VAC17_YEAST - dbPTM
VAC17_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VAC17_YEAST
UniProt AC P25591
Protein Name vacuole-related protein 17
Gene Name VAC17
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 423
Subcellular Localization Vacuole membrane
Peripheral membrane protein
Cytoplasmic side .
Protein Description Vacuole-specific MYO2 receptor required for vacuole inheritance. Binds simultaneously to MYO2 and to VAC8, a vacuolar membrane protein, forming a transport complex which moves the attached vacuole membrane along actin cables into the bud. Once the vacuole arrives in the bud, VAC17 is degraded, depositing the vacuole in its correct location..
Protein Sequence MATQALEDITERLLIRSQEAILQLDLWIQRQQRSSICQTTDQESLDKLSQQYNQYMSQLNSLYVRSESVRDKLSKEQQRRLITEDNEHQRIEDLVREFQDITLRLNELATVPNEAPNDSPQSQSTRSSLGSFQPRPLKIIERQRLCMVTPSKPPKKSVGFNPINEVDCPSKTNSLPCSPKKQPARNRTLRAAKSHDTGLNKSKKPSSSDTYESFFKNRQRLSLTFFDEMDDEDFDSDQDTIILPNISTPPHVGVTAKGAEFEPLRRYNSHESILSNKPAPSKSLNLGSFSASFFRPSNPTFGTSISNVQVNCHPTVAATMAPSRNGPRISSSKALLSSFIARSDTHTVKENNTNLKHASFMDKFNSSLSTISESFQSKRGRKNKGMNEERISNHNVAQEQKNNMDISVSIEELQDALNTELLF
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
2Acetylation------MATQALEDI
------CCHHHHHHH
14.3922814378
47UbiquitinationTDQESLDKLSQQYNQ
CCHHHHHHHHHHHHH
56.1617644757
119PhosphorylationPNEAPNDSPQSQSTR
CCCCCCCCCCCCCHH
31.3223749301
122PhosphorylationAPNDSPQSQSTRSSL
CCCCCCCCCCHHHHC
29.4923749301
149PhosphorylationRQRLCMVTPSKPPKK
EEEEEEECCCCCCCC
8.5821440633
152UbiquitinationLCMVTPSKPPKKSVG
EEEECCCCCCCCCCC
67.5517644757
155UbiquitinationVTPSKPPKKSVGFNP
ECCCCCCCCCCCCCC
67.2317644757
156UbiquitinationTPSKPPKKSVGFNPI
CCCCCCCCCCCCCCC
57.0317644757
170PhosphorylationINEVDCPSKTNSLPC
CCCCCCCCCCCCCCC
59.4520377248
171UbiquitinationNEVDCPSKTNSLPCS
CCCCCCCCCCCCCCC
36.5517644757
174PhosphorylationDCPSKTNSLPCSPKK
CCCCCCCCCCCCCCC
38.6320377248
178PhosphorylationKTNSLPCSPKKQPAR
CCCCCCCCCCCCCCC
37.5020377248
194PhosphorylationRTLRAAKSHDTGLNK
HHHHHHHHCCCCCCC
23.1328889911
248PhosphorylationIILPNISTPPHVGVT
EEECCCCCCCCCCCC
36.7228889911
267PhosphorylationEFEPLRRYNSHESIL
CCCCCCCCCCCHHHH
18.0021440633
269PhosphorylationEPLRRYNSHESILSN
CCCCCCCCCHHHHCC
21.5020377248
272PhosphorylationRRYNSHESILSNKPA
CCCCCCHHHHCCCCC
24.3319684113
275PhosphorylationNSHESILSNKPAPSK
CCCHHHHCCCCCCCC
40.9319684113
277UbiquitinationHESILSNKPAPSKSL
CHHHHCCCCCCCCCC
38.9017644757
282UbiquitinationSNKPAPSKSLNLGSF
CCCCCCCCCCCCCCE
58.8817644757
333UbiquitinationGPRISSSKALLSSFI
CCCCCCCHHHHHHHH
45.0317644757
337PhosphorylationSSSKALLSSFIARSD
CCCHHHHHHHHHHCC
24.8522369663
338PhosphorylationSSKALLSSFIARSDT
CCHHHHHHHHHHCCC
22.2022369663
353PhosphorylationHTVKENNTNLKHASF
CCCCCCCCCCCCHHH
54.2128889911
363UbiquitinationKHASFMDKFNSSLST
CCHHHHHHHHHHHHH
34.3617644757
378UbiquitinationISESFQSKRGRKNKG
HHHHHHHHHCCCCCC
48.3517644757
392PhosphorylationGMNEERISNHNVAQE
CCCHHHHHCCCHHHH
37.9521440633

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 VAC17_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VAC17_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 VAC17_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYO2_YEASTMYO2physical
12594460
VAC8_YEASTVAC8physical
12594460
MYO2_YEASTMYO2physical
12642614
ATG17_YEASTATG17physical
11283351
ATG18_YEASTATG18physical
18467557
MYO2_YEASTMYO2genetic
18804442
MYO2_YEASTMYO2physical
18804442
MYO2_YEASTMYO2physical
22753895
PEP12_YEASTPEP12genetic
26322385
VPS45_YEASTVPS45genetic
26322385
TOR1_YEASTTOR1genetic
26322385
SCH9_YEASTSCH9genetic
26322385
VPS16_YEASTVPS16genetic
27373154
STP1_YEASTSTP1genetic
27708008
TOR1_YEASTTOR1genetic
27708008
SRN2_YEASTSRN2genetic
27708008
MKS1_YEASTMKS1genetic
27708008
SERC_YEASTSER1genetic
27708008
PDE2_YEASTPDE2genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VAC17_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The cyclin-dependent kinase Cdk1 directly regulates vacuoleinheritance.";
Peng Y., Weisman L.S.;
Dev. Cell 15:478-485(2008).
Cited for: PHOSPHORYLATION AT SER-119; THR-149; SER-178 AND THR-248, INTERACTIONWITH MYO2, FUNCTION, AND MUTAGENESIS OF SER-119; THR-149; SER-178;PHE-225 AND THR-248.

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