MCR1_YEAST - dbPTM
MCR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCR1_YEAST
UniProt AC P36060
Protein Name NADH-cytochrome b5 reductase 2
Gene Name MCR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 302
Subcellular Localization NADH-cytochrome b5 reductase p32 form: Mitochondrion intermembrane space.
NADH-cytochrome b5 reductase p34 form: Mitochondrion outer membrane
Single-pass membrane protein. Mitochondrion intermembrane space .
Protein Description The outer membrane form may mediate the reduction of outer membrane cytochrome b5, and the soluble inter-membrane space form may transfer electrons from external NADH to cytochrome c, thereby mediating an antimycin-insensitive, energy-coupled oxidation of external NADH by yeast mitochondria. Involved in the reduction of D-erythroascorbyl free radicals..
Protein Sequence MFSRLSRSHSKALPIALGTVAIAAATAFYFANRNQHSFVFNESNKVFKGDDKWIDLPISKIEEESHDTRRFTFKLPTEDSEMGLVLASALFAKFVTPKGSNVVRPYTPVSDLSQKGHFQLVVKHYEGGKMTSHLFGLKPNDTVSFKGPIMKWKWQPNQFKSITLLGAGTGINPLYQLAHHIVENPNDKTKVNLLYGNKTPQDILLRKELDALKEKYPDKFNVTYFVDDKQDDQDFDGEISFISKDFIQEHVPGPKESTHLFVCGPPPFMNAYSGEKKSPKDQGELIGILNNLGYSKDQVFKF
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
6Phosphorylation--MFSRLSRSHSKAL
--CCCCCCHHHCCHH		30.5425533186
37PhosphorylationFANRNQHSFVFNESN
HHCCCCCEEEEECCC		17.2227214570
48AcetylationNESNKVFKGDDKWID
ECCCCEEECCCCEEE		65.5024489116
52AcetylationKVFKGDDKWIDLPIS
CEEECCCCEEECCHH		51.2824489116
52UbiquitinationKVFKGDDKWIDLPIS
CEEECCCCEEECCHH		51.2824961812
98UbiquitinationFAKFVTPKGSNVVRP
HHHHCCCCCCCCCCC		66.6524961812
106PhosphorylationGSNVVRPYTPVSDLS
CCCCCCCCCCHHHHH		17.0827017623
110PhosphorylationVRPYTPVSDLSQKGH
CCCCCCHHHHHCCCC		33.7527017623
129AcetylationVKHYEGGKMTSHLFG
EEEECCCEEEEEECC		50.2724489116
131PhosphorylationHYEGGKMTSHLFGLK
EECCCEEEEEECCCC		19.2419823750
132PhosphorylationYEGGKMTSHLFGLKP
ECCCEEEEEECCCCC		18.0719823750
138AcetylationTSHLFGLKPNDTVSF
EEEECCCCCCCEEEE		42.0024489116
142PhosphorylationFGLKPNDTVSFKGPI
CCCCCCCEEEEECCC		25.3719823750
144PhosphorylationLKPNDTVSFKGPIMK
CCCCCEEEEECCCCC		24.2719823750
146AcetylationPNDTVSFKGPIMKWK
CCCEEEEECCCCCEE		57.1624489116
153AcetylationKGPIMKWKWQPNQFK
ECCCCCEECCCCCCC		30.3624489116
160UbiquitinationKWQPNQFKSITLLGA
ECCCCCCCEEEEECC		31.0517644757
188UbiquitinationIVENPNDKTKVNLLY
HHHCCCCCCEEEEEE		57.8117644757
188AcetylationIVENPNDKTKVNLLY
HHHCCCCCCEEEEEE		57.8124489116
190AcetylationENPNDKTKVNLLYGN
HCCCCCCEEEEEECC		34.5624489116
255UbiquitinationQEHVPGPKESTHLFV
HHCCCCCCCCCEEEE		70.9317644757
276UbiquitinationMNAYSGEKKSPKDQG
CCCCCCCCCCHHHHH		63.1817644757
277UbiquitinationNAYSGEKKSPKDQGE
CCCCCCCCCHHHHHH		68.6317644757
277AcetylationNAYSGEKKSPKDQGE
CCCCCCCCCHHHHHH		68.6324489116
278PhosphorylationAYSGEKKSPKDQGEL
CCCCCCCCHHHHHHH		48.5322369663
280AcetylationSGEKKSPKDQGELIG
CCCCCCHHHHHHHHH		70.5424489116
296UbiquitinationLNNLGYSKDQVFKF-
HHHCCCCHHHCCCC-		43.6323749301
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 MCR1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCR1_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 MCR1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ALO_YEASTALO1physical
18467557
YAJ9_YEASTYAR029Wgenetic
20093466
TPS1_YEASTTPS1genetic
20093466
DPB3_YEASTDPB3genetic
20093466
SLX5_YEASTSLX5genetic
20093466
ALAM_YEASTALT1genetic
20093466
PHO23_YEASTPHO23genetic
20093466
MSB4_YEASTMSB4genetic
20093466
SIN3_YEASTSIN3genetic
20093466
MCH5_YEASTMCH5genetic
20093466
NIP80_YEASTNIP100genetic
20093466
IPK1_YEASTIPK1genetic
21987634
CYK2_YEASTHOF1genetic
21987634
GEP3_YEASTGEP3genetic
21987634
FABD_YEASTMCT1genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
MGR1_YEASTMGR1genetic
27708008
IMG2_YEASTIMG2genetic
27708008
GPR1_YEASTGPR1genetic
27708008
CGR1_YEASTCGR1genetic
27708008
YJ24_YEASTKCH1genetic
27708008
ALAM_YEASTALT1genetic
27708008
PHO23_YEASTPHO23genetic
27708008
MSB4_YEASTMSB4genetic
27708008
NIP80_YEASTNIP100genetic
27708008
YP148_YEASTYPR148Cgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MCR1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-278, AND MASSSPECTROMETRY.

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