YD090_YEAST - dbPTM
YD090_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YD090_YEAST
UniProt AC Q03193
Protein Name Uncharacterized membrane protein YDR090C
Gene Name YDR090C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 310
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MISEKAATALATIATVCWCVQLIPQIIYNWKKKDCTGLPPLMMFLWVVSGIPFAIYFCVSKGNVILQVQPHLFMFFCSISFVQSCYYPPISMARSKIVMIVAAIIAADVGMEVGFILWLRPLYEKGVKWPDLIFGISASVLLAVGLLPPYFELAKRKGRVIGINFAFLFIDSLGAWLSIISVILGNMDIMGIILYSIVAGMELGIFASHFIWWCRFRFLAKGNTFDEESGQAQKEEPDEKIEQDISKSDRNVTNYNLDNCSIPDDASSFADDFNIYDSTDGGTLSRAQTLHAVHGVVVRTDPDRYSRLSV
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
224PhosphorylationRFLAKGNTFDEESGQ
HHHHCCCCCCCCCCC
40.9220377248
229PhosphorylationGNTFDEESGQAQKEE
CCCCCCCCCCCCHHC
33.8722369663
234UbiquitinationEESGQAQKEEPDEKI
CCCCCCCHHCCCHHH
68.0423749301
240UbiquitinationQKEEPDEKIEQDISK
CHHCCCHHHHHHCCH
59.9523749301
246PhosphorylationEKIEQDISKSDRNVT
HHHHHHCCHHHCCCC
34.1028889911
247UbiquitinationKIEQDISKSDRNVTN
HHHHHCCHHHCCCCC
57.6223749301
248PhosphorylationIEQDISKSDRNVTNY
HHHHCCHHHCCCCCC
34.7028889911
251N-linked_GlycosylationDISKSDRNVTNYNLD
HCCHHHCCCCCCCCC
50.37-
259N-linked_GlycosylationVTNYNLDNCSIPDDA
CCCCCCCCCCCCCCH
25.30-
289PhosphorylationGTLSRAQTLHAVHGV
CCCCHHHHHEEECEE
21.3721440633
305PhosphorylationVRTDPDRYSRLSV--
EECCCCCCCCCCC--
12.9127017623
306PhosphorylationRTDPDRYSRLSV---
ECCCCCCCCCCC---
27.8628889911
309PhosphorylationPDRYSRLSV------
CCCCCCCCC------
25.3521440633

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 YD090_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YD090_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 YD090_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APC11_YEASTAPC11genetic
27708008
CDC53_YEASTCDC53genetic
27708008
RPB1_YEASTRPO21genetic
27708008
TCPD_YEASTCCT4genetic
27708008
TFB1_YEASTTFB1genetic
27708008
RPB7_YEASTRPB7genetic
27708008
ACT_YEASTACT1genetic
27708008
PRP43_YEASTPRP43genetic
27708008
RRP3_YEASTRRP3genetic
27708008
ARP4_YEASTARP4genetic
27708008
KRE9_YEASTKRE9genetic
27708008
PRS7_YEASTRPT1genetic
27708008
MED14_YEASTRGR1genetic
27708008
DCP2_YEASTDCP2genetic
27708008
CAP_YEASTSRV2genetic
27708008
NUF2_YEASTNUF2genetic
27708008
PROF_YEASTPFY1genetic
27708008
RPB2_YEASTRPB2genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YD090_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND MASSSPECTROMETRY.

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