EAR1_YEAST - dbPTM
EAR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EAR1_YEAST
UniProt AC Q03212
Protein Name Protein EAR1
Gene Name EAR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 550
Subcellular Localization Endosome membrane
Single-pass type II membrane protein . Vacuole membrane
Single-pass type II membrane protein .
Protein Description Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane (By similarity)..
Protein Sequence MSFKFLIESLLLGSISGQIRCGRSSVIPRGDVSYGGDDTDELNMDIMLFAFGTLIVVYIVICIVYFFTKQIATRLITAYYNEHGPGQRISLFSDYDENNAHVHSRRLMENMSLRWPNNLDDADEVRDKLAQLSPEEQFYYKQGEEYIKQNPPFLLNQGLLQQSEDSNPDTTREDPIMNEQTRQYIQEEGAYAWEFSPNPDMPNHTVIVENKTEVSFLNYNYDASISTNLPIPCINKVYYCEFKIFETDGPLNSDENVSKGVISFGLSTQPYPYFRLPGRHHHSIAYDSNGARRFNDSFKLNEQLRTLFPQCEKGDIVGIGYRSRSGTVFFTRNGKKLNEKSVGGHIRGWKFQYLYPIIGSNVPCQIHVNFGTYGFVYIEANVKKWGYAKSNGIKLPPPSYEDYGKDTLLESGGEDNDFDEDFSDGDSDNIAAGSTTNLNDDIIIRNGEILPPPPGFEFTMSPPTGKKIINEEINLDSLPMLPPSYSDDEHHSKNDKSAISGRIIGTSRNLITDEASFDSVDNDNEDENDHERDPEQFSEFDDYESRMHGI
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
110N-linked_GlycosylationHSRRLMENMSLRWPN
HHHHHHHHCCCCCCC		16.04-
128UbiquitinationDADEVRDKLAQLSPE
CHHHHHHHHHHCCHH		34.8523749301
141UbiquitinationPEEQFYYKQGEEYIK
HHHHHHHHHHHHHHH		40.2123749301
203N-linked_GlycosylationSPNPDMPNHTVIVEN
CCCCCCCCCEEEECC		36.50-
210N-linked_GlycosylationNHTVIVENKTEVSFL
CCEEEECCCCEEEEC		45.73-
253PhosphorylationETDGPLNSDENVSKG
ECCCCCCCCCCCCCC		54.7228889911
256N-linked_GlycosylationGPLNSDENVSKGVIS
CCCCCCCCCCCCEEE		48.64-
295N-linked_GlycosylationSNGARRFNDSFKLNE
CCCCCCCCCCHHHHH		42.05-
313UbiquitinationTLFPQCEKGDIVGIG
HHCCCCCCCCEEEEE		70.3023749301
327PhosphorylationGYRSRSGTVFFTRNG
EEECCCCEEEEECCC		18.5228889911
384UbiquitinationYIEANVKKWGYAKSN
EEEEEECCCEEECCC		41.3818433149
461PhosphorylationPGFEFTMSPPTGKKI
CCCEEEECCCCCCCC		25.3529734811
484PhosphorylationSLPMLPPSYSDDEHH
CCCCCCCCCCCCCCC		35.0220377248
485PhosphorylationLPMLPPSYSDDEHHS
CCCCCCCCCCCCCCC		23.1520377248
486PhosphorylationPMLPPSYSDDEHHSK
CCCCCCCCCCCCCCC		42.8121440633
492PhosphorylationYSDDEHHSKNDKSAI
CCCCCCCCCCCHHHH		34.7520377248
496UbiquitinationEHHSKNDKSAISGRI
CCCCCCCHHHHHHHC		51.7023749301
506PhosphorylationISGRIIGTSRNLITD
HHHHCCCCCCCCCCC		17.6927017623
516PhosphorylationNLITDEASFDSVDND
CCCCCCHHCCCCCCC		27.7821440633
519PhosphorylationTDEASFDSVDNDNED
CCCHHCCCCCCCCCC		29.3821440633
538PhosphorylationERDPEQFSEFDDYES
CCCHHHHHCCHHHHH		36.7328889911
543PhosphorylationQFSEFDDYESRMHGI
HHHCCHHHHHHHCCC		20.0419779198
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EAR1_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 EAR1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSP5_YEASTRSP5physical
18367543
RL8A_YEASTRPL8Agenetic
27708008
VRP1_YEASTVRP1genetic
27708008
COG7_YEASTCOG7genetic
27708008
IST3_YEASTIST3genetic
27708008
VPS53_YEASTVPS53genetic
27708008
ASF1_YEASTASF1genetic
27708008
DBP7_YEASTDBP7genetic
27708008
YPT6_YEASTYPT6genetic
27708008
TLG2_YEASTTLG2genetic
27708008
DCAM_YEASTSPE2genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EAR1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516 AND SER-519, ANDMASS SPECTROMETRY.
"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 THR-327, AND MASSSPECTROMETRY.

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