Q8N752 (KC1AL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Wnt signaling pathway
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW cell morphogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Inferred from electronic annotation. Source: Compara
Molecular_function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 337	337	Casein kinase I isoform alpha-like		PRO_0000192830
Regions
	Domain	17 – 285	269	Protein kinase
	Nucleotide binding	23 – 31	9	ATP By similarity
Sites
	Active site	136	1	Proton acceptor By similarity
	Binding site	46	1	ATP By similarity
Natural variations
	Natural variant	5	1	S → G. Ref.5 Corresponds to variant rs56224973 [ dbSNP | Ensembl ].		VAR_042074
	Natural variant	21	1	R → Q in a colorectal cancer sample; somatic mutation. Ref.4 Corresponds to variant rs56158728 [ dbSNP | Ensembl ].		VAR_036450
	Natural variant	21	1	R → W. Ref.5		VAR_042075
	Natural variant	42	1	D → E. Ref.3 Corresponds to variant rs9576175 [ dbSNP | Ensembl ].		VAR_042076
	Natural variant	170	1	R → S. Ref.5 Corresponds to variant rs17773251 [ dbSNP | Ensembl ].		VAR_034047
	Natural variant	177	1	E → K. Ref.5 Corresponds to variant rs17054882 [ dbSNP | Ensembl ].		VAR_042077
	Natural variant	220	1	P → L. Ref.5 Corresponds to variant rs56252856 [ dbSNP | Ensembl ].		VAR_042078
	Natural variant	230	1	K → N. Ref.5 Corresponds to variant rs56252523 [ dbSNP | Ensembl ].		VAR_042079
	Natural variant	257	1	A → T. Ref.5 Corresponds to variant rs55895045 [ dbSNP | Ensembl ].		VAR_042080
Experimental info
	Sequence conflict	225	1	R → K in AAH28723. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8N752 [UniParc]. Last modified July 22, 2008. Version 2. Checksum: 6110F854D739B142	FASTA	337	39,086
	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

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. , 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. , 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. , 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. , 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.
IPI	IPI00167096.
RefSeq	NP_660204.2. NM_145203.5.
UniGene	Hs.512897.
3D structure databases
ProteinModelPortal	Q8N752.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8N752. 5 interactions.
STRING	9606.ENSP00000369126.
PTM databases
PhosphoSite	Q8N752.
Polymorphism databases
DMDM	212286065.
Proteomic databases
PaxDb	Q8N752.
PRIDE	Q8N752.
Protocols and materials databases
DNASU	122011.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379800; ENSP00000369126; ENSG00000180138.
GeneID	122011.
KEGG	hsa:122011.
UCSC	uc001uwm.1. human.
Organism-specific databases
CTD	122011.
GeneCards	GC13M037677.
H-InvDB	HIX0011244.
HGNC	HGNC:20289. CSNK1A1L.
neXtProt	NX_Q8N752.
PharmGKB	PA134917108.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000182055.
HOVERGEN	HBG000176.
InParanoid	Q8N752.
KO	K08957.
OMA	PYREDKH.
OrthoDB	EOG4SQWX6.
PhylomeDB	Q8N752.
Gene expression databases
Bgee	Q8N752.
CleanEx	HS_CSNK1A1L.
Genevestigator	Q8N752.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q8N752.
ChEMBL	CHEMBL5520.
GenomeRNAi	122011.
NextBio	80837.

Entry information

Entry name

KC1AL_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.