FMP42_YEAST - dbPTM
FMP42_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FMP42_YEAST
UniProt AC Q04991
Protein Name Protein FMP42
Gene Name FMP42
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 504
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MTSTRTLRYAQVACACIWCLFSAGIIFGFAALKPILISEGVYHELCDPKDGDRLLCTAQDLKLNFIFALSATVTNIMALPVGKILDMYGPRVCGIIGSCLLFLASGNFISAKHLVSLWDPYLVGYTLLAVAGPFVFISCFQLANSFPQRSGTVLALLTGSFDSSSALFLLYRLLYQNWFPTLNVSRFFTLYLIVPVFILACQLTIMPHSSYKTVNHIAKIAVEGLDENGRLIEGDTGSGIIPDEQERQSLIAIEREEDSIPSRPQRRKSVLETYVEDKLQKKSGGIFGVLHGKSAYEQIKSPWFYLMLLFALVAMLRINYFIATVRTQEEYLLNDPDLALKLNSIFDMLLPLGGAVSIPFIGLLLDHTDTLSTLTILFTTSTAIGVFGLIPNSFTWNLIGIVLLVVYRPFYYTVVSDYSSKVFGFDTFGTVYGLLSCICGIFNMSQNLLDKWTHTTFNMNPFPINLTLVILTVVFSLTLTFYIRSQILPKPVNERGLSSNYQTI
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
189PhosphorylationLNVSRFFTLYLIVPV
CCHHHHHHHHHHHHH		16.2827017623
191PhosphorylationVSRFFTLYLIVPVFI
HHHHHHHHHHHHHHH		7.4227017623
211PhosphorylationTIMPHSSYKTVNHIA
CCCCCCCCCCHHHHH		17.4427017623
236PhosphorylationGRLIEGDTGSGIIPD
CCCCCCCCCCCCCCC		44.0722369663
238PhosphorylationLIEGDTGSGIIPDEQ
CCCCCCCCCCCCCHH		28.9822369663
249PhosphorylationPDEQERQSLIAIERE
CCHHHHHHHEEEECC		28.1517330950
259PhosphorylationAIEREEDSIPSRPQR
EEECCCCCCCCCHHH		39.4128889911
269PhosphorylationSRPQRRKSVLETYVE
CCHHHHHHHHHHHHH		30.0725521595
273PhosphorylationRRKSVLETYVEDKLQ
HHHHHHHHHHHHHHH		28.8022890988
274PhosphorylationRKSVLETYVEDKLQK
HHHHHHHHHHHHHHH		7.7722890988
278UbiquitinationLETYVEDKLQKKSGG
HHHHHHHHHHHHCCC		39.0324961812
283PhosphorylationEDKLQKKSGGIFGVL
HHHHHHHCCCEEEEE		49.6517563356
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 FMP42_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FMP42_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 FMP42_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATH_YEASTVMA13physical
18467557
FZO1_YEASTFZO1genetic
21987634
UGO1_YEASTUGO1genetic
21987634
ISC1_YEASTISC1genetic
21987634
GEP4_YEASTGEP4genetic
21987634
PT130_YEASTPET130genetic
21987634
MG101_YEASTMGM101genetic
21987634
MMM1_YEASTMMM1genetic
21987634
PFD5_YEASTGIM5genetic
21987634
YTA12_YEASTYTA12genetic
21987634
GATA_YEASTHER2genetic
21987634
GEP3_YEASTGEP3genetic
21987634
DPOG_YEASTMIP1genetic
21987634
VATH_YEASTVMA13physical
22615397
TAPT1_YEASTEMP65genetic
27708008
SLX5_YEASTSLX5genetic
27708008
MTU1_YEASTSLM3genetic
27708008
FADH_YEASTSFA1genetic
27708008
RT103_YEASTRTT103genetic
27708008
AIM11_YEASTAIM11genetic
27708008
RAD4_YEASTRAD4genetic
27708008
UBP6_YEASTUBP6genetic
27708008
MST27_YEASTMST27genetic
27708008
PIH1_YEASTPIH1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
YJ24_YEASTKCH1genetic
27708008
CBF1_YEASTCBF1genetic
27708008
YNL5_YEASTYNL115Cgenetic
27708008
ATG3_YEASTATG3genetic
27708008
PHSG_YEASTGPH1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FMP42_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 THR-236; SER-238; SER-249AND SER-269, 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-283, 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-238; SER-249 ANDSER-269, AND MASS SPECTROMETRY.

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