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Protein
Submitted name:

Casein kinase I isoform alpha

Gene

Csnk1a1

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein inferred from homologyi

Functioni

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB-KW

GO - Biological processi

  1. cell morphogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinaseUniRule annotation, Transferase

Keywords - Ligandi

ATP-bindingUniRule annotation, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_280715. GLI3 is processed to GLI3R by the proteasome.
REACT_287195. Degradation of GLI2 by the proteasome.
REACT_289020. Degradation of beta-catenin by the destruction complex.
REACT_309382. S33 mutants of beta-catenin aren't phosphorylated.
REACT_314194. APC truncation mutants have impaired AXIN binding.
REACT_318496. T41 mutants of beta-catenin aren't phosphorylated.
REACT_320639. S45 mutants of beta-catenin aren't phosphorylated.
REACT_321501. S37 mutants of beta-catenin aren't phosphorylated.
REACT_327682. Activation of SMO.
REACT_331147. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_341164. AXIN missense mutants destabilize the destruction complex.
REACT_341833. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_345474. Beta-catenin phosphorylation cascade.
REACT_350048. truncations of AMER1 destabilize the destruction complex.

Names & Taxonomyi

Protein namesi
Submitted name:
Casein kinase I isoform alphaImported
Gene namesi
Name:Csnk1a1Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi71098. Csnk1a1.

Subcellular locationi

GO - Cellular componenti

  1. ribonucleoprotein complex Source: Ensembl
Complete GO annotation...

Expressioni

Gene expression databases

ExpressionAtlasiD3ZRE3. baseline and differential.

Structurei

3D structure databases

ProteinModelPortaliD3ZRE3.
SMRiD3ZRE3. Positions 17-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the protein kinase superfamily.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00760000119040.
OMAiCKPPITE.
OrthoDBiEOG7CZK5W.
PhylomeDBiD3ZRE3.
TreeFamiTF354246.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D3ZRE3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ
60 70 80 90 100
KARHPQLLYE SKLYKILQGG VGIPHIRWYG QEKDYNVLVM DLLGPSLEDL
110 120 130 140 150
FNFCSRRFTM KTVLMLADQM ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC
160 170 180 190 200
NKCLESPVGK RKRSMTVSPS QDPSFSGLNQ LFLIDFGLAK KYRDNRTRQH
210 220 230 240 250
IPYREDKNLT GTARYASINA HLGIEQSRRD DMESLGYVLM YFNRTSLPWQ
260 270 280 290 300
GLKAATKKQK YEKISEKKMS TPVEVLCKGF PAEFAMYLNY CRGLRFEEAP
310 320 330 340 350
DYMYLRQLFR ILFRTLNHQY DYTFDWTMLK QKAAQQAASS SGQGQQAQTP
360
TGKQTDKTKS NMKGF
Length:365
Mass (Da):41,933
Last modified:April 19, 2010 - v1
Checksum:i0EC9BBB44E951A24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06095450 Genomic DNA. No translation available.

Genome annotation databases

EnsembliENSRNOT00000044346; ENSRNOP00000051516; ENSRNOG00000017106.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06095450 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortaliD3ZRE3.
SMRiD3ZRE3. Positions 17-330.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000044346; ENSRNOP00000051516; ENSRNOG00000017106.

Organism-specific databases

RGDi71098. Csnk1a1.

Phylogenomic databases

GeneTreeiENSGT00760000119040.
OMAiCKPPITE.
OrthoDBiEOG7CZK5W.
PhylomeDBiD3ZRE3.
TreeFamiTF354246.

Enzyme and pathway databases

ReactomeiREACT_280715. GLI3 is processed to GLI3R by the proteasome.
REACT_287195. Degradation of GLI2 by the proteasome.
REACT_289020. Degradation of beta-catenin by the destruction complex.
REACT_309382. S33 mutants of beta-catenin aren't phosphorylated.
REACT_314194. APC truncation mutants have impaired AXIN binding.
REACT_318496. T41 mutants of beta-catenin aren't phosphorylated.
REACT_320639. S45 mutants of beta-catenin aren't phosphorylated.
REACT_321501. S37 mutants of beta-catenin aren't phosphorylated.
REACT_327682. Activation of SMO.
REACT_331147. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_341164. AXIN missense mutants destabilize the destruction complex.
REACT_341833. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_345474. Beta-catenin phosphorylation cascade.
REACT_350048. truncations of AMER1 destabilize the destruction complex.

Miscellaneous databases

NextBioi35569587.

Gene expression databases

ExpressionAtlasiD3ZRE3. baseline and differential.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Ensembl
    Submitted (JUN-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiD3ZRE3_RAT
AccessioniPrimary (citable) accession number: D3ZRE3
Entry historyi
Integrated into UniProtKB/TrEMBL: April 19, 2010
Last sequence update: April 19, 2010
Last modified: March 31, 2015
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.