YD206_YEAST - dbPTM
YD206_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YD206_YEAST
UniProt AC Q12424
Protein Name Putative cation exchanger YDL206W
Gene Name YDL206W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 762
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Putative cation exchanger..
Protein Sequence MHKPLRWLITIAFYVSNVILIGYSLSSNGSISEFYLHSVVLIECFSLLGVVTSDCLTPSLSYISSNIFHISDRVSGMTLLALGNALPDITSTYQSMKSGVTSLAIGELFGGIFFLLTVVIGLMGCVATIQFQHDKSIETYTEESFDQNLSYDRSNYILDVGIFTFMLLVSGTFLADGRLYFWECIVMVLTYCCCAVYLIKSYKYPCEINDALEREVEIKKTVLANNHITVPNRFTLTTTSDITSTDDGIRYVRPLGDTQIDEDNAISLDPTRLPSKSLDNISRFNQGIPERRDLIRRRIRGYLRSHYHGWVRMTLQDLLNIWEKQNLFNNTVKSLSLPSDDTHLFTKASLDEEGRPLIRKRMNSLQPKDFYKYLSLRNGENSNALDTAISAPQNEYQTYYNEPTSLFLTVPQKKTSKKSLSCDRIPNLVRSNNIILNDEATRTQESTNALNSISDVIDNSLLQYERDDIILDRTLSLCSTKSRTAWHSFQLYNYLTDVSLEIGFFEFLSLLVTTPVSIILYLSIPSEISQTDHDLPLSYLQNIQLIASPIILNQLITNNFSFWLLILSLVIAILLYFKTRTIPNKFNSDIIFTVAFLLSLACLSKAVHIIVVTLTHWINVFNISETILGLTIFTWGNSIGDLVSNITFVKIGVLEIAIGACFGSPLLYFLFGVGFDGIMIMLGDKTGKIVSGRDSNILMHHIDFKVDKNLINTGVGILIAFLIFTVLIPLNDWKIDKKISIALLTLYIVVTCISVFLEVHQV
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
28N-linked_GlycosylationIGYSLSSNGSISEFY
EEEECCCCCCCCHHH		44.87-
148N-linked_GlycosylationTEESFDQNLSYDRSN
CHHHHCCCCCCCCCC		32.57-
201PhosphorylationCAVYLIKSYKYPCEI
HHHHHHHHCCCCCHH		21.6228889911
280N-linked_GlycosylationLPSKSLDNISRFNQG
CCCCCCCHHHHHCCC		39.15-
329N-linked_GlycosylationWEKQNLFNNTVKSLS
HHHCCCCCCCCCCCC		46.56-
334PhosphorylationLFNNTVKSLSLPSDD
CCCCCCCCCCCCCCC		20.8930377154
336PhosphorylationNNTVKSLSLPSDDTH
CCCCCCCCCCCCCCC		45.3725752575
364PhosphorylationLIRKRMNSLQPKDFY
HHHHHHHCCCCHHHH		21.0223749301
476PhosphorylationIILDRTLSLCSTKSR
HHHHCHHHCCCCCCC		27.0728889911
479PhosphorylationDRTLSLCSTKSRTAW
HCHHHCCCCCCCCHH		44.1328889911
645N-linked_GlycosylationSIGDLVSNITFVKIG
CHHHHHHHCEEEEEC		29.82-
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 YD206_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YD206_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 YD206_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MKAR_YEASTIFA38physical
16093310
TECR_YEASTTSC13physical
16093310
HSP71_YEASTSSA1physical
22940862
SSB1_YEASTSSB1physical
22940862
CDC24_YEASTCDC24genetic
27708008
CND2_YEASTBRN1genetic
27708008
TFB1_YEASTTFB1genetic
27708008
SEC20_YEASTSEC20genetic
27708008
RSP5_YEASTRSP5genetic
27708008
ACT_YEASTACT1genetic
27708008
STT3_YEASTSTT3genetic
27708008
NUP57_YEASTNUP57genetic
27708008
CDC12_YEASTCDC12genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
SMC4_YEASTSMC4genetic
27708008
RU1C_YEASTYHC1genetic
27708008
ORC1_YEASTORC1genetic
27708008
MCM1_YEASTMCM1genetic
27708008
NOP2_YEASTNOP2genetic
27708008
RPC6_YEASTRPC34genetic
27708008
PROF_YEASTPFY1genetic
27708008
ASA1_YEASTASA1genetic
27708008
RPN7_YEASTRPN7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YD206_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-336, AND MASSSPECTROMETRY.

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