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P30085

- KCY_HUMAN

UniProt

P30085 - KCY_HUMAN

Protein

UMP-CMP kinase

Gene

CMPK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity.3 PublicationsUniRule annotation

    Catalytic activityi

    ATP + (d)CMP = ADP + (d)CDP.UniRule annotation
    ATP + UMP = ADP + UDP.UniRule annotation
    ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

    Cofactori

    Binds 1 magnesium ion per monomer.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391NMPUniRule annotation
    Binding sitei100 – 1001CMPUniRule annotation
    Binding sitei134 – 1341ATPUniRule annotation
    Binding sitei140 – 1401NMPUniRule annotation
    Binding sitei151 – 1511NMPUniRule annotation
    Binding sitei179 – 1791ATP; via carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 186ATPUniRule annotation
    Nucleotide bindingi61 – 633NMPUniRule annotation
    Nucleotide bindingi93 – 964NMPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cytidylate kinase activity Source: UniProtKB-HAMAP
    3. nucleoside diphosphate kinase activity Source: UniProtKB
    4. UMP kinase activity Source: Ensembl
    5. uridine kinase activity Source: ProtInc

    GO - Biological processi

    1. CDP biosynthetic process Source: Ensembl
    2. dCDP biosynthetic process Source: Ensembl
    3. dUDP biosynthetic process Source: Ensembl
    4. nucleobase-containing small molecule interconversion Source: Reactome
    5. nucleobase-containing small molecule metabolic process Source: Reactome
    6. nucleoside diphosphate phosphorylation Source: UniProtKB
    7. nucleoside triphosphate biosynthetic process Source: UniProtKB
    8. ovulation cycle process Source: Ensembl
    9. phthalate metabolic process Source: Ensembl
    10. pyrimidine ribonucleotide biosynthetic process Source: ProtInc
    11. small molecule metabolic process Source: Reactome
    12. UDP biosynthetic process Source: Ensembl
    13. UMP biosynthetic process Source: GOC

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Pyrimidine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08663-MONOMER.
    BRENDAi2.7.4.14. 2681.
    ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    SABIO-RKP30085.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UMP-CMP kinaseUniRule annotation (EC:2.7.4.14UniRule annotation)
    Alternative name(s):
    Deoxycytidylate kinaseUniRule annotation
    Short name:
    CKUniRule annotation
    Short name:
    dCMP kinaseUniRule annotation
    Nucleoside-diphosphate kinaseUniRule annotation (EC:2.7.4.6UniRule annotation)
    Uridine monophosphate/cytidine monophosphate kinaseUniRule annotation
    Short name:
    UMP/CMP kinaseUniRule annotation
    Short name:
    UMP/CMPKUniRule annotation
    Gene namesi
    Name:CMPK1UniRule annotation
    Synonyms:CMK, CMPKUniRule annotation, UCK, UMK, UMPK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18170. CMPK1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Predominantly nuclear.

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleolus Source: HPA
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162382539.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 196196UMP-CMP kinasePRO_0000158949Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431N6-acetyllysineBy similarity
    Modified residuei55 – 551N6-acetyllysine1 Publication
    Modified residuei106 – 1061N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP30085.
    PaxDbiP30085.
    PRIDEiP30085.

    2D gel databases

    OGPiP30085.
    SWISS-2DPAGEP30085.

    PTM databases

    PhosphoSiteiP30085.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiP30085.
    BgeeiP30085.
    CleanExiHS_CMPK1.
    GenevestigatoriP30085.

    Organism-specific databases

    HPAiHPA053730.
    HPA058604.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    BioGridi119700. 2 interactions.
    IntActiP30085. 1 interaction.
    MINTiMINT-5000978.
    STRINGi9606.ENSP00000360939.

    Structurei

    Secondary structure

    1
    196
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi16 – 2712
    Beta strandi30 – 334
    Helixi34 – 4310
    Helixi50 – 589
    Helixi65 – 8218
    Beta strandi88 – 936
    Helixi98 – 10811
    Turni109 – 1113
    Beta strandi113 – 1219
    Helixi124 – 13613
    Helixi145 – 16824
    Beta strandi172 – 1765
    Helixi181 – 19414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TEVX-ray2.10A1-196[»]
    ProteinModelPortaliP30085.
    SMRiP30085. Positions 3-196.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30085.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni33 – 6331NMPbindAdd
    BLAST
    Regioni133 – 14311LIDAdd
    BLAST

    Domaini

    Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.

    Sequence similaritiesi

    Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0563.
    HOVERGENiHBG108060.
    InParanoidiP30085.
    KOiK13800.
    OrthoDBiEOG7X0VJ0.
    PhylomeDBiP30085.
    TreeFamiTF354283.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00235. Adenylate_kinase_Adk.
    MF_03172. Adenylate_kinase_UMP_CMP_kin.
    InterProiIPR000850. Adenylat/UMP-CMP_kin.
    IPR027417. P-loop_NTPase.
    IPR006266. UMP_CMP_kinase.
    [Graphical view]
    PANTHERiPTHR23359. PTHR23359. 1 hit.
    PRINTSiPR00094. ADENYLTKNASE.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01359. UMP_CMP_kin_fam. 1 hit.
    PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30085-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKPLVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG    50
    ELIEKYIKEG KIVPVEITIS LLKREMDQTM AANAQKNKFL IDGFPRNQDN 100
    LQGWNKTMDG KADVSFVLFF DCNNEICIER CLERGKSSGR SDDNRESLEK 150
    RIQTYLQSTK PIIDLYEEMG KVKKIDASKS VDEVFDEVVQ IFDKEG 196
    Length:196
    Mass (Da):22,222
    Last modified:December 1, 2000 - v3
    Checksum:i6837B1E6D7543768
    GO
    Isoform 2 (identifier: P30085-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         26-74: Missing.

    Show »
    Length:147
    Mass (Da):16,548
    Checksum:i535CD9D8F1B4A0F2
    GO

    Sequence cautioni

    The sequence AAF17709.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH14961.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAD96734.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAG60709.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAI13471.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI14972.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti27 – 271Y → I AA sequence (PubMed:8313870)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei26 – 7449Missing in isoform 2. 1 PublicationVSP_046683Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF070416 mRNA. Translation: AAF17709.1. Different initiation.
    AF259961 mRNA. Translation: AAG22609.1.
    AF110643 mRNA. Translation: AAD48583.1.
    AF087865 mRNA. Translation: AAP97174.1.
    AF112216 mRNA. Translation: AAF17204.1.
    AK223014 mRNA. Translation: BAD96734.1. Different initiation.
    AK298502 mRNA. Translation: BAG60709.1. Different initiation.
    AL513322, AL607122 Genomic DNA. Translation: CAI13471.1. Sequence problems.
    AL607122, AL513322 Genomic DNA. Translation: CAI14972.1. Sequence problems.
    BC014961 mRNA. Translation: AAH14961.1. Different initiation.
    PIRiB45482.
    RefSeqiNP_001129612.1. NM_001136140.1.
    NP_057392.1. NM_016308.2.
    UniGeneiHs.731647.

    Genome annotation databases

    EnsembliENST00000371873; ENSP00000360939; ENSG00000162368.
    ENST00000450808; ENSP00000398192; ENSG00000162368.
    GeneIDi51727.
    KEGGihsa:51727.

    Polymorphism databases

    DMDMi12644008.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF070416 mRNA. Translation: AAF17709.1 . Different initiation.
    AF259961 mRNA. Translation: AAG22609.1 .
    AF110643 mRNA. Translation: AAD48583.1 .
    AF087865 mRNA. Translation: AAP97174.1 .
    AF112216 mRNA. Translation: AAF17204.1 .
    AK223014 mRNA. Translation: BAD96734.1 . Different initiation.
    AK298502 mRNA. Translation: BAG60709.1 . Different initiation.
    AL513322 , AL607122 Genomic DNA. Translation: CAI13471.1 . Sequence problems.
    AL607122 , AL513322 Genomic DNA. Translation: CAI14972.1 . Sequence problems.
    BC014961 mRNA. Translation: AAH14961.1 . Different initiation.
    PIRi B45482.
    RefSeqi NP_001129612.1. NM_001136140.1.
    NP_057392.1. NM_016308.2.
    UniGenei Hs.731647.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TEV X-ray 2.10 A 1-196 [» ]
    ProteinModelPortali P30085.
    SMRi P30085. Positions 3-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119700. 2 interactions.
    IntActi P30085. 1 interaction.
    MINTi MINT-5000978.
    STRINGi 9606.ENSP00000360939.

    Chemistry

    ChEMBLi CHEMBL5681.
    DrugBanki DB00441. Gemcitabine.

