Q9HCP0 (KC1G1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Casein kinase I isoform gamma-1
Short name=CKI-gamma 1
EC=2.7.11.1

Gene names

Name:

CSNK1G1

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	422 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine/threonine-protein kinase. 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. Regulates fast synaptic transmission mediated by glutamate By similarity. Phosphorylates CLSPN. Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Repressed by 2-(2-hydroxyethylamino)-6-(3-chloroanilino)-9-isopropylpurine (DB08325).
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm.
Post-translational modification	Autophosphorylated 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	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW protein autophosphorylation Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: Compara peptide binding Inferred from electronic annotation. Source: Compara protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1L (identifier: Q9HCP0-1)

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 1S (identifier: Q9HCP0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     370-422: VVSSTNGELN...KRKKTAQRHK → SLRTVTAEHYDVNNSAIWHRGRGT

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 422

422

Casein kinase I isoform gamma-1

PRO_0000192839

Regions

Domain

44 – 315

272

Protein kinase

Nucleotide binding

50 – 58

9

ATP By similarity

Sites

Active site

164

1

Proton acceptor By similarity

Binding site

73

1

ATP By similarity

Amino acid modifications

Modified residue

344

1

Phosphoserine Ref.6

Natural variations

Alternative sequence

370 – 422

53

VVSST…AQRHK → SLRTVTAEHYDVNNSAIWHR GRGT in isoform 1S.

VSP_004748

Natural variant

206

1

R → K. Ref.9
Corresponds to variant rs55799101 [ dbSNP | Ensembl ].

VAR_042084

Natural variant

329

1

V → I. Ref.9
Corresponds to variant rs55699712 [ dbSNP | Ensembl ].

VAR_042085

Experimental info

Mutagenesis

169

1

N → A: Loss of kinase activity. Ref.7

Secondary structure

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422

Helix Strand Turn

Details...

