GALK1_HUMAN
ID GALK1_HUMAN Reviewed; 392 AA.
AC P51570; B2RC07; B4E1G6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Galactokinase {ECO:0000305};
DE EC=2.7.1.6 {ECO:0000269|PubMed:12694189, ECO:0000269|PubMed:7542884};
DE AltName: Full=Galactose kinase;
GN Name=GALK1 {ECO:0000312|HGNC:HGNC:4118}; Synonyms=GALK;
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], AND VARIANT GALAC2 MET-32.
RX PubMed=7670469; DOI=10.1038/ng0795-307;
RA Stambolian D., Ai Y., Sidjanin D., Nesburn K., Sathe G., Rosenberg M.,
RA Bergsma D.J.;
RT "Cloning of the galactokinase cDNA and identification of mutations in two
RT families with cataracts.";
RL Nat. Genet. 10:307-312(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8908517; DOI=10.1101/gr.6.10.980;
RA Bergsma D.J., Ai Y., Skach W.R., Nesburn K., Anoia E., van Horn S.,
RA Stambolian D.;
RT "Fine structure of the human galactokinase GALK1 gene.";
RL Genome Res. 6:980-985(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [8]
RP PROTEIN SEQUENCE OF 6-17; 22-37; 70-97; 205-239; 257-267; 288-296 AND
RP 343-388, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7542884; DOI=10.1006/bbrc.1995.2023;
RA Ai Y., Basu M., Bergsma D.J., Stambolian D.;
RT "Comparison of the enzymatic activities of human galactokinase GALK1 and a
RT related human galactokinase protein GK2.";
RL Biochem. Biophys. Res. Commun. 212:687-691(1995).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-392 IN COMPLEX WITH D-GALACTOSE
RP AND ATP ANALOG, SUBUNIT, AND SUBSTRATE-BINDING SITES.
RX PubMed=15590630; DOI=10.1074/jbc.m412916200;
RA Thoden J.B., Timson D.J., Reece R.J., Holden H.M.;
RT "Molecular structure of human galactokinase: implications for type II
RT galactosemia.";
RL J. Biol. Chem. 280:9662-9670(2005).
RN [14]
RP VARIANT GALAC2 THR-28.
RX PubMed=10521295; DOI=10.1086/302611;
RA Kalaydjieva L., Perez-Lezaun A., Angelicheva D., Onengut S., Dye D.,
RA Bosshard N.U., Jordanova A., Savov A., Yanakiev P., Kremensky I.,
RA Radeva B., Hallmayer J., Markov A., Nedkova V., Tournev I., Aneva L.,
RA Gitzelmann R.;
RT "A founder mutation in the GK1 gene is responsible for galactokinase
RT deficiency in Roma (Gypsies).";
RL Am. J. Hum. Genet. 65:1299-1307(1999).
RN [15]
RP VARIANTS GALAC2 THR-28; ARG-36; TYR-44; SER-346 AND SER-349.
RX PubMed=10790206;
RX DOI=10.1002/(sici)1098-1004(200005)15:5<447::aid-humu6>3.0.co;2-m;
RA Kolosha V., Anoia E., de Cespedes C., Gitzelmann R., Shih L., Casco T.,
RA Saborio M., Trejos R., Buist N., Tedesco T., Skach W., Mitelmann O.,
RA Ledee D., Huang K., Stambolian D.;
RT "Novel mutations in 13 probands with galactokinase deficiency.";
RL Hum. Mutat. 15:447-453(2000).
RN [16]
RP VARIANT GALAC2 VAL-198.
RX PubMed=11231902; DOI=10.1086/319512;
RA Okano Y., Asada M., Fujimoto A., Ohtake A., Murayama K., Hsiao K.-J.,
RA Choeh K., Yang Y., Cao Q., Reichardt J.K.V., Niihira S., Imamura T.,
RA Yamano T.;
RT "A genetic factor for age-related cataract: identification and
RT characterization of a novel galactokinase variant, 'Osaka,' in Asians.";
RL Am. J. Hum. Genet. 68:1036-1042(2001).
