Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q64516 (GLPK_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 89. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol kinase
Short name=GK
Short name=Glycerokinase
EC=2.7.1.30
Alternative name(s):
ATP:glycerol 3-phosphotransferase
Gene names
Name:Gk
Synonyms:Gyk
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Key enzyme in the regulation of glycerol uptake and metabolism By similarity.

Catalytic activity

ATP + glycerol = ADP + sn-glycerol 3-phosphate.

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.

Subcellular location

Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm By similarity. Note: Bound to the mitochondrial surface or cytoplasmic By similarity.

Sequence similarities

Belongs to the FGGY kinase family.

Ontologies

Keywords
   Biological processGlycerol metabolism
   Cellular componentCytoplasm
Membrane
Mitochondrion
Mitochondrion outer membrane
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycerol-3-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glycerol kinase activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q64516-3)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q64516-2)

The sequence of this isoform differs from the canonical sequence as follows:
     245-250: Missing.
Isoform 1 (identifier: Q64516-1)

The sequence of this isoform differs from the canonical sequence as follows:
     245-250: Missing.
     528-556: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559Glycerol kinase
PRO_0000059538

Regions

Nucleotide binding433 – 4375ATP By similarity

Sites

Binding site201Substrate By similarity
Binding site241ATP By similarity
Binding site941Substrate By similarity
Binding site1481Substrate By similarity
Binding site2651Substrate By similarity
Binding site2871ATP By similarity
Binding site3321ATP; via carbonyl oxygen By similarity

Natural variations

Alternative sequence245 – 2506Missing in isoform 1 and isoform 2.
VSP_034650
Alternative sequence528 – 55629Missing in isoform 1.
VSP_034651

Experimental info

Sequence conflict551Q → R in BAC31861. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 09A58CB47AB5CD41

FASTA55961,227
        10         20         30         40         50         60 
MAAAKKAVLG PLVGAVDQGT SSTRFLVFNS KTAELLSHHQ VEIKQEFPRE GWVEQDPKEI 

        70         80         90        100        110        120 
LQSVYECIEK TCEKLGQLNI DISNIKAIGV SNQRETTVVW DKVTGEPLYN AVVWLDLRTQ 

       130        140        150        160        170        180 
STVENLSKRI PGNNNFVKSK TGLPLSTYFS AVKLRWLLDN VKKVQEAVEE NRALFGTIDS 

       190        200        210        220        230        240 
WLIWSLTGGI HGGVHCTDVT NASRTMLFNI HSLEWDKELC EFFGIPMEIL PNVRSSSEIY 

       250        260        270        280        290        300 
GLMKISHSLK AGALEGVPIS GCLGDQSAAL VGQMCFQDGQ AKNTYGTGCF LLCNTGHKCV 

       310        320        330        340        350        360 
FSEHGLLTTV AYKLGRDKPV YYALEGSVAI AGAVIRWLRD NLGIIKSSEE IEKLAKEVGT 

       370        380        390        400        410        420 
SYGCYFVPAF SGLYAPYWEP SARGIICGLT QFTNKCHIAF AALEAVCFQT REILDAMNRD 

       430        440        450        460        470        480 
CGIPLSHLQV DGGMTSNKIL MQLQADILYI PVVKPSMPET TALGAAMAAG AAEGVGVWSL 

       490        500        510        520        530        540 
EPEDLSAVTM ERFEPQINAE ESEIRYSTWK KAVMKSIGWV TTQSPESGDP SIFCSLPLGF 

       550 
FIVSSMVMLI GARYISGIP

« Hide

Isoform 2 [UniParc].

Checksum: 386A4ED070B2A9CC
Show »

FASTA55360,562
Isoform 1 [UniParc].

Checksum: C3E1C56887683B55
Show »

FASTA52457,458

References

« Hide 'large scale' references
[1]"Isolation, mapping, and functional expression of the mouse X chromosome glycerol kinase gene."
Huq A.H., Lovell R.S., Sampson M.J., Decker W.K., Dinulos M.B., Disteche C.M., Craigen W.J.
Genomics 36:530-534(1996) [PubMed: 8884278] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: BALB/c.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Strain: C57BL/6J and NOD.
Tissue: Retina and Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U48403 mRNA. Translation: AAC52824.1.
AK044308 mRNA. Translation: BAC31861.1.
AK088373 mRNA. Translation: BAC40312.1.
AL645567, AL672056 Genomic DNA. Translation: CAM16667.1.
AL645567, AL672056 Genomic DNA. Translation: CAM16668.1.
AL672056, AL645567 Genomic DNA. Translation: CAM25261.1.
AL672056, AL645567 Genomic DNA. Translation: CAM25262.1.
BC003767 mRNA. Translation: AAH03767.1.
IPIIPI00135446.
IPI00224993.
IPI00404687.
RefSeqNP_032220.1. NM_008194.3.
NP_997609.1. NM_212444.2.
UniGeneMm.246682.

3D structure databases

ProteinModelPortalQ64516.
SMRQ64516. Positions 10-523.
ModBaseSearch...

Protein-protein interaction databases

IntActQ64516. 1 interaction.
STRINGQ64516.

Proteomic databases

PRIDEQ64516.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026039; ENSMUSP00000026039; ENSMUSG00000025059.
ENSMUST00000113978; ENSMUSP00000109611; ENSMUSG00000025059.
ENSMUST00000156390; ENSMUSP00000119564; ENSMUSG00000025059.
GeneID14933.
KEGGmmu:14933.
NMPDRfig|10090.3.peg.21824.
UCSCuc009trv.1. mouse.
uc009trx.1. mouse.

Organism-specific databases

CTD14933.
MGIMGI:106594. Gyk.

Phylogenomic databases

eggNOGroNOG10665.
HOGENOMHBG511469.
HOVERGENHBG002451.
InParanoidQ64516.
OMAFEPQINP.
OrthoDBEOG41G33T.

Gene expression databases

ArrayExpressQ64516.
BgeeQ64516.
CleanExMM_GYK.
GenevestigatorQ64516.

Family and domain databases

InterProIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
KOK00864.
PANTHERPTHR10196. FGGY_kin. 1 hit.
PTHR10196:SF9. Glycerol_kin. 1 hit.
PfamPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01311. Glycerol_kin. 1 hit.
PROSITEPS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameGLPK_MOUSE
AccessionPrimary (citable) accession number: Q64516
Secondary accession number(s): B1ASZ1, Q8C2M1, Q8C8X0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 22, 2008
Last modified: November 16, 2011
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents