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Q8N752 (KC1AL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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

Names and origin

Protein namesRecommended name:
Casein kinase I isoform alpha-like

Short name=CKI-alpha-like
EC=2.7.11.1
Alternative name(s):
CK1
Gene names
Name:CSNK1A1L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Cytoplasm By similarity.

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 diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Casein kinase I isoform alpha-like
PRO_0000192830

Regions

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

Sites

Active site1361Proton acceptor By similarity
Binding site461ATP By similarity

Natural variations

Natural variant51S → G. Ref.5
Corresponds to variant rs56224973 [ dbSNP | Ensembl ].
VAR_042074
Natural variant211R → Q in a colorectal cancer sample; somatic mutation. Ref.4
Corresponds to variant rs56158728 [ dbSNP | Ensembl ].
VAR_036450
Natural variant211R → W. Ref.5
Corresponds to variant rs56158728 [ dbSNP | Ensembl ].
VAR_042075
Natural variant421D → E. Ref.3
Corresponds to variant rs9576175 [ dbSNP | Ensembl ].
VAR_042076
Natural variant1701R → S. Ref.5
Corresponds to variant rs17773251 [ dbSNP | Ensembl ].
VAR_034047
Natural variant1771E → K. Ref.5
Corresponds to variant rs17054882 [ dbSNP | Ensembl ].
VAR_042077
Natural variant2201P → L. Ref.5
Corresponds to variant rs56252856 [ dbSNP | Ensembl ].
VAR_042078
Natural variant2301K → N. Ref.5
Corresponds to variant rs56252523 [ dbSNP | Ensembl ].
VAR_042079
Natural variant2571A → T. Ref.5
Corresponds to variant rs55895045 [ dbSNP | Ensembl ].
VAR_042080

Experimental info

Sequence conflict2251R → K in AAH28723. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8N752 [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: 6110F854D739B142

FASTA33739,086
        10         20         30         40         50         60 
MTNNSGSKAE LVVGGKYKLV RKIGSGSFGD VYLGITTTNG EDVAVKLESQ KVKHPQLLYE 

        70         80         90        100        110        120 
SKLYTILQGG VGIPHMHWYG QEKDNNVLVM DLLGPSLEDL FNFCSRRFTM KTVLMLADQM 

       130        140        150        160        170        180 
ISRIEYVHTK NFLHRDIKPD NFLMGTGRHC NKLFLIDFGL AKKYRDNRTR QHIPYREDKH 

       190        200        210        220        230        240 
LIGTVRYASI NAHLGIEQSR RDDMESLGYV FMYFNRTSLP WQGLRAMTKK QKYEKISEKK 

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

       310        320        330 
LKQKAAQQAA SSSGQGQQAQ TQTGKQTEKN KNNVKDN 

« Hide

References

[1]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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], VARIANT GLU-42.
Tissue: Testis.
[4]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-21.
[5]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-5; TRP-21; SER-170; LYS-177; LEU-220; ASN-230 AND THR-257.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL391383 Genomic DNA. Translation: CAI15195.1.
CH471075 Genomic DNA. Translation: EAX08587.1.
BC028723 mRNA. Translation: AAH28723.1.
RefSeqNP_660204.2. NM_145203.5.
UniGeneHs.512897.

3D structure databases

ProteinModelPortalQ8N752.
SMRQ8N752. Positions 13-302.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125755. 5 interactions.
IntActQ8N752. 5 interactions.
STRING9606.ENSP00000369126.

Chemistry

BindingDBQ8N752.
ChEMBLCHEMBL5520.
GuidetoPHARMACOLOGY1996.

PTM databases

PhosphoSiteQ8N752.

Polymorphism databases

DMDM212286065.

Proteomic databases

PaxDbQ8N752.
PRIDEQ8N752.

Protocols and materials databases

DNASU122011.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379800; ENSP00000369126; ENSG00000180138.
GeneID122011.
KEGGhsa:122011.
UCSCuc001uwm.1. human.

Organism-specific databases

CTD122011.
GeneCardsGC13M037677.
H-InvDBHIX0011244.
HGNCHGNC:20289. CSNK1A1L.
neXtProtNX_Q8N752.
PharmGKBPA134917108.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000182055.
HOVERGENHBG000176.
InParanoidQ8N752.
KOK08957.
OMAPYREDKH.
OrthoDBEOG7CZK5W.
PhylomeDBQ8N752.
TreeFamTF354246.

Enzyme and pathway databases

SignaLinkQ8N752.

Gene expression databases

BgeeQ8N752.
CleanExHS_CSNK1A1L.
GenevestigatorQ8N752.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 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

GenomeRNAi122011.
NextBio80837.
PROQ8N752.

Entry information

Entry nameKC1AL_HUMAN
AccessionPrimary (citable) accession number: Q8N752
Secondary accession number(s): Q5T2N2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: July 22, 2008
Last modified: February 19, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM