YL413_YEAST - dbPTM
YL413_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YL413_YEAST
UniProt AC Q06689
Protein Name Cell membrane protein YLR413W
Gene Name YLR413W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 675
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MNFKILLPICALLTLTTFLLTIIATAGSTSNYKPITNIYIGDADISKINVTKVMPQVGPILTVLGSALTAPNTTVDTIFGALKAIASTEALSPLLHLLSNAANTSATLSSLTQLAPMALLGTNTATTTTFSALDELLTTSKNTTELLDGFSTLMSSMSTNTSSTSASLENTVLTLLVDSTNPIGTTESLITLNNMTTEEKTKLSPVFELFASSKNITATCDALETIMNSTIPTSTVSSLFSSLKTSLAEGGNATETIMQLGSLVPSSLKPAVQAVVTLFDETTSQNVTLSVLSTMIAENITQSSSAKAAMGALTDLLNYTTNQTELLTSVESLALSKEAASSTNQLVALDEILSASANASTVVSIIPTLESQLANNTVLLKYVPYLFSLLAASSDPVSSFSSLVNITKWAETNAATFMPMLKILNSAVNMTTITPEQLKEMTPSILEYLHIPVIYRLSIFTMCRAHLNRTMYSCSKSHAVQNMDFRSIVYNNIEGSDFKPYMDALNIGKDDLHLDGELQDRQHMYVPAVKAALAMNLMCIITSFFLMVFLLLLSRRSVVSQKLWLALGFISCWICIFSGLGSTIFSVILNMMKSGSKKDNYDVIISGSSPFYGLMWSGFVFAVLVFLCIAYCWWSSRKGAAIVEAEKAVQESDSTTSRIIEEHESPIDAEKNFAR
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
49N-linked_GlycosylationDADISKINVTKVMPQ
CCCHHHCCCCEECCC		38.86-
72N-linked_GlycosylationGSALTAPNTTVDTIF
HHHHCCCCCHHHHHH		46.01-
103N-linked_GlycosylationHLLSNAANTSATLSS
HHHHHHCCCCCHHHH		31.96-
142N-linked_GlycosylationELLTTSKNTTELLDG
HHHHCCCCHHHHHHH		52.58-
160N-linked_GlycosylationLMSSMSTNTSSTSAS
HHHHHCCCCCCCCCH		30.56-
194N-linked_GlycosylationESLITLNNMTTEEKT
HHHEECCCCCHHHHH		32.08-
202AcetylationMTTEEKTKLSPVFEL
CCHHHHHCCCHHHHH		59.0224489116
215N-linked_GlycosylationELFASSKNITATCDA
HHHHCCCCCHHHHHH		38.50-
228N-linked_GlycosylationDALETIMNSTIPTST
HHHHHHHHCCCCHHH		31.95-
252N-linked_GlycosylationTSLAEGGNATETIMQ
HHHHCCCCHHHHHHH		55.32-
286N-linked_GlycosylationFDETTSQNVTLSVLS
CCCCCCCCCHHHHHH		28.63-
299N-linked_GlycosylationLSTMIAENITQSSSA
HHHHHHHCCCCCHHH		33.32-
318N-linked_GlycosylationGALTDLLNYTTNQTE
HHHHHHHHCCCCHHH		39.13-
322N-linked_GlycosylationDLLNYTTNQTELLTS
HHHHCCCCHHHHHHH		38.69-
358N-linked_GlycosylationEILSASANASTVVSI
HHHHHCCCCHHHHHH		31.74-
375N-linked_GlycosylationTLESQLANNTVLLKY
CHHHHHCCCCCHHHH		53.98-
405N-linked_GlycosylationSSFSSLVNITKWAET
CCCHHHHHHHHHHHH		41.32-
429N-linked_GlycosylationKILNSAVNMTTITPE
HHHHHHCCCCCCCHH		23.07-
468N-linked_GlycosylationTMCRAHLNRTMYSCS
HHHHHHHHHHHHHCC		27.75-
652PhosphorylationAEKAVQESDSTTSRI
HHHHHHHCCCCHHHH		21.5522369663
654PhosphorylationKAVQESDSTTSRIIE
HHHHHCCCCHHHHHH		42.7522369663
655PhosphorylationAVQESDSTTSRIIEE
HHHHCCCCHHHHHHH		33.5122369663
656PhosphorylationVQESDSTTSRIIEEH
HHHCCCCHHHHHHHC		21.6922369663
657PhosphorylationQESDSTTSRIIEEHE
HHCCCCHHHHHHHCC		22.9022369663
665PhosphorylationRIIEEHESPIDAEKN
HHHHHCCCCCCHHHH		29.1222369663
671UbiquitinationESPIDAEKNFAR---
CCCCCHHHHCCC---		60.1223749301
671AcetylationESPIDAEKNFAR---
CCCCCHHHHCCC---		60.1224489116
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 YL413_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YL413_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 YL413_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MEP3_YEASTMEP3physical
18467557
TCB3_YEASTTCB3physical
18467557
TCB3_YEASTTCB3physical
22615397
SSB1_YEASTSSB1physical
22940862
YL413_YEASTINA1physical
22940862
HSP71_YEASTSSA1physical
22940862
HSP72_YEASTSSA2physical
22940862
DED1_YEASTDED1physical
22940862
INO4_YEASTINO4genetic
27708008
TRM44_YEASTTRM44genetic
27708008
SHG1_YEASTSHG1genetic
27708008
ACA1_YEASTACA1genetic
27708008
CSK2B_YEASTCKB1genetic
27708008
YKJ1_YEASTYKL091Cgenetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
MSC1_YEASTMSC1genetic
27708008
NTH2_YEASTNTG2genetic
27708008
BUB3_YEASTBUB3genetic
27708008
SGF11_YEASTSGF11genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YL413_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-654; THR-655 ANDSER-665, AND MASS SPECTROMETRY.
"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-654; THR-655 ANDSER-665, AND MASS SPECTROMETRY.
"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-665, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND MASSSPECTROMETRY.
Ubiquitylation
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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-671, AND MASSSPECTROMETRY.

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