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P32189

- GLPK_HUMAN

UniProt

P32189 - GLPK_HUMAN

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Protein
Glycerol kinase
Gene
GK
Organism
Homo sapiens (Human)
Status
Reviewed - 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 – 201Substrate By similarity
Binding sitei24 – 241ATP By similarity
Binding sitei94 – 941Substrate By similarity
Binding sitei148 – 1481Substrate By similarity
Binding sitei265 – 2651Substrate By similarity
Binding sitei287 – 2871ATP By similarity
Binding sitei332 – 3321ATP; via carbonyl oxygen By similarity

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glycerol kinase activity Source: UniProtKB
  3. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. glycerol catabolic process Source: UniProtKB-UniPathway
  3. glycerol metabolic process Source: BHF-UCL
  4. glycerol-3-phosphate biosynthetic process Source: BHF-UCL
  5. small molecule metabolic process Source: Reactome
  6. triglyceride biosynthetic process Source: Reactome
  7. 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

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: Chromosome X

Organism-specific databases

HGNCiHGNC:4289. GK.

Subcellular locationi

Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm
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: UniProt
  3. mitochondrial outer membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Involvement in diseasei

Glycerol kinase deficiency (GKD) [MIM:307030]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Glycerol kinase
PRO_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

ArrayExpressiP32189.
BgeeiP32189.
CleanExiHS_GK.
GenevestigatoriP32189.

Organism-specific databases

HPAiHPA060687.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108975. 12 interactions.
IntActiP32189. 11 interactions.
STRINGi9606.ENSP00000368226.

Structurei

3D structure databases

ProteinModelPortaliP32189.
SMRiP32189. Positions 13-520.

Family & Domainsi

Sequence similaritiesi

Belongs to the FGGY kinase family.

Phylogenomic databases

eggNOGiCOG0554.
HOGENOMiHOG000222134.
HOVERGENiHBG002451.
InParanoidiP32189.
KOiK00864.
OMAiDNLGIAK.
OrthoDBiEOG7VTDMZ.
PhylomeDBiP32189.
TreeFamiTF321504.

Family and domain databases

InterProiIPR018485. 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]
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. Align

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

MAASKKAVLG PLVGAVDQGT SSTRFLVFNS KTAELLSHHQ VEIKQEFPRE    50
GWVEQDPKEI LHSVYECIEK TCEKLGQLNI DISNIKAIGV SNQRETTVVW 100
DKITGEPLYN AVVWLDLRTQ STVESLSKRI PGNNNFVKSK TGLPLSTYFS 150
AVKLRWLLDN VRKVQKAVEE KRALFGTIDS WLIWSLTGGV NGGVHCTDVT 200
NASRTMLFNI HSLEWDKQLC EFFGIPMEIL PNVRSSSEIY GLMKISHSVK 250
AGALEGVPIS GCLGDQSAAL VGQMCFQIGQ AKNTYGTGCF LLCNTGHKCV 300
FSDHGLLTTV AYKLGRDKPV YYALEGSVAI AGAVIRWLRD NLGIIKTSEE 350
IEKLAKEVGT SYGCYFVPAF SGLYAPYWEP SARGIICGLT QFTNKCHIAF 400
AALEAVCFQT REILDAMNRD CGIPLSHLQV DGGMTSNKIL MQLQADILYI 450
PVVKPSMPET TALGAAMAAG AAEGVGVWSL EPEDLSAVTM ERFEPQINAE 500
ESEIRYSTWK KAVMKSMGWV TTQSPESGDP SIFCSLPLGF FIVSSMVMLI 550
GARYISGIP 559
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.

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.
VSP_000770
Alternative sequencei528 – 55629Missing in isoform 1 and isoform 4.
VSP_000771Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
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]
GeneIDi2710.
KEGGihsa:2710.
UCSCiuc004dci.4. human. [P32189-1]
uc010ngj.3. human. [P32189-2]
uc011mjz.2. human. [P32189-3]

Polymorphism databases

DMDMi205830913.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS14225.1. [P32189-4 ]
CCDS35224.1. [P32189-1 ]
CCDS48090.1. [P32189-2 ]
PIRi I37427. S36175.
RefSeqi NP_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 ]
UniGenei Hs.1466.

3D structure databases

ProteinModelPortali P32189.
SMRi P32189. Positions 13-520.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108975. 12 interactions.
IntActi P32189. 11 interactions.
STRINGi 9606.ENSP00000368226.

Chemistry

BindingDBi P32189.
ChEMBLi CHEMBL2300.

PTM databases

PhosphoSitei P32189.

Polymorphism databases

DMDMi 205830913.

Proteomic databases

MaxQBi P32189.
PaxDbi P32189.
PRIDEi P32189.

Protocols and materials databases

DNASUi 2710.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000378943 ; ENSP00000368226 ; ENSG00000198814 . [P32189-2 ]
ENST00000378945 ; ENSP00000368228 ; ENSG00000198814 . [P32189-1 ]
ENST00000378946 ; ENSP00000368229 ; ENSG00000198814 . [P32189-4 ]
GeneIDi 2710.
KEGGi hsa:2710.
UCSCi uc004dci.4. human. [P32189-1 ]
uc010ngj.3. human. [P32189-2 ]
uc011mjz.2. human. [P32189-3 ]

Organism-specific databases

CTDi 2710.
GeneCardsi GC0XP030671.
HGNCi HGNC:4289. GK.
HPAi HPA060687.
MIMi 300474. gene.
307030. phenotype.
neXtProti NX_P32189.
Orphaneti 284414. Glycerol kinase deficiency, adult form.
284408. Glycerol kinase deficiency, infantile form.
284411. Glycerol kinase deficiency, juvenile form.
PharmGKBi PA28700.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0554.
HOGENOMi HOG000222134.
HOVERGENi HBG002451.
InParanoidi P32189.
KOi K00864.
OMAi DNLGIAK.
OrthoDBi EOG7VTDMZ.
PhylomeDBi P32189.
TreeFami TF321504.

Enzyme and pathway databases

UniPathwayi UPA00618 ; UER00672 .
Reactomei REACT_1190. Triglyceride Biosynthesis.

Miscellaneous databases

GenomeRNAii 2710.
NextBioi 10712.
PROi P32189.
SOURCEi Search...

Gene expression databases

ArrayExpressi P32189.
Bgeei P32189.
CleanExi HS_GK.
Genevestigatori P32189.

Family and domain databases

InterProi IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view ]
Pfami PF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01311. glycerol_kin. 1 hit.
PROSITEi PS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 151 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

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