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P32189

- GLPK_HUMAN

UniProt

P32189 - GLPK_HUMAN

Protein

Glycerol kinase

Gene

GK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (22 Jul 2008)
      Previous versions | rss
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    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
    3. protein binding Source: IntAct

    GO - Biological processi

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

    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

    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FGGY kinase family.Curated

    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. 5 PublicationsVSP_000770
    Alternative sequencei528 – 55629Missing in isoform 1 and isoform 4. 4 PublicationsVSP_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...
    MobiDBi 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

    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: October 1, 2014
    This is version 152 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