RN [17]
RP VARIANTS GALAC2 CYS-68; MET-288 AND PRO-384.
RX PubMed=11139256; DOI=10.1002/1098-1004(2001)17:1<77::aid-humu20>3.0.co;2-h;
RA Hunter M., Angelicheva D., Levy H.L., Pueschel S.M., Kalaydjieva L.;
RT "Novel mutations in the GALK1 gene in patients with galactokinase
RT deficiency.";
RL Hum. Mutat. 17:77-78(2001).
RN [18]
RP CHARACTERIZATION OF VARIANTS GALAC2 THR-28; MET-32; ARG-36; TYR-44; CYS-68;
RP VAL-198; MET-288; SER-346; SER-349 AND PRO-384, CATALYTIC ACTIVITY,
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12694189; DOI=10.1046/j.1432-1033.2003.03538.x;
RA Timson D.J., Reece R.J.;
RT "Functional analysis of disease-causing mutations in human galactokinase.";
RL Eur. J. Biochem. 270:1767-1774(2003).
RN [19]
RP VARIANTS MET-184; ASP-274 AND ALA-338.
RX PubMed=12942049;
RA Maraini G., Hejtmancik J.F., Shiels A., Mackay D.S., Aldigeri R.,
RA Jiao X.D., Williams S.L., Sperduto R.D., Reed G.;
RT "Galactokinase gene mutations and age-related cataract. Lack of association
RT in an Italian population.";
RL Mol. Vis. 9:397-400(2003).
RN [20]
RP VARIANTS GALAC2 MET-32 AND GLN-239.
RX PubMed=15024738; DOI=10.1002/humu.9223;
RA Sangiuolo F., Magnani M., Stambolian D., Novelli G.;
RT "Biochemical characterization of two GALK1 mutations in patients with
RT galactokinase deficiency.";
RL Hum. Mutat. 23:396-396(2004).
CC -!- FUNCTION: Catalyzes the transfer of a phosphate from ATP to alpha-D-
CC galactose and participates in the first committed step in the
CC catabolism of galactose. {ECO:0000269|PubMed:12694189,
CC ECO:0000269|PubMed:7542884}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate
CC + H(+); Xref=Rhea:RHEA:13553, ChEBI:CHEBI:15378, ChEBI:CHEBI:28061,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58336, ChEBI:CHEBI:456216; EC=2.7.1.6;
CC Evidence={ECO:0000269|PubMed:12694189, ECO:0000269|PubMed:7542884};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13554;
CC Evidence={ECO:0000305|PubMed:7542884};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=970 uM for alpha-D-galactose {ECO:0000269|PubMed:12694189};
CC KM=34 uM for ATP {ECO:0000269|PubMed:12694189};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000269|PubMed:12694189, ECO:0000269|PubMed:7542884}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:15590630}.
CC -!- INTERACTION:
CC P51570; Q9NPJ4: PNRC2; NbExp=3; IntAct=EBI-2269932, EBI-726549;
CC -!- DISEASE: Galactosemia 2 (GALAC2) [MIM:230200]: A form of galactosemia,
CC an inborn error of galactose metabolism typically manifesting in the
CC neonatal period, after ingestion of galactose, with jaundice,
CC hepatosplenomegaly, hepatocellular insufficiency, food intolerance,
CC hypoglycemia, renal tubular dysfunction, muscle hypotonia, sepsis and
CC cataract. GALAC2 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:10521295, ECO:0000269|PubMed:10790206,
CC ECO:0000269|PubMed:11139256, ECO:0000269|PubMed:11231902,
CC ECO:0000269|PubMed:12694189, ECO:0000269|PubMed:15024738,
CC ECO:0000269|PubMed:7670469}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG64778.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW89316.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Galactosemia Proteins Database;
CC URL="http://www.protein-variants.eu/galactosemia/";
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DR EMBL; U26401; AAA96147.1; -; mRNA.
DR EMBL; L76927; AAB51607.1; -; Genomic_DNA.
