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Q9JM01 (CDKL3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cyclin-dependent kinase-like 3

EC=2.7.11.22
Alternative name(s):
Serine/threonine protein kinase NKIATRE
Gene names
Name:Cdkl3
Synonyms:Nkiatre
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Isoform 2: Nucleus. Cytoplasm Ref.1.

Isoform 3: Cytoplasm Ref.1.

Tissue specificity

Highly expressed in brain, and to a lower extent in heart and testis. Ref.1

Domain

The [NKR]KIAxRE motif seems to be a cyclin-binding region.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9JM01-1)

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.
Isoform 2 (identifier: Q9JM01-2)

Also known as: NKIATRE alpha; p57 alpha isoform;

The sequence of this isoform differs from the canonical sequence as follows:
     504-505: DQ → AK
     506-593: Missing.
Note: Found in the nucleus and cytoplasm.
Isoform 3 (identifier: Q9JM01-3)

Also known as: NKIATRE beta; p52 beta isoform;

The sequence of this isoform differs from the canonical sequence as follows:
     458-593: Missing.
Note: Found in the cytoplasm.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 593593Cyclin-dependent kinase-like 3
PRO_0000085823

Regions

Domain4 – 286283Protein kinase
Nucleotide binding10 – 189ATP By similarity
Motif45 – 517[NKR]KIAxRE

Sites

Active site1251Proton acceptor By similarity
Binding site331ATP By similarity

Natural variations

Alternative sequence458 – 593136Missing in isoform 3.
VSP_016158
Alternative sequence504 – 5052DQ → AK in isoform 2.
VSP_016159
Alternative sequence506 – 59388Missing in isoform 2.
VSP_016160

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 22, 2005. Version 2.
Checksum: 40F8C846EA421E0B

FASTA59367,553
        10         20         30         40         50         60 
MEMYETLGKV GEGSYGTVMK CKHKDTGRIV AIKIFYEKPE KSVNKIATRE IKFLKQFRHE 

        70         80         90        100        110        120 
NLVNLIEVFR QKKKIHLVFE FIDHTVLDEL QHYCHGLESK RLRKYLFQIL RAIEYLHNNN 

       130        140        150        160        170        180 
IIHRDIKPEN ILVSQSGITK LCDFGFARTL AAPGDVYTDY VATRWYRAPE LVLKDTTYGK 

       190        200        210        220        230        240 
PVDIWALGCM IIEMATGNPY LPSSSDLDLL HKIVLKVGNL TPHLHNIFSK SPIFAGVVLP 

       250        260        270        280        290        300 
QVQHPKNARK KYPKLNGLLA DIVHACLQID PAERISSTDL LHHDYFTRDG FIEKFIPELR 

       310        320        330        340        350        360 
AKLLQEAKVN SFIKPKENFK ENEPVRDEKK PVFTNPLLYG NPTLYGKEVD RDKRAKELKV 

       370        380        390        400        410        420 
RVIKAKGGKG DVPDLKKTES EGEHRQQGTA EDTHPTSLDR KPSVSELTNP VHPSANSDTV 

       430        440        450        460        470        480 
KEDPHSGGCM IMPPINLTSS NLLAANPSSN LSHPNSRLTE RTKKRRTSSQ TIGQTLSNSR 

       490        500        510        520        530        540 
QEDTGPTQVQ TEKGAFNERT GQNDQIASGN KRKLNFSKCD RKEFHFPELP FTIQAKEMKG 

       550        560        570        580        590 
MEVKQIKVLK RESKKTDSPK IPTLLSMDSN QEKQEVFNIF PGWCKRGNLN WPS 

« Hide

Isoform 2 (NKIATRE alpha) (p57 alpha isoform) [UniParc].

Checksum: 89747921FF2CE683
Show »

FASTA50557,243
Isoform 3 (NKIATRE beta) (p52 beta isoform) [UniParc].

Checksum: 99D0782794099CDA
Show »

FASTA45751,895

References

« Hide 'large scale' references
[1]"NKIATRE is a novel conserved cdc2-related kinase."
Haq R., Randall S., Midmer M., Yee K., Zanke B.
Genomics 71:131-141(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Brain and Jejunum.
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF112183 mRNA. Translation: AAF34870.1.
AF112184 mRNA. Translation: AAF34871.1.
AABR03073386 Genomic DNA. No translation available.
AABR03074822 Genomic DNA. No translation available.
AABR03073552 Genomic DNA. No translation available.
RefSeqNP_068540.1. NM_021772.2. [Q9JM01-3]
UniGeneRn.154405.
Rn.229441.

3D structure databases

ProteinModelPortalQ9JM01.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000060584.

PTM databases

PhosphoSiteQ9JM01.

Proteomic databases

PaxDbQ9JM01.
PRIDEQ9JM01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000059040; ENSRNOP00000055819; ENSRNOG00000005097. [Q9JM01-1]
GeneID60396.
KEGGrno:60396.
UCSCRGD:619874. rat. [Q9JM01-1]

Organism-specific databases

CTD51265.
RGD619874. Cdkl3.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00650000093115.
HOGENOMHOG000233024.
HOVERGENHBG080204.
KOK08824.
OMACKHKNTG.
OrthoDBEOG7992PS.
PhylomeDBQ9JM01.

Gene expression databases

GenevestigatorQ9JM01.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio612104.
PROQ9JM01.

Entry information

Entry nameCDKL3_RAT
AccessionPrimary (citable) accession number: Q9JM01
Secondary accession number(s): Q9JM02
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: May 14, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families