GALK2_HUMAN
ID GALK2_HUMAN Reviewed; 458 AA.
AC Q01415; Q7Z4Q4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=N-acetylgalactosamine kinase;
DE EC=2.7.1.157;
DE AltName: Full=GalNAc kinase;
DE AltName: Full=Galactokinase 2;
GN Name=GALK2; Synonyms=GK2;
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).
RX PubMed=1438294; DOI=10.1073/pnas.89.22.10887;
RA Lee R.T., Peterson C.L., Calman A.F., Herskowitz I., O'Donnell J.J.;
RT "Cloning of a human galactokinase gene (GK2) on chromosome 15 by
RT complementation in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10887-10891(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Guo J.H., Zan Q., Yu L.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [6]
RP CHARACTERIZATION.
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 [7]
RP POSSIBLE FUNCTION.
RX PubMed=8798585; DOI=10.1074/jbc.271.39.23653;
RA Pastuszak I., O'Donnell J., Elbein A.D.;
RT "Identification of the GalNAc kinase amino acid sequence.";
RL J. Biol. Chem. 271:23653-23656(1996).
RN [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH GALNAC AND ATP,
RP SUBUNIT, FUNCTION, AND SUBSTRATE-BINDING SITES.
RX PubMed=16006554; DOI=10.1074/jbc.m505730200;
RA Thoden J.B., Holden H.M.;
RT "The molecular architecture of human N-acetylgalactosamine kinase.";
RL J. Biol. Chem. 280:32784-32791(2005).
CC -!- FUNCTION: Acts on GalNAc. Also acts as a galactokinase when galactose
CC is present at high concentrations. May be involved in a salvage pathway
CC for the reutilization of free GalNAc derived from the degradation of
CC complex carbohydrates. {ECO:0000269|PubMed:16006554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-alpha-D-galactosamine = ADP + H(+) + N-acetyl-
CC alpha-D-galactosamine 1-phosphate; Xref=Rhea:RHEA:12617,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:40356,
CC ChEBI:CHEBI:61970, ChEBI:CHEBI:456216; EC=2.7.1.157;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16006554}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q01415-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01415-2; Sequence=VSP_042897;
CC -!- SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.
CC {ECO:0000305}.
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DR EMBL; M84443; AAA58612.1; -; mRNA.
DR EMBL; AF461816; AAP97708.1; -; mRNA.
DR EMBL; BT006901; AAP35547.1; -; mRNA.
DR EMBL; AC013452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC036102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005141; AAH05141.1; -; mRNA.
DR CCDS; CCDS32236.1; -. [Q01415-2]
DR CCDS; CCDS42034.1; -. [Q01415-1]
DR PIR; A46366; A46366.
DR RefSeq; NP_001001556.1; NM_001001556.2. [Q01415-2]
DR RefSeq; NP_002035.1; NM_002044.3. [Q01415-1]
DR PDB; 2A2C; X-ray; 1.65 A; A=1-458.
DR PDB; 2A2D; X-ray; 2.20 A; A=1-458.
DR PDBsum; 2A2C; -.
DR PDBsum; 2A2D; -.
DR AlphaFoldDB; Q01415; -.
DR SMR; Q01415; -.
DR BioGRID; 108858; 18.
DR IntAct; Q01415; 8.
DR STRING; 9606.ENSP00000453129; -.
DR GlyGen; Q01415; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q01415; -.
DR PhosphoSitePlus; Q01415; -.
DR BioMuta; GALK2; -.
DR DMDM; 399518; -.
DR EPD; Q01415; -.
DR jPOST; Q01415; -.
DR MassIVE; Q01415; -.
DR MaxQB; Q01415; -.
DR PaxDb; Q01415; -.
DR PeptideAtlas; Q01415; -.
DR PRIDE; Q01415; -.
DR ProteomicsDB; 57943; -. [Q01415-1]
DR ProteomicsDB; 57944; -. [Q01415-2]
DR Antibodypedia; 24645; 268 antibodies from 26 providers.
DR DNASU; 2585; -.
