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P78368 (KC1G2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 gamma-2

Short name=CKI-gamma 2
EC=2.7.11.1
Gene names
Name:CSNK1G2
Synonyms:CK1G2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Phosphorylates COL4A3BP/CERT, MTA1 and SMAD3. Involved in brain development and vesicular trafficking and neurotransmitter releasing from small synaptic vesicles. Regulates fast synaptic transmission mediated by glutamate. SMAD3 phosphorylation promotes its ligand-dependent ubiquitination and subsequent proteasome degradation, thus inhibiting SMAD3-mediated TGF-beta responses. Hyperphosphorylation of the serine-repeat motif of COL4A3BP/CERT leads to its inactivation by dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis. Triggers PER1 proteasomal degradation probably through phosphorylation. Ref.7 Ref.8 Ref.9 Ref.11 Ref.12

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Stimulated by estrogen. Repressed by 5-iodotubercidin (DB04604). Ref.8

Subunit structure

Monomer By similarity. Interacts with MTA1 (short isoform) in the cytoplasm. Interacts with SMAD3. Ref.8 Ref.11

Subcellular location

Cytoplasm Ref.8.

Tissue specificity

Testis.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 415415Casein kinase I isoform gamma-2
PRO_0000192842

Regions

Domain46 – 316271Protein kinase
Nucleotide binding52 – 609ATP By similarity

Sites

Active site1651Proton acceptor By similarity
Binding site751ATP By similarity

Natural variations

Natural variant1891F → L. Ref.16
VAR_042086
Natural variant1941E → G. Ref.16
VAR_042087
Natural variant1961I → T. Ref.16
VAR_042088
Natural variant2061Y → C. Ref.16
VAR_042089
Natural variant2061Y → H. Ref.16
VAR_042090
Natural variant2071R → S. Ref.16
VAR_042091
Natural variant2081E → Q. Ref.16
VAR_042092
Natural variant2171R → C. Ref.16
VAR_042093
Natural variant2231T → M. Ref.16
VAR_042094

Experimental info

Sequence conflict1131K → N in AAP88924. Ref.2
Sequence conflict1131K → N in AAH20972. Ref.6

Secondary structure

.................................................. 415
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P78368 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 036A39148A1DA038

FASTA41547,457
        10         20         30         40         50         60 
MDFDKKGGKG ETEEGRRMSK AGGGRSSHGI RSSGTSSGVL MVGPNFRVGK KIGCGNFGEL 

        70         80         90        100        110        120 
RLGKNLYTNE YVAIKLEPIK SRAPQLHLEY RFYKQLSATE GVPQVYYFGP CGKYNAMVