ID KCY_HUMAN Reviewed; 196 AA. AC P30085; B4DPU7; E9PGI8; Q53GB7; Q5SVZ0; Q96C07; Q9UBQ8; Q9UIA2; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 3. DT 09-DEC-2015, entry version 166. DE RecName: Full=UMP-CMP kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE EC=2.7.4.14 {ECO:0000255|HAMAP-Rule:MF_03172}; DE AltName: Full=Deoxycytidylate kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=CK {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=dCMP kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE AltName: Full=Nucleoside-diphosphate kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE EC=2.7.4.6 {ECO:0000255|HAMAP-Rule:MF_03172}; DE AltName: Full=Uridine monophosphate/cytidine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=UMP/CMP kinase {ECO:0000255|HAMAP-Rule:MF_03172}; DE Short=UMP/CMPK {ECO:0000255|HAMAP-Rule:MF_03172}; GN Name=CMPK1 {ECO:0000255|HAMAP-Rule:MF_03172}; GN Synonyms=CMK, CMPK {ECO:0000255|HAMAP-Rule:MF_03172}, UCK, UMK, UMPK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=10462544; RA Van Rompay A.R., Johansson M., Karlsson A.; RT "Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP RT kinase: molecular characterization of the human enzyme."; RL Mol. Pharmacol. 56:562-569(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, RP CHROMOSOMAL LOCATION, AND IDENTIFICATION OF START CODON. RC TISSUE=Macrophage; RX PubMed=11681623; DOI=10.1016/S0024-3205(01)01322-4; RA Pearman A.T., Castro-Faria-Neto H.C., McIntyre T.M., Prescott S.M., RA Stafforini D.M.; RT "Characterization of human UMP-CMP kinase enzymatic activity and 5' RT untranslated region."; RL Life Sci. 69:2361-2370(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=11912132; RA Liou J.-Y., Dutschman G.E., Lam W., Jiang Z., Cheng Y.-C.; RT "Characterization of human UMP/CMP kinase and its phosphorylation of RT D- and L-form deoxycytidine analogue monophosphates."; RL Cancer Res. 62:1624-1631(2002). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Pituitary; RA Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., RA Luo M., Chen J., Hu R.; RT "Human UMP-CMP kinase gene."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Fan Y.X., Yu L., Dai F.Y., Zhou Y., Huang J., Zhao S.Y.; RT "Cloning and characterization of a new human cDNA homologous to pig RT UMP-CMP kinase mRNA."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hypothalamus; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal RT axis and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Small intestine; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [9] 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP PROTEIN SEQUENCE OF 1-29. RC TISSUE=Liver; RX PubMed=8313870; DOI=10.1002/elps.11501401181; RA Hughes G.J., Frutiger S., Paquet N., Pasquali C., Sanchez J.-C., RA Tissot J.-D., Bairoch A., Appel R.D., Hochstrasser D.F.; RT "Human liver protein map: update 1993."; RL Electrophoresis 14:1216-1222(1993). RN [12] RP PROTEIN SEQUENCE OF 1-10. RC TISSUE=Liver; RX PubMed=1286669; DOI=10.1002/elps.11501301201; RA Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., RA Appel R.D., Hughes G.J.; RT "Human liver protein map: a reference database established by RT microsequencing and gel comparison."; RL Electrophoresis 13:992-1001(1992). RN [13] RP PROTEIN SEQUENCE OF 1-16; 62-73; 89-106; 152-171 AND 180-196, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Colon carcinoma; RA Bienvenut W.V., Bilsland A.E., Keith W.N.; RL Submitted (JAN-2010) to UniProtKB. RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [15] 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., RA Buerckstuemmer T., 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 [16] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23416111; DOI=10.1016/j.biocel.2013.02.004; RA Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.; RT "The human adenylate kinase 9 is a nucleoside mono- and diphosphate RT kinase."; RL Int. J. Biochem. Cell Biol. 45:925-931(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION RP BY 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=15163660; DOI=10.1074/jbc.M401989200; RA Segura-Pena D., Sekulic N., Ort S., Konrad M., Lavie A.; RT "Substrate-induced conformational changes in human UMP/CMP kinase."; RL J. Biol. Chem. 279:33882-33889(2004). CC -!- FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside CC monophosphates at the expense of ATP. Plays an important role in CC de novo pyrimidine nucleotide biosynthesis. Has preference for UMP CC and CMP as phosphate acceptors. Also displays broad nucleoside CC diphosphate kinase activity. {ECO:0000255|HAMAP-Rule:MF_03172, CC ECO:0000269|PubMed:10462544, ECO:0000269|PubMed:11912132, CC ECO:0000269|PubMed:23416111}. CC -!- CATALYTIC ACTIVITY: ATP + (d)CMP = ADP + (d)CDP. CC {ECO:0000255|HAMAP-Rule:MF_03172}. CC -!- CATALYTIC ACTIVITY: ATP + UMP = ADP + UDP. {ECO:0000255|HAMAP- CC Rule:MF_03172}. CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP + CC nucleoside triphosphate. {ECO:0000255|HAMAP-Rule:MF_03172}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per monomer.; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03172}. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly CC nuclear. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P30085-1; Sequence=Displayed; CC Name=2; CC IsoId=P30085-2; Sequence=VSP_046683; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:11681623}. CC -!- DOMAIN: Consists of three domains, a large central CORE domain and CC two small peripheral domains, NMPbind and LID, which undergo CC movements during catalysis. The LID domain closes over the site of CC phosphoryl transfer upon ATP binding. Assembling and dissambling CC the active center during each catalytic cycle provides an CC effective means to prevent ATP hydrolysis. CC -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03172}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF17709.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=AAH14961.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=BAD96734.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=BAG60709.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=CAI13471.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAI14972.1; Type=Erroneous gene model prediction; 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; AF070416; AAF17709.1; ALT_INIT; mRNA. DR EMBL; AF259961; AAG22609.1; -; mRNA. DR EMBL; AF110643; AAD48583.1; -; mRNA. DR EMBL; AF087865; AAP97174.1; -; mRNA. DR EMBL; AF112216; AAF17204.1; -; mRNA. DR EMBL; AK223014; BAD96734.1; ALT_INIT; mRNA. DR EMBL; AK298502; BAG60709.1; ALT_INIT; mRNA. DR EMBL; AL513322; CAI13471.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL607122; CAI13471.1; JOINED; Genomic_DNA. DR EMBL; AL607122; CAI14972.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL513322; CAI14972.1; JOINED; Genomic_DNA. DR EMBL; BC014961; AAH14961.1; ALT_INIT; mRNA. DR PIR; B45482; B45482. DR RefSeq; NP_001129612.1; NM_001136140.1. DR RefSeq; NP_057392.1; NM_016308.2. DR UniGene; Hs.731647; -. DR UniGene; Hs.745001; -. DR PDB; 1TEV; X-ray; 2.10 A; A=1-196. DR PDBsum; 1TEV; -. DR ProteinModelPortal; P30085; -. DR SMR; P30085; 3-196. DR BioGrid; 119700; 10. DR IntAct; P30085; 1. DR MINT; MINT-5000978; -. DR STRING; 9606.ENSP00000360939; -. DR ChEMBL; CHEMBL5681; -. DR DrugBank; DB00441; Gemcitabine. DR DrugBank; DB00709; Lamivudine. DR PhosphoSite; P30085; -. DR DMDM; 12644008; -. DR OGP; P30085; -. DR SWISS-2DPAGE; P30085; -. DR MaxQB; P30085; -. DR PaxDb; P30085; -. DR PRIDE; P30085; -. DR DNASU; 51727; -. DR Ensembl; ENST00000371873; ENSP00000360939; ENSG00000162368. DR Ensembl; ENST00000450808; ENSP00000398192; ENSG00000162368. DR GeneID; 51727; -. DR KEGG; hsa:51727; -. DR CTD; 51727; -. DR GeneCards; CMPK1; -. DR