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UniProtKB/Swiss-Prot entry P53204


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

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Entry information
Entry name NMA2_YEAST
Primary accession number P53204
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 59)
Name and origin of the protein
Protein name Nicotinamide-nucleotide adenylyltransferase 2
Synonyms EC 2.7.7.1
NAD(+) pyrophosphorylase 2
NAD(+) diphosphorylase 2
NMN adenylyltransferase 2
Gene name
Name: NMA2
OrderedLocusNames: YGR010W
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 96604 / S288c / FY1679;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[2]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1074/jbc.M111773200; PubMed=11884393 [NCBI, ExPASy, EBI, Israel, Japan]
Anderson R.M., Bitterman K.J., Wood J.G., Medvedik O., Cohen H., Lin S.S., Manchester J.K., Gordon J.I., Sinclair D.A.;
"Manipulation of a nuclear NAD+ salvage pathway delays aging without altering steady-state NAD+ levels.";
J. Biol. Chem. 277:18881-18890(2002).
[3]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, 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
Z72795; CAA96993.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S64299; S64299.
RefSeq NP_011524.1; -.
3D structure databases
HSSP Q9HAN9; 1KR2. [HSSP ENTRY / PDB]
ModBase P53204.
Protein-protein interaction databases
DIP DIP:1227N; -.
IntAct P53204; 8.
Enzyme and pathway databases
BioCyc MetaCyc:YGR010W-MON; -.
Organism-specific databases
CYGD YGR010w; -.
SGD S000003242; NMA2.
Yeast-GFP YGR010W.
Gene expression databases
ArrayExpress P53204; -.
GermOnline YGR010W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0000309; Molecular function: nicotinamide-nucleotide adenylyltransferase activity (inferred from electronic annotation from EC).
GO:0004515; Molecular function: nicotinate-nucleotide adenylyltransferase activity (inferred from genetic interaction from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0009435; Biological process: NAD biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR004820; Cytidylyltransf.
IPR005248; NAMN_adtrnsfrase.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
PANTHER PTHR12039; NAMN_adtrnsfrase; 1.
Pfam PF01467; CTP_transf_2; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00482; NAMN_adtrnsfrase; 1.
Genome annotation databases
Ensembl YGR010W; Saccharomyces cerevisiae. [Contig view]
GeneID 852893; -.
GenomeReviews Y13135_GR; YGR010W.
KEGG sce:YGR010W; -.
NMPDR fig|4932.3.peg.2634; -.
Phylogenomic databases
HOGENOM P53204; -.
Other
LinkHub P53204; -.
NextBio 972562; -.
ProtoNet P53204.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Nucleotidyltransferase; Nucleus; Phosphoprotein; Pyridine nucleotide biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   395  395     Nicotinamide-nucleotide adenylyltransferase 2. PRO_0000135019
MOD_RES   85    85        Phosphoserine. 
Sequence information
Length: 395 AA [This is the length of the unprocessed precursor] Molecular weight: 44909 Da [This is the MW of the unprocessed precursor] CRC64: 4A358AF7885B6568 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDPTKAPDFK PPQPNEELQP PPDPTHTIPK SGPIVPYVLA DYNSSIDAPF NLDIYKTLSS 

        70         80         90        100        110        120 
RKKNANSSNR MDHIPLNTSD FQPLSRDVSS EEESEGQSNG IDATLQDVTM TGNLGVLKSQ 

       130        140        150        160        170        180 
IADLEEVPHT IVRQARTIED YEFPVHRLTK KLQDPEKLPL IIVACGSFSP ITYLHLRMFE 

       190        200        210        220        230        240 
MALDDINEQT RFEVVGGYFS PVSDNYQKRG LAPAYHRVRM CELACERTSS WLMVDAWESL 

       250        260        270        280        290        300 
QSSYTRTAKV LDHFNHEINI KRGGIMTVDG EKMGVKIMLL AGGDLIESMG EPHVWADSDL 

       310        320        330        340        350        360 
HHILGNYGCL IVERTGSDVR SFLLSHDIMY EHRRNILIIK QLIYNDISST KVRLFIRRGM 

       370        380        390 
SVQYLLPNSV IRYIQEYNLY INQSEPVKQV LDSKE 

P53204 in FASTA format

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