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UniProtKB/Swiss-Prot entry P46151


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MTHR1_YEAST
Primary accession number P46151
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 68)
Name and origin of the protein
Protein name Methylenetetrahydrofolate reductase 1
Synonym EC 1.5.1.20
Gene name
Name: MET12
OrderedLocusNames: YPL023C
ORFNames: LPB8C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131.
PubMed=6095044 [NCBI, ExPASy, EBI, Israel, Japan]
Yang E., Friedberg E.C.;
"Molecular cloning and nucleotide sequence analysis of the Saccharomyces cerevisiae RAD1 gene.";
Mol. Cell. Biol. 4:2161-2169(1984).
[3]
IDENTIFICATION.
DOI=10.1038/ng0694-195; PubMed=7920641 [NCBI, ExPASy, EBI, Israel, Japan]
Goyette P., Sumner J.S., Milos R., Duncan A.M.V., Rosenblatt D.S., Matthews R.G., Rozen R.;
"Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification.";
Nat. Genet. 7:195-200(1994).
[4]
ERRATUM.
PubMed=7951330 [NCBI, ExPASy, EBI, Israel, Japan]
Goyette P., Sumner J.S., Milos R., Duncan A.M.V., Rosenblatt D.S., Matthews R.G., Rozen R.;
Nat. Genet. 7:551-551(1994).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-359, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-301; SER-358; SER-359 AND THR-407, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U36624; AAB68164.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02070; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR S63459; S63459.
RefSeq NP_015302.1; -.
3D structure databases
HSSP P00394; 1B5T. [HSSP ENTRY / PDB]
ModBase P46151.
Protein-protein interaction databases
DIP DIP:2825N; -.
IntAct P46151; -.
Organism-specific databases
CYGD YPL023c; -.
SGD S000005944; MET12.
Yeast-GFP YPL023C.
Gene expression databases
ArrayExpress P46151; -.
GermOnline YPL023C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0004489; Molecular function: methylenetetrahydrofolate reductase (NADPH) activity (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006555; Biological process: methionine metabolic process (traceable author statement from SGD).
QuickGo view.
Family and domain databases
InterPro IPR004621; Fadh2_euk.
IPR003171; Mehydrof_redctse.
Graphical view of domain structure.
Pfam PF02219; MTHFR; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00677; fadh2_euk; 1.
BLOCKS P46151.
Proteomic databases
PeptideAtlas P46151; -.
Genome annotation databases
Ensembl YPL023C; Saccharomyces cerevisiae. [Contig view]
GeneID 856084; -.
GenomeReviews U00094_GR; YPL023C.
KEGG sce:YPL023C; -.
NMPDR fig|4932.3.peg.6436; -.
Phylogenomic databases
HOGENOM P46151; -.
Other
LinkHub P46151; -.
ProtoNet P46151.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; FAD; Flavoprotein; NADP; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   657  657     Methylenetetrahydrofolate reductase 1. PRO_0000190255
MOD_RES   120   120        Phosphoserine. 
MOD_RES   301   301        Phosphoserine. 
MOD_RES   358   358        Phosphoserine. 
MOD_RES   359   359        Phosphoserine. 
MOD_RES   407   407        Phosphothreonine. 
CONFLICT   110   111        DP -> NL (in Ref. 2). 
CONFLICT   115   116        ED -> VV (in Ref. 2). 
CONFLICT   119   119        D -> V (in Ref. 2). 
CONFLICT   124   131        ESPFKYAV -> RLLNMRLF (in Ref. 2). 
Sequence information
Length: 657 AA [This is the length of the unprocessed precursor] Molecular weight: 73942 Da [This is the MW of the unprocessed precursor] CRC64: D75612EA92D67500 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSIRDLYHAR ASPFISLEFF PPKTELGTRN LMERMHRMTA LDPLFITVTW GAGGTTAEKT 

        70         80         90        100        110        120 
LTLASLAQQT LNIPVCMHLT CTNTEKAIID DALDRCYNAG IRNILALRGD PPIGEDWLDS 

       130        140        150        160        170        180 
QSNESPFKYA VDLVRYIKQS YGDKFCVGVA AYPEGHCEGE AEGHEQDPLK DLVYLKEKVE 

       190        200        210        220        230        240 
AGADFVITQL FYDVEKFLTF EMLFRERISQ DLPLFPGLMP INSYLLFHRA AKLSHASIPP 

       250        260        270        280        290        300 
AILSRFPPEI QSDDNAVKSI GVDILIELIQ EIYQRTSGRI KGFHFYTLNL EKAIAQIVSQ 

       310        320        330        340        350        360 
SPVLSHIVNE SSEEEGEDET SGEIGSIENV PIEDADGDIV LDDSNEETVA NRKRRRHSSL 

       370        380        390        400        410        420 
DSAKLIFNRA IVTEKGLRYN NENGSMPSKK ALISISKGHG TLGRDATWDE FPNGRFGDSR 

       430        440        450        460        470        480 
SPAYGEIDGY GPSIKVSKSK ALELWGIPKT IGDLKDIFIK YLEGSTDAIP WSDLGLSAET 

       490        500        510        520        530        540 
ALIQEELIQL NYRGYLTLAS QPATNATLSS DKIFGWGPAK GRLYQKAFVE MFIHRQQWET 

       550        560        570        580        590        600 
TLKPKLDHYG RRKFSYYAGD SSGSFETNLD PHSSSVVTWG VFPNSPVKQT TIIEEESFKA 

       610        620        630        640        650 
WRDEAFSIWS EWAKLFPRNT PANILLRLVH KDYCLVSIVH HDFKETDELW EMLLDQA 

P46151 in FASTA format

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View entry in raw text format (no links)
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