PRM5_YEAST - dbPTM
PRM5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRM5_YEAST
UniProt AC P40476
Protein Name Pheromone-regulated membrane protein 5
Gene Name PRM5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 318
Subcellular Localization Membrane
Single-pass membrane protein .
Protein Description
Protein Sequence MTVITIAKRGLPKLTTSTSSTTTASSSSTITSVASSSSSLPLLSNSTSSSIIPSITPPSRNGNPYILDSGDMPNGTVFIVVGGIAGVIFLAILLWWVITTYSSHRLTRSVQDYESKMFSTQHTQFYGDSPYMDYPAKENFQDQVHISESDISPGNKDESVKDALVSHTNNEKPFLSNFERPLFSLASESNRNSLFISPTGDILYKTRLSKLYQESPRLLQKPVIMTSDNVSTNSLVSTISSSSASSLDNGNEKEVGEDIRKPAKIASSPSRKLLNSPESDGSVNRNHSKGNLLVVQSKRKPTPSTYLEHMLEGKEQDE
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
2Phosphorylation------MTVITIAKR
------CCEEEEECC		22.1819823750
5Phosphorylation---MTVITIAKRGLP
---CCEEEEECCCCC		15.5619823750
116UbiquitinationSVQDYESKMFSTQHT
CHHHHHHHHHCCCCC		31.8323749301
129PhosphorylationHTQFYGDSPYMDYPA
CCCCCCCCCCCCCCC		17.3617330950
147PhosphorylationFQDQVHISESDISPG
CCCCEEECHHHCCCC		19.0321440633
149PhosphorylationDQVHISESDISPGNK
CCEEECHHHCCCCCC		33.1924961812
152PhosphorylationHISESDISPGNKDES
EECHHHCCCCCCCHH		31.5724961812
159PhosphorylationSPGNKDESVKDALVS
CCCCCCHHHHHHHHH		44.6028889911
187PhosphorylationRPLFSLASESNRNSL
CCHHHHHCCCCCCCE		47.0230377154
189PhosphorylationLFSLASESNRNSLFI
HHHHHCCCCCCCEEE		38.3030377154
197PhosphorylationNRNSLFISPTGDILY
CCCCEEECCCCHHHH		14.7428132839
199PhosphorylationNSLFISPTGDILYKT
CCEEECCCCHHHHHH		40.4728132839
205UbiquitinationPTGDILYKTRLSKLY
CCCHHHHHHHHHHHH		24.5923749301
210UbiquitinationLYKTRLSKLYQESPR
HHHHHHHHHHHHCCH		56.6723749301
215PhosphorylationLSKLYQESPRLLQKP
HHHHHHHCCHHHCCC		10.3725005228
267PhosphorylationRKPAKIASSPSRKLL
HHHHHHCCCCCHHHC		46.3727717283
268PhosphorylationKPAKIASSPSRKLLN
HHHHHCCCCCHHHCC		20.2028889911
270PhosphorylationAKIASSPSRKLLNSP
HHHCCCCCHHHCCCC		43.9523749301
272UbiquitinationIASSPSRKLLNSPES
HCCCCCHHHCCCCCC		62.7623749301
276PhosphorylationPSRKLLNSPESDGSV
CCHHHCCCCCCCCCC		29.9819823750
279PhosphorylationKLLNSPESDGSVNRN
HHCCCCCCCCCCCCC		51.1317330950
282PhosphorylationNSPESDGSVNRNHSK
CCCCCCCCCCCCCCC		22.6217330950
288PhosphorylationGSVNRNHSKGNLLVV
CCCCCCCCCCCEEEE		45.8917330950
302PhosphorylationVQSKRKPTPSTYLEH
EECCCCCCCCHHHHH		32.6723749301
304PhosphorylationSKRKPTPSTYLEHML
CCCCCCCCHHHHHHH		31.9624961812
305PhosphorylationKRKPTPSTYLEHMLE
CCCCCCCHHHHHHHC		33.0724961812
314UbiquitinationLEHMLEGKEQDE---
HHHHHCCCCCCC---		42.7123749301
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 PRM5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRM5_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 PRM5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC24_YEASTCDC24genetic
27708008
RPB1_YEASTRPO21genetic
27708008
FCF1_YEASTFCF1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
SWC4_YEASTSWC4genetic
27708008
ZPR1_YEASTZPR1genetic
27708008
NDC80_YEASTNDC80genetic
27708008
SLN1_YEASTSLN1genetic
27708008
NU192_YEASTNUP192genetic
27708008
PRI2_YEASTPRI2genetic
27708008
PRS7_YEASTRPT1genetic
27708008
ORC1_YEASTORC1genetic
27708008
MED11_YEASTMED11genetic
27708008
SPC24_YEASTSPC24genetic
27708008
SEC12_YEASTSEC12genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRM5_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-279 AND SER-282, ANDMASS 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-279, AND MASSSPECTROMETRY.
"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-129; SER-279; SER-282AND SER-288, AND MASS SPECTROMETRY.

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