ID KCY_HUMAN Reviewed; 196 AA. AC P30085; B2R6S5; B4DPU7; E9PGI8; Q53GB7; Q5SVZ0; Q96C07; Q9UBQ8; Q9UIA2; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 3. DT 27-MAR-2024, entry version 224. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CATALYTIC ACTIVITY, SUBCELLULAR RP LOCATION, AND FUNCTION. RX PubMed=10462544; DOI=10.1124/mol.56.3.562; RA Van Rompay A.R., Johansson M., Karlsson A.; RT "Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: RT molecular characterization of the human enzyme."; RL Mol. Pharmacol. 56:562-569(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CHROMOSOMAL RP 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 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 D- and RT 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 UMP-CMP RT 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., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT 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] (ISOFORMS 2 AND 3). 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 [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., 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] 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 [13] 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 [14] 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA 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 [16] 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 [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-73, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [20] 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 de CC novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP CC as phosphate acceptors. Also displays broad nucleoside diphosphate CC 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: CC Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03172}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, CC ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03172}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03172}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03172}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'- CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={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 -!- INTERACTION: CC P30085-3; P07384: CAPN1; NbExp=3; IntAct=EBI-23373346, EBI-1542113; CC P30085-3; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-23373346, EBI-7062247; CC P30085-3; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-23373346, EBI-744081; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03172, CC ECO:0000269|PubMed:10462544, ECO:0000269|PubMed:11912132}. Cytoplasm CC {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:10462544, CC ECO:0000269|PubMed:11912132}. Note=Predominantly cytoplasmic, less than CC 15% nuclear. {ECO:0000269|PubMed:11912132}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=3; CC Name=1; CC IsoId=P30085-1; Sequence=Displayed; CC Name=2; CC IsoId=P30085-2; Sequence=VSP_046683; CC Name=3; CC IsoId=P30085-3; Sequence=VSP_060085; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:11681623}. CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two CC small peripheral domains, NMPbind and LID, which undergo movements CC during catalysis. The LID domain closes over the site of phosphoryl CC transfer upon ATP binding. Assembling and dissambling the active center CC during each catalytic cycle provides an effective means to prevent ATP CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_03172, CC ECO:0000305|PubMed:15163660}. CC -!- MISCELLANEOUS: [Isoform 3]: May be produced from an in-frame upstream CC initiation codon. However, experimental evidence indicates that use of CC the downstream initiation codon is more likely (isoform 1 sequence). CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03172}. CC -!- SEQUENCE CAUTION: CC Sequence=BAG60709.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; -; 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; -; mRNA. DR EMBL; AK298502; BAG60709.1; ALT_INIT; mRNA. DR EMBL; AK312693; BAG35572.1; -; mRNA. DR EMBL; AL513322; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL607122; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX06869.1; -; Genomic_DNA. DR EMBL; CH471059; EAX06871.1; -; Genomic_DNA. DR EMBL; BC014961; AAH14961.1; -; mRNA. DR CCDS; CCDS549.1; -. [P30085-3] DR CCDS; CCDS90947.1; -. [P30085-1] DR PIR; B45482; B45482. DR RefSeq; NP_001129612.1; NM_001136140.1. DR RefSeq; NP_057392.1; NM_016308.2. [P30085-3] DR PDB; 1TEV; X-ray; 2.10 A; A=1-196. DR PDB; 7E9V; X-ray; 2.10 A; A=1-196. DR PDBsum; 1TEV; -. DR PDBsum; 7E9V; -. DR AlphaFoldDB; P30085; -. DR SMR; P30085; -. DR BioGRID; 119700; 107. DR IntAct; P30085; 15. DR MINT; P30085; -. DR STRING; 9606.ENSP00000360939; -. DR BindingDB; P30085; -. DR ChEMBL; CHEMBL5681; -. DR DrugBank; DB03403; Cytidine-5'-Monophosphate. DR DrugBank; DB01262; Decitabine. DR DrugBank; DB00441; Gemcitabine. DR DrugBank; DB00709; Lamivudine. DR DrugBank; DB08934; Sofosbuvir. DR DrugBank; DB04444; Tetrafluoroaluminate Ion. DR DrugBank; DB03435; Uridine-5'-Diphosphate. DR DrugCentral; P30085; -. DR GlyGen; P30085; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P30085; -. DR MetOSite; P30085; -. DR PhosphoSitePlus; P30085; -. DR SwissPalm; P30085; -. DR BioMuta; CMPK1; -. DR DMDM; 12644008; -. DR OGP; P30085; -. DR EPD; P30085; -. DR jPOST; P30085; -. DR MassIVE; P30085; -. DR MaxQB; P30085; -. DR PaxDb; 9606-ENSP00000360939; -. DR