DR EMBL; AK303832; BAG64778.1; ALT_INIT; mRNA.
DR EMBL; AK314890; BAG37404.1; -; mRNA.
DR EMBL; BT007005; AAP35651.1; -; mRNA.
DR EMBL; AC087749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89316.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC001166; AAH01166.1; -; mRNA.
DR CCDS; CCDS11728.1; -.
DR PDB; 1WUU; X-ray; 2.50 A; A/B/C/D=2-392.
DR PDB; 6GR2; X-ray; 2.49 A; A/B/C/D/E/F/G/H=2-392.
DR PDB; 6Q3W; X-ray; 1.96 A; A/B/C/D=2-392.
DR PDB; 6Q3X; X-ray; 2.10 A; A/B=2-392.
DR PDB; 6Q8Z; X-ray; 2.40 A; A/B/C/D=2-392.
DR PDB; 6Q90; X-ray; 2.40 A; A/B/C/D=2-392.
DR PDB; 6Q91; X-ray; 2.40 A; A/B/C/D=2-392.
DR PDB; 6QJE; X-ray; 2.40 A; A/B/C/D=2-392.
DR PDB; 6ZFH; X-ray; 2.44 A; A/B/C/D/E/F/G/H=2-392.
DR PDB; 6ZGV; X-ray; 2.30 A; A/B/D/E=2-392.
DR PDB; 6ZGW; X-ray; 2.30 A; A/B/D/E=2-392.
DR PDB; 6ZGX; X-ray; 1.86 A; A/B/D/E=2-392.
DR PDB; 6ZGY; X-ray; 2.30 A; A/B/D/E=2-392.
DR PDB; 6ZGZ; X-ray; 2.30 A; A/B/D/E=2-392.
DR PDB; 7RCL; X-ray; 2.40 A; A/B/C/D=1-392.
DR PDB; 7RCM; X-ray; 2.10 A; A/B=1-392.
DR PDB; 7S49; X-ray; 2.20 A; A/B=1-392.
DR PDB; 7S4C; X-ray; 2.20 A; A/B=1-392.
DR PDBsum; 1WUU; -.
DR PDBsum; 6GR2; -.
DR PDBsum; 6Q3W; -.
DR PDBsum; 6Q3X; -.
DR PDBsum; 6Q8Z; -.
DR PDBsum; 6Q90; -.
DR PDBsum; 6Q91; -.
DR PDBsum; 6QJE; -.
DR PDBsum; 6ZFH; -.
DR PDBsum; 6ZGV; -.
DR PDBsum; 6ZGW; -.
DR PDBsum; 6ZGX; -.
DR PDBsum; 6ZGY; -.
DR PDBsum; 6ZGZ; -.
DR PDBsum; 7RCL; -.
DR PDBsum; 7RCM; -.
DR PDBsum; 7S49; -.
DR PDBsum; 7S4C; -.
DR AlphaFoldDB; P51570; -.
DR SMR; P51570; -.
DR BioGRID; 108857; 55.
DR IntAct; P51570; 35.
DR MINT; P51570; -.
DR STRING; 9606.ENSP00000465930; -.
DR BindingDB; P51570; -.
DR ChEMBL; CHEMBL1293257; -.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR GlyGen; P51570; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51570; -.
DR PhosphoSitePlus; P51570; -.
DR BioMuta; GALK1; -.
DR DMDM; 1730187; -.
DR OGP; P51570; -.
DR REPRODUCTION-2DPAGE; IPI00019383; -.
DR CPTAC; CPTAC-375; -.
DR CPTAC; CPTAC-376; -.
DR EPD; P51570; -.
DR jPOST; P51570; -.
DR MassIVE; P51570; -.
DR MaxQB; P51570; -.
DR PaxDb; P51570; -.
DR PeptideAtlas; P51570; -.
DR PRIDE; P51570; -.
DR Antibodypedia; 2046; 292 antibodies from 32 providers.
DR DNASU; 2584; -.
DR Ensembl; ENST00000225614.6; ENSP00000225614.1; ENSG00000108479.13.
DR Ensembl; ENST00000588479.6; ENSP00000465930.1; ENSG00000108479.13.
DR GeneID; 2584; -.
DR MANE-Select; ENST00000588479.6; ENSP00000465930.1; NM_000154.2; NP_000145.1.
DR CTD; 2584; -.
DR DisGeNET; 2584; -.
DR GeneCards; GALK1; -.
DR HGNC; HGNC:4118; GALK1.
DR HPA; ENSG00000108479; Tissue enhanced (liver).
DR MalaCards; GALK1; -.
DR MIM; 230200; phenotype.
DR MIM; 604313; gene.
DR neXtProt; NX_P51570; -.
DR OpenTargets; ENSG00000108479; -.
DR Orphanet; 79237; Galactokinase deficiency.
DR PharmGKB; PA28533; -.
DR VEuPathDB; HostDB:ENSG00000108479; -.
DR eggNOG; KOG0631; Eukaryota.
DR GeneTree; ENSGT00950000183187; -.
DR HOGENOM; CLU_017814_2_0_1; -.
DR InParanoid; P51570; -.
DR OMA; NTHQDYK; -.
DR PhylomeDB; P51570; -.
DR TreeFam; TF354326; -.
DR BioCyc; MetaCyc:HS03112-MON; -.
DR BRENDA; 2.7.1.6; 2681.
DR PathwayCommons; P51570; -.
DR Reactome; R-HSA-5609976; Defective GALK1 causes GALCT2.
DR Reactome; R-HSA-70370; Galactose catabolism.
DR SABIO-RK; P51570; -.
DR SignaLink; P51570; -.
DR UniPathway; UPA00214; -.
DR BioGRID-ORCS; 2584; 29 hits in 1075 CRISPR screens.
DR EvolutionaryTrace; P51570; -.
DR GenomeRNAi; 2584; -.
DR Pharos; P51570; Tbio.
DR PRO; PR:P51570; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P51570; protein.
DR Bgee; ENSG00000108479; Expressed in right lobe of liver and 95 other tissues.
DR ExpressionAtlas; P51570; baseline and differential.
DR Genevisible; P51570; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004335; F:galactokinase activity; IDA:UniProtKB.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
DR GO; GO:0019402; P:galactitol metabolic process; IEA:Ensembl.
DR GO; GO:0019388; P:galactose catabolic process; TAS:Reactome.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IEA:Ensembl.
DR GO; GO:0006012; P:galactose metabolic process; IMP:UniProtKB.
DR GO; GO:0061623; P:glycolytic process from galactose; IEA:Ensembl.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR000705; Galactokinase.
DR InterPro; IPR019741; Galactokinase_CS.
DR InterPro; IPR019539; GalKase_N.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR006206; Mevalonate/galactokinase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10457:SF6; PTHR10457:SF6; 1.
DR Pfam; PF10509; GalKase_gal_bdg; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF000530; Galactokinase; 1.
DR PRINTS; PR00473; GALCTOKINASE.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00131; gal_kin; 1.
