ID   UCK2_HUMAN              Reviewed;         261 AA.
AC   Q9BZX2; Q5VV91; Q7KZV3; Q92528; Q96KG5; Q9BU42;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Uridine-cytidine kinase 2;
DE            Short=UCK 2;
DE            EC=2.7.1.48 {ECO:0000269|PubMed:11306702, ECO:0000269|PubMed:11494055};
DE   AltName: Full=Cytidine monophosphokinase 2;
DE   AltName: Full=Testis-specific protein TSA903;
DE   AltName: Full=Uridine monophosphokinase 2;
GN   Name=UCK2; Synonyms=UMPK;
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 2), AND TISSUE SPECIFICITY.
RX   PubMed=8812458; DOI=10.1006/geno.1996.0467;
RA   Ozaki K., Kuroki T., Hayashi S., Nakamura Y.;
RT   "Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a
RT   differential mRNA display method.";
RL   Genomics 36:316-319(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RX   PubMed=11306702; DOI=10.1124/mol.59.5.1181;
RA   Van Rompay A.R., Norda A., Linden K., Johansson M., Karlsson A.;
RT   "Phosphorylation of uridine and cytidine nucleoside analogs by two human
RT   uridine-cytidine kinases.";
RL   Mol. Pharmacol. 59:1181-1186(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 MRNA] (ISOFORM 2).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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 15-261 (ISOFORM 1), FUNCTION, CATALYTIC
RP   ACTIVITY, AND PATHWAY.
RC   TISSUE=Fibrosarcoma;
RX   PubMed=11494055;
RA   Koizumi K., Shimamoto Y., Azuma A., Wataya Y., Matsuda A., Sasaki T.,
RA   Fukushima M.;
RT   "Cloning and expression of uridine/cytidine kinase cDNA from human
RT   fibrosarcoma cells.";
RL   Int. J. Mol. Med. 8:273-278(2001).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
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-254, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-250 IN COMPLEXES WITH ADP;
RP   CYTIDINE; CMP; CTP AND UTP, AND SUBUNIT.
RX   PubMed=15130468; DOI=10.1016/j.str.2004.02.038;
RA   Suzuki N.N., Koizumi K., Fukushima M., Matsuda A., Inagaki F.;
RT   "Structural basis for the specificity, catalysis, and regulation of human
RT   uridine-cytidine kinase.";
RL   Structure 12:751-764(2004).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADP AND CMP, AND
RP   SUBUNIT.
RX   PubMed=15735337; DOI=10.1107/s0907444904032937;
RA   Appleby T.C., Larson G., Cheney I.W., Walker H., Wu J.Z., Zhong W.,
RA   Hong Z., Yao N.;
RT   "Structure of human uridine-cytidine kinase 2 determined by SIRAS using a
RT   rotating-anode X-ray generator and a single samarium derivative.";
RL   Acta Crystallogr. D 61:278-284(2005).
CC   -!- FUNCTION: Phosphorylates uridine and cytidine to uridine monophosphate
CC       and cytidine monophosphate (PubMed:11306702, PubMed:11494055). Does not
CC       phosphorylate deoxyribonucleosides or purine ribonucleosides
CC       (PubMed:11306702). Can use ATP or GTP as a phosphate donor
CC       (PubMed:11306702). Can also phosphorylate cytidine and uridine
CC       nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-
CC       thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine,
CC       5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-
CC       anisoylcytidine (PubMed:11306702). {ECO:0000269|PubMed:11306702,
CC       ECO:0000269|PubMed:11494055}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC         Evidence={ECO:0000269|PubMed:11306702, ECO:0000269|PubMed:11494055};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC         Evidence={ECO:0000269|PubMed:11306702, ECO:0000269|PubMed:11494055};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC       CTP from cytidine: step 1/3. {ECO:0000269|PubMed:11306702,
CC       ECO:0000269|PubMed:11494055}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       UMP from uridine: step 1/1. {ECO:0000269|PubMed:11306702,
CC       ECO:0000269|PubMed:11494055}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15130468,
CC       ECO:0000269|PubMed:15735337}.
CC   -!- INTERACTION:
CC       Q9BZX2; Q9BZX2: UCK2; NbExp=3; IntAct=EBI-1053938, EBI-1053938;
CC       Q9BZX2-1; Q9BZX2-1: UCK2; NbExp=2; IntAct=EBI-21013535, EBI-21013535;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BZX2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BZX2-2; Sequence=VSP_014262;
CC   -!- TISSUE SPECIFICITY: According to PubMed:8812458; testis-specific.
CC       According to PubMed:11306702, placenta-specific.
CC       {ECO:0000269|PubMed:8812458}.
CC   -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR   EMBL; D78335; BAA11349.1; -; mRNA.
DR   EMBL; AF236637; AAK14053.1; -; mRNA.
DR   EMBL; BT006860; AAP35506.1; -; mRNA.
DR   EMBL; CR456857; CAG33138.1; -; mRNA.
DR   EMBL; AL451074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL358115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002906; AAH02906.2; -; mRNA.
DR   EMBL; AB062451; BAB56162.1; -; mRNA.
DR   CCDS; CCDS1252.1; -. [Q9BZX2-1]
DR   RefSeq; NP_036606.2; NM_012474.4. [Q9BZX2-1]
DR   PDB; 1UDW; X-ray; 2.60 A; A/B=1-250.
DR   PDB; 1UEI; X-ray; 2.60 A; A/B=1-250.
DR   PDB; 1UEJ; X-ray; 2.61 A; A/B=1-250.
DR   PDB; 1UFQ; X-ray; 2.50 A; A/B/C/D=1-250.
DR   PDB; 1UJ2; X-ray; 1.80 A; A/B=1-250.
DR   PDB; 1XRJ; X-ray; 2.00 A; A/B=1-261.
DR   PDB; 6N53; X-ray; 2.70 A; A/B=1-250.
DR   PDB; 6N54; X-ray; 2.42 A; A/B=1-250.
DR   PDB; 6N55; X-ray; 3.08 A; A/B/C/D/E/F/G/H=1-250.
DR   PDB; 6PWZ; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-250.
DR   PDB; 7SQL; X-ray; 2.40 A; A/B/C/D=1-250.
DR   PDBsum; 1UDW; -.
DR   PDBsum; 1UEI; -.
DR   PDBsum; 1UEJ; -.
DR   PDBsum; 1UFQ; -.
DR   PDBsum; 1UJ2; -.
DR   PDBsum; 1XRJ; -.
DR   PDBsum; 6N53; -.
DR   PDBsum; 6N54; -.
DR   PDBsum; 6N55; -.
DR   PDBsum; 6PWZ; -.
DR   PDBsum; 7SQL; -.
DR   AlphaFoldDB; Q9BZX2; -.
DR   SMR; Q9BZX2; -.
DR   BioGRID; 113217; 75.
DR   IntAct; Q9BZX2; 11.
DR   STRING; 9606.ENSP00000356853; -.
DR   BindingDB; Q9BZX2; -.
DR   ChEMBL; CHEMBL2469; -.
DR   DrugBank; DB02097; Cytidine.
DR   DrugBank; DB03403; Cytidine-5'-Monophosphate.
DR   DrugBank; DB02431; Cytidine-5'-Triphosphate.
DR   DrugBank; DB04005; Uridine 5'-triphosphate.
DR   DrugCentral; Q9BZX2; -.
DR   GlyCosmos; Q9BZX2; 1 site, 1 glycan.
DR   GlyGen; Q9BZX2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BZX2; -.
DR   PhosphoSitePlus; Q9BZX2; -.
DR   BioMuta; UCK2; -.
DR   DMDM; 20455356; -.
DR   EPD; Q9BZX2; -.
DR   jPOST; Q9BZX2; -.
DR   MassIVE; Q9BZX2; -.
DR   MaxQB; Q9BZX2; -.
DR   PaxDb; 9606-ENSP00000356853; -.
DR   PeptideAtlas; Q9BZX2; -.
DR   ProteomicsDB; 79917; -. [Q9BZX2-1]
DR   ProteomicsDB; 79918; -. [Q9BZX2-2]
DR   Pumba; Q9BZX2; -.
DR   Antibodypedia; 34333; 223 antibodies from 27 providers.
DR   DNASU; 7371; -.
DR   Ensembl; ENST00000367879.9; ENSP00000356853.4; ENSG00000143179.16. [Q9BZX2-1]
DR   Ensembl; ENST00000469256.6; ENSP00000476692.1; ENSG00000143179.16. [Q9BZX2-2]
DR   Ensembl; ENST00000470820.1; ENSP00000476327.1; ENSG00000143179.16. [Q9BZX2-2]
DR   GeneID; 7371; -.
DR   KEGG; hsa:7371; -.
DR   MANE-Select; ENST00000367879.9; ENSP00000356853.4; NM_012474.5; NP_036606.2.
DR   UCSC; uc021pec.2; human. [Q9BZX2-1]
DR   AGR; HGNC:12562; -.
DR   CTD; 7371; -.
DR   DisGeNET; 7371; -.
DR   GeneCards; UCK2; -.
DR   HGNC; HGNC:12562; UCK2.
DR   HPA; ENSG00000143179; Low tissue specificity.
DR   MIM; 609329; gene.
DR   neXtProt; NX_Q9BZX2; -.
DR   OpenTargets; ENSG00000143179; -.
