VTC2_YEAST - dbPTM
VTC2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VTC2_YEAST
UniProt AC P43585
Protein Name Vacuolar transporter chaperone 2
Gene Name VTC2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 828
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. [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 MLFGVKLANEVYPPWKGSYINYEGLKKFLKEDSVKDGSNDKKARWDDSDESKFVEELDKELEKVYGFQLKKYNNLMERLSHLEKQTDTEAAIKALDADAFQRVLEELLSESTELDNFKRLNFTGFAKIVKKHDKLYPKYPSVKSLLEVRLKELPSHSEEYSPLLYRISFLYNILRSNFNTASEPLASASKFSSIVSNDIDMNFRSFKFWVHNDNLMEVKTRILRHLPVLVYANVPSENDDLVNRFESDISNNDEIVGSSSSTSSVEHGLGARSFDPLINTLYFDNEHFELYNDKLLKLNSAPTLRLRWTGQLSDKPDIFLEKKTLIEDEATGKSEFDLTKLQLKQKFINGFIFEGDKKFKEQTLKKLKESGTAGRDLERLEEDFSEIQNFIIKNELQPVFRTVYTRTAFQIPGDDKIRVTIDSNIVFIKEDSFDRERPIRDPNTWHRTDIDANVANPLKFLRGGEYAKFPYSVMEIKVKSSLDSSMSASSMISNVKLPKKHGQWLNDLTNSHLVKEIPKFSIFVQGVASLYGDDEKLDILPFWLPDLETDIRQDPKQAYEEEKKKLLKQKEIQKKIDGMRRLSNLKEPQHQAAVPVSQEENERITSQGDLEADGSSDEETEQEPHSKRSKKVRRRKPKATFLRILAGRDPKLMGVDSEEEEIELPPGVKKPLNLLKNAGPVNVEAKVWLANERTFNRWLSVTSLLSVLTFSIYNSVKKAEYPTLANYMAYVYFGLTIFCALWSYSIYMKRVDIIQQRSGQHLDAPLGPVLVSIVLFVTLVVNFVMAFRNAAKSRQELQIQNLEVPERIPEVLRPLQNYLFKLMGPSSD
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
26SuccinylationYINYEGLKKFLKEDS
CCCHHHHHHHHHHCC		52.9523954790
26AcetylationYINYEGLKKFLKEDS
CCCHHHHHHHHHHCC		52.9524489116
93AcetylationTDTEAAIKALDADAF
CCHHHHHHHHCHHHH		37.8624489116
93UbiquitinationTDTEAAIKALDADAF
CCHHHHHHHHCHHHH		37.8615699485
118AcetylationSTELDNFKRLNFTGF
CCCCHHCCCCCCCCH		63.3324489116
127AcetylationLNFTGFAKIVKKHDK
CCCCCHHHHHHHCCC		45.8524489116
144PhosphorylationPKYPSVKSLLEVRLK
CCCCCHHHHHHHHHH		35.7121440633
151AcetylationSLLEVRLKELPSHSE
HHHHHHHHHCCCCCH		46.7924489116
151UbiquitinationSLLEVRLKELPSHSE
HHHHHHHHHCCCCCH		46.7924961812
176PhosphorylationFLYNILRSNFNTASE
HHHHHHHHCCCCCCC		42.1822890988
180PhosphorylationILRSNFNTASEPLAS
HHHHCCCCCCCCCCC		27.6722890988
182PhosphorylationRSNFNTASEPLASAS
HHCCCCCCCCCCCHH		37.3922369663
187PhosphorylationTASEPLASASKFSSI
CCCCCCCCHHHHHHH		40.5322369663
189PhosphorylationSEPLASASKFSSIVS
CCCCCCHHHHHHHHC		31.5722890988
190UbiquitinationEPLASASKFSSIVSN
CCCCCHHHHHHHHCC		49.3215699485
192PhosphorylationLASASKFSSIVSNDI
CCCHHHHHHHHCCCC		23.9222369663
193PhosphorylationASASKFSSIVSNDID
CCHHHHHHHHCCCCC		30.0922369663
196PhosphorylationSKFSSIVSNDIDMNF
HHHHHHHCCCCCCCC		27.4122369663
201OxidationIVSNDIDMNFRSFKF
HHCCCCCCCCCEEEE		5.3615665377
205PhosphorylationDIDMNFRSFKFWVHN