Beta strand

49 – 52

4

Beta strand

54 – 62

9

Turn

64 – 66

3

Beta strand

69 – 76

8

Helix

84 – 94

11

Beta strand

104 – 110

7

Beta strand

113 – 119

7

Helix

125 – 131

7

Turn

132 – 134

3

Helix

138 – 157

20

Helix

167 – 169

3

Beta strand

170 – 172

3

Turn

175 – 178

4

Beta strand

183 – 185

3

Turn

197 – 199

3

Turn

215 – 217

3

Helix

220 – 223

4

Helix

230 – 246

17

Turn

250 – 253

4

Helix

259 – 272

14

Helix

275 – 278

4

Turn

279 – 281

3

Helix

284 – 295

12

Helix

304 – 317

14

Turn

327 – 330

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1L [UniParc]. Last modified March 1, 2001. Version 1. Checksum: B875922349B97645	FASTA	422	48,511
	10 20 30 40 50 60 MDHPSREKDE RQRTTKPMAQ RSAHCSRPSG SSSSSGVLMV GPNFRVGKKI GCGNFGELRL 70 80 90 100 110 120 GKNLYTNEYV AIKLEPIKSR APQLHLEYRF YKQLGSAGEG LPQVYYFGPC GKYNAMVLEL 130 140 150 160 170 180 LGPSLEDLFD LCDRTFTLKT VLMIAIQLLS RMEYVHSKNL IYRDVKPENF LIGRQGNKKE 190 200 210 220 230 240 HVIHIIDFGL AKEYIDPETK KHIPYREHKS LTGTARYMSI NTHLGKEQSR RDDLEALGHM 250 260 270 280 290 300 FMYFLRGSLP WQGLKADTLK ERYQKIGDTK RNTPIEALCE NFPEEMATYL RYVRRLDFFE 310 320 330 340 350 360 KPDYEYLRTL FTDLFEKKGY TFDYAYDWVG RPIPTPVGSV HVDSGASAIT RESHTHRDRP 370 380 390 400 410 420 SQQQPLRNQV VSSTNGELNV DDPTGAHSNA PITAHAEVEV VEEAKCCCFF KRKRKKTAQR HK
	Isoform 1S [UniParc]. Checksum: 2979A77D92F62261	FASTA	393	45,414
	10 20 30 40 50 60 MDHPSREKDE RQRTTKPMAQ RSAHCSRPSG SSSSSGVLMV GPNFRVGKKI GCGNFGELRL 70 80 90 100 110 120 GKNLYTNEYV AIKLEPIKSR APQLHLEYRF YKQLGSAGEG LPQVYYFGPC GKYNAMVLEL 130 140 150 160 170 180 LGPSLEDLFD LCDRTFTLKT VLMIAIQLLS RMEYVHSKNL IYRDVKPENF LIGRQGNKKE 190 200 210 220 230 240 HVIHIIDFGL AKEYIDPETK KHIPYREHKS LTGTARYMSI NTHLGKEQSR RDDLEALGHM 250 260 270 280 290 300 FMYFLRGSLP WQGLKADTLK ERYQKIGDTK RNTPIEALCE NFPEEMATYL RYVRRLDFFE 310 320 330 340 350 360 KPDYEYLRTL FTDLFEKKGY TFDYAYDWVG RPIPTPVGSV HVDSGASAIT RESHTHRDRP 370 380 390 SQQQPLRNQS LRTVTAEHYD VNNSAIWHRG RGT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression analysis and chromosome mapping of human casein kinase 1 gamma1 (CSNK1G1): identification of two types of cDNA encoding the kinase protein associated with heterologous carboxy-terminal sequences." Kusuda J., Hirai M., Tanuma R., Hashimoto K. Cytogenet. Cell Genet. 90:298-302(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1L AND 1S).
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] (ISOFORM 1L). Tissue: Muscle.
[5]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[6]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Role for casein kinase 1 in the phosphorylation of Claspin on critical residues necessary for the activation of Chk1." Meng Z., Capalbo L., Glover D.M., Dunphy W.G. Mol. Biol. Cell 22:2834-2847(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS CLSPN KINASE, MUTAGENESIS OF ASN-169.
[8]	"Structure of human casein kinase 1 gamma-1 in complex with (3-chloroanilino)-9-isopropylpurine (casp target)." Bunkoczi G., Rellos P., Das S., Savitsky P., Niesen F., Sobott F., Fedorov O., Pike A.C.W., Von Delft F., Sundstrom M., Arrowsmith C., Edwards A., Weigelt J., Knapp S. Submitted (JUL-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 45-352 IN COMPLEX WITH DB08325.
[9]	"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] LYS-206 AND ILE-329.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB042563 mRNA. Translation: BAB17839.1.
AB042562 mRNA. Translation: BAB17838.1.
AL832551 mRNA. Translation: CAI46142.1.
CH471082 Genomic DNA. Translation: EAW77670.1.
BC017236 mRNA. Translation: AAH17236.2.
BC130613 mRNA. Translation: AAI30614.1.
BC136504 mRNA. Translation: AAI36505.1.

IPI

IPI00219823.
IPI00791893.

RefSeq

NP_071331.2. NM_022048.3.

UniGene

Hs.646508.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CMW	X-ray	1.75	A	45-352	[»]

ProteinModelPortal

Q9HCP0.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000305777.

PTM databases

PhosphoSite

Q9HCP0.

Polymorphism databases

DMDM

18202957.

Proteomic databases

PaxDb

Q9HCP0.

PRIDE

Q9HCP0.

Protocols and materials databases

DNASU

53944.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000303032; ENSP00000307753; ENSG00000169118.
ENST00000303052; ENSP00000305777; ENSG00000169118.

GeneID

53944.

KEGG

hsa:53944.

UCSC

uc002anf.3. human.
uc002anj.3. human.

Organism-specific databases

CTD

53944.

GeneCards

GC15M064457.

HGNC

HGNC:2454. CSNK1G1.

HPA

HPA018209.

MIM

606274. gene.

neXtProt

NX_Q9HCP0.

PharmGKB

PA26954.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000182054.

HOVERGEN

HBG000176.

InParanoid

Q9HCP0.

KO

K08958.

OMA

SDRRGEW.

OrthoDB

EOG4GHZP4.

PhylomeDB

Q9HCP0.

Enzyme and pathway databases

BRENDA

2.7.11.1. 2681.

Pathway_Interaction_DB

foxopathway. FoxO family signaling.
hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.

Gene expression databases

Bgee

Q9HCP0.

CleanEx

HS_CSNK1G1.

Genevestigator

Q9HCP0.

GermOnline

ENSG00000169118. Homo sapiens.

Family and domain databases

InterPro

IPR022247. Casein_kinase-1_gamma_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF12605. CK1gamma_C. 1 hit.
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

Q9HCP0.

ChEMBL

CHEMBL2426.

ChiTaRS

CSNK1G1. human.

EvolutionaryTrace

Q9HCP0.

GenomeRNAi

53944.

NextBio

56260.

SOURCE

Search...

Entry information

Entry name

KC1G1_HUMAN

Accession

Primary (citable) accession number: Q9HCP0
Secondary accession number(s): Q5JPH1, Q96AE9, Q9HCP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 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.