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Protein

Glycerol kinase

Gene

GK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Key enzyme in the regulation of glycerol uptake and metabolism.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201SubstrateBy similarity
Binding sitei24 – 241ATPBy similarity
Binding sitei94 – 941SubstrateBy similarity
Binding sitei148 – 1481SubstrateBy similarity
Binding sitei265 – 2651SubstrateBy similarity
Binding sitei287 – 2871ATPBy similarity
Binding sitei332 – 3321ATP; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi433 – 4375ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glycerol kinase activity Source: UniProtKB

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. glucose homeostasis Source: Ensembl
  3. glycerol-3-phosphate biosynthetic process Source: BHF-UCL
  4. glycerol catabolic process Source: UniProtKB-UniPathway
  5. glycerol metabolic process Source: BHF-UCL
  6. small molecule metabolic process Source: Reactome
  7. triglyceride biosynthetic process Source: Reactome
  8. triglyceride metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycerol metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.30. 2681.
ReactomeiREACT_1190. Triglyceride Biosynthesis.
UniPathwayiUPA00618; UER00672.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol kinase (EC:2.7.1.30)
Short name:
GK
Short name:
Glycerokinase
Alternative name(s):
ATP:glycerol 3-phosphotransferase
Gene namesi
Name:GK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:4289. GK.

Subcellular locationi

  1. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side
  2. Cytoplasm

  3. Note: In sperm and fetal tissues, the majority of the enzyme is bound to mitochondria, but in adult tissues, such as liver found in the cytoplasm.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. mitochondrial outer membrane Source: UniProtKB-SubCell
  4. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

Glycerol kinase deficiency (GKD)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA metabolic disorder manifesting as 3 clinically distinct forms: infantile, juvenile, and adult. The infantile form is the most severe and is associated with severe developmental delay and adrenal insufficiency. Patients with the adult form have no symptoms and are often detected fortuitously. GKD results in hyperglycerolemia, a condition characterized by the accumulation of glycerol in the blood and urine.

See also OMIM:307030
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti294 – 2941N → D in GKD. 1 Publication
VAR_015433
Natural varianti446 – 4461D → V in GKD. 1 Publication
VAR_001377
Natural varianti509 – 5091W → R in GKD. 1 Publication
VAR_010138

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi307030. phenotype.
Orphaneti284414. Glycerol kinase deficiency, adult form.
284408. Glycerol kinase deficiency, infantile form.
284411. Glycerol kinase deficiency, juvenile form.
PharmGKBiPA28700.

Polymorphism and mutation databases

BioMutaiGK.
DMDMi205830913.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Glycerol kinasePRO_0000059535Add
BLAST

Proteomic databases

MaxQBiP32189.
PaxDbiP32189.
PRIDEiP32189.

PTM databases

PhosphoSiteiP32189.

Expressioni

Tissue specificityi

Highly expressed in the liver, kidney and testis. Isoform 2 and isoform 3 are expressed specifically in testis and fetal liver, but not in the adult liver.

Gene expression databases

BgeeiP32189.
CleanExiHS_GK.
ExpressionAtlasiP32189. baseline and differential.
GenevestigatoriP32189.

Organism-specific databases

HPAiHPA060687.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NR4A1P227363EBI-3926629,EBI-721550

Protein-protein interaction databases

BioGridi108975. 22 interactions.
IntActiP32189. 11 interactions.
STRINGi9606.ENSP00000368226.

Structurei

3D structure databases

ProteinModelPortaliP32189.
SMRiP32189. Positions 13-520.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FGGY kinase family.Curated

Phylogenomic databases

eggNOGiCOG0554.
GeneTreeiENSGT00530000063143.
HOGENOMiHOG000222134.
HOVERGENiHBG002451.
InParanoidiP32189.
KOiK00864.
OMAiWWLTGGP.
OrthoDBiEOG7VTDMZ.
PhylomeDBiP32189.
TreeFamiTF321504.

