VTA1_YEAST - dbPTM
VTA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VTA1_YEAST
UniProt AC Q06263
Protein Name Vacuolar protein sorting-associated protein VTA1
Gene Name VTA1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 330
Subcellular Localization Cytoplasm . Endosome membrane
Peripheral membrane protein .
Protein Description Has a role in the formation of the multivesicular body (MVB). Required for the sorting of lipids to form intralumenal vesicles and for fluid-phase transport to the vacuole. Required for sorting the plasma membrane proteins STE2 and STE3 into the MVB. Acts a cofactor of VSP4, promotes the oligomerization of VPS4 and stimulates its ATPase activity by 6- to 8-fold..
Protein Sequence MASNAARVVATAKDFDKVGLGIIGYYLQLYAVELILSEEDRSQEMTALATELLDTIEAFKKEIGGESEAEDSDKSLHVMNTLIHDQEKAKIYMLNFTMSLYNEKLKQLKDGPWDVMLKRSLWCCIDLFSCILHLWKENISETSTNSLQKRIKYCKIYLSKLAKGEIGSSDEKTLDYADFADDSEEIKDEDVDHQTSDLENNNNDKVEGLAPKDQTTSYEPVDEVPEFIDDADSVNEEEQTVDKNEDAITKDEQQVVKKEVDLTRPSAPSEPAAAEHKSYTKDELTKIMDRASKIEQIQKLAKYAISALNYEDLPTAKDELTKALDLLNSI
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
67PhosphorylationKKEIGGESEAEDSDK
HHHHCCCCCCCCCCC		45.4425533186
72PhosphorylationGESEAEDSDKSLHVM
CCCCCCCCCCCHHHH		38.1424961812
75PhosphorylationEAEDSDKSLHVMNTL
CCCCCCCCHHHHHHH		28.7924909858
168PhosphorylationLAKGEIGSSDEKTLD
HHCCCCCCCCCCCCC		40.0328889911
173PhosphorylationIGSSDEKTLDYADFA
CCCCCCCCCCHHHHC		23.8622369663
176PhosphorylationSDEKTLDYADFADDS
CCCCCCCHHHHCCCC		15.9322369663
183PhosphorylationYADFADDSEEIKDED
HHHHCCCCHHHCCCC		37.3622369663
195PhosphorylationDEDVDHQTSDLENNN
CCCCCCCCCCCCCCC		22.3122369663
196PhosphorylationEDVDHQTSDLENNNN
CCCCCCCCCCCCCCC		33.3625521595
233PhosphorylationEFIDDADSVNEEEQT
HHCCCHHHCCHHHHH		28.6725521595
240PhosphorylationSVNEEEQTVDKNEDA
HCCHHHHHCCCCCCC		33.6720377248
249PhosphorylationDKNEDAITKDEQQVV
CCCCCCCCHHHHHHH		33.8819823750
263PhosphorylationVKKEVDLTRPSAPSE
HHHHCCCCCCCCCCC		35.7519823750
266PhosphorylationEVDLTRPSAPSEPAA
HCCCCCCCCCCCCCH		49.9019823750
269PhosphorylationLTRPSAPSEPAAAEH
CCCCCCCCCCCHHHC		56.8021440633
286AcetylationYTKDELTKIMDRASK
CCHHHHHHHHHHHHH		48.9724489116
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 VTA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VTA1_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 VTA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS60_YEASTVPS60physical
14701806
VPS4_YEASTVPS4physical
15086794
SNF7_YEASTSNF7physical
15086794
DID2_YEASTDID2physical
15086794
BPH1_YEASTBPH1genetic
15296494
VPS4_YEASTVPS4physical
16193069
DID2_YEASTDID2physical
16601096
SNF7_YEASTSNF7physical
16601096
VTA1_YEASTVTA1physical
16505166
VPS4_YEASTVPS4physical
16505166
VPS4_YEASTVPS4physical
17130288
VPS4_YEASTVPS4physical
17408385
VPS4_YEASTVPS4physical
18467557
IST1_YEASTIST1physical
18467557
VPS4_YEASTVPS4physical
18719252
VPS60_YEASTVPS60physical
18194651
VPS4_YEASTVPS4physical
18194651
VPS4_YEASTVPS4physical
18032582
VPS4_YEASTVPS4physical
20696398
VTA1_YEASTVTA1physical
20696398
SPR3_YEASTSPR3physical
22875988
YJE9_YEASTYJL049Wphysical
26510789
VPS4_YEASTVPS4physical
25164817
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VTA1_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-67; SER-233 AND SER-269,AND MASS SPECTROMETRY.

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