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Reviewed, UniProtKB/Swiss-Prot P48729 (KC1A_HUMAN)

Last modified November 25, 2008. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Casein kinase I isoform alpha
      Short name=CKI-alpha
    EC=2.7.11.1
Alternative name(s):
    CK1
Gene names
Name: CSNK1A1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 on 'Ser-45'.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Monomer. Interacts with the Axin complex.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords

   Biological processWnt signaling pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processWnt receptor signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

protein amino acid phosphorylation

Traceable author statement. Source: ProtInc

   Cellular componentcytosol Ref.8

Inferred from Experiment. Source: Reactome

   Molecular functionATP binding

Inferred from electronic annotation. Source: InterPro

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P48729-1)

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: P48729-2)

The sequence of this isoform differs from the canonical sequence as follows:
     152-152: K → KCLESPVGKRKRSMTVSTSQDPSFSGLNQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Casein kinase I isoform alpha
PRO_0000192822

Regions

Domain17 – 285269Protein kinase
Nucleotide binding23 – 319ATP By similarity

Sites

Active site1361Proton acceptor By similarity
Binding site461ATP By similarity

Amino acid modifications

Modified residue3211Phosphothreonine

Natural variations

Alternative sequence1521K → KCLESPVGKRKRSMTVSTSQ DPSFSGLNQ in isoform 2.
VSP_035455
Natural variant2971D → H in a breast pleomorphic lobular carcinoma sample; somatic mutation.
VAR_042073

Experimental info

Sequence conflict451V → L in CAA56710. Ref.1
Sequence conflict741P → T in AAV38633. Ref.4
Sequence conflict2311Q → K in AAH08717. Ref.7
Sequence conflict2501K → E in AAY84562. Ref.5
Sequence conflict3301T → S in CAA56710. Ref.1
Sequence conflict3301T → S in AAV38632 and AAV38633. Ref.4

Sequences

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

Last modified May 23, 2003. Version 2.
Checksum: 1B2085AE33CAFAC2

FASTA33738,915
        10         20         30         40         50         60 
MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ KARHPQLLYE 

        70         80         90        100        110        120 
SKLYKILQGG VGIPHIRWYG QEKDYNVLVM DLLGPSLEDL FNFCSRRFTM KTVLMLADQM 

       130        140        150        160        170        180 
ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC NKLFLIDFGL AKKYRDNRTR QHIPYREDKN 

       190        200        210        220        230        240 
LTGTARYASI NAHLGIEQSR RDDMESLGYV LMYFNRTSLP WQGLKAATKK QKYEKISEKK 

       250        260        270        280        290        300 
MSTPVEVLCK GFPAEFAMYL NYCRGLRFEE APDYMYLRQL FRILFRTLNH QYDYTFDWTM 

       310        320        330 
LKQKAAQQAA SSSGQGQQAQ TPTGKQTDKT KSNMKGF 

« Hide

Isoform 2 [UniParc].

Checksum: 11756FB15947D9F5
Show »

36541,937

References

« Hide 'large scale' references
[1]"Cloning and chromosomal localization of the gene coding for human protein kinase CK1."
Tapia C., Featherstone T., Gomez C., Taillon-Miller P., Allende C.C., Allende J.E.
FEBS Lett. 349:307-312(1994) [PubMed: 8050587] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family."
Fish K.J., Cegielska A., Getman M.E., Landes G.M., Virshup D.M.
J. Biol. Chem. 270:14875-14883(1995) [PubMed: 7797465] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Huang B., Li H., Yang S.
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[8]"Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism."
Liu C., Li Y., Semenov M., Han C., Baeg G.-H., Tan Y., Zhang Z., Lin X., He X.
Cell 108:837-847(2002) [PubMed: 11955436] [Abstract]
Cited for: ROLE IN WNT SIGNALING.
[9]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321, MASS SPECTROMETRY.
Tissue: Epithelium.
[10]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-321, MASS SPECTROMETRY.
[11]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-297.
+Additional computationally mapped references.

Cross-references

Sequence databases

X80693 mRNA. Translation: CAA56710.1.
L37042 mRNA. Translation: AAC41760.1.
CR542206 mRNA. Translation: CAG47002.1.
BT019829 mRNA. Translation: AAV38632.1.
BT019830 mRNA. Translation: AAV38633.1.
DQ082865 mRNA. Translation: AAY84562.1.
CH471062 Genomic DNA. Translation: EAW61769.1.
BC008717 mRNA. Translation: AAH08717.1.
PIRA57011.
S46254.
RefSeqNP_001883.4.
UniGeneHs.529862
Hs.699188

3D structure databases

HSSPHSSP built from PDB template 1CKI based on UniProtKB Q06486.
SMRP48729. Positions 10-302.
ModBaseSearch...

PTM databases

PhosphoSiteP48729.

Genome annotation databases

EnsemblENSG00000113712. Homo sapiens. [Contig view]
GeneID1452.

Organism-specific databases

H-InvDBHIX0005302.
HGNCHGNC:2451. CSNK1A1.
MIM600505. gene.
PharmGKBPA26951.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENP48729.

Enzyme and pathway databases

ReactomeREACT_11045. Signaling by Wnt.

Gene expression databases

ArrayExpressP48729.
CleanExHS_CSNK1A1.
GermOnlineENSG00000113712. Homo sapiens.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubP48729.
NextBio5955.
SOURCESearch...

Entry information

Entry nameKC1A_HUMAN
AccessionPrimary (citable) accession number: P48729
Secondary accession number(s): Q4JJA0 expand/collapse secondary AC list , Q5U046, Q5U047, Q6FGA2, Q96HD2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 23, 2003
Last modified: November 25, 2008
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents