29674565
FABG_YEASTOAR1genetic
29674565
EF1G2_YEASTTEF4genetic
29674565
PRS7_YEASTRPT1genetic
29674565
SAC1_YEASTSAC1genetic
29674565
BET3_YEASTBET3genetic
29674565
TAD3_YEASTTAD3genetic
29674565
NAB6_YEASTNAB6genetic
29674565
NOP12_YEASTNOP12genetic
29674565
TYSY_YEASTCDC21genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VNX1_YEAST

loading...

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-13; THR-26; SER-110;SER-120 AND SER-121, AND MASS 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 SER-120, 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-26 AND SER-110, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-121, ANDMASS 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 SER-110 AND SER-120, ANDMASS SPECTROMETRY.

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