ID A0A5F9ZHE0_HUMAN Unreviewed; 486 AA. AC A0A5F9ZHE0; DT 11-DEC-2019, integrated into UniProtKB/TrEMBL. DT 11-DEC-2019, sequence version 1. DT 02-OCT-2024, entry version 25. DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007}; DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007}; GN Name=GCK {ECO:0000313|Ensembl:ENSP00000500264.1}; 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 {ECO:0000313|Ensembl:ENSP00000500264.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000500264.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11237011; DOI=10.1038/35057062; RG International Human Genome Sequencing Consortium; RA Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J., RA Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K., RA Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P., RA McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J., RA Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C., RA Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J., RA Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C., RA Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I., RA Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S., RA Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S., RA Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S., RA Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A., RA Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R., RA Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A., RA Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W., RA Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T., RA Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E., RA Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B., RA Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L., RA Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y., RA Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C., RA Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W., RA Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P., RA Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M., RA Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A., RA Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A., RA Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M., RA Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R., RA Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A., RA Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J., RA Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N., RA Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L., RA Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G., RA Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R., RA Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G., RA Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W., RA Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J., RA Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M., RA McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J., RA Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E., RA Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J., RA Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F., RA Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A., RA Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K., RA Shizuya H., Choi S., Chen Y.J.; RT "Initial sequencing and analysis of the human genome."; RL Nature 409:860-921(2001). RN [2] {ECO:0000313|Ensembl:ENSP00000500264.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., RA Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., RA Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., RA Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., RA Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., RA Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [3] {ECO:0000313|Ensembl:ENSP00000500264.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496913; DOI=10.1038/nature03001; RG International Human Genome Sequencing Consortium; RT "Finishing the euchromatic sequence of the human genome."; RL Nature 431:931-945(2004). RN [4] {ECO:0000313|Ensembl:ENSP00000500264.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2024) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); CC Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1; CC Evidence={ECO:0000256|ARBA:ARBA00000435}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; CC Evidence={ECO:0000256|ARBA:ARBA00000435}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); CC Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; CC EC=2.7.1.1; Evidence={ECO:0000256|ARBA:ARBA00044613}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; CC Evidence={ECO:0000256|ARBA:ARBA00044613}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 1/4. CC {ECO:0000256|ARBA:ARBA00004888}. CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism. CC {ECO:0000256|ARBA:ARBA00005028}. CC -!- SIMILARITY: Belongs to the hexokinase family. CC {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}. 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; AC006454; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KF458452; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; A0A5F9ZHE0; -. DR SMR; A0A5F9ZHE0; -. DR MassIVE; A0A5F9ZHE0; -. DR PeptideAtlas; A0A5F9ZHE0; -. DR Antibodypedia; 2045; 618 antibodies from 35 providers. DR Ensembl; ENST00000671824.1; ENSP00000500264.1; ENSG00000106633.18. DR HGNC; HGNC:4195; GCK. DR VEuPathDB; HostDB:ENSG00000106633; -. DR GeneTree; ENSGT00950000182787; -. DR OMA; ADCVQQF; -. DR UniPathway; UPA00109; UER00180. DR UniPathway; UPA00242; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000106633; Expressed in pituitary gland and 100 other cell types or tissues. DR ExpressionAtlas; A0A5F9ZHE0; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0005536; F:D-glucose binding; IEA:InterPro. DR GO; GO:0004340; F:glucokinase activity; IEA:RHEA. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 1. DR Gene3D; 3.40.367.20; -; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR001312; Hexokinase. DR InterPro; IPR019807; Hexokinase_BS. DR InterPro; IPR022673; Hexokinase_C. DR InterPro; IPR022672; Hexokinase_N. DR PANTHER; PTHR19443; HEXOKINASE; 1. DR PANTHER; PTHR19443:SF3; HEXOKINASE-4; 1. DR Pfam; PF00349; Hexokinase_1; 1. DR Pfam; PF03727; Hexokinase_2; 2. DR PRINTS; PR00475; HEXOKINASE. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR PROSITE; PS00378; HEXOKINASE_1; 1. DR PROSITE; PS51748; HEXOKINASE_2; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU362007}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU362007}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A5F9ZHE0, KW ECO:0007829|ProteomicsDB:A0A5F9ZHE0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}. FT DOMAIN 16..215 FT /note="Hexokinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00349" FT DOMAIN 222..287 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" FT DOMAIN 309..476 FT /note="Hexokinase C-terminal" FT /evidence="ECO:0000259|Pfam:PF03727" FT COILED 13..40 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 486 AA; 54386 MW; CCC0D74620A62C27 CRC64; MLDDRARMEA AKKEKVEQIL AEFQLQEEDL KKVMRRMQKE MDRGLRLETH EEASVKMLPT YVRSTPEGSE VGDFLSLDLG GTNFRVMLVK VGEGEEGQWS VKTKHQMYSI PEDAMTGTAE MLFDYISECI SDFLDKHQMK HKKLPLGFTF SFPVRHEDID KGILLNWTKG FKASGAEGNN VVGLLRDAIK RRGDFEMDVV AMVNDTVATM ISCYYEDHQC EVGMIVGTGC NACYMEEMQN VELVEGDEGR MCVNTEWGAF GDSGELDEFL LEYDRLVDES SANPGDRACR GGSETPPARF LGLTQHSPKY EKLIGGKYMG ELVRLVLLRL VDENLLFHGE ASEQLRTRGA FETRFVSQVE SDTGDRKQIY NILSTLGLRP STTDCDIVRR ACESVSTRAA HMCSAGLAGV INRMRESRSE DVMRITVGVD GSVYKLHPSF KERFHASVRR LTPSCEITFI ESEEGSGRGA ALVSAVACKK ACMLGQ //