VTC3_YEAST - dbPTM
VTC3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VTC3_YEAST
UniProt AC Q02725
Protein Name Vacuolar transporter chaperone 3
Gene Name VTC3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 835
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description Component of the vacuolar transporter chaperone (VTC) complex, which plays a role in vacuolar membrane fusion. Required for LMA1 release prior to membrane fusion. [PubMed: 11823419 Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules]
Protein Sequence MLFGIKLANDVYPPWKDSYIDYERLKKLLKESVIHDGRSSVDSWSERNESDFVEALDKELEKVYTFQISKYNAVLRKLDDLEENTKSAEKIQKINSEQFKNTLEECLDEAQRLDNFDRLNFTGFIKIVKKHDKLHPNYPSVKSLLQVRLKELPFNNSEEYSPLLYRISYLYEFLRSNYDHPNTVSKSLASTSKLSHFSNLEDASFKSYKFWVHDDNIMEVKARILRHLPALVYASVPNENDDFVDNLESDVRVQPEARLNIGSKSNSLSSDGNSNQDVEIGKSKSVIFPQSYDPTITTLYFDNDFFDLYNNRLLKISGAPTLRLRWIGKLLDKPDIFLEKRTFTENTETGNSSFEEIRLQMKAKFINNFIFKNDPSYKNYLINQLRERGTQKEELEKLSRDFDNIQNFIVEEKLQPVLRATYNRTAFQIPGDQSIRVTIDSNIMYIREDSLDKNRPIRNPENWHRDDIDSNIPNPLRFLRAGEYSKFPYSVMEIKVINQDNSQMPNYEWIKDLTNSHLVNEVPKFSLYLQGVASLFGEDDKYVNILPFWLPDLETDIRKNPQEAYEEEKKTLQKQKSIHDKLDNMRRLSKISVPDGKTTERQGQKDQNTRHVIADLEDHESSDEEGTALPKKSAVKKGKKFKTNAAFLKILAGKNISENGNDPYSDDTDSASSFQLPPGVKKPVHLLKNAGPVKVEAKVWLANERTFNRWLSVTTLLSVLTFSIYNSVQKAEFPQLADLLAYVYFFLTLFCGVWAYRTYLKRLTLIKGRSGKHLDAPVGPILVAVVLIVTLVVNFSVAFKEAARRERGLVNVSSQPSLPRTLKPIQDFIFNLVGE
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
6Ubiquitination--MLFGIKLANDVYP
--CCCCCEECCCCCC		41.7619722269
30AcetylationERLKKLLKESVIHDG
HHHHHHHHHHHCCCC		59.3822865919
39PhosphorylationSVIHDGRSSVDSWSE
HHCCCCCCCCCCCHH		40.0020377248
40PhosphorylationVIHDGRSSVDSWSER
HCCCCCCCCCCCHHH		28.6922369663
43PhosphorylationDGRSSVDSWSERNES
CCCCCCCCCHHHCHH		30.2822369663
45PhosphorylationRSSVDSWSERNESDF
CCCCCCCHHHCHHHH		30.5422890988
50PhosphorylationSWSERNESDFVEALD
CCHHHCHHHHHHHHH		39.6422369663
77UbiquitinationKYNAVLRKLDDLEEN
HHHHHHHHHHHHHHH		52.7017644757
86UbiquitinationDDLEENTKSAEKIQK
HHHHHHHHHHHHHHH		60.2917644757
122PhosphorylationNFDRLNFTGFIKIVK
CCCCCCHHHHHHHHH		30.0619779198
150UbiquitinationSLLQVRLKELPFNNS
HHHHHHHHCCCCCCC		46.7917644757
183PhosphorylationSNYDHPNTVSKSLAS
HCCCCCCCCCHHHHC		30.5225704821
185PhosphorylationYDHPNTVSKSLASTS
CCCCCCCCHHHHCCC		17.9419779198
187PhosphorylationHPNTVSKSLASTSKL
CCCCCCHHHHCCCCC		22.9722369663
190PhosphorylationTVSKSLASTSKLSHF
CCCHHHHCCCCCCCC		38.2122369663
191PhosphorylationVSKSLASTSKLSHFS
CCHHHHCCCCCCCCC		25.0322369663
192PhosphorylationSKSLASTSKLSHFSN
CHHHHCCCCCCCCCC		29.1622369663
193AcetylationKSLASTSKLSHFSNL
HHHHCCCCCCCCCCC		54.8424489116
193UbiquitinationKSLASTSKLSHFSNL
HHHHCCCCCCCCCCC		54.8417644757
195PhosphorylationLASTSKLSHFSNLED
HHCCCCCCCCCCCCC		26.6522369663
198PhosphorylationTSKLSHFSNLEDASF
CCCCCCCCCCCCCCC		34.7722369663
204PhosphorylationFSNLEDASFKSYKFW
CCCCCCCCCCEEEEE		45.5922890988
206UbiquitinationNLEDASFKSYKFWVH
CCCCCCCCEEEEEEE		50.8317644757
209AcetylationDASFKSYKFWVHDDN
CCCCCEEEEEEECCC		39.5824489116
249PhosphorylationDFVDNLESDVRVQPE
CCHHCHHCCCCCCCC		44.5724961812
263PhosphorylationEARLNIGSKSNSLSS
CCCCCCCCCCCCCCC		29.1624909858
264UbiquitinationARLNIGSKSNSLSSD
CCCCCCCCCCCCCCC		48.7423749301
265PhosphorylationRLNIGSKSNSLSSDG
CCCCCCCCCCCCCCC		33.0922369663
267PhosphorylationNIGSKSNSLSSDGNS
CCCCCCCCCCCCCCC		36.4022369663
269PhosphorylationGSKSNSLSSDGNSNQ
CCCCCCCCCCCCCCC		26.6322369663
270PhosphorylationSKSNSLSSDGNSNQD
CCCCCCCCCCCCCCC		55.6322369663
274PhosphorylationSLSSDGNSNQDVEIG
CCCCCCCCCCCEEEC		41.2022369663
282UbiquitinationNQDVEIGKSKSVIFP
CCCEEECCCCEEECC		61.4423749301
283PhosphorylationQDVEIGKSKSVIFPQ