HGNC; HGNC:18170; CMPK1. DR HPA; HPA053730; -. DR HPA; HPA058604; -. DR MIM; 191710; gene. DR neXtProt; NX_P30085; -. DR PharmGKB; PA162382539; -. DR eggNOG; KOG3079; Eukaryota. DR eggNOG; COG0563; LUCA. DR HOGENOM; HOG000238771; -. DR HOVERGEN; HBG108060; -. DR InParanoid; P30085; -. DR KO; K13800; -. DR OrthoDB; EOG7X0VJ0; -. DR PhylomeDB; P30085; -. DR TreeFam; TF354283; -. DR BioCyc; MetaCyc:HS08663-MONOMER; -. DR BRENDA; 2.7.4.14; 2681. DR Reactome; R-HSA-499943; Synthesis and interconversion of nucleotide di- and triphosphates. DR SABIO-RK; P30085; -. DR ChiTaRS; CMPK1; human. DR EvolutionaryTrace; P30085; -. DR GeneWiki; CMPK; -. DR GenomeRNAi; 51727; -. DR NextBio; 35473968; -. DR PRO; PR:P30085; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; P30085; -. DR CleanEx; HS_CMPK1; -. DR ExpressionAtlas; P30085; baseline and differential. DR Genevisible; P30085; HS. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB. DR GO; GO:0004849; F:uridine kinase activity; TAS:ProtInc. DR GO; GO:0009041; F:uridylate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome. DR GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; TAS:Reactome. DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IDA:UniProtKB. DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IDA:UniProtKB. DR GO; GO:0009220; P:pyrimidine ribonucleotide biosynthetic process; TAS:ProtInc. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006222; P:UMP biosynthetic process; TAS:GOC. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR HAMAP; MF_03172; Adenylate_kinase_UMP_CMP_kin; 1. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006266; UMP_CMP_kinase. DR PANTHER; PTHR23359; PTHR23359; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01359; UMP_CMP_kin_fam; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; KW Nucleotide-binding; Nucleus; Phosphoprotein; Pyrimidine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 196 UMP-CMP kinase. FT /FTId=PRO_0000158949. FT NP_BIND 13 18 ATP. {ECO:0000255|HAMAP-Rule:MF_03172}. FT NP_BIND 61 63 NMP. {ECO:0000255|HAMAP-Rule:MF_03172}. FT NP_BIND 93 96 NMP. {ECO:0000255|HAMAP-Rule:MF_03172}. FT REGION 33 63 NMPbind. FT REGION 133 143 LID. FT BINDING 39 39 NMP. {ECO:0000255|HAMAP-Rule:MF_03172}. FT BINDING 100 100 CMP. {ECO:0000255|HAMAP-Rule:MF_03172}. FT BINDING 134 134 ATP. {ECO:0000255|HAMAP-Rule:MF_03172}. FT BINDING 140 140 NMP. {ECO:0000255|HAMAP-Rule:MF_03172}. FT BINDING 151 151 NMP. {ECO:0000255|HAMAP-Rule:MF_03172}. FT BINDING 179 179 ATP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_03172}. FT MOD_RES 33 33 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 43 43 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9DBP5}. FT MOD_RES 55 55 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 106 106 N6-succinyllysine. FT {ECO:0000250|UniProtKB:Q9DBP5}. FT MOD_RES 180 180 Phosphoserine. FT {ECO:0000250|UniProtKB:Q4KM73}. FT VAR_SEQ 26 74 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_046683. FT CONFLICT 27 27 Y -> I (in Ref. 11; AA sequence). FT {ECO:0000305}. FT STRAND 4 9 {ECO:0000244|PDB:1TEV}. FT HELIX 16 27 {ECO:0000244|PDB:1TEV}. FT STRAND 30 33 {ECO:0000244|PDB:1TEV}. FT HELIX 34 43 {ECO:0000244|PDB:1TEV}. FT HELIX 50 58 {ECO:0000244|PDB:1TEV}. FT HELIX 65 82 {ECO:0000244|PDB:1TEV}. FT STRAND 88 93 {ECO:0000244|PDB:1TEV}. FT HELIX 98 108 {ECO:0000244|PDB:1TEV}. FT TURN 109 111 {ECO:0000244|PDB:1TEV}. FT STRAND 113 121 {ECO:0000244|PDB:1TEV}. FT HELIX 124 136 {ECO:0000244|PDB:1TEV}. FT HELIX 145 168 {ECO:0000244|PDB:1TEV}. FT STRAND 172 176 {ECO:0000244|PDB:1TEV}. FT HELIX 181 194 {ECO:0000244|PDB:1TEV}. SQ SEQUENCE 196 AA; 22222 MW; 6837B1E6D7543768 CRC64; MKPLVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG ELIEKYIKEG KIVPVEITIS LLKREMDQTM AANAQKNKFL IDGFPRNQDN LQGWNKTMDG KADVSFVLFF DCNNEICIER CLERGKSSGR SDDNRESLEK RIQTYLQSTK PIIDLYEEMG KVKKIDASKS VDEVFDEVVQ IFDKEG //