DR   PharmGKB; PA362; -.
DR   VEuPathDB; HostDB:ENSG00000143179; -.
DR   eggNOG; KOG4203; Eukaryota.
DR   GeneTree; ENSGT01020000230412; -.
DR   HOGENOM; CLU_021278_1_1_1; -.
DR   InParanoid; Q9BZX2; -.
DR   OMA; TVKPMHE; -.
DR   OrthoDB; 180154at2759; -.
DR   PhylomeDB; Q9BZX2; -.
DR   TreeFam; TF316686; -.
DR   BioCyc; MetaCyc:HS07003-MONOMER; -.
DR   BRENDA; 2.7.1.48; 2681.
DR   PathwayCommons; Q9BZX2; -.
DR   Reactome; R-HSA-73614; Pyrimidine salvage.
DR   SABIO-RK; Q9BZX2; -.
DR   SignaLink; Q9BZX2; -.
DR   UniPathway; UPA00574; UER00637.
DR   UniPathway; UPA00579; UER00640.
DR   BioGRID-ORCS; 7371; 22 hits in 1163 CRISPR screens.
DR   ChiTaRS; UCK2; human.
DR   EvolutionaryTrace; Q9BZX2; -.
DR   GeneWiki; UCK2; -.
DR   GenomeRNAi; 7371; -.
DR   Pharos; Q9BZX2; Tbio.
DR   PRO; PR:Q9BZX2; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9BZX2; Protein.
DR   Bgee; ENSG00000143179; Expressed in mucosa of transverse colon and 157 other cell types or tissues.
DR   ExpressionAtlas; Q9BZX2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043771; F:cytidine kinase activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004849; F:uridine kinase activity; IDA:UniProtKB.
DR   GO; GO:0044211; P:CTP salvage; IDA:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0044206; P:UMP salvage; IDA:UniProtKB.
DR   CDD; cd02023; UMPK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006083; PRK/URK.
DR   InterPro; IPR000764; Uridine_kinase-like.
DR   NCBIfam; TIGR00235; udk; 1.
DR   PANTHER; PTHR10285; URIDINE KINASE; 1.
DR   PANTHER; PTHR10285:SF131; URIDINE-CYTIDINE KINASE 2; 1.
DR   Pfam; PF00485; PRK; 1.
DR   PRINTS; PR00988; URIDINKINASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   Genevisible; Q9BZX2; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..261
FT                   /note="Uridine-cytidine kinase 2"
FT                   /id="PRO_0000164455"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         27..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:15130468,
FT                   ECO:0000269|PubMed:15735337"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15130468,
FT                   ECO:0000269|PubMed:15735337"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15130468,
FT                   ECO:0000269|PubMed:15735337"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15130468,
FT                   ECO:0000269|PubMed:15735337"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15130468,
FT                   ECO:0000269|PubMed:15735337"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15130468,
FT                   ECO:0000269|PubMed:15735337"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15130468,
FT                   ECO:0000269|PubMed:15735337"
FT   BINDING         213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000269|PubMed:15130468,
FT                   ECO:0000269|PubMed:15735337"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   VAR_SEQ         1..150
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8812458, ECO:0000303|Ref.3,
FT                   ECO:0000303|Ref.4"
FT                   /id="VSP_014262"
FT   CONFLICT        202
FT                   /note="K -> Q (in Ref. 1; BAA11349)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="V -> E (in Ref. 1; BAA11349)"
FT                   /evidence="ECO:0000305"
FT   STRAND          21..26
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           33..43
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           51..53
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   STRAND          55..60
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           61..64
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           70..77
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           91..102
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   STRAND          107..113
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   TURN            114..117
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   STRAND          118..126
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   STRAND          130..135
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   TURN            137..140
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           143..148
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   STRAND          150..156
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           159..173
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           178..187
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           189..196
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           198..203
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   STRAND          205..209
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:1UJ2"
FT   HELIX           215..230
FT                   /evidence="ECO:0007829|PDB:1UJ2"
SQ   SEQUENCE   261 AA;  29299 MW;  71791346F091EBFD CRC64;
     MAGDSEQTLQ NHQQPNGGEP FLIGVSGGTA SGKSSVCAKI VQLLGQNEVD YRQKQVVILS
     QDSFYRVLTS EQKAKALKGQ FNFDHPDAFD NELILKTLKE ITEGKTVQIP VYDFVSHSRK
     EETVTVYPAD VVLFEGILAF YSQEVRDLFQ MKLFVDTDAD TRLSRRVLRD ISERGRDLEQ
     ILSQYITFVK PAFEEFCLPT KKYADVIIPR GADNLVAINL IVQHIQDILN GGPSKRQTNG
     CLNGYTPSRK RQASESSSRP H
//