Family and domain databases

InterProiIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
PfamiPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000538. GlpK. 1 hit.
TIGRFAMsiTIGR01311. glycerol_kin. 1 hit.
PROSITEiPS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: P32189-3) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAASKKAVLG PLVGAVDQGT SSTRFLVFNS KTAELLSHHQ VEIKQEFPRE
60 70 80 90 100
GWVEQDPKEI LHSVYECIEK TCEKLGQLNI DISNIKAIGV SNQRETTVVW
110 120 130 140 150
DKITGEPLYN AVVWLDLRTQ STVESLSKRI PGNNNFVKSK TGLPLSTYFS
160 170 180 190 200
AVKLRWLLDN VRKVQKAVEE KRALFGTIDS WLIWSLTGGV NGGVHCTDVT
210 220 230 240 250
NASRTMLFNI HSLEWDKQLC EFFGIPMEIL PNVRSSSEIY GLMKISHSVK
260 270 280 290 300
AGALEGVPIS GCLGDQSAAL VGQMCFQIGQ AKNTYGTGCF LLCNTGHKCV
310 320 330 340 350
FSDHGLLTTV AYKLGRDKPV YYALEGSVAI AGAVIRWLRD NLGIIKTSEE
360 370 380 390 400
IEKLAKEVGT SYGCYFVPAF SGLYAPYWEP SARGIICGLT QFTNKCHIAF
410 420 430 440 450
AALEAVCFQT REILDAMNRD CGIPLSHLQV DGGMTSNKIL MQLQADILYI
460 470 480 490 500
PVVKPSMPET TALGAAMAAG AAEGVGVWSL EPEDLSAVTM ERFEPQINAE
510 520 530 540 550
ESEIRYSTWK KAVMKSMGWV TTQSPESGDP SIFCSLPLGF FIVSSMVMLI

GARYISGIP
Length:559
Mass (Da):61,245
Last modified:July 22, 2008 - v3
Checksum:i18268B7A4C6A09F3
GO
Isoform 1 (identifier: P32189-1) [UniParc]FASTAAdd to basket

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

Show »
Length:524
Mass (Da):57,489
Checksum:i0FAA29ADC6054154
GO
Isoform 2 (identifier: P32189-2) [UniParc]FASTAAdd to basket

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

Show »
Length:553
Mass (Da):60,593
Checksum:i145FA42A6BEA104F
GO
Isoform 4 (identifier: P32189-4) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.

Show »
Length:530
Mass (Da):58,141
Checksum:iAC9EEBB80003DEE7
GO

Sequence cautioni

The sequence CAA48346.1 differs from that shown. Reason: Frameshift at positions 201, 210 and 459. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791N → K.1 Publication
Corresponds to variant rs17857267 [ dbSNP | Ensembl ].
VAR_068980
Natural varianti131 – 1311P → T.1 Publication
Corresponds to variant rs17854203 [ dbSNP | Ensembl ].
VAR_068981
Natural varianti185 – 1851S → N.
VAR_001374
Natural varianti232 – 2321N → H.
VAR_001375
Natural varianti294 – 2941N → D in GKD. 1 Publication
VAR_015433
Natural varianti382 – 3821A → T.
VAR_001376
Natural varianti446 – 4461D → V in GKD. 1 Publication
VAR_001377
Natural varianti509 – 5091W → R in GKD. 1 Publication
VAR_010138

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei245 – 2506Missing in isoform 1 and isoform 2. 5 PublicationsVSP_000770
Alternative sequencei528 – 55629Missing in isoform 1 and isoform 4. 4 PublicationsVSP_000771Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13943 mRNA. Translation: AAA52576.1.
X78211 Genomic DNA. No translation available.
AJ252550
, AJ252551, AJ252552, AJ252553, AJ252554, AJ252555, AJ252556, AJ252557, AJ252558, AJ252559, AJ252560, AJ252561, AJ252562, AJ252563, AJ252564, AJ252565, AJ252566, AJ252567, AJ252568, AJ252569, AJ252570 Genomic DNA. Translation: CAB54859.1.
AJ252550
, AJ252551, AJ252552, AJ252553, AJ252554, AJ252555, AJ252556, AJ252557, AJ252559, AJ252560, AJ252561, AJ252562, AJ252563, AJ252564, AJ252565, AJ252566, AJ252567, AJ252568, AJ252569, AJ252570 Genomic DNA. Translation: CAB54858.1.
AJ252550
, AJ252551, AJ252552, AJ252553, AJ252554, AJ252555, AJ252556, AJ252557, AJ252559, AJ252560, AJ252561, AJ252562, AJ252563, AJ252564, AJ252565, AJ252566, AJ252567, AJ252568, AJ252570 Genomic DNA. Translation: CAB54857.1.
AK313215 mRNA. Translation: BAG36030.1.
AC005913 Genomic DNA. No translation available.
AC112496 Genomic DNA. No translation available.
AC117404 Genomic DNA. No translation available.
BC037549 mRNA. Translation: AAH37549.1.
BC042421 mRNA. Translation: AAH42421.1.
BC071595 mRNA. Translation: AAH71595.1.
X68285 mRNA. Translation: CAA48346.1. Frameshift.
X69886 mRNA. Translation: CAA49512.1.
CCDSiCCDS14225.1. [P32189-4]
CCDS35224.1. [P32189-1]
CCDS48090.1. [P32189-2]
CCDS75963.1. [P32189-3]
PIRiI37427. S36175.
RefSeqiNP_000158.1. NM_000167.5. [P32189-1]
NP_001121599.1. NM_001128127.2. [P32189-2]
NP_001191948.1. NM_001205019.1. [P32189-3]
NP_976325.1. NM_203391.3. [P32189-4]
UniGeneiHs.1466.

Genome annotation databases

EnsembliENST00000378943; ENSP00000368226; ENSG00000198814. [P32189-2]
ENST00000378945; ENSP00000368228; ENSG00000198814. [P32189-1]
ENST00000378946; ENSP00000368229; ENSG00000198814. [P32189-4]
ENST00000427190; ENSP00000401720; ENSG00000198814. [P32189-3]
GeneIDi2710.
KEGGihsa:2710.
UCSCiuc004dci.4. human. [P32189-1]
uc010ngj.3. human. [P32189-2]
uc011mjz.2. human. [P32189-3]

Polymorphism and mutation databases

BioMutaiGK.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13943 mRNA. Translation: AAA52576.1.
X78211 Genomic DNA. No translation available.
AJ252550
, AJ252551, AJ252552, AJ252553, AJ252554, AJ252555, AJ252556, AJ252557, AJ252558, AJ252559, AJ252560, AJ252561, AJ252562, AJ252563, AJ252564, AJ252565, AJ252566, AJ252567, AJ252568, AJ252569, AJ252570 Genomic DNA. Translation: CAB54859.1.
AJ252550
, AJ252551, AJ252552, AJ252553, AJ252554, AJ252555, AJ252556, AJ252557, AJ252559, AJ252560, AJ252561, AJ252562, AJ252563, AJ252564, AJ252565, AJ252566, AJ252567, AJ252568, AJ252569, AJ252570 Genomic DNA. Translation: CAB54858.1.
AJ252550
, AJ252551, AJ252552, AJ252553, AJ252554, AJ252555, AJ252556, AJ252557, AJ252559, AJ252560, AJ252561, AJ252562, AJ252563, AJ252564, AJ252565, AJ252566, AJ252567, AJ252568, AJ252570 Genomic DNA. Translation: CAB54857.1.
AK313215 mRNA. Translation: BAG36030.1.
AC005913 Genomic DNA. No translation available.
AC112496 Genomic DNA. No translation available.
AC117404 Genomic DNA. No translation available.
BC037549 mRNA. Translation: AAH37549.1.
BC042421 mRNA. Translation: AAH42421.1.
BC071595 mRNA. Translation: AAH71595.1.
X68285 mRNA. Translation: CAA48346.1. Frameshift.
X69886 mRNA. Translation: CAA49512.1.
CCDSiCCDS14225.1. [P32189-4]
CCDS35224.1. [P32189-1]
CCDS48090.1. [P32189-2]
CCDS75963.1. [P32189-3]
PIRiI37427. S36175.
RefSeqiNP_000158.1. NM_000167.5. [P32189-1]
NP_001121599.1. NM_001128127.2. [P32189-2]
NP_001191948.1. NM_001205019.1. [P32189-3]
NP_976325.1. NM_203391.3. [P32189-4]
UniGeneiHs.1466.

3D structure databases

ProteinModelPortaliP32189.
SMRiP32189. Positions 13-520.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108975. 22 interactions.
IntActiP32189. 11 interactions.
STRINGi9606.ENSP00000368226.

Chemistry

BindingDBiP32189.
ChEMBLiCHEMBL2300.

PTM databases

PhosphoSiteiP32189.

Polymorphism and mutation databases

BioMutaiGK.
DMDMi205830913.

Proteomic databases

MaxQBiP32189.
PaxDbiP32189.
PRIDEiP32189.