DR PROSITE; PS00106; GALACTOKINASE; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Cataract;
KW Direct protein sequencing; Disease variant; Galactose metabolism; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..392
FT /note="Galactokinase"
FT /id="PRO_0000184645"
FT ACT_SITE 186
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 43..46
FT /ligand="substrate"
FT BINDING 134..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 183..186
FT /ligand="substrate"
FT BINDING 236
FT /ligand="substrate"
FT SITE 37
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 28
FT /note="P -> T (in GALAC2; founder Romani mutation;
FT dbSNP:rs104894572)"
FT /evidence="ECO:0000269|PubMed:10521295,
FT ECO:0000269|PubMed:10790206, ECO:0000269|PubMed:12694189"
FT /id="VAR_008514"
FT VARIANT 32
FT /note="V -> M (in GALAC2; dbSNP:rs104894576)"
FT /evidence="ECO:0000269|PubMed:12694189,
FT ECO:0000269|PubMed:15024738, ECO:0000269|PubMed:7670469"
FT /id="VAR_002547"
FT VARIANT 36
FT /note="G -> R (in GALAC2)"
FT /evidence="ECO:0000269|PubMed:10790206,
FT ECO:0000269|PubMed:12694189"
FT /id="VAR_023486"
FT VARIANT 44
FT /note="H -> Y (in GALAC2; dbSNP:rs1555748926)"
FT /evidence="ECO:0000269|PubMed:10790206,
FT ECO:0000269|PubMed:12694189"
FT /id="VAR_023487"
FT VARIANT 68
FT /note="R -> C (in GALAC2; dbSNP:rs1365349586)"
FT /evidence="ECO:0000269|PubMed:11139256,
FT ECO:0000269|PubMed:12694189"
FT /id="VAR_023488"
FT VARIANT 184
FT /note="I -> M (in dbSNP:rs773416476)"
FT /evidence="ECO:0000269|PubMed:12942049"
FT /id="VAR_023489"
FT VARIANT 198
FT /note="A -> V (in GALAC2; mild deficiency; Osaka;
FT dbSNP:rs80084721)"
FT /evidence="ECO:0000269|PubMed:11231902,
FT ECO:0000269|PubMed:12694189"
FT /id="VAR_015746"
FT VARIANT 239
FT /note="R -> Q (in GALAC2; dbSNP:rs575139300)"
FT /evidence="ECO:0000269|PubMed:15024738"
FT /id="VAR_023490"
FT VARIANT 274
FT /note="G -> D (in dbSNP:rs959842362)"
FT /evidence="ECO:0000269|PubMed:12942049"
FT /id="VAR_023491"
FT VARIANT 288
FT /note="T -> M (in GALAC2; dbSNP:rs759284637)"
FT /evidence="ECO:0000269|PubMed:11139256,
FT ECO:0000269|PubMed:12694189"
FT /id="VAR_023492"
FT VARIANT 338
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:12942049"
FT /id="VAR_023493"
FT VARIANT 346
FT /note="G -> S (in GALAC2; dbSNP:rs375690568)"
FT /evidence="ECO:0000269|PubMed:10790206,
FT ECO:0000269|PubMed:12694189"
FT /id="VAR_023494"
FT VARIANT 349
FT /note="G -> S (in GALAC2; dbSNP:rs754967473)"
FT /evidence="ECO:0000269|PubMed:10790206,
FT ECO:0000269|PubMed:12694189"
FT /id="VAR_023495"
FT VARIANT 384
FT /note="A -> P (in GALAC2; dbSNP:rs1184406839)"
FT /evidence="ECO:0000269|PubMed:11139256,
FT ECO:0000269|PubMed:12694189"
FT /id="VAR_023496"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 29..39
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 54..67
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1WUU"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6Q3X"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1WUU"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 141..156
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 163..178
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:6ZGX"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 231..249
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 272..296
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 300..316
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 348..357
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:6ZGX"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6ZGY"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:6ZGX"
FT STRAND 387..391
FT /evidence="ECO:0007829|PDB:6ZGX"
SQ SEQUENCE 392 AA; 42272 MW; 8D7CFF8FDB0E4718 CRC64;
MAALRQPQVA ELLAEARRAF REEFGAEPEL AVSAPGRVNL IGEHTDYNQG LVLPMALELM
TVLVGSPRKD GLVSLLTTSE GADEPQRLQF PLPTAQRSLE PGTPRWANYV KGVIQYYPAA
PLPGFSAVVV SSVPLGGGLS SSASLEVATY TFLQQLCPDS GTIAARAQVC QQAEHSFAGM
PCGIMDQFIS LMGQKGHALL IDCRSLETSL VPLSDPKLAV LITNSNVRHS LASSEYPVRR
RQCEEVARAL GKESLREVQL EELEAARDLV SKEGFRRARH VVGEIRRTAQ AAAALRRGDY
RAFGRLMVES HRSLRDDYEV SCPELDQLVE AALAVPGVYG SRMTGGGFGG CTVTLLEASA
APHAMRHIQE HYGGTATFYL SQAADGAKVL CL
