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KCY_MOUSE
ID   KCY_MOUSE               Reviewed;         196 AA.
AC   Q9DBP5; Q8BK17; Q8VD05; Q9DCS7;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 160.
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; Synonyms=Cmk, Cmpk, Uck, Umk, Umpk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   [4]
RP   PROTEIN SEQUENCE OF 1-16; 27-39; 62-73 AND 89-96, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43, SUCCINYLATION [LARGE SCALE
RP   ANALYSIS] AT LYS-106, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Embryonic fibroblast, and Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
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   -!- 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         Evidence={ECO:0000255|HAMAP-Rule:MF_03172};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_03172};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03172}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}.
CC       Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}. Note=Predominantly
CC       nuclear. {ECO:0000255|HAMAP-Rule:MF_03172}.
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   -!- SIMILARITY: Belongs to the adenylate kinase family. UMP-CMP kinase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03172}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH17684.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB22163.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC36852.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE27170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE29352.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE36771.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAM19996.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK077534; BAC36852.1; ALT_INIT; mRNA.
DR   EMBL; AK002526; BAB22163.1; ALT_INIT; mRNA.
DR   EMBL; AL670035; CAM19996.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK162173; BAE36771.1; ALT_INIT; mRNA.
DR   EMBL; AK150162; BAE29352.1; ALT_INIT; mRNA.
DR   EMBL; AK146436; BAE27170.1; ALT_INIT; mRNA.
DR   EMBL; AK004827; BAB23595.1; -; mRNA.
DR   EMBL; BC017684; AAH17684.1; ALT_INIT; mRNA.
DR   RefSeq; NP_079923.3; NM_025647.3.
DR   AlphaFoldDB; Q9DBP5; -.
DR   SMR; Q9DBP5; -.
DR   BioGRID; 211574; 1.
DR   IntAct; Q9DBP5; 4.
DR   MINT; Q9DBP5; -.
DR   STRING; 10090.ENSMUSP00000030491; -.
DR   iPTMnet; Q9DBP5; -.
DR   PhosphoSitePlus; Q9DBP5; -.
DR   SwissPalm; Q9DBP5; -.
DR   REPRODUCTION-2DPAGE; IPI00331146; -.
DR   REPRODUCTION-2DPAGE; Q9DBP5; -.
DR   UCD-2DPAGE; Q9DBP5; -.
DR   CPTAC; non-CPTAC-3799; -.
DR   EPD; Q9DBP5; -.
DR   jPOST; Q9DBP5; -.
DR   MaxQB; Q9DBP5; -.
DR   PaxDb; Q9DBP5; -.
DR   PeptideAtlas; Q9DBP5; -.
DR   PRIDE; Q9DBP5; -.
DR   ProteomicsDB; 263423; -.
DR   TopDownProteomics; Q9DBP5; -.
DR   DNASU; 66588; -.
DR   GeneID; 66588; -.
DR   KEGG; mmu:66588; -.
DR   UCSC; uc008ueg.2; mouse.
DR   CTD; 51727; -.
DR   MGI; MGI:1913838; Cmpk1.
DR   eggNOG; KOG3079; Eukaryota.
DR   InParanoid; Q9DBP5; -.
DR   OrthoDB; 1378291at2759; -.
DR   PhylomeDB; Q9DBP5; -.
DR   TreeFam; TF354283; -.
DR   Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR   BioGRID-ORCS; 66588; 20 hits in 73 CRISPR screens.
DR   ChiTaRS; Cmpk1; mouse.
DR   PRO; PR:Q9DBP5; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q9DBP5; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISO:MGI.
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; ISS:UniProtKB.
DR   GO; GO:0050145; F:nucleoside monophosphate kinase activity; ISO:MGI.
DR   GO; GO:0033862; F:UMP kinase activity; ISO:MGI.
DR   GO; GO:0009041; F:uridylate kinase activity; ISO:MGI.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0046705; P:CDP biosynthetic process; ISO:MGI.
DR   GO; GO:0006240; P:dCDP biosynthetic process; ISO:MGI.
DR   GO; GO:0006227; P:dUDP biosynthetic process; ISO:MGI.
DR   GO; GO:0006165; P:nucleoside diphosphate phosphorylation; ISS:UniProtKB.
DR   GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006225; P:UDP biosynthetic process; ISO: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   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW   Isopeptide bond; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase; Ubl conjugation.
FT   CHAIN           1..196
FT                   /note="UMP-CMP kinase"
FT                   /id="PRO_0000158950"
FT   REGION          33..63
FT                   /note="NMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
FT   REGION          133..143
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03172"
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:0000250|UniProtKB:P30085"
FT   MOD_RES         43
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         55
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P30085"
FT   MOD_RES         106
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
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:0000250|UniProtKB:P30085"
SQ   SEQUENCE   196 AA;  22165 MW;  7972B629D7542294 CRC64;
     MKPLVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG ELIEKYIKEG
     KIVPVEITIS LLKREMDQTM AANAQKNKFL IDGFPRNQDN LQGWNKTMDG KADVSFVLFF
     DCNNEICIER CLERGKSSGR SDDNRESLEK RIQTYLESTK PIIDLYEEMG KVKKIDASKS
     VDEVFGEVVK IFDKEG
 
 
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