YNF8_YEAST - dbPTM
YNF8_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YNF8_YEAST
UniProt AC P53947
Protein Name Vacuolar membrane protein YNL058C
Gene Name YNL058C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 316
Subcellular Localization Vacuole membrane
Single-pass membrane protein .
Protein Description
Protein Sequence MVKKNFIPSVSLVRRDLPTLVTTTTSSTALSKPTSSVVSETSSKSLPSLTSSAFSTSSGATSSSSLIVASITPPSTAGNPFILNAADKPNGTVYIAVGAVIGAIFISILIWWLVSSYLSRRFTMTNSYANDSKNLYRGHHKHSSSLQSNPFDINDEKSYMQDDWDSMSQLESSQYEDAASPFNPIQDPFTDNRRSLFISPTLQVSQYEKSHSRHQSKDTNIFIDDPFLYVGTYLEEEEEEEEERKLNLNRPQRAASPERKEKKINSMEGYHKRNQSSLGLIPVASATSNTSSPKKAHKRQAPSMFLDDVLNGREII
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
19PhosphorylationLVRRDLPTLVTTTTS
HHCCCCCEEEEEECC
40.9527017623
25PhosphorylationPTLVTTTTSSTALSK
CEEEEEECCCCCCCC
20.7027017623
31PhosphorylationTTSSTALSKPTSSVV
ECCCCCCCCCCCCCC
33.8430377154
36PhosphorylationALSKPTSSVVSETSS
CCCCCCCCCCCCCCC
29.0827017623
133UbiquitinationNSYANDSKNLYRGHH
CCCCCCCCCCCCCCC
54.5623749301
143PhosphorylationYRGHHKHSSSLQSNP
CCCCCCCCCCCCCCC
26.8219779198
144PhosphorylationRGHHKHSSSLQSNPF
CCCCCCCCCCCCCCC
34.4823749301
145PhosphorylationGHHKHSSSLQSNPFD
CCCCCCCCCCCCCCC
33.1821440633
148PhosphorylationKHSSSLQSNPFDIND
CCCCCCCCCCCCCCC
52.3319823750
195PhosphorylationPFTDNRRSLFISPTL
CCCCCCCCEEECCCE
25.1329650682
199PhosphorylationNRRSLFISPTLQVSQ
CCCCEEECCCEECHH
12.4227017623
209AcetylationLQVSQYEKSHSRHQS
EECHHHHHHHCCCCC
48.8424489116
256PhosphorylationNRPQRAASPERKEKK
CCHHHCCCHHHHHHH
26.7217287358
266PhosphorylationRKEKKINSMEGYHKR
HHHHHHHHHCCHHHC
22.9921440633
270PhosphorylationKINSMEGYHKRNQSS
HHHHHCCHHHCCHHC
7.2927017623
276PhosphorylationGYHKRNQSSLGLIPV
CHHHCCHHCCCCEEE
30.9519823750
277PhosphorylationYHKRNQSSLGLIPVA
HHHCCHHCCCCEEEC
19.3820377248
285PhosphorylationLGLIPVASATSNTSS
CCCEEECCCCCCCCC
32.1120377248
287PhosphorylationLIPVASATSNTSSPK
CEEECCCCCCCCCCC
21.7319684113
288PhosphorylationIPVASATSNTSSPKK
EEECCCCCCCCCCCH
37.5219684113
290PhosphorylationVASATSNTSSPKKAH
ECCCCCCCCCCCHHH
30.2820377248
291PhosphorylationASATSNTSSPKKAHK
CCCCCCCCCCCHHHH
49.2219684113
292PhosphorylationSATSNTSSPKKAHKR
CCCCCCCCCCHHHHC
38.4119823750
303PhosphorylationAHKRQAPSMFLDDVL
HHHCCCCCCCHHHHH
25.7821440633

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 YNF8_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YNF8_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 YNF8_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EIF3J_YEASTHCR1genetic
27708008
LTE1_YEASTLTE1genetic
27708008
REI1_YEASTREI1genetic
27708008
PDE2_YEASTPDE2genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YNF8_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-292, AND MASSSPECTROMETRY.
"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-256, AND MASSSPECTROMETRY.

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