YD338_YEAST - dbPTM
YD338_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YD338_YEAST
UniProt AC Q05497
Protein Name Uncharacterized transporter YDR338C
Gene Name YDR338C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 695
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MAGILSKTLSEVHPSLRTNGMGIGNTHRRISLGFLPPNKKNPLVRKFRARTRNIDQRSFRSLTDDFGSNVHEPNPYLGNIDEEPDLYYHDEEDGELSRTISLPSRVSETPELSPQDVDWILHEHERRYSSVCNSDNEEASQSNTPDRIQEYSGRELEYDEFMNRLQAQKQKLTRSAVTDAKGTSHHRRPSFVSVTSRGSVPTIYQEIDENDSEALAELAHSHVTFKSEARVLASYSFPLIFTFLLEQIFPMVCSLTVGHLGKNELAAVSLASMTSNITLAIFEGIATSLDTLCPQAYGSGRFYSVGVHLQRCIAFSLVIYIPFAVMWWYSEPLLSYIIPEKELINLTSRFLRVLILGAPAYIFFENLKRFLQAQGIFDAGIYVLTICAPLNVLVSYTLVWNKYIGVGFIGAAIAVVLNFWLMFFLLLFYALYIDGRKCWGGFSRKAFTHWNDLGHLAFSGIIMLEAEELSYELLTLFSAYYGVSYLAAQSAVSTMAALLYMIPFAIGISTSTRIANFIGAKRTDFAHISSQVGLSFSFIAGFINCCILVFGRNLIANIYSKDPEVIKLIAQVLPLVGIVQNFDSLNAVAGSCLRGQGMQSLGSIVNLMAYYLFGIPLALILSWFFDMKLYGLWIGIGSAMLLIGLVEAYYVLFPDWDKIMTYAEILKETEDDEVDSDEYLTDSDDPDENTALLGA
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
31PhosphorylationGNTHRRISLGFLPPN
CCCCCCEECCCCCCC		22.1919779198
58PhosphorylationTRNIDQRSFRSLTDD
CCCCCHHHHHHHCCC		21.2721440633
61PhosphorylationIDQRSFRSLTDDFGS
CCHHHHHHHCCCCCC		33.3428889911
63PhosphorylationQRSFRSLTDDFGSNV
HHHHHHHCCCCCCCC		34.4719779198
76PhosphorylationNVHEPNPYLGNIDEE
CCCCCCCCCCCCCCC		33.6019779198
87PhosphorylationIDEEPDLYYHDEEDG
CCCCCCCEEECCCCC		13.2128889911
101PhosphorylationGELSRTISLPSRVSE
CCEEEEEECCCCCCC		33.3525752575
109PhosphorylationLPSRVSETPELSPQD
CCCCCCCCCCCCHHH		17.9819779198
113PhosphorylationVSETPELSPQDVDWI
CCCCCCCCHHHCHHH		20.8928889911
128PhosphorylationLHEHERRYSSVCNSD
HHHCHHHHHHHCCCC		16.1223749301
129PhosphorylationHEHERRYSSVCNSDN
HHCHHHHHHHCCCCC		17.9323749301
130PhosphorylationEHERRYSSVCNSDNE
HCHHHHHHHCCCCCH		23.0423749301
134PhosphorylationRYSSVCNSDNEEASQ
HHHHHCCCCCHHHHH		36.3623749301
140PhosphorylationNSDNEEASQSNTPDR
CCCCHHHHHCCCCHH		37.1023749301
142PhosphorylationDNEEASQSNTPDRIQ
CCHHHHHCCCCHHHH		39.9323749301
144PhosphorylationEEASQSNTPDRIQEY
HHHHHCCCCHHHHHC		31.6423749301
190PhosphorylationTSHHRRPSFVSVTSR
CCCCCCCCEEEEECC		36.1528889911
199PhosphorylationVSVTSRGSVPTIYQE
EEEECCCCCCCEEEE		24.6629688323
202PhosphorylationTSRGSVPTIYQEIDE
ECCCCCCCEEEECCC		30.1129688323
204PhosphorylationRGSVPTIYQEIDEND
CCCCCCEEEECCCCC		11.5429688323
212PhosphorylationQEIDENDSEALAELA
EECCCCCHHHHHHHH		36.0321440633
221PhosphorylationALAELAHSHVTFKSE
HHHHHHHHCCCCCHH		17.6629688323
224PhosphorylationELAHSHVTFKSEARV
HHHHHCCCCCHHHHH		21.6629688323
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 YD338_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YD338_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 YD338_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP71_YEASTSSA1physical
19536198
CALM_YEASTCMD1genetic
27708008
PRP3_YEASTPRP3genetic
27708008
FDFT_YEASTERG9genetic
27708008
CDC11_YEASTCDC11genetic
27708008
SC61A_YEASTSEC61genetic
27708008
ERO1_YEASTERO1genetic
27708008
LIP1_YEASTLIP1genetic
27708008
MED4_YEASTMED4genetic
27708008
EI2BG_YEASTGCD1genetic
27708008
ASA1_YEASTASA1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YD338_YEAST

loading...

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-61 AND TYR-87, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory