Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q00055

- GPD1_YEAST

UniProt

Q00055 - GPD1_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glycerol-3-phosphate dehydrogenase [NAD(+)] 1

Gene

GPD1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

Catalyzes the production and accumulation of glycerol during hyperosmotic stress conditions. Glycerol acts as a osmoregulator that prevents loss of water and turgor of the cells.1 Publication

Catalytic activityi

sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei129 – 1291NADBy similarity
Binding sitei152 – 1521NAD; via amide nitrogenBy similarity
Binding sitei152 – 1521SubstrateBy similarity
Binding sitei185 – 1851NAD; via amide nitrogenBy similarity
Active sitei245 – 2451Proton acceptorBy similarity
Binding sitei310 – 3101NADBy similarity
Binding sitei339 – 3391NADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 466NADBy similarity

GO - Molecular functioni

  1. glycerol-3-phosphate dehydrogenase [NAD+] activity Source: SGD
  2. NAD binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. glycerol-3-phosphate catabolic process Source: InterPro
  3. intracellular accumulation of glycerol Source: SGD
  4. NADH oxidation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:YDL022W-MONOMER.
YEAST:YDL022W-MONOMER.
BRENDAi1.1.1.8. 984.
ReactomeiREACT_191569. Synthesis of PA.
REACT_234352. Triglyceride Biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate dehydrogenase [NAD(+)] 1 (EC:1.1.1.8)
Gene namesi
Name:GPD1
Synonyms:DAR1, HOR1, OSG1
Ordered Locus Names:YDL022W
ORF Names:D2830
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

SGDiS000002180. GPD1.

Subcellular locationi

Cytoplasm. Peroxisome

GO - Cellular componenti

  1. cytosol Source: SGD
  2. glycerol-3-phosphate dehydrogenase complex Source: InterPro
  3. nucleus Source: SGD
  4. peroxisome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 391390Glycerol-3-phosphate dehydrogenase [NAD(+)] 1PRO_0000138100Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei24 – 241Phosphoserine1 Publication
Modified residuei27 – 271Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ00055.
PaxDbiQ00055.
PeptideAtlasiQ00055.

Expressioni

Inductioni

By osmotic stress and by methylglyoxal in a HOG pathway-dependent manner.2 Publications

Gene expression databases

ExpressionAtlasiQ00055. differential.
GenevestigatoriQ00055.

Interactioni

Protein-protein interaction databases

BioGridi32033. 57 interactions.
DIPiDIP-6393N.
IntActiQ00055. 3 interactions.
MINTiMINT-2788005.
STRINGi4932.YDL022W.

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 406Combined sources
Helixi44 – 5916Combined sources
Turni61 – 633Combined sources
Beta strandi64 – 718Combined sources
Beta strandi76 – 794Combined sources
Helixi82 – 865Combined sources
Turni87 – 893Combined sources
Turni93 – 953Combined sources
Beta strandi103 – 1097Combined sources
Helixi111 – 1155Combined sources
Beta strandi119 – 1235Combined sources
Helixi127 – 1293Combined sources
Helixi130 – 1378Combined sources
Turni138 – 1403Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi160 – 1623Combined sources
Helixi164 – 1729Combined sources
Beta strandi175 – 1806Combined sources
Helixi185 – 1895Combined sources
Beta strandi194 – 1996Combined sources
Beta strandi209 – 2124Combined sources
Helixi215 – 2228Combined sources
Beta strandi227 – 2337Combined sources
Helixi235 – 25723Combined sources
Helixi261 – 28323Combined sources
Helixi289 – 2946Combined sources
Turni296 – 2983Combined sources
Helixi299 – 3079Combined sources
Helixi310 – 32011Combined sources
Helixi325 – 3339Combined sources
Helixi340 – 35415Combined sources
Helixi361 – 37111Combined sources
Helixi379 – 3835Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FGWX-ray2.45A/B1-391[»]
ProteinModelPortaliQ00055.
SMRiQ00055. Positions 33-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni310 – 3112Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG0240.
GeneTreeiENSGT00390000003114.
HOGENOMiHOG000246855.
InParanoidiQ00055.
KOiK00006.
OMAiHEWLETC.
OrthoDBiEOG7V76H7.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR017751. G3P_DH_NAD-dep_euk.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11728. PTHR11728. 1 hit.
PfamiPF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSiPR00077. GPDHDRGNASE.
SUPFAMiSSF48179. SSF48179. 1 hit.
TIGRFAMsiTIGR03376. glycerol3P_DH. 1 hit.
PROSITEiPS00957. NAD_G3PDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00055-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAAADRLNL TSGHLNAGRK RSSSSVSLKA AEKPFKVTVI GSGNWGTTIA 
        60         70         80         90        100
KVVAENCKGY PEVFAPIVQM WVFEEEINGE KLTEIINTRH QNVKYLPGIT 
       110        120        130        140        150
LPDNLVANPD LIDSVKDVDI IVFNIPHQFL PRICSQLKGH VDSHVRAISC 
       160        170        180        190        200
LKGFEVGAKG VQLLSSYITE ELGIQCGALS GANIATEVAQ EHWSETTVAY 
       210        220        230        240        250
HIPKDFRGEG KDVDHKVLKA LFHRPYFHVS VIEDVAGISI CGALKNVVAL 
       260        270        280        290        300
GCGFVEGLGW GNNASAAIQR VGLGEIIRFG QMFFPESREE TYYQESAGVA 
       310        320        330        340        350
DLITTCAGGR NVKVARLMAT SGKDAWECEK ELLNGQSAQG LITCKEVHEW 
       360        370        380        390 
LETCGSVEDF PLFEAVYQIV YNNYPMKNLP DMIEELDLHE D
Length:391
Mass (Da):42,869
Last modified:January 23, 2007 - v4
Checksum:iF5F1F7F111F707D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1075DNLVA → TIWLL in AAA18631. (PubMed:1676389)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti16 – 161N → D in strain: WFB. 1 Publication
Natural varianti143 – 1431S → A in strain: WFB. 1 Publication
Natural varianti164 – 1641L → P in strain: WFB. 1 Publication
Natural varianti183 – 1831N → S in strain: WFB. 1 Publication
Natural varianti225 – 2251P → S in strain: WFB. 1 Publication
Natural varianti256 – 2561E → V in strain: WFB. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z24454 Genomic DNA. Translation: CAA80827.1.
X76859 Genomic DNA. Translation: CAA54189.1.
U04621 Genomic DNA. Translation: AAA64936.1.
AY598965 Genomic DNA. Translation: AAT27375.1.
AY598968 Genomic DNA. Translation: AAT27378.1.
Z48432 Genomic DNA. Translation: CAA88337.1.
Z74071 Genomic DNA. Translation: CAA98582.1.
EF596737 Genomic DNA. Translation: ABQ58864.1.
M38740 Genomic DNA. Translation: AAA18631.1.
BK006938 Genomic DNA. Translation: DAA11828.1.
PIRiS40059.
RefSeqiNP_010262.1. NM_001180081.1.

Genome annotation databases

EnsemblFungiiYDL022W; YDL022W; YDL022W.
GeneIDi851539.
KEGGisce:YDL022W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 Z24454 Genomic DNA. Translation: CAA80827.1 .
X76859 Genomic DNA. Translation: CAA54189.1 .
U04621 Genomic DNA. Translation: AAA64936.1 .
AY598965 Genomic DNA. Translation: AAT27375.1 .
AY598968 Genomic DNA. Translation: AAT27378.1 .
Z48432 Genomic DNA. Translation: CAA88337.1 .
Z74071 Genomic DNA. Translation: CAA98582.1 .
EF596737 Genomic DNA. Translation: ABQ58864.1 .
M38740 Genomic DNA. Translation: AAA18631.1 .
BK006938 Genomic DNA. Translation: DAA11828.1 .
PIRi S40059.
RefSeqi NP_010262.1. NM_001180081.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4FGW X-ray 2.45 A/B 1-391 [» ]
ProteinModelPortali Q00055.
SMRi Q00055. Positions 33-385.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32033. 57 interactions.
DIPi DIP-6393N.
IntActi Q00055. 3 interactions.
MINTi MINT-2788005.
STRINGi 4932.YDL022W.

Proteomic databases

MaxQBi Q00055.
PaxDbi Q00055.
PeptideAtlasi Q00055.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL022W ; YDL022W ; YDL022W .
GeneIDi 851539.
KEGGi sce:YDL022W.

Organism-specific databases

SGDi S000002180. GPD1.