CCEEECCCCEEECCC		25.5821440633
285PhosphorylationVEIGKSKSVIFPQSY
EEECCCCEEECCCCC		27.7728889911
333AcetylationWIGKLLDKPDIFLEK
HHHHHHCCCCEEEEE		44.5524489116
364AcetylationIRLQMKAKFINNFIF
HHHHHHHHHHHHCCC		41.0624489116
376PhosphorylationFIFKNDPSYKNYLIN
CCCCCCHHHHHHHHH		52.1619823750
377PhosphorylationIFKNDPSYKNYLINQ
CCCCCHHHHHHHHHH		14.5119823750
380PhosphorylationNDPSYKNYLINQLRE
CCHHHHHHHHHHHHH		12.5719823750
390PhosphorylationNQLRERGTQKEELEK
HHHHHCCCCHHHHHH		42.5619823750
486AcetylationLRAGEYSKFPYSVME
HHCCCCCCCCCCEEE		49.8322865919
569UbiquitinationQEAYEEEKKTLQKQK
HHHHHHHHHHHHHHH		55.1022817900
570UbiquitinationEAYEEEKKTLQKQKS
HHHHHHHHHHHHHHH		58.7222817900
574UbiquitinationEEKKTLQKQKSIHDK
HHHHHHHHHHHHHHH		63.9122817900
581AcetylationKQKSIHDKLDNMRRL
HHHHHHHHHHHHHHH		43.5122865919
589PhosphorylationLDNMRRLSKISVPDG
HHHHHHHHCCCCCCC		26.5724930733
592PhosphorylationMRRLSKISVPDGKTT
HHHHHCCCCCCCCCC		31.1922369663
609PhosphorylationQGQKDQNTRHVIADL
CCCCCCCCCEEEEEC		19.2719795423
621PhosphorylationADLEDHESSDEEGTA
EECHHCCCCCCCCCC		39.4022369663
622PhosphorylationDLEDHESSDEEGTAL
ECHHCCCCCCCCCCC		46.1622369663
627PhosphorylationESSDEEGTALPKKSA
CCCCCCCCCCCCHHH		28.4422369663
649UbiquitinationKTNAAFLKILAGKNI
CCCHHHHHHHCCCCC		29.2622817900
654UbiquitinationFLKILAGKNISENGN
HHHHHCCCCCCCCCC		45.5623749301
664PhosphorylationSENGNDPYSDDTDSA
CCCCCCCCCCCCCCC		27.8221440633
665PhosphorylationENGNDPYSDDTDSAS
CCCCCCCCCCCCCCC		34.1021440633
668PhosphorylationNDPYSDDTDSASSFQ
CCCCCCCCCCCCCCC		36.5221440633
670PhosphorylationPYSDDTDSASSFQLP
CCCCCCCCCCCCCCC		31.9517330950
672PhosphorylationSDDTDSASSFQLPPG
CCCCCCCCCCCCCCC		35.3217330950
673PhosphorylationDDTDSASSFQLPPGV
CCCCCCCCCCCCCCC		19.4117330950
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 VTC3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VTC3_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 VTC3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VMA22_YEASTVMA22physical
10688190
VTC3_YEASTVTC3physical
22940862
SSB1_YEASTSSB1physical
22940862
ENO2_YEASTENO2physical
22940862
HSP71_YEASTSSA1physical
22940862
PDC1_YEASTPDC1physical
22940862
HSP72_YEASTSSA2physical
22940862
DED1_YEASTDED1physical
22940862
KPYK1_YEASTCDC19physical
22940862
DYR_YEASTDFR1genetic
27708008
TFS2_YEASTDST1genetic
27708008
MRM2_YEASTMRM2genetic
27708008
SEI1_YEASTFLD1genetic
27708008
MKT1_YEASTMKT1genetic
27708008
BRE5_YEASTBRE5genetic
27708008
OKP1_YEASTOKP1genetic
27708008
ORC4_YEASTORC4genetic
27708008
FAB1_YEASTFAB1genetic
27708008
PHB2_YEASTPHB2genetic
27708008
MED20_YEASTSRB2genetic
27708008
MPC2_YEASTMPC2genetic
27708008
FLX1_YEASTFLX1genetic
27708008
SNX4_YEASTSNX4genetic
27708008
TDA4_YEASTTDA4genetic
27708008
PAM17_YEASTPAM17genetic
27708008
ELO3_YEASTELO3genetic
27708008
YD089_YEASTYDR089Wphysical
27587415
VTC4_YEASTVTC4physical
25315834
VTC1_YEASTVTC1physical
25315834
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VTC3_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-43; THR-183; THR-191;SER-192; SER-195; SER-198; SER-265; SER-267; SER-269; SER-270;SER-274; SER-283; SER-285; SER-592; SER-621; SER-622; THR-627; SER-672AND SER-673, 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-195; SER-198; SER-589;SER-592; SER-621 AND SER-622, 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-589 AND SER-592, ANDMASS SPECTROMETRY.
"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-43; SER-198; SER-270;SER-592; SER-621 AND SER-622, AND MASS SPECTROMETRY.
"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-621 AND SER-622, ANDMASS SPECTROMETRY.

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