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Q14410 (GLPK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Glycerol kinase 2

Short name=GK 2
Short name=Glycerokinase 2
EC=2.7.1.30
Alternative name(s):
ATP:glycerol 3-phosphotransferase 2
Glycerol kinase, testis specific 2
Gene names
Name:GK2
Synonyms:GKP2, GKTA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length553 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: In sperm the majority of the enzyme is bound to mitochondria By similarity.

Sequence similarities

Belongs to the FGGY kinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 553553Glycerol kinase 2
PRO_0000059536

Regions

Nucleotide binding427 – 4315ATP By similarity

Sites

Binding site201Substrate By similarity
Binding site241ATP By similarity
Binding site941Substrate By similarity
Binding site1481Substrate By similarity
Binding site2591Substrate By similarity
Binding site2811ATP By similarity
Binding site3261ATP; via carbonyl oxygen By similarity

Experimental info

Sequence conflict2381E → G in BAF84930. Ref.2
Sequence conflict3691A → T in BAF84930. Ref.2
Sequence conflict4991R → C in BAF84930. Ref.2
Sequence conflict5281S → C in CAA55365. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q14410 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 8CE43A0686BC4AD6

FASTA55360,594
        10         20         30         40         50         60 
MAAPKTAAVG PLVGAVVQGT NSTRFLVFNS KTAELLSHHK VELTQEFPKE GWVEQDPKEI 

        70         80         90        100        110        120 
LQSVYECIAR TCEKLDELNI DISNIKAVGV SNQRETTVIW DKLTGEPLYN AVVWLDLRTQ 

       130        140        150        160        170        180 
TTVEDLSKKI PGNSNFVKSK TGLPLSTYFS AVKLRWMLDN VRNVQKAVEE GRALFGTIDS 

       190        200        210        220        230        240 
WLIWSLTGGV NGGVHCTDVT NASRTMLFNI HSLEWDKELC DFFEIPMDLL PNVFSSSEIY 

       250        260        270        280        290        300 
GLIKTGALEG VPISGCLGDQ CAALVGQMCF QEGQAKNTYG TGCFLLCNTG RKCVFSEHGL 

       310        320        330        340        350        360 
LTTVAYKLGR EKPAYYALEG SVAIAGAVIR WLRDNLGIIE TSGDIERLAK EVGTSYGCYF 

       370        380        390        400        410        420 
VPAFSGLYAP YWEPSARGIL CGLTQFTNKC HIAFAALEAV CFQTREILEA MNRDCGIPLR 

       430        440        450        460        470        480 
HLQVDGGMTN NKVLMQLQAD ILHIPVIKPF MPETTALGAA MAAGAAEGVS VWSLEPQALS 

       490        500        510        520        530        540 
VLRMERFEPQ IQATESEIRY ATWKKAVMKS MGWVTSQSPE GGDPSIFSSL PLGFFIVSSM 

       550 
VMLIGARYIS GVP 

« Hide

References

« Hide 'large scale' references
[1]"The glycerol kinase gene family: structure of the Xp gene, and related intronless retroposons."
Sargent C.A., Young C., Marsh S., Ferguson-Smith M.A., Affara N.A.
Hum. Mol. Genet. 3:1317-1324(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78712 mRNA. Translation: CAA55365.1.
AK292241 mRNA. Translation: BAF84930.1.
CH471057 Genomic DNA. Translation: EAX05842.1.
BC029820 mRNA. Translation: AAH29820.1.
BC048274 mRNA. Translation: AAH48274.2.
BC058888 mRNA. Translation: AAH58888.1.
PIRI37417.
RefSeqNP_149991.2. NM_033214.2.
UniGeneHs.98008.

3D structure databases

ProteinModelPortalQ14410.
SMRQ14410. Positions 13-514.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000351706.

PTM databases

PhosphoSiteQ14410.

Polymorphism databases

DMDM212286188.

Proteomic databases

PaxDbQ14410.
PRIDEQ14410.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358842; ENSP00000351706; ENSG00000196475.
GeneID2712.
KEGGhsa:2712.
UCSCuc003hlu.3. human.

Organism-specific databases

CTD2712.
GeneCardsGC04M080255.
H-InvDBHIX0004328.
HGNCHGNC:4291. GK2.
MIM600148. gene.
neXtProtNX_Q14410.
PharmGKBPA28702.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0554.
HOGENOMHOG000222134.
HOVERGENHBG002451.
InParanoidQ14410.
KOK00864.
OMARMERFEP.
OrthoDBEOG7VTDMZ.
PhylomeDBQ14410.
TreeFamTF321504.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00618; UER00672.

Gene expression databases

BgeeQ14410.
GenevestigatorQ14410.

Family and domain databases

InterProIPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
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

GenomeRNAi2712.
NextBio10720.
PROQ14410.
SOURCESearch...

Entry information

Entry nameGLPK2_HUMAN
AccessionPrimary (citable) accession number: Q14410
Secondary accession number(s): A8K876, Q6PD73, Q86XV8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 22, 2008
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM