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 27-MAR-2024, entry version 217. DE RecName: Full=Glycerol kinase {ECO:0000305|PubMed:37021775}; DE Short=Glycerokinase; DE EC=2.7.1.30 {ECO:0000269|PubMed:37021775}; DE AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000303|PubMed:8499898}; GN Name=GK {ECO:0000312|HGNC:HGNC:4289}; 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), FUNCTION, AND CATALYTIC ACTIVITY. 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 FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION (ISOFORMS 3 AND RP 4), AND TISSUE SPECIFICITY (ISOFORMS 2; 3 AND 4). RX PubMed=15845384; DOI=10.1016/j.bbrc.2005.03.143; RA Ohira R.H., Dipple K.M., Zhang Y.H., McCabe E.R.; RT "Human and murine glycerol kinase: influence of exon 18 alternative RT splicing on function."; RL Biochem. Biophys. Res. Commun. 331:239-246(2005). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND PATHWAY. RX PubMed=37021775; DOI=10.1042/bsr20222258; RA Rani R.M., Syngkli S., Nongkhlaw J., Das B.; RT "Expression and characterisation of human glycerol kinase: the role of RT solubilising agents and molecular chaperones."; RL Biosci. Rep. 43:0-0(2023). RN [11] 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 [12] 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 [13] 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: Kinase that plays a key role in glycerol metabolism, CC catalyzing its phosphorylation to produce sn-glycerol 3-phosphate. Sn- CC glycerol 3-phosphate is a crucial intermediate in various metabolic CC pathways, such as the synthesis of glycerolipids and triglycerides, CC glycogenesis, glycolysis and gluconeogenesis. CC {ECO:0000269|PubMed:15845384, ECO:0000269|PubMed:37021775}. 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; Evidence={ECO:0000269|PubMed:15845384, CC ECO:0000269|PubMed:37021775}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21645; CC Evidence={ECO:0000305|PubMed:37021775}; CC -!- ACTIVITY REGULATION: Potassium and magnesium-dependent. CC {ECO:0000269|PubMed:37021775}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=5.022 uM for glycerol {ECO:0000269|PubMed:37021775}; CC KM=0.767 mM for ATP {ECO:0000269|PubMed:37021775}; CC KM=0.223 mM for phosphoenolpyruvate {ECO:0000269|PubMed:37021775}; CC pH dependence: CC Optimum pH is 7.7. {ECO:0000269|PubMed:37021775}; CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. CC {ECO:0000305|PubMed:15845384, ECO:0000305|PubMed:37021775}. CC -!- INTERACTION: CC P32189; P22736: NR4A1; NbExp=3; IntAct=EBI-3926629, EBI-721550; CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane CC {ECO:0000305|PubMed:15845384}; Single-pass membrane protein CC {ECO:0000255}. Nucleus {ECO:0000269|PubMed:15845384}. Cytoplasm, CC cytosol {ECO:0000305|PubMed:15845384}. Note=Glycerol kinase activity is CC more cytosolic in some tissues. It probably represents the expression CC of isoforms lacking a transmembrane domain. CC {ECO:0000305|PubMed:15845384}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion outer membrane CC {ECO:0000305|PubMed:15845384}; Single-pass membrane protein CC {ECO:0000255}. Nucleus {ECO:0000269|PubMed:15845384}. Note=In sperm and CC fetal tissues, the majority of the activity is associated with CC mitochondria. {ECO:0000305|PubMed:15845384}. CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytosol CC {ECO:0000305|PubMed:15845384}. Note=In adult tissues, such as liver the CC glycerol kinase activity is more cytosolic. It probably represents the CC expression of this isoform which lacks a transmembrane domain. CC {ECO:0000305|PubMed:15845384}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=3; Synonyms=GK+EX18 {ECO:0000303|PubMed:15845384}; 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; Synonyms=GK-EX18 {ECO:0000303|PubMed:15845384}; CC IsoId=P32189-4; Sequence=VSP_000771; CC -!- TISSUE SPECIFICITY: [Isoform 2]: Widely expressed in fetal and adult CC tissues. {ECO:0000269|PubMed:15845384}. CC -!- TISSUE SPECIFICITY: [Isoform 3]: Widely expressed in fetal and adult CC tissues. {ECO:0000269|PubMed:15845384}. CC -!- TISSUE SPECIFICITY: [Isoform 4]: The sole isoform expressed in adult CC liver and kidney. {ECO:0000269|PubMed:15845384}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 96. DR IntAct; P32189; 46. 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 PaxDb; 9606-ENSP00000401720; -. DR PeptideAtlas; P32189; -. DR ProteomicsDB; 1347; -. DR ProteomicsDB; 54841; -. [P32189-3] DR ProteomicsDB; 54842; -. [P32189-1] DR ProteomicsDB; 54843; -. [P32189-2] DR Pumba; P32189; -. DR Antibodypedia; 10331; 366 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 AGR; HGNC:4289; -. 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; 2734344at2759; -. 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; 11 hits in 787 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 164 other cell types or tissues. DR ExpressionAtlas; P32189; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004370; F:glycerol kinase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; IDA:UniProtKB. 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 Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR000577; Carb_kinase_FGGY. DR InterPro; IPR018483; Carb_kinase_FGGY_CS. DR InterPro; IPR018485; FGGY_C. DR InterPro; IPR018484; FGGY_N. DR InterPro; IPR042018; GK1-3_metazoa. DR InterPro; IPR005999; Glycerol_kin. DR NCBIfam; TIGR01311; glycerol_kin; 1. DR PANTHER; PTHR10196:SF56; GLYCEROL KINASE; 1. DR PANTHER; PTHR10196; SUGAR KINASE; 1. DR Pfam; PF02782; FGGY_C; 1. DR Pfam; PF00370; FGGY_N; 1. DR PIRSF; PIRSF000538; GlpK; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR PROSITE; PS00933; FGGY_KINASES_1; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. DR Genevisible; P32189; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cytoplasm; Disease variant; KW Glycerol metabolism; Kinase; Membrane; Metal-binding; Mitochondrion; KW Mitochondrion outer membrane; Nucleotide-binding; Nucleus; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1..559 FT /note="Glycerol kinase" FT /id="PRO_0000059535" FT TRANSMEM 532..552 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 20 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 20 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 20 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 21 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 24 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 94 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 94 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 95 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 95 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 148 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 148 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 252 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /ligand_note="allosteric inhibitor" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 265 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 265 FT /ligand="sn-glycerol 3-phosphate" FT /ligand_id="ChEBI:CHEBI:57597" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 266 FT /ligand="glycerol" FT /ligand_id="ChEBI:CHEBI:17754" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 287 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 287 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 332 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 332 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 433 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 433 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" FT BINDING 437 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P0A6F3" 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 //