dbPTM

VTC2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VTC2_SCHPO
UniProt AC	O13718
Protein Name	Vacuolar transporter chaperone 2
Gene Name	vtc2
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	734
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	MRFSDSIEAGIYEPWRDKYMNYPELKHLLKTEEEAPSWGENDESKFVSVMDAQLEKVYAFHLEILKELNESVDWVKSKVSASQEPDGPPISKEEAIKLLERLDSCTETVKKLEKYTRLNLTGFFKIVKKHDKLYPGYSLRPVFQVRLRACPLGSVQFNPLLAEIFSLYNTLRDGLSAPSNSVQVKPKHEHNVDYNSSMYRRRTFRFWVHPDNVMEVKTYIMRHLPVLYYSGKQGFDKDQNGVSGILDPISTCLYLDNSNFDLYSQNLERSEQAYSLRLHWYGKLTPKTDIIVERMVRQGSTLSHSEDRFTIREKKVRELLSGRYDFRKVEDDHSTTASDQKKKLIEDVEQLIVDNHLQPVLRSVYTRTAFQIPGDDEVRINLDSDWVMIREDSLDIERPCRDPEDWHRHDIDDADFPYKHLRKGEYSRFPYSVLEIRECVRYDEDEPLWISELRNSHLISEIDGFSKYEHGVAILFEKYVSLLPMWVFSMDQDIRKDLQEVYSHPEGSAGSRNVYIKRRNQRVLKQNMTPEPSQPSPLVNRLKANEMHPVSEEPEDNREVYRNEHGDHFNFRSIPGLLKPSTYGSFKHHGKTFVTPPHIKKPEIPLRVSGPIKVEAKVWLANERTFLKWLHVVVLLGSLALALYNSAGERLGQAFGVVYTLLAIFIGFYAWKLHAKRSQMIKSRSPAPMTDYWGPLIVGTALAISLIVNMSFALKDAVYQNLIEPDRLLVKLFT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
179	Phosphorylation	RDGLSAPSNSVQVKP HCCCCCCCCCCCCCC	41.26	25720772
181	Phosphorylation	GLSAPSNSVQVKPKH CCCCCCCCCCCCCCC	20.47	28889911
334	Phosphorylation	RKVEDDHSTTASDQK EECCCCCCCCCHHHH	34.15	21712547
335	Phosphorylation	KVEDDHSTTASDQKK ECCCCCCCCCHHHHH	23.98	21712547
336	Phosphorylation	VEDDHSTTASDQKKK CCCCCCCCCHHHHHH	27.46	21712547
338	Phosphorylation	DDHSTTASDQKKKLI CCCCCCCHHHHHHHH	38.18	24763107
503	Phosphorylation	KDLQEVYSHPEGSAG HHHHHHHCCCCCCCC	37.43	21712547
508	Phosphorylation	VYSHPEGSAGSRNVY HHCCCCCCCCCCCEE	28.00	21712547
511	Phosphorylation	HPEGSAGSRNVYIKR CCCCCCCCCCEEEEH	22.01	21712547
529	Phosphorylation	RVLKQNMTPEPSQPS HHHHCCCCCCCCCCC	31.86	28889911
533	Phosphorylation	QNMTPEPSQPSPLVN CCCCCCCCCCCHHHH	53.73	29996109
536	Phosphorylation	TPEPSQPSPLVNRLK CCCCCCCCHHHHHHH	24.19	21712547
583	Phosphorylation	GLLKPSTYGSFKHHG CCCCCCCCCCCCCCC	18.34	28889911
585	Phosphorylation	LKPSTYGSFKHHGKT CCCCCCCCCCCCCEE	22.25	24763107

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_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of VTC2_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 VTC2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of VTC2_SCHPO !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of VTC2_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-181; THR-529 ANDTYR-583, AND MASS SPECTROMETRY.	18257517 [Abstract]