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Protein

UMP-CMP kinase

Gene

CMPK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.UniRule annotation3 Publications

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

Mg2+Note: Binds 1 Mg2+ 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

  • ATP binding Source: UniProtKB-KW
  • cytidylate kinase activity Source: UniProtKB-HAMAP
  • nucleoside diphosphate kinase activity Source: UniProtKB
  • uridine kinase activity Source: ProtInc
  • uridylate kinase activity Source: UniProtKB-HAMAP

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18170. CMPK1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162382539.

Chemistry

DrugBankiDB00441. Gemcitabine.
DB00709. Lamivudine.

Polymorphism and mutation databases

DMDMi12644008.

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 residuei33 – 331Phosphoserine1 Publication
Modified residuei43 – 431N6-acetyllysineBy similarity
Modified residuei55 – 551N6-acetyllysine1 Publication
Modified residuei106 – 1061N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP30085.
PaxDbiP30085.
PRIDEiP30085.

2D gel databases

OGPiP30085.
SWISS-2DPAGEP30085.

PTM databases

PhosphoSiteiP30085.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiP30085.
CleanExiHS_CMPK1.
ExpressionAtlasiP30085. baseline and differential.
GenevisibleiP30085. HS.

Organism-specific databases

HPAiHPA053730.
HPA058604.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi119700. 5 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 – 96Combined sources
Helixi16 – 2712Combined sources
Beta strandi30 – 334Combined sources
Helixi34 – 4310Combined sources
Helixi50 – 589Combined sources
Helixi65 – 8218Combined sources
Beta strandi88 – 936Combined sources
Helixi98 – 10811Combined sources
Turni109 – 1113Combined sources
Beta strandi113 – 1219Combined sources
Helixi124 – 13613Combined sources
Helixi145 – 16824Combined sources
Beta strandi172 – 1765Combined sources
Helixi181 – 19414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
HOGENOMiHOG000238771.
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. AlignAdd to basket

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

        10         20         30         40         50
MKPLVVFVLG GPGAGKGTQC ARIVEKYGYT HLSAGELLRD ERKNPDSQYG
60 70 80 90 100
ELIEKYIKEG KIVPVEITIS LLKREMDQTM AANAQKNKFL IDGFPRNQDN
110 120 130 140 150
LQGWNKTMDG KADVSFVLFF DCNNEICIER CLERGKSSGR SDDNRESLEK
160 170 180 190
RIQTYLQSTK PIIDLYEEMG KVKKIDASKS VDEVFDEVVQ IFDKEG
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.Curated
The sequence AAH14961.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAD96734.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAG60709.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAI13471.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI14972.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi119700. 5 interactions.
IntActiP30085. 1 interaction.
MINTiMINT-5000978.
STRINGi9606.ENSP00000360939.

Chemistry

ChEMBLiCHEMBL5681.
DrugBankiDB00441. Gemcitabine.
DB00709. Lamivudine.

PTM databases

PhosphoSiteiP30085.

Polymorphism and mutation databases

DMDMi12644008.

2D gel databases

OGPiP30085.
SWISS-2DPAGEP30085.

Proteomic databases

MaxQBiP30085.
PaxDbiP30085.
PRIDEiP30085.

Protocols and materials databases

DNASUi51727.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51727.
GeneCardsiGC01P047799.
HGNCiHGNC:18170. CMPK1.
HPAiHPA053730.
HPA058604.
MIMi191710. gene.
neXtProtiNX_P30085.
PharmGKBiPA162382539.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0563.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiP30085.
KOiK13800.
OrthoDBiEOG7X0VJ0.
PhylomeDBiP30085.
TreeFamiTF354283.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiCMPK1. human.
EvolutionaryTraceiP30085.
GeneWikiiCMPK.
GenomeRNAii51727.
NextBioi35473968.
PROiP30085.
SOURCEiSearch...

Gene expression databases

BgeeiP30085.
CleanExiHS_CMPK1.
ExpressionAtlasiP30085. baseline and differential.
GenevisibleiP30085. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "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: July 22, 2015
This is version 162 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.