Protocols and materials databases

DNASUi2710.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378943; ENSP00000368226; ENSG00000198814. [P32189-2]
ENST00000378945; ENSP00000368228; ENSG00000198814. [P32189-1]
ENST00000378946; ENSP00000368229; ENSG00000198814. [P32189-4]
ENST00000427190; ENSP00000401720; ENSG00000198814. [P32189-3]
GeneIDi2710.
KEGGihsa:2710.
UCSCiuc004dci.4. human. [P32189-1]
uc010ngj.3. human. [P32189-2]
uc011mjz.2. human. [P32189-3]

Organism-specific databases

CTDi2710.
GeneCardsiGC0XP030671.
HGNCiHGNC:4289. GK.
HPAiHPA060687.
MIMi300474. gene.
307030. phenotype.
neXtProtiNX_P32189.
Orphaneti284414. Glycerol kinase deficiency, adult form.
284408. Glycerol kinase deficiency, infantile form.
284411. Glycerol kinase deficiency, juvenile form.
PharmGKBiPA28700.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0554.
GeneTreeiENSGT00530000063143.
HOGENOMiHOG000222134.
HOVERGENiHBG002451.
InParanoidiP32189.
KOiK00864.
OMAiWWLTGGP.
OrthoDBiEOG7VTDMZ.
PhylomeDBiP32189.
TreeFamiTF321504.

Enzyme and pathway databases

UniPathwayiUPA00618; UER00672.
BRENDAi2.7.1.30. 2681.
ReactomeiREACT_1190. Triglyceride Biosynthesis.

Miscellaneous databases

ChiTaRSiGK. human.
GenomeRNAii2710.
NextBioi10712.
PROiP32189.
SOURCEiSearch...

Gene expression databases

BgeeiP32189.
CleanExiHS_GK.
ExpressionAtlasiP32189. baseline and differential.
GenevestigatoriP32189.

Family and domain databases

InterProiIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
PfamiPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000538. GlpK. 1 hit.
TIGRFAMsiTIGR01311. glycerol_kin. 1 hit.
PROSITEiPS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic scanning for expressed sequences in Xp21 identifies the glycerol kinase gene."
    Guo W., Worley K.C., Adams V., Mason J., Sylvester-Jackson D.E., Zhang Y.-H., Towbin J.A., Fogt D.D., Madu S., Wheeler D.A., McCabe E.R.B.
    Nat. Genet. 4:367-372(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "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 [GENOMIC DNA / MRNA] (ISOFORM 2).
    Tissue: Fetal brain.
  3. "Five cases of isolated glycerol kinase deficiency, including two families: failure to find genotype:phenotype correlation."
    Sargent C.A., Kidd A., Moore S., Dean J., Besley G.T.N., Affara N.A.
    J. Med. Genet. 37:434-441(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
  4. "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.
    , 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] (ISOFORM 1).
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1; 3 AND 4), VARIANTS LYS-79 AND THR-131.
    Tissue: Blood and Brain.
  7. "Cloning of the X-linked glycerol kinase deficiency gene and its identification by sequence comparison to the Bacillus subtilis homologue."
    Sargent C.A., Affara N.A., Bentley E., Pelmear A., Bailey D.M.D., Davey P., Dow D., Leversha M., Aplin H., Besley G.T.N., Ferguson-Smith M.A.
    Hum. Mol. Genet. 2:97-106(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 77-559 (ISOFORM 3).
    Tissue: Fetal brain.
  8. "Isolation of the human Xp21 glycerol kinase gene by positional cloning."
    Walker A.P., Muscatelli F., Monaco A.P.
    Hum. Mol. Genet. 2:107-114(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 130-559 (ISOFORM 1).
    Tissue: Fetal liver.
  9. "Mutations and phenotype in isolated glycerol kinase deficiency."
    Walker A.P., Muscatelli F., Stafford A.N., Chelly J., Dahl N., Blomquist H.K., Delanghe J., Willems P.J., Steinmann B., Monaco A.P.
    Am. J. Hum. Genet. 58:1205-1211(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GKD VAL-446.
  10. "Clinical heterogeneity and novel mutations in the glycerol kinase gene in three families with isolated glycerol kinase deficiency."
    Sjarif D.R., Sinke R.J., Duran M., Beemer F.A., Kleijer W.J., Ploos van Amstel J.K., Poll-The B.T.
    J. Med. Genet. 35:650-656(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GKD ARG-509.
  11. "Glycerol as a correlate of impaired glucose tolerance: dissection of a complex system by use of a simple genetic trait."
    Gaudet D., Arsenault S., Perusse L., Vohl M.C., St Pierre J., Bergeron J., Despres J.P., Dewar K., Daly M.J., Hudson T., Rioux J.D.
    Am. J. Hum. Genet. 66:1558-1568(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GKD ASP-294.

Entry informationi

Entry nameiGLPK_HUMAN
AccessioniPrimary (citable) accession number: P32189
Secondary accession number(s): A6NJP5
, B2R833, Q6IQ27, Q8IVR5, Q9UMP0, Q9UMP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: July 22, 2008
Last modified: April 29, 2015
This is version 158 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

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.