Phylogenomic databases

eggNOGi COG0240.
GeneTreei ENSGT00390000003114.
HOGENOMi HOG000246855.
InParanoidi Q00055.
KOi K00006.
OMAi HEWLETC.
OrthoDBi EOG7V76H7.

Enzyme and pathway databases

BioCyci MetaCyc:YDL022W-MONOMER.
YEAST:YDL022W-MONOMER.
BRENDAi 1.1.1.8. 984.
Reactomei REACT_191569. Synthesis of PA.
REACT_234352. Triglyceride Biosynthesis.

Miscellaneous databases

NextBioi 968943.

Gene expression databases

ExpressionAtlasi Q00055. differential.
Genevestigatori Q00055.

Family and domain databases

Gene3Di 1.10.1040.10. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR008927. 6-PGluconate_DH_C-like.
IPR013328. DH_multihelical.
IPR006168. G3P_DH_NAD-dep.
IPR006109. G3P_DH_NAD-dep_C.
IPR017751. G3P_DH_NAD-dep_euk.
IPR011128. G3P_DH_NAD-dep_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PANTHERi PTHR11728. PTHR11728. 1 hit.
Pfami PF07479. NAD_Gly3P_dh_C. 1 hit.
PF01210. NAD_Gly3P_dh_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000114. Glycerol-3-P_dh. 1 hit.
PRINTSi PR00077. GPDHDRGNASE.
SUPFAMi SSF48179. SSF48179. 1 hit.
TIGRFAMsi TIGR03376. glycerol3P_DH. 1 hit.
PROSITEi PS00957. NAD_G3PDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A gene encoding sn-glycerol 3-phosphate dehydrogenase (NAD+) complements an osmosensitive mutant of Saccharomyces cerevisiae."
    Larsson K., Ansell R., Eriksson P., Adler L.
    Mol. Microbiol. 10:1101-1111(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-49.
  2. "GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway."
    Albertyn J., Hohmann S., Thevelein J.M., Prior B.A.
    Mol. Cell. Biol. 14:4135-4144(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
  3. "Cloning, sequence, and disruption of the Saccharomyces diastaticus DAR1 gene encoding a glycerol-3-phosphate dehydrogenase."
    Wang H.T., Rahaim P., Robbins P., Yocum R.R.
    J. Bacteriol. 176:7091-7095(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Diastaticus / ATCC 62933 / NRC 5704 / J132b.
  4. "Research on the mechanism of osmotolerance and thermotolerance of yeast."
    Ma X., Guo Y., Zhang F., Yu H., Kuang J., Yao J., Li Z., He G.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-16; ALA-143; PRO-164; SER-183; SER-225 AND VAL-256.
    Strain: FHS and WFB.
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "The effects of co-expression of ScGPD1 and AtNHX1 on the salt tolerance of yeast."
    Fu C., Zheng D.
    Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "Cloning and characterisation of the Saccharomyces cerevisiae glycerol-3-phosphate dehydrogenase (GUT2) promoter."
    Sleep D., Ogden J.E., Roberts N.A., Goodey A.R.
    Gene 101:89-96(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
  9. Bienvenut W.V., Peters C.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-19 AND 271-278, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
    Norbeck J., Blomberg A.
    FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 8-16; 95-108 AND 160-173.
    Strain: ATCC 38531 / Y41.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Distinct intracellular localization of Gpd1p and Gpd2p, the two yeast isoforms of NAD+-dependent glycerol-3-phosphate dehydrogenase, explains their different contributions to redox-driven glycerol production."
    Valadi A., Granath K., Gustafsson L., Adler L.
    J. Biol. Chem. 279:39677-39685(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  15. "The HOG MAP kinase pathway is required for the induction of methylglyoxal-responsive genes and determines methylglyoxal resistance in Saccharomyces cerevisiae."
    Aguilera J., Rodriguez-Vargas S., Prieto J.A.
    Mol. Microbiol. 56:228-239(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  16. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  17. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Entry informationi

Entry nameiGPD1_YEAST
AccessioniPrimary (citable) accession number: Q00055
Secondary accession number(s): A5YWB0
, D6VRW8, Q6J5J2, Q6J5J5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 807 molecules/cell in log phase SD medium.1 Publication

Caution

Was originally thought to be GUT2, the FAD-dependent glycerol-3-phosphate dehydrogenase.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
© 2002– 2015 UniProt Consortium | License & Disclaimer