DR Ensembl; ENST00000327171.7; ENSP00000316632.3; ENSG00000156958.15. [Q01415-2]
DR Ensembl; ENST00000560031.6; ENSP00000453129.1; ENSG00000156958.15. [Q01415-1]
DR GeneID; 2585; -.
DR KEGG; hsa:2585; -.
DR MANE-Select; ENST00000560031.6; ENSP00000453129.1; NM_002044.4; NP_002035.1.
DR UCSC; uc001zxi.3; human. [Q01415-1]
DR CTD; 2585; -.
DR DisGeNET; 2585; -.
DR GeneCards; GALK2; -.
DR HGNC; HGNC:4119; GALK2.
DR HPA; ENSG00000156958; Low tissue specificity.
DR MIM; 137028; gene.
DR neXtProt; NX_Q01415; -.
DR OpenTargets; ENSG00000156958; -.
DR PharmGKB; PA28534; -.
DR VEuPathDB; HostDB:ENSG00000156958; -.
DR eggNOG; KOG0631; Eukaryota.
DR GeneTree; ENSGT00950000183187; -.
DR InParanoid; Q01415; -.
DR OMA; PVCYNLR; -.
DR OrthoDB; 860024at2759; -.
DR PhylomeDB; Q01415; -.
DR TreeFam; TF324235; -.
DR BRENDA; 2.7.1.157; 2681.
DR PathwayCommons; Q01415; -.
DR SignaLink; Q01415; -.
DR BioGRID-ORCS; 2585; 17 hits in 1079 CRISPR screens.
DR ChiTaRS; GALK2; human.
DR EvolutionaryTrace; Q01415; -.
DR GenomeRNAi; 2585; -.
DR Pharos; Q01415; Tbio.
DR PRO; PR:Q01415; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q01415; protein.
DR Bgee; ENSG00000156958; Expressed in calcaneal tendon and 190 other tissues.
DR ExpressionAtlas; Q01415; baseline and differential.
DR Genevisible; Q01415; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004335; F:galactokinase activity; IDA:UniProtKB.
DR GO; GO:0033858; F:N-acetylgalactosamine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0006012; P:galactose metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 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 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; Alternative splicing; ATP-binding; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..458
FT /note="N-acetylgalactosamine kinase"
FT /id="PRO_0000184647"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 49..52
FT /ligand="substrate"
FT BINDING 139..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16006554"
FT BINDING 187..190
FT /ligand="substrate"
FT SITE 43
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..17
FT /note="MATESPATRRVQVAEHP -> MPVLYD (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_042897"
FT VARIANT 182
FT /note="I -> V (in dbSNP:rs35507772)"
FT /id="VAR_049123"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 35..47
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 58..73
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2A2D"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:2A2C"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 239..257
FT /evidence="ECO:0007829|PDB:2A2C"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 328..351
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 356..373
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 380..391
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 404..413
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:2A2C"
FT HELIX 417..429
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:2A2C"
FT STRAND 453..457
FT /evidence="ECO:0007829|PDB:2A2C"
SQ SEQUENCE 458 AA; 50378 MW; 192B774938F32947 CRC64;
MATESPATRR VQVAEHPRLL KLKEMFNSKF GSIPKFYVRA PGRVNIIGEH IDYCGYSVLP
MAVEQDVLIA VEPVKTYALQ LANTNPLYPD FSTSANNIQI DKTKPLWHNY FLCGLKGIQE
HFGLSNLTGM NCLVDGNIPP SSGLSSSSAL VCCAGLVTLT VLGRNLSKVE LAEICAKSER
YIGTEGGGMD QSISFLAEEG TAKLIEFSPL RATDVKLPSG AVFVIANSCV EMNKAATSHF
NIRVMECRLA AKLLAKYKSL QWDKVLRLEE VQAKLGISLE EMLLVTEDAL HPEPYNPEEI
CRCLGISLEE LRTQILSPNT QDVLIFKLYQ RAKHVYSEAA RVLQFKKICE EAPENMVQLL
GELMNQSHMS CRDMYECSCP ELDQLVDICR KFGAQGSRLT GAGWGGCTVS MVPADKLPSF
LANVHKAYYQ RSDGSLAPEK QSLFATKPGG GALVLLEA