    PTM databases

    PhosphoSitei P30085.

    Polymorphism databases

    DMDMi 12644008.

    2D gel databases

    OGPi P30085.
    SWISS-2DPAGE P30085.

    Proteomic databases

    MaxQBi P30085.
    PaxDbi P30085.
    PRIDEi P30085.

    Protocols and materials databases

    DNASUi 51727.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371873 ; ENSP00000360939 ; ENSG00000162368 .
    ENST00000450808 ; ENSP00000398192 ; ENSG00000162368 .
    GeneIDi 51727.
    KEGGi hsa:51727.

    Organism-specific databases

    CTDi 51727.
    GeneCardsi GC01P047799.
    HGNCi HGNC:18170. CMPK1.
    HPAi HPA053730.
    HPA058604.
    MIMi 191710. gene.
    neXtProti NX_P30085.
    PharmGKBi PA162382539.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0563.
    HOVERGENi HBG108060.
    InParanoidi P30085.
    KOi K13800.
    OrthoDBi EOG7X0VJ0.
    PhylomeDBi P30085.
    TreeFami TF354283.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS08663-MONOMER.
    BRENDAi 2.7.4.14. 2681.
    Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    SABIO-RK P30085.

    Miscellaneous databases

    EvolutionaryTracei P30085.
    GeneWikii CMPK.
    GenomeRNAii 51727.
    NextBioi 35473968.
    PROi P30085.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30085.
    Bgeei P30085.
    CleanExi HS_CMPK1.
    Genevestigatori P30085.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00235. Adenylate_kinase_Adk.
    MF_03172. Adenylate_kinase_UMP_CMP_kin.
    InterProi IPR000850. Adenylat/UMP-CMP_kin.
    IPR027417. P-loop_NTPase.
    IPR006266. UMP_CMP_kinase.
    [Graphical view ]
    PANTHERi PTHR23359. PTHR23359. 1 hit.
    PRINTSi PR00094. ADENYLTKNASE.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR01359. UMP_CMP_kin_fam. 1 hit.
    PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Phosphorylation of deoxycytidine analog monophosphates by UMP-CMP kinase: molecular characterization of the human enzyme."
      Van Rompay A.R., Johansson M., Karlsson A.
      Mol. Pharmacol. 56:562-569(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, FUNCTION.
    2. "Characterization of human UMP-CMP kinase enzymatic activity and 5' untranslated region."
      Pearman A.T., Castro-Faria-Neto H.C., McIntyre T.M., Prescott S.M., Stafforini D.M.
      Life Sci. 69:2361-2370(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CHROMOSOMAL LOCATION, IDENTIFICATION OF START CODON.
      Tissue: Macrophage.
    3. "Characterization of human UMP/CMP kinase and its phosphorylation of D- and L-form deoxycytidine analogue monophosphates."
      Liou J.-Y., Dutschman G.E., Lam W., Jiang Z., Cheng Y.-C.
      Cancer Res. 62:1624-1631(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
    4. "Human UMP-CMP kinase gene."
      Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Pituitary.
    5. "Cloning and characterization of a new human cDNA homologous to pig UMP-CMP kinase mRNA."
      Fan Y.X., Yu L., Dai F.Y., Zhou Y., Huang J., Zhao S.Y.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hypothalamus.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    8. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Small intestine.
    9. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Muscle.
    11. Cited for: PROTEIN SEQUENCE OF 1-29.
      Tissue: Liver.
    12. "Human liver protein map: a reference database established by microsequencing and gel comparison."
      Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
      Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10.
      Tissue: Liver.
    13. Bienvenut W.V., Bilsland A.E., Keith W.N.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-16; 62-73; 89-106; 152-171 AND 180-196, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "The human adenylate kinase 9 is a nucleoside mono- and diphosphate kinase."
      Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.
      Int. J. Biochem. Cell Biol. 45:925-931(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    17. "Substrate-induced conformational changes in human UMP/CMP kinase."
      Segura-Pena D., Sekulic N., Ort S., Konrad M., Lavie A.
      J. Biol. Chem. 279:33882-33889(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

    Entry informationi

    Entry nameiKCY_HUMAN
    AccessioniPrimary (citable) accession number: P30085
    Secondary accession number(s): B4DPU7
    , E9PGI8, Q53GB7, Q5SVZ0, Q96C07, Q9UBQ8, Q9UIA2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 152 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3