ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry O43026


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name G3P2_SCHPO
Primary accession number O43026
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on June 1, 1998 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 61)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase 2
Synonyms GAPDH 2
EC 1.2.1.12
Gene name
Name: gpd3
ORFNames: SPBC354.12
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 [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).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-151; THR-153; THR-154; THR-182; THR-184; SER-192; SER-203; SER-209; THR-211; THR-237 AND SER-241, 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
CU329671; CAA17812.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T40292; T40292.
RefSeq NP_595236.1; -.
3D structure databases
HSSP P56649; 1CRW. [HSSP ENTRY / PDB]
SMR O43026; 5-335.
ModBase O43026.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-003322-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC354.12; -.
Gene expression databases
ArrayExpress O43026; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay 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 O43026.
Genome annotation databases
GeneID 2540975; -.
KEGG spo:SPBC354.12; -.
NMPDR fig|4896.1.peg.1102; -.
Other
ProtoNet O43026.
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   335  335     Glyceraldehyde-3-phosphate dehydrogenase 2. PRO_0000145581
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   125   125        Phosphoserine. 
MOD_RES   151   151        Phosphoserine. 
MOD_RES   153   153        Phosphothreonine. 
MOD_RES   154   154        Phosphothreonine. 
MOD_RES   182   182        Phosphothreonine. 
MOD_RES   184   184        Phosphothreonine. 
MOD_RES   192   192        Phosphoserine. 
MOD_RES   203   203        Phosphoserine. 
MOD_RES   209   209        Phosphoserine. 
MOD_RES   211   211        Phosphothreonine. 
MOD_RES   237   237        Phosphothreonine. 
MOD_RES   241   241        Phosphoserine. 
Sequence information
Length: 335 AA [This is the length of the unprocessed precursor] Molecular weight: 35675 Da [This is the MW of the unprocessed precursor] CRC64: F0A0FB6AED5EB625 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAIPKVGING FGRIGRIVLR NAILTGKIQV VAVNDPFIDL DYMAYMFKYD STHGRFEGSV 

        70         80         90        100        110        120 
ETKGGKLVID GHSIDVHNER DPANIKWSAS GAEYVIESTG VFTTKETASA HLKGGAKRVI 

       130        140        150        160        170        180 
ISAPSKDAPM FVVGVNLEKF 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 KGVLGYTEDS VVSTDFCGDN HSSIFDASAG 

       310        320        330 
IQLSPQFVKL VSWYDNEWGY SHRVVDLVAY TASKD 

O43026 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!