Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q04409 (EMI2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative glucokinase-2

EC=2.7.1.2
Alternative name(s):
Early meiotic induction protein 2
Glucose kinase 2
Short name=GLK-2
Gene names
Name:EMI2
Ordered Locus Names:YDR516C
ORF Names:D9719.21
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Putative glucokinase involved in phosphorylation of aldohexoses and glucose uptake By similarity. Involved in sporulation. Required for the full activation of the early meiotic inducer IME1. Ref.4

Catalytic activity

ATP + D-glucose = ADP + D-glucose 6-phosphate.

Subcellular location

Cytoplasm Ref.5.

Induction

Repressed by glucose through the MIG1 and MIG2 repressors. Ref.3

Miscellaneous

Present with 10600 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the hexokinase family.

Contains 1 hexokinase type-1 domain.

Contains 1 hexokinase type-2 domain.

Ontologies

Keywords
   Biological processGlycolysis
Sporulation
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

sporulation resulting in formation of a cellular spore

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glucokinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Putative glucokinase-2
PRO_0000197604

Regions

Domain14 – 231218Hexokinase type-1
Domain244 – 500257Hexokinase type-2
Nucleotide binding487 – 4926ATP By similarity
Region159 – 18527Glucose-binding By similarity

Sites

Binding site1101ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04409 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7C624ECAB4C57883

FASTA50055,921
        10         20         30         40         50         60 
MSFENLHKVN AEALEDAVVE ICSSLQVDAA KLDELTAYFI ECMEKGLNNT SVGEEKTVDK 

        70         80         90        100        110        120 
GLPMIPTYVT SLPNGTERGV LLAADLGGTH FRVCSVTLNG DGTFDMQQLK SKIPEEYLND 

       130        140        150        160        170        180 
KDVTSEELFS YLGRRTRAFV RKHHPELLKS TGENIKPLKM GFTFSYPVDQ TSLSSGTLIR 

       190        200        210        220        230        240 
WTKSFKIEDT VGKDVVRLYQ EQLDIQGLSM INVVALTNDT VGTFLSHCYT SGSRPSSAGE 

       250        260        270        280        290        300 
ISEPVIGCIF GTGTNGCYME DIENIKKLPD ELRTRLLHEG KTQMCINIEW GSFDNELKHL 

       310        320        330        340        350        360 
SATKYDIDID QKFSPNPGYH LFEKRISGMY LGELLRNILV DLHARGLILG QYRNYDQLPH 

       370        380        390        400        410        420 
RLKTPFQLCS EVLSRIEIDD STNLRETELS FLQSLRLPTT FEERKAIQNL VRSITRRSAY 

       430        440        450        460        470        480 
LAAVPIAAIL IKTNALNKRY HGEVEIGFDG YVIEYYPGFR SMLRHALALS PIGTEGERKI 

       490        500 
HLRLAKDGSG VGAALCALVA 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Characterization of three related glucose repressors and genes they regulate in Saccharomyces cerevisiae."
Lutfiyya L.L., Iyer V.R., DeRisi J., DeVit M.J., Brown P.O., Johnston M.
Genetics 150:1377-1391(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[4]"Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae."
Enyenihi A.H., Saunders W.S.
Genetics 163:47-54(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33057 Genomic DNA. Translation: AAB64957.1.
BK006938 Genomic DNA. Translation: DAA12347.1.
PIRS69573.
RefSeqNP_010804.3. NM_001180824.3.

3D structure databases

ProteinModelPortalQ04409.
SMRQ04409. Positions 27-497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32567. 75 interactions.
DIPDIP-4977N.
IntActQ04409. 7 interactions.
MINTMINT-544411.
STRING4932.YDR516C.

Proteomic databases

PaxDbQ04409.
PeptideAtlasQ04409.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR516C; YDR516C; YDR516C.
GeneID852128.
KEGGsce:YDR516C.

Organism-specific databases

CYGDYDR516c.
SGDS000002924. EMI2.

Phylogenomic databases

eggNOGCOG5026.
GeneTreeENSGT00390000017159.
HOGENOMHOG000162670.
OMACINIEWG.
OrthoDBEOG79SF68.

Enzyme and pathway databases

BioCycYEAST:G3O-30035-MONOMER.

Gene expression databases

GenevestigatorQ04409.

Family and domain databases

InterProIPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERPTHR19443. PTHR19443. 1 hit.
PfamPF00349. Hexokinase_1. 1 hit.
PF03727. Hexokinase_2. 1 hit.
[Graphical view]
PRINTSPR00475. HEXOKINASE.
PROSITEPS00378. HEXOKINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio970522.

Entry information

Entry nameEMI2_YEAST
AccessionPrimary (citable) accession number: Q04409
Secondary accession number(s): D6VTD7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families