OSM1_YEAST - dbPTM
OSM1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSM1_YEAST
UniProt AC P21375
Protein Name Fumarate reductase 2
Gene Name OSM1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 501
Subcellular Localization Mitochondrion .
Protein Description Irreversibly catalyzes the reduction of fumarate to succinate. Together with the second isozyme of soluble fumarate reductase (FRD1), essential for anaerobic growth. Involved in maintaining redox balance during oxygen deficiency conditions. Reduction of fumarate is the main source of succinate during fermentation, and under anaerobic conditions, the formation of succinate is strictly required for the reoxidation of FADH(2)..
Protein Sequence MIRSVRRVFIYVSIFVLIIVLKRTLSGTDQTSMKQPVVVIGSGLAGLTTSNRLISKYRIPVVLLDKAASIGGNSIKASSGINGAHTDTQQNLKVMDTPELFLKDTLHSAKGRGVPSLMDKLTKESKSAIRWLQTEFDLKLDLLAQLGGHSVPRTHRSSGKLPPGFEIVQALSKKLKDISSKDSNLVQIMLNSEVVDIELDNQGHVTGVVYMDENGNRKIMKSHHVVFCSGGFGYSKEMLKEYSPNLIHLPTTNGKQTTGDGQKILSKLGAELIDMDQVQVHPTGFIDPNDRENNWKFLAAEALRGLGGILLHPTTGRRFTNELSTRDTVTMEIQSKCPKNDNRALLVMSDKVYENYTNNINFYMSKNLIKKVSINDLIRQYDLQTTASELVTELKSYSDVNTKDTFDRPLIINAFDKDISTESTVYVGEVTPVVHFTMGGVKINEKSQVIKKNSESVLSNGIFAAGEVSGGVHGANRLGGSSLLECVVFGKTAADNIAKLY
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
26PhosphorylationIVLKRTLSGTDQTSM
HHHHHHCCCCCCCCC		38.7525752575
31PhosphorylationTLSGTDQTSMKQPVV
HCCCCCCCCCCCCEE		33.3327017623
76UbiquitinationSIGGNSIKASSGING
HCCCCCCCCCCCCCC		41.8722817900
78PhosphorylationGGNSIKASSGINGAH
CCCCCCCCCCCCCCC		24.8928889911
103AcetylationDTPELFLKDTLHSAK
CCHHHHHHHHHHHHC		41.1324489116
105PhosphorylationPELFLKDTLHSAKGR
HHHHHHHHHHHHCCC		25.4527017623
108PhosphorylationFLKDTLHSAKGRGVP
HHHHHHHHHCCCCCC		34.4927017623
160AcetylationRTHRSSGKLPPGFEI
CCCCCCCCCCCCHHH		60.8224489116
173AcetylationEIVQALSKKLKDISS
HHHHHHHHHHCCCCC		64.0824489116
349PhosphorylationNRALLVMSDKVYENY
CEEEEEEECHHHHHC		27.1427017623
356PhosphorylationSDKVYENYTNNINFY
ECHHHHHCCCCCCEE		10.0227017623
357PhosphorylationDKVYENYTNNINFYM
CHHHHHCCCCCCEEC		33.1127017623
363PhosphorylationYTNNINFYMSKNLIK
CCCCCCEECCHHHCC		8.9427017623
365PhosphorylationNNINFYMSKNLIKKV
CCCCEECCHHHCCEE		13.6527017623
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 OSM1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSM1_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 OSM1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FRDS_YEASTFRD1genetic
18408719
LTE1_YEASTLTE1genetic
20093466
RS8A_YEASTRPS8Agenetic
20093466
RS8B_YEASTRPS8Agenetic
20093466
TPS1_YEASTTPS1genetic
20093466
RHEB_YEASTRHB1genetic
20093466
TAH1_YEASTTAH1genetic
20093466
GCS1_YEASTGCS1genetic
20093466
GLT1_YEASTGLT1genetic
20093466
CMR1_YEASTCMR1genetic
20093466
VMS1_YEASTVMS1genetic
20093466
TPS2_YEASTTPS2genetic
20093466
TRM1_YEASTTRM1genetic
20093466
MGDP1_YEASTYER134Cgenetic
20093466
MSH4_YEASTMSH4genetic
20093466
ATG18_YEASTATG18genetic
20093466
KEX1_YEASTKEX1genetic
20093466
PUS2_YEASTPUS2genetic
20093466
LIN1_YEASTLIN1genetic
20093466
OM45_YEASTOM45genetic
20093466
FIS1_YEASTFIS1genetic
20093466
GVP36_YEASTGVP36genetic
20093466
MPH1_YEASTMPH1genetic
20093466
MNN11_YEASTMNN11genetic
20093466
CYT2_YEASTCYT2genetic
20093466
YL179_YEASTYLR179Cgenetic
20093466
RS30A_YEASTRPS30Agenetic
20093466
RS30B_YEASTRPS30Agenetic
20093466
SPH1_YEASTSPH1genetic
20093466
PRM6_YEASTPRM6genetic
20093466
ERG2_YEASTERG2genetic
20093466
BUD7_YEASTBUD7genetic
20093466
ISW2_YEASTISW2genetic
20093466
RU2A_YEASTLEA1genetic
20093466
ATG5_YEASTATG5genetic
20093466
PPT2_YEASTPPT2genetic
21623372
PFKA1_YEASTPFK1genetic
21623372
NCBP2_YEASTCBC2genetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
TPS1_YEASTTPS1genetic
27708008
GPR1_YEASTGPR1genetic
27708008
GLT1_YEASTGLT1genetic
27708008
GCS1_YEASTGCS1genetic
27708008
VMS1_YEASTVMS1genetic
27708008
TPS2_YEASTTPS2genetic
27708008
DIN7_YEASTDIN7genetic
27708008
SWA2_YEASTSWA2genetic
27708008
LSM6_YEASTLSM6genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
RV167_YEASTRVS167genetic
27708008
GMC1_YEASTGMC1genetic
27708008
ACA1_YEASTACA1genetic
27708008
RAD51_YEASTRAD51genetic
27708008
MGDP1_YEASTYER134Cgenetic
27708008
ODPA_YEASTPDA1genetic
27708008
MSH4_YEASTMSH4genetic
27708008
ATG18_YEASTATG18genetic
27708008
MRM2_YEASTMRM2genetic
27708008
LAM1_YEASTYSP1genetic
27708008
PTH_YEASTPTH1genetic
27708008
GVP36_YEASTGVP36genetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
ESL1_YEASTESL1genetic
27708008
MPH1_YEASTMPH1genetic
27708008
CYT2_YEASTCYT2genetic
27708008
VPS51_YEASTVPS51genetic
27708008
RNP1_YEASTRNP1genetic
27708008
YL179_YEASTYLR179Cgenetic
27708008
SPH1_YEASTSPH1genetic
27708008
PRM6_YEASTPRM6genetic
27708008
PLB3_YEASTPLB3genetic
27708008
YPQ1_YEASTYPQ1genetic
27708008
HMI1_YEASTHMI1genetic
27708008
TGL5_YEASTTGL5genetic
27708008
BUD7_YEASTBUD7genetic
27708008
ISW2_YEASTISW2genetic
27708008
MGR2_YEASTMGR2genetic
27708008
ATG5_YEASTATG5genetic
27708008
DPOZ_YEASTREV3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OSM1_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-26, AND MASSSPECTROMETRY.

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