CCCCCCCEEEEEEEC		28.7521440633
250PhosphorylationNRFESDISNNDEIVG
HHHHHHCCCCCCCCC		34.2719795423
258PhosphorylationNNDEIVGSSSSTSSV
CCCCCCCCCCCCCCC		19.0219795423
259PhosphorylationNDEIVGSSSSTSSVE
CCCCCCCCCCCCCCC		23.5219795423
260PhosphorylationDEIVGSSSSTSSVEH
CCCCCCCCCCCCCCC		39.0617330950
261PhosphorylationEIVGSSSSTSSVEHG
CCCCCCCCCCCCCCC		33.9719795423
262PhosphorylationIVGSSSSTSSVEHGL
CCCCCCCCCCCCCCC		27.2819795423
263PhosphorylationVGSSSSTSSVEHGLG
CCCCCCCCCCCCCCC		34.0417330950
264PhosphorylationGSSSSTSSVEHGLGA
CCCCCCCCCCCCCCC		31.4517330950
300PhosphorylationDKLLKLNSAPTLRLR
CCEECCCCCCEEEEE		46.1721440633
315AcetylationWTGQLSDKPDIFLEK
EEECCCCCCCEEEEE		41.0124489116
334PhosphorylationEDEATGKSEFDLTKL
CCCCCCCCCCCCCHH		44.8623749301
339PhosphorylationGKSEFDLTKLQLKQK
CCCCCCCCHHHHHHH		31.3927017623
340AcetylationKSEFDLTKLQLKQKF
CCCCCCCHHHHHHHH		41.3424489116
346AcetylationTKLQLKQKFINGFIF
CHHHHHHHHHCCCCC		46.7724489116
357AcetylationGFIFEGDKKFKEQTL
CCCCCCCHHHHHHHH		71.6024489116
358AcetylationFIFEGDKKFKEQTLK
CCCCCCHHHHHHHHH		67.4224489116
416AcetylationFQIPGDDKIRVTIDS
EECCCCCCEEEEECC		36.8324489116
459AcetylationANVANPLKFLRGGEY
CCCCCCHHHHCCCCC		43.5424489116
468AcetylationLRGGEYAKFPYSVME
HCCCCCCCCCCCEEE		46.0724489116
477AcetylationPYSVMEIKVKSSLDS
CCCEEEEEEECCCCC		30.2424489116
480PhosphorylationVMEIKVKSSLDSSMS
EEEEEEECCCCCCCC		38.8430377154
481PhosphorylationMEIKVKSSLDSSMSA
EEEEEECCCCCCCCH		30.4021440633
485PhosphorylationVKSSLDSSMSASSMI
EECCCCCCCCHHHHH		19.2028889911
487PhosphorylationSSLDSSMSASSMISN
CCCCCCCCHHHHHHC		27.2621440633
489PhosphorylationLDSSMSASSMISNVK
CCCCCCHHHHHHCCC		17.0921440633
490PhosphorylationDSSMSASSMISNVKL
CCCCCHHHHHHCCCC		21.6117330950
493PhosphorylationMSASSMISNVKLPKK
CCHHHHHHCCCCCHH		27.2517330950
583PhosphorylationIDGMRRLSNLKEPQH
HHHHHHHHCCCCCCC		38.0017330950
586UbiquitinationMRRLSNLKEPQHQAA
HHHHHCCCCCCCCCC		72.1523749301
597PhosphorylationHQAAVPVSQEENERI
CCCCCCCCHHHHHCC		26.2929136822
605PhosphorylationQEENERITSQGDLEA
HHHHHCCCCCCCCCC		22.6322890988
606PhosphorylationEENERITSQGDLEAD
HHHHCCCCCCCCCCC		29.7822890988
615PhosphorylationGDLEADGSSDEETEQ
CCCCCCCCCCHHCCC		34.8522369663
616PhosphorylationDLEADGSSDEETEQE
CCCCCCCCCHHCCCC		55.3522369663
620PhosphorylationDGSSDEETEQEPHSK
CCCCCHHCCCCCCCH		40.7022890988
626PhosphorylationETEQEPHSKRSKKVR
HCCCCCCCHHCHHHH		40.2422890988
627UbiquitinationTEQEPHSKRSKKVRR
CCCCCCCHHCHHHHH		58.6223749301
653OxidationAGRDPKLMGVDSEEE
CCCCHHHCCCCCCCC		6.4915665377
657PhosphorylationPKLMGVDSEEEEIEL
HHHCCCCCCCCCCCC		44.4922369663
700PhosphorylationRTFNRWLSVTSLLSV
CHHHHHHHHHHHHHH		19.1830377154
702PhosphorylationFNRWLSVTSLLSVLT
HHHHHHHHHHHHHHH		15.4130377154
703PhosphorylationNRWLSVTSLLSVLTF
HHHHHHHHHHHHHHH		25.7630377154
706PhosphorylationLSVTSLLSVLTFSIY
HHHHHHHHHHHHHHH		22.0021551504
709PhosphorylationTSLLSVLTFSIYNSV
HHHHHHHHHHHHHCC		17.1230377154
711PhosphorylationLLSVLTFSIYNSVKK
HHHHHHHHHHHCCCC		20.9430377154
721PhosphorylationNSVKKAEYPTLANYM
HCCCCCCCCCHHHHH		13.3330377154
736PhosphorylationAYVYFGLTIFCALWS
HHHHHHHHHHHHHHH		16.6430377154
743PhosphorylationTIFCALWSYSIYMKR
HHHHHHHHHHHHHHH		15.1730377154
744PhosphorylationIFCALWSYSIYMKRV
HHHHHHHHHHHHHHH		6.3630377154
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 VTC2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VTC2_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 VTC2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VTC3_YEASTVTC3genetic
11102525
COS7_YEASTCOS7physical
16093310
SSB1_YEASTSSB1physical
22940862
KPYK1_YEASTCDC19physical
22940862
VTC2_YEASTVTC2physical
22940862
PABP_YEASTPAB1physical
22940862
HSP72_YEASTSSA2physical
22940862
HSP71_YEASTSSA1physical
22940862
SCC1_YEASTMCD1genetic
27708008
CDC11_YEASTCDC11genetic
27708008
CALM_YEASTCMD1genetic
27708008
TECR_YEASTTSC13genetic
27708008
NSE4_YEASTNSE4genetic
27708008
ERF3_YEASTSUP35genetic
27708008
PCF11_YEASTPCF11genetic
27708008
SLD5_YEASTSLD5genetic
27708008
CDC20_YEASTCDC20genetic
27708008
YHI0_YEASTYHR020Wgenetic
27708008
MPPA_YEASTMAS2genetic
27708008
MED11_YEASTMED11genetic
27708008
RNA1_YEASTRNA1genetic
27708008
YTM1_YEASTYTM1genetic
27708008
SEC23_YEASTSEC23genetic
27708008
YD089_YEASTYDR089Wphysical
27587415
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VTC2_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-182; SER-187; SER-192;SER-193; SER-196; SER-490; SER-615; SER-616 AND SER-657, AND MASSSPECTROMETRY.
"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-615 AND SER-616, ANDMASS 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-583 AND SER-657, 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-182; SER-196; SER-264;SER-583; SER-615; SER-616 AND SER-657, AND MASS 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-196 AND SER-657, ANDMASS 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-187, AND MASSSPECTROMETRY.

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