GLPK_HUMAN
ID GLPK_HUMAN Reviewed; 559 AA.
AC P32189; A6NJP5; B2R833; Q6IQ27; Q8IVR5; Q9UMP0; Q9UMP1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Glycerol kinase;
DE Short=GK;
DE Short=Glycerokinase;
DE EC=2.7.1.30;
DE AltName: Full=ATP:glycerol 3-phosphotransferase;
GN Name=GK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8401584; DOI=10.1038/ng0893-367;
RA Guo W., Worley K.C., Adams V., Mason J., Sylvester-Jackson D.E.,
RA Zhang Y.-H., Towbin J.A., Fogt D.D., Madu S., Wheeler D.A., McCabe E.R.B.;
RT "Genomic scanning for expressed sequences in Xp21 identifies the glycerol
RT kinase gene.";
RL Nat. Genet. 4:367-372(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=7987308; DOI=10.1093/hmg/3.8.1317;
RA Sargent C.A., Young C., Marsh S., Ferguson-Smith M.A., Affara N.A.;
RT "The glycerol kinase gene family: structure of the Xp gene, and related
RT intronless retroposons.";
RL Hum. Mol. Genet. 3:1317-1324(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
RX PubMed=10851254; DOI=10.1136/jmg.37.6.434;
RA Sargent C.A., Kidd A., Moore S., Dean J., Besley G.T.N., Affara N.A.;
RT "Five cases of isolated glycerol kinase deficiency, including two families:
RT failure to find genotype:phenotype correlation.";
RL J. Med. Genet. 37:434-441(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANTS
RP LYS-79 AND THR-131.
RC TISSUE=Blood, and Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 77-559 (ISOFORM 3).
RC TISSUE=Fetal brain;
RX PubMed=8499912; DOI=10.1093/hmg/2.2.97;
RA Sargent C.A., Affara N.A., Bentley E., Pelmear A., Bailey D.M.D., Davey P.,
RA Dow D., Leversha M., Aplin H., Besley G.T.N., Ferguson-Smith M.A.;
RT "Cloning of the X-linked glycerol kinase deficiency gene and its
RT identification by sequence comparison to the Bacillus subtilis homologue.";
RL Hum. Mol. Genet. 2:97-106(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 130-559 (ISOFORM 1).
RC TISSUE=Fetal liver;
RX PubMed=8499898; DOI=10.1093/hmg/2.2.107;
RA Walker A.P., Muscatelli F., Monaco A.P.;
RT "Isolation of the human Xp21 glycerol kinase gene by positional cloning.";
RL Hum. Mol. Genet. 2:107-114(1993).
RN [9]
RP VARIANT GKD VAL-446.
RX PubMed=8651297;
RA Walker A.P., Muscatelli F., Stafford A.N., Chelly J., Dahl N.,
RA Blomquist H.K., Delanghe J., Willems P.J., Steinmann B., Monaco A.P.;
RT "Mutations and phenotype in isolated glycerol kinase deficiency.";
RL Am. J. Hum. Genet. 58:1205-1211(1996).
RN [10]
RP VARIANT GKD ARG-509.
RX PubMed=9719371; DOI=10.1136/jmg.35.8.650;
RA Sjarif D.R., Sinke R.J., Duran M., Beemer F.A., Kleijer W.J.,
RA Ploos van Amstel J.K., Poll-The B.T.;
RT "Clinical heterogeneity and novel mutations in the glycerol kinase gene in
RT three families with isolated glycerol kinase deficiency.";
RL J. Med. Genet. 35:650-656(1998).
RN [11]
RP VARIANT GKD ASP-294.
RX PubMed=10736265; DOI=10.1086/302903;
RA Gaudet D., Arsenault S., Perusse L., Vohl M.C., St Pierre J., Bergeron J.,
RA Despres J.P., Dewar K., Daly M.J., Hudson T., Rioux J.D.;
RT "Glycerol as a correlate of impaired glucose tolerance: dissection of a
RT complex system by use of a simple genetic trait.";
RL Am. J. Hum. Genet. 66:1558-1568(2000).
CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC metabolism.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC EC=2.7.1.30;
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC -!- INTERACTION:
CC P32189; P22736: NR4A1; NbExp=3; IntAct=EBI-3926629, EBI-721550;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane
CC protein; Cytoplasmic side. Cytoplasm. Note=In sperm and fetal tissues,
CC the majority of the enzyme is bound to mitochondria, but in adult
CC tissues, such as liver found in the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=3;
CC IsoId=P32189-3; Sequence=Displayed;
CC Name=1;
CC IsoId=P32189-1; Sequence=VSP_000770, VSP_000771;
CC Name=2;
CC IsoId=P32189-2; Sequence=VSP_000770;
CC Name=4;
CC IsoId=P32189-4; Sequence=VSP_000771;
CC -!- TISSUE SPECIFICITY: Highly expressed in the liver, kidney and testis.
CC Isoform 2 and isoform 3 are expressed specifically in testis and fetal
CC liver, but not in the adult liver.
CC -!- DISEASE: Glycerol kinase deficiency (GKD) [MIM:307030]: A metabolic
CC disorder manifesting as 3 clinically distinct forms: infantile,
CC juvenile, and adult. The infantile form is the most severe and is
CC associated with severe developmental delay and adrenal insufficiency.
CC Patients with the adult form have no symptoms and are often detected
CC fortuitously. GKD results in hyperglycerolemia, a condition
CC characterized by the accumulation of glycerol in the blood and urine.
CC {ECO:0000269|PubMed:10736265, ECO:0000269|PubMed:8651297,
CC ECO:0000269|PubMed:9719371}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA48346.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L13943; AAA52576.1; -; mRNA.
DR EMBL; X78211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ252550; CAB54859.1; -; Genomic_DNA.
DR EMBL; AJ252551; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252552; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252553; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252554; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252555; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252556; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252557; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252558; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252559; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252560; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252561; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252562; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252563; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252564; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252565; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252566; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252567; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252568; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252569; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252570; CAB54859.1; JOINED; Genomic_DNA.
DR EMBL; AJ252550; CAB54858.1; -; Genomic_DNA.
DR EMBL; AJ252551; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252552; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252553; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252554; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252555; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252556; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252557; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252559; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252560; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252561; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252562; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252563; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252564; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252565; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252566; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252567; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252568; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252569; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252570; CAB54858.1; JOINED; Genomic_DNA.
DR EMBL; AJ252550; CAB54857.1; -; Genomic_DNA.
DR EMBL; AJ252551; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252552; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252553; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252554; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252555; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252556; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252557; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252559; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252560; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252561; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252562; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252563; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252564; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252565; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252566; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252567; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252568; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AJ252570; CAB54857.1; JOINED; Genomic_DNA.
DR EMBL; AK313215; BAG36030.1; -; mRNA.
DR EMBL; AC005913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037549; AAH37549.1; -; mRNA.
DR EMBL; BC042421; AAH42421.1; -; mRNA.
DR EMBL; BC071595; AAH71595.1; -; mRNA.
DR EMBL; X68285; CAA48346.1; ALT_FRAME; mRNA.
DR EMBL; X69886; CAA49512.1; -; mRNA.
DR CCDS; CCDS14225.1; -. [P32189-4]
DR CCDS; CCDS35224.1; -. [P32189-1]
DR CCDS; CCDS48090.1; -. [P32189-2]
DR CCDS; CCDS75963.1; -. [P32189-3]
DR PIR; I37427; S36175.
DR RefSeq; NP_000158.1; NM_000167.5. [P32189-1]
DR RefSeq; NP_001121599.1; NM_001128127.2. [P32189-2]
DR RefSeq; NP_001191948.1; NM_001205019.1. [P32189-3]
DR RefSeq; NP_976325.1; NM_203391.3. [P32189-4]
DR AlphaFoldDB; P32189; -.
DR SMR; P32189; -.
DR BioGRID; 108975; 94.
DR IntAct; P32189; 44.
DR MINT; P32189; -.
DR STRING; 9606.ENSP00000401720; -.
DR BindingDB; P32189; -.
DR ChEMBL; CHEMBL2300; -.
DR MoonDB; P32189; Curated.
DR iPTMnet; P32189; -.
DR PhosphoSitePlus; P32189; -.
DR SwissPalm; P32189; -.
DR BioMuta; GK; -.
DR DMDM; 205830913; -.
DR EPD; P32189; -.
DR jPOST; P32189; -.
DR MassIVE; P32189; -.
DR MaxQB; P32189; -.
DR PeptideAtlas; P32189; -.
DR PRIDE; P32189; -.
DR ProteomicsDB; 1347; -.
DR ProteomicsDB; 54841; -. [P32189-3]
DR ProteomicsDB; 54842; -. [P32189-1]
DR ProteomicsDB; 54843; -. [P32189-2]
DR Antibodypedia; 10331; 335 antibodies from 34 providers.
DR DNASU; 2710; -.
DR Ensembl; ENST00000378943.7; ENSP00000368226.3; ENSG00000198814.14. [P32189-2]
DR Ensembl; ENST00000378945.7; ENSP00000368228.3; ENSG00000198814.14. [P32189-1]
DR Ensembl; ENST00000378946.7; ENSP00000368229.3; ENSG00000198814.14. [P32189-4]
DR Ensembl; ENST00000427190.6; ENSP00000401720.2; ENSG00000198814.14. [P32189-3]
DR GeneID; 2710; -.
DR KEGG; hsa:2710; -.
DR MANE-Select; ENST00000427190.6; ENSP00000401720.2; NM_001205019.2; NP_001191948.1.
DR UCSC; uc004dch.5; human. [P32189-3]
DR CTD; 2710; -.
DR DisGeNET; 2710; -.
DR GeneCards; GK; -.
DR GeneReviews; GK; -.
DR HGNC; HGNC:4289; GK.
DR HPA; ENSG00000198814; Tissue enhanced (intestine, kidney, liver).
DR MalaCards; GK; -.
DR MIM; 300474; gene.
DR MIM; 307030; phenotype.
DR neXtProt; NX_P32189; -.
DR OpenTargets; ENSG00000198814; -.
DR Orphanet; 284414; Glycerol kinase deficiency, adult form.
DR Orphanet; 284411; Glycerol kinase deficiency, juvenile form.
DR PharmGKB; PA28700; -.
DR VEuPathDB; HostDB:ENSG00000198814; -.
DR eggNOG; KOG2517; Eukaryota.
DR GeneTree; ENSGT01000000214434; -.
DR HOGENOM; CLU_009281_2_2_1; -.
DR InParanoid; P32189; -.
DR OMA; FMLMNIG; -.
DR OrthoDB; 519426at2759; -.
DR PhylomeDB; P32189; -.
DR TreeFam; TF321504; -.
DR BRENDA; 2.7.1.30; 2681.
DR PathwayCommons; P32189; -.
DR Reactome; R-HSA-75109; Triglyceride biosynthesis.
DR SignaLink; P32189; -.
DR SIGNOR; P32189; -.
DR UniPathway; UPA00618; UER00672.
DR BioGRID-ORCS; 2710; 10 hits in 709 CRISPR screens.
DR ChiTaRS; GK; human.
DR GenomeRNAi; 2710; -.
DR Pharos; P32189; Tbio.
DR PRO; PR:P32189; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P32189; protein.
DR Bgee; ENSG00000198814; Expressed in jejunal mucosa and 163 other tissues.
DR ExpressionAtlas; P32189; baseline and differential.
DR Genevisible; P32189; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004370; F:glycerol kinase activity; IMP:BHF-UCL.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006071; P:glycerol metabolic process; IMP:BHF-UCL.
DR GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:BHF-UCL.
DR CDD; cd07792; FGGY_GK1-3_metazoa; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR042018; GK1-3_metazoa.
DR InterPro; IPR005999; Glycerol_kin.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR PROSITE; PS00933; FGGY_KINASES_1; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Disease variant;
KW Glycerol metabolism; Kinase; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..559
FT /note="Glycerol kinase"
FT /id="PRO_0000059535"
FT BINDING 20
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 433..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 245..250
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7987308,
FT ECO:0000303|PubMed:8401584, ECO:0000303|PubMed:8499898"
FT /id="VSP_000770"
FT VAR_SEQ 528..556
FT /note="Missing (in isoform 1 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8401584,
FT ECO:0000303|PubMed:8499898"
FT /id="VSP_000771"
FT VARIANT 79
FT /note="N -> K (in dbSNP:rs17857267)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_068980"
FT VARIANT 131
FT /note="P -> T (in dbSNP:rs17854203)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_068981"
FT VARIANT 185
FT /note="S -> N"
FT /id="VAR_001374"
FT VARIANT 232
FT /note="N -> H"
FT /id="VAR_001375"
FT VARIANT 294
FT /note="N -> D (in GKD; dbSNP:rs132630331)"
FT /evidence="ECO:0000269|PubMed:10736265"
FT /id="VAR_015433"
FT VARIANT 382
FT /note="A -> T"
FT /id="VAR_001376"
FT VARIANT 446
FT /note="D -> V (in GKD; dbSNP:rs132630328)"
FT /evidence="ECO:0000269|PubMed:8651297"
FT /id="VAR_001377"
FT VARIANT 509
FT /note="W -> R (in GKD; dbSNP:rs132630330)"
FT /evidence="ECO:0000269|PubMed:9719371"
FT /id="VAR_010138"
SQ SEQUENCE 559 AA; 61245 MW; 18268B7A4C6A09F3 CRC64;
MAASKKAVLG PLVGAVDQGT SSTRFLVFNS KTAELLSHHQ VEIKQEFPRE GWVEQDPKEI
LHSVYECIEK TCEKLGQLNI DISNIKAIGV SNQRETTVVW DKITGEPLYN AVVWLDLRTQ
STVESLSKRI PGNNNFVKSK TGLPLSTYFS AVKLRWLLDN VRKVQKAVEE KRALFGTIDS
WLIWSLTGGV NGGVHCTDVT NASRTMLFNI HSLEWDKQLC EFFGIPMEIL PNVRSSSEIY
GLMKISHSVK AGALEGVPIS GCLGDQSAAL VGQMCFQIGQ AKNTYGTGCF LLCNTGHKCV
FSDHGLLTTV AYKLGRDKPV YYALEGSVAI AGAVIRWLRD NLGIIKTSEE IEKLAKEVGT
SYGCYFVPAF SGLYAPYWEP SARGIICGLT QFTNKCHIAF AALEAVCFQT REILDAMNRD
CGIPLSHLQV DGGMTSNKIL MQLQADILYI PVVKPSMPET TALGAAMAAG AAEGVGVWSL
EPEDLSAVTM ERFEPQINAE ESEIRYSTWK KAVMKSMGWV TTQSPESGDP SIFCSLPLGF
FIVSSMVMLI GARYISGIP