PeptideAtlas; P30085; -. DR ProteomicsDB; 20330; -. DR ProteomicsDB; 54633; -. [P30085-1] DR Pumba; P30085; -. DR TopDownProteomics; P30085-1; -. [P30085-1] DR Antibodypedia; 32884; 562 antibodies from 33 providers. DR DNASU; 51727; -. DR Ensembl; ENST00000371873.10; ENSP00000360939.5; ENSG00000162368.15. [P30085-3] DR Ensembl; ENST00000699075.1; ENSP00000514114.1; ENSG00000162368.15. [P30085-1] DR GeneID; 51727; -. DR KEGG; hsa:51727; -. DR MANE-Select; ENST00000371873.10; ENSP00000360939.5; NM_016308.3; NP_057392.1. [P30085-3] DR UCSC; uc001cri.3; human. [P30085-1] DR AGR; HGNC:18170; -. DR CTD; 51727; -. DR DisGeNET; 51727; -. DR GeneCards; CMPK1; -. DR HGNC; HGNC:18170; CMPK1. DR HPA; ENSG00000162368; Low tissue specificity. DR MIM; 191710; gene. DR neXtProt; NX_P30085; -. DR OpenTargets; ENSG00000162368; -. DR PharmGKB; PA162382539; -. DR VEuPathDB; HostDB:ENSG00000162368; -. DR eggNOG; KOG3079; Eukaryota. DR GeneTree; ENSGT00940000160589; -. DR HOGENOM; CLU_032354_0_2_1; -. DR InParanoid; P30085; -. DR OMA; DVCVQRC; -. DR OrthoDB; 1330004at2759; -. DR PhylomeDB; P30085; -. DR TreeFam; TF354283; -. DR BioCyc; MetaCyc:HS08663-MONOMER; -. DR BRENDA; 2.7.4.14; 2681. DR PathwayCommons; P30085; -. DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates. DR SABIO-RK; P30085; -. DR SignaLink; P30085; -. DR BioGRID-ORCS; 51727; 675 hits in 1148 CRISPR screens. DR ChiTaRS; CMPK1; human. DR EvolutionaryTrace; P30085; -. DR GeneWiki; CMPK; -. DR GenomeRNAi; 51727; -. DR Pharos; P30085; Tchem. DR PRO; PR:P30085; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P30085; Protein. DR Bgee; ENSG00000162368; Expressed in jejunal mucosa and 207 other cell types or tissues. DR ExpressionAtlas; P30085; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0036430; F:CMP kinase activity; IEA:RHEA. DR GO; GO:0004127; F:cytidylate kinase activity; IBA:GO_Central. DR GO; GO:0036431; F:dCMP kinase activity; IEA:RHEA. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB. DR GO; GO:0050145; F:nucleoside monophosphate kinase activity; EXP:Reactome. DR GO; GO:0033862; F:UMP kinase activity; IDA:MGI. DR GO; GO:0004849; F:uridine kinase activity; TAS:ProtInc. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0046705; P:CDP biosynthetic process; IBA:GO_Central. DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0009220; P:pyrimidine ribonucleotide biosynthetic process; TAS:ProtInc. DR GO; GO:0006225; P:UDP biosynthetic process; IDA:MGI. DR CDD; cd01428; ADK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR033690; Adenylat_kinase_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006266; UMP_CMP_kinase. DR NCBIfam; TIGR01359; UMP_CMP_kin_fam; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1. DR Pfam; PF00406; ADK; 1. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00113; ADENYLATE_KINASE; 1. DR SWISS-2DPAGE; P30085; -. DR Genevisible; P30085; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing; KW ATP-binding; Cytoplasm; Direct protein sequencing; Isopeptide bond; Kinase; KW Nucleotide-binding; Nucleus; Phosphoprotein; Pyrimidine biosynthesis; KW Reference proteome; Transferase; Ubl conjugation. FT CHAIN 1..196 FT /note="UMP-CMP kinase" FT /id="PRO_0000158949" FT REGION 33..63 FT /note="NMP" FT /evidence="ECO:0000269|PubMed:15163660" FT REGION 133..143 FT /note="LID" FT /evidence="ECO:0000269|PubMed:15163660" FT BINDING 13..18 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 39 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 61..63 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 93..96 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 100 FT /ligand="CMP" FT /ligand_id="ChEBI:CHEBI:60377" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 134 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 140 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 151 FT /ligand="a ribonucleoside 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:58043" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT BINDING 179 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03172" FT MOD_RES 33 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 43 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9DBP5" FT MOD_RES 55 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 106 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9DBP5" FT MOD_RES 180 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q4KM73" FT CROSSLNK 73 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1 FT /note="M -> MLSRCRSGLLHVLGLSFLLQTRRPILLCSPRLM (in isoform FT 3)" FT /id="VSP_060085" FT VAR_SEQ 26..74 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046683" FT CONFLICT 27 FT /note="Y -> I (in Ref. 12; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:1TEV" FT HELIX 16..27 FT /evidence="ECO:0007829|PDB:1TEV" FT STRAND 30..33 FT /evidence="ECO:0007829|PDB:1TEV" FT HELIX 34..43 FT /evidence="ECO:0007829|PDB:1TEV" FT HELIX 50..58 FT /evidence="ECO:0007829|PDB:1TEV" FT HELIX 65..82 FT /evidence="ECO:0007829|PDB:1TEV" FT STRAND 88..93 FT /evidence="ECO:0007829|PDB:1TEV" FT HELIX 98..108 FT /evidence="ECO:0007829|PDB:1TEV" FT TURN 109..111 FT /evidence="ECO:0007829|PDB:1TEV" FT STRAND 113..121 FT /evidence="ECO:0007829|PDB:1TEV" FT HELIX 124..136 FT /evidence="ECO:0007829|PDB:1TEV" FT HELIX 145..168 FT /evidence="ECO:0007829|PDB:1TEV" FT STRAND 172..176 FT /evidence="ECO:0007829|PDB:1TEV" FT HELIX 181..194 FT /evidence="ECO:0007829|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 //