VTC4_SCHPO - dbPTM
VTC4_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VTC4_SCHPO
UniProt AC P78810
Protein Name Vacuolar transporter chaperone 4
Gene Name vtc4
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 721
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..
Protein Sequence MKFGQLLKETLMYEYKYSYVNYDKLKKEIKRRNDQGGWSEEDESDFVELLEKELDKVYSFQKNKSAEVMERIRFCEEQTDEVVRRLDSDNPPNENDFAILETELTDIMATVHDLAKFSELNYTAFYKIIKKHDKHTGWILKPVFAARLNAKPFFKEQYDLLVVKLSKLYDFVRTRGSPIKGDSAAGGTQQNFVRQTTKYWVHPNNVTELKIYILKHLPVLVFNPNKEFAREDAAITSIYYDNDDLDFYLGRLEKREGAEAIRLRWYGNMDNNNIFVERKTHREDWTGEKSVKARFPLKEKYVNAFLRGDYTVEEAFAKMRKDGKKSLKEIESLERLAKEVQYTVLSRGMKPYVRSFYERTAFQLPGDARVRISLDTNLSLIREDGPSRAGNNWRRMDIGIDYPFDQLPDEDIVRFPYAILEVKLQTQFGQDPPEWVNNLVNSHLVEAVPKFSKFIHGVSTLFYDRVTLLPYWFPQMDIDIRKPATHTFIQGRSQSGTHSSSVSANVLTDSENTPIHADGDNYVDEESRIGSSSTRNDNSTFQTSDSFQELDERTNLLDISKRKGRDSFVAALNSRLKDIKDSFFLETVPKFEEPTEPTVIYEQKYVSPPGKRIYVPVRVEPKTYFALERTYLDYLRYSILMGSIGITLFSFAKTRSGILGAASFTLVALFAIFYSTFLYLWRAVNIAKHNAVRYDDRFGPTAICVITFAAISANVILNFNA
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
493PhosphorylationHTFIQGRSQSGTHSS
EEEEECCCCCCCCCC
35.2128889911
495PhosphorylationFIQGRSQSGTHSSSV
EEECCCCCCCCCCCE
47.0828889911
497PhosphorylationQGRSQSGTHSSSVSA
ECCCCCCCCCCCEEE
24.6728889911
501PhosphorylationQSGTHSSSVSANVLT
CCCCCCCCEEEEECC
24.0928889911
508PhosphorylationSVSANVLTDSENTPI
CEEEEECCCCCCCCC
32.9529996109
531PhosphorylationDEESRIGSSSTRNDN
CCCCCCCCCCCCCCC
20.8125720772
532PhosphorylationEESRIGSSSTRNDNS
CCCCCCCCCCCCCCC
30.4325720772
533PhosphorylationESRIGSSSTRNDNST
CCCCCCCCCCCCCCC
32.8425720772
534PhosphorylationSRIGSSSTRNDNSTF
CCCCCCCCCCCCCCC
35.1228889911
539PhosphorylationSSTRNDNSTFQTSDS
CCCCCCCCCCCCCCC
33.2025720772
540PhosphorylationSTRNDNSTFQTSDSF
CCCCCCCCCCCCCCH
26.4725720772
543PhosphorylationNDNSTFQTSDSFQEL
CCCCCCCCCCCHHHH
30.2525720772
544PhosphorylationDNSTFQTSDSFQELD
CCCCCCCCCCHHHHH
22.0725720772
546PhosphorylationSTFQTSDSFQELDER
CCCCCCCCHHHHHHH
28.7028889911
567PhosphorylationSKRKGRDSFVAALNS
HHHCCHHHHHHHHHH
21.9128889911
574PhosphorylationSFVAALNSRLKDIKD
HHHHHHHHHHHHHHH
39.5821712547
582PhosphorylationRLKDIKDSFFLETVP
HHHHHHHHHCCEECC
16.9424763107

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 VTC4_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VTC4_SCHPO !!

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 VTC4_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VTC4_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VTC4_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495; THR-497; SER-501;THR-534 AND SER-546, AND MASS SPECTROMETRY.

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