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UniProtKB/Swiss-Prot entry P78958


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

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Entry information
Entry name G3P1_SCHPO
Primary accession number P78958
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on May 1, 1997 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 65)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase 1
Synonyms GAPDH 1
EC 1.2.1.12
Gene name
Name: tdh1
Synonyms: gpd1
ORFNames: SPBC32F12.11
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Orlandi I., Popolo L., Cavadini P., Vai M.;
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-125, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(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
X85332; CAA59681.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329671; CAA19372.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T40235; T40235.
RefSeq NP_596154.1; -.
3D structure databases
HSSP P56649; 1DSS. [HSSP ENTRY / PDB]
SMR P78958; 5-335.
ModBase P78958.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-004190-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC32F12.11; -.
Gene expression databases
ArrayExpress P78958; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (non-traceable author statement from GeneDB_SPombe).
GO:0009992; Biological process: cellular water homeostasis (inferred from expression pattern from GeneDB_SPombe).
GO:0006094; Biological process: gluconeogenesis (inferred by curator from GeneDB_SPombe).
GO:0006096; Biological process: glycolysis (inferred by curator from GeneDB_SPombe).
GO:0006970; Biological process: response to osmotic stress (inferred from expression pattern from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR000173; GlycerAld_3-P_DHase.
IPR006424; Glyceraldehyde-3-P_DHase_1.
Graphical view of domain structure.
PANTHER PTHR10836; GAP_DH; 1.
Pfam PF02800; Gp_dh_C; 1.
PF00044; Gp_dh_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000149; GAP_DH; 1.
PRINTS PR00078; G3PDHDRGNASE.
TIGRFAMs TIGR01534; GAPDH-I; 1.
PROSITE PS00071; GAPDH; 1.
BLOCKS P78958.
Genome annotation databases
GeneID 2540547; -.
KEGG spo:SPBC32F12.11; -.
NMPDR fig|4896.1.peg.2020; -.
Other
ProtoNet P78958.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   336  336     Glyceraldehyde-3-phosphate dehydrogenase 1. PRO_0000145580
NP_BIND   13    14  2     NAD (By similarity). 
REGION   151   153  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   211   212  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   152   152        Nucleophile (By similarity). 
BINDING   35    35        NAD (By similarity). 
BINDING   80    80        NAD; via carbonyl oxygen (By similarity). 
BINDING   182   182        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   234   234        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   316   316        NAD (By similarity). 
SITE   179   179  1     Activates thiol group during catalysis (By similarity). 
MOD_RES   59    59        Phosphoserine. 
MOD_RES   125   125        Phosphoserine. 
Sequence information
Length: 336 AA [This is the length of the unprocessed precursor] Molecular weight: 35870 Da [This is the MW of the unprocessed precursor] CRC64: 38E58E194FF4747A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAIPKVGING FGRIGRIVLR NALVAKTIQV VAINDPFIDL EYMAYMFKYD STHGRFDGSV 

        70         80         90        100        110        120 
EIKDGKLVID GNAIDVHNER DPADIKWSTS GADYVIESTG VFTTQETASA HLKGGAKRVI 

       130        140        150        160        170        180 
ISAPSKDAPM YVVGVNEEKF NPSEKVISNA SCTTNCLAPL AKVINDTFGI EEGLMTTVHA 

       190        200        210        220        230        240 
TTATQKTVDG PSKKDWRGGR GASANIIPSS TGAAKAVGKV IPALNGKLTG MAFRVPTPDV 

       250        260        270        280        290        300 
SVVDLTVKLA KPTNYEDIKA AIKAASEGPM KGVLGYTEDA VVSTDFCGDN HSSIFDASAG 

       310        320        330 
IQLSPQFVKL VSWYDNEWGY SRRVVDLVAY TAAKDN 

P78958 in FASTA format

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