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Q04899 (CDK18_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase 18
EC=2.7.11.22
Alternative name(s):
Cell division protein kinase 18
PCTAIRE-motif protein kinase 3
Serine/threonine-protein kinase PCTAIRE-3
Gene names
Name:Cdk18
Synonyms:Pctaire3, Pctk3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in signal transduction cascades in terminally differentiated cells.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Tissue specificity

In brain, kidney, intestine and at a much lower level, in fetal tissues.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Caution

It is uncertain whether Met-1 or Met-4 is the initiator.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Cyclin-dependent kinase 18
PRO_0000086491

Regions

Domain121 – 402282Protein kinase
Nucleotide binding127 – 1359ATP By similarity

Sites

Active site2421Proton acceptor By similarity
Binding site1501ATP By similarity

Amino acid modifications

Modified residue121Phosphoserine By similarity
Modified residue511Phosphoserine By similarity
Modified residue661Phosphoserine Ref.3 Ref.4
Modified residue751Phosphoserine By similarity
Modified residue1091Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04899 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 3FC500519714F7E0

FASTA45151,848
        10         20         30         40         50         60 
MNKMKNFKRR LSLSVPRPET IEESLAEFTE QFNQLHTQTN EDGTDEPEQL SPGMQYQQRQ 

        70         80         90        100        110        120 
NQRRFSMEDL NKRLSLPMDI RLPQEFLQKL QLENPGLPKP LTRMSRRASL SDIGFGKLET 

       130        140        150        160        170        180 
YVKLDKLGEG TYATVFKGRS KLTENLVALK EIRLEHEEGA PCTAIREVSL LKDLKHANIV 

       190        200        210        220        230        240 
TLHDLIHTDR SLTLVFEYLD SDLKQYLDHC GNLMNMHNVK IFMFQLLRGL AYCHHRKILH 

       250        260        270        280        290        300 
RDLKPQNLLI NERGELKLAD FGLARAKSVP TKTYSNEVVT LWYRPPDVLL GSTEYSTPID 

       310        320        330        340        350        360 
MWGVGCILYE MATGKPLFPG STVKEELHLI FRLLGTPTEE SWPGVTSISE FRAYNFPRYL 

       370        380        390        400        410        420 
PQPLLSHAPR LDTEGINLLS SLLLYESKSR MSAEAALNHP YFQSLGDRVH QLHDTASIFS 

       430        440        450 
LKEIQLQKDP GYRGLAFQHP GRGKSRRQSI F

« Hide

References

« Hide 'large scale' references
[1]"PCTAIRE-1 and PCTAIRE-3, two members of a novel cdc2/CDC28-related protein kinase gene family."
Okuda T., Cleveland J.L., Downing J.R.
Oncogene 7:2249-2258(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[3]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, MASS SPECTROMETRY.
Tissue: Melanoma.
[4]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, MASS SPECTROMETRY.
Tissue: Macrophage.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X69026 mRNA. Translation: CAA48788.1.
AK004998 mRNA. Translation: BAB23732.1.
IPIIPI00111168.
PIRS30436.
RefSeqNP_032821.1. NM_008795.2.
UniGeneMm.28130.

3D structure databases

ProteinModelPortalQ04899.
SMRQ04899. Positions 68-428.
ModBaseSearch...

PTM databases

PhosphoSiteQ04899.

Proteomic databases

PaxDbQ04899.
PRIDEQ04899.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027697; ENSMUSP00000027697; ENSMUSG00000026437.
ENSMUST00000112362; ENSMUSP00000107981; ENSMUSG00000026437.
GeneID18557.
KEGGmmu:18557.

Organism-specific databases

CTD5129.
MGIMGI:97518. Cdk18.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
HOVERGENHBG014652.
InParanoidQ04899.
KOK15596.
OMAHTDRSLT.

Enzyme and pathway databases

BRENDA2.7.11.22. 3474.

Gene expression databases

ArrayExpressQ04899.
BgeeQ04899.
CleanExMM_PCTK3.
GenevestigatorQ04899.
GermOnlineENSMUSG00000026437. Mus musculus.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294380.
SOURCESearch...

Entry information

Entry nameCDK18_MOUSE
AccessionPrimary (citable) accession number: Q04899
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents