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UniProtKB/Swiss-Prot entry P07487


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

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Entry information
Entry name G3P2_DROME
Primary accession number P07487
Secondary accession numbers A5XCW0 Q541C2 Q9VXM7
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on June 1, 2001 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 85)
Name and origin of the protein
Protein name Glyceraldehyde-3-phosphate dehydrogenase 2
Synonyms EC 1.2.1.12
Glyceraldehyde-3-phosphate dehydrogenase II
GAPDH II
Gene name
Name: Gapdh2
ORFNames: CG8893
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2989282 [NCBI, ExPASy, EBI, Israel, Japan]
Tso J.Y., Sun X.-H., Wu R.;
"Structure of two unlinked Drosophila melanogaster glyceraldehyde-3-phosphate dehydrogenase genes.";
J. Biol. Chem. 260:8220-8228(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-80.
STRAIN=AF8, AF9, HFL1, HFL2, HFL3, HFL4, MA2, MA7, SC1, SC2, VT1, VT2, VT3, VT4, Zh23, and Zh33;
DOI=10.1093/molbev/msm057; PubMed=17379620 [NCBI, ExPASy, EBI, Israel, Japan]
Flowers J., Sezgin E., Kumagai S., Duvernell D., Matzkin L., Schmidt P., Eanes W.;
"Adaptive evolution of metabolic pathways in Drosophila.";
Mol. Biol. Evol. 24:1347-1354(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Head;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273 AND THR-274, AND MASS SPECTROMETRY.
DOI=10.1039/b617545g; PubMed=17372656 [NCBI, ExPASy, EBI, Israel, Japan]
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells.";
Mol. Biosyst. 3:275-286(2007).
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
M11255; AAA28561.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864106; ABH06741.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864107; ABH06742.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864108; ABH06743.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864109; ABH06744.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864110; ABH06745.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864111; ABH06746.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864112; ABH06747.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864113; ABH06748.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864114; ABH06749.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864115; ABH06750.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864116; ABH06751.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864117; ABH06752.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864118; ABH06753.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864119; ABH06754.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864120; ABH06755.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ864121; ABH06756.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014298; AAF48531.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014298; AAN09371.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY094940; AAM11293.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B22366; B22366.
RefSeq NP_525091.1; -.
NP_542445.1; -.
UniGene Dm.6789
3D structure databases
HSSP P56649; 1CRW. [HSSP ENTRY / PDB]
SMR P07487; 2-332.
ModBase P07487.
Protein-protein interaction databases
DIP DIP:17969N; -.
IntAct P07487; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-002069-MON; -.
DMEL-XXX-02:DMEL-XXX-02-002070-MON; -.
Organism-specific databases
FlyBase FBgn0001092; Gapdh2.
Gene expression databases
ArrayExpress P07487; -.
GermOnline CG8893; Drosophila melanogaster.
Ontologies
GO
GO:0005811; Cellular component: lipid particle (inferred from direct assay from FlyBase).
GO:0004365; Molecular function: glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity (inferred from direct assay from FlyBase).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006096; Biological process: glycolysis (inferred from expression pattern from FlyBase).
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 P07487.
ProtoNet P07487.
Genome annotation databases
Ensembl CG8893; Drosophila melanogaster. [Contig view]
GeneID 32545; -.
KEGG dme:Dmel_CG8893; -.
Phylogenomic databases
HOGENOM P07487; -.
Other
NextBio 779058; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   332  332     Glyceraldehyde-3-phosphate dehydrogenase 2. PRO_0000145522
NP_BIND   11    12  2     NAD (By similarity). 
REGION   148   150  3     Glyceraldehyde 3-phosphate binding (By similarity). 
REGION   208   209  2     Glyceraldehyde 3-phosphate binding (By similarity). 
ACT_SITE   149   149        Nucleophile (By similarity). 
BINDING   32    32        NAD (By similarity). 
BINDING   77    77        NAD; via carbonyl oxygen (By similarity). 
BINDING   179   179        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   231   231        Glyceraldehyde 3-phosphate (By similarity). 
BINDING   313   313        NAD (By similarity). 
SITE   176   176  1     Activates thiol group during catalysis (By similarity). 
MOD_RES   273   273        Phosphotyrosine. 
MOD_RES   274   274        Phosphothreonine. 
VARIANT   80    80  1     A -> V (in strain: MA2). 
CONFLICT   38    38        N -> K (in Ref. 1; AAA28561). 
Sequence information
Length: 332 AA [This is the length of the unprocessed precursor] Molecular weight: 35369 Da [This is the MW of the unprocessed precursor] CRC64: 5D5D274B8D3B4839 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKIGINGFG RIGRLVLRAA IDKGANVVAV NDPFIDVNYM VYLFKFDSTH GRFKGTVAAE 

        70         80         90        100        110        120 
GGFLVVNGQK ITVFSERDPA NINWASAGAE YIVESTGVFT TIDKASTHLK GGAKKVIISA 

       130        140        150        160        170        180 
PSADAPMFVC GVNLDAYKPD MKVVSNASCT TNCLAPLAKV INDNFEIVEG LMTTVHATTA 

       190        200        210        220        230        240 
TQKTVDGPSG KLWRDGRGAA QNIIPASTGA AKAVGKVIPA LNGKLTGMAF RVPTPNVSVV 

       250        260        270        280        290        300 
DLTVRLGKGA SYDEIKAKVQ EAANGPLKGI LGYTDEEVVS TDFLSDTHSS VFDAKAGISL 

       310        320        330 
NDKFVKLISW YDNEFGYSNR VIDLIKYMQS KD 

P07487 in FASTA format

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