KCY_HUMAN
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 03-AUG-2022, entry version 215.
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};
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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 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; 81.
DR IntAct; P30085; 14.
DR MINT; P30085; -.
DR STRING; 9606.ENSP00000360939; -.
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; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P30085; -.
DR MetOSite; P30085; -.
DR PhosphoSitePlus; P30085; -.
DR SwissPalm; P30085; -.
DR BioMuta; CMPK1; -.
DR DMDM; 12644008; -.
DR OGP; P30085; -.
DR SWISS-2DPAGE; P30085; -.
DR EPD; P30085; -.
DR jPOST; P30085; -.
DR MassIVE; P30085; -.
DR MaxQB; P30085; -.
DR PaxDb; P30085; -.
DR PeptideAtlas; P30085; -.
DR PRIDE; P30085; -.
DR ProteomicsDB; 20330; -.
DR ProteomicsDB; 54633; -. [P30085-1]
DR TopDownProteomics; P30085-1; -. [P30085-1]
DR Antibodypedia; 32884; 501 antibodies from 33 providers.
DR DNASU; 51727; -.
DR Ensembl; ENST00000371873.10; ENSP00000360939.5; ENSG00000162368.14. [P30085-3]
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 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; RFQFTHL; -.
DR OrthoDB; 1378291at2759; -.
DR PhylomeDB; P30085; -.
DR TreeFam; TF354283; -.
DR BioCyc; MetaCyc:HS08663-MON; -.
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; 641 hits in 1059 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 205 other tissues.
DR ExpressionAtlas; P30085; baseline and differential.
DR Genevisible; P30085; HS.
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: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:0006225; P:UDP biosynthetic process; IDA:MGI.
DR CDD; cd01428; ADK; 1.
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; IPR033690; Adenylat_kinase_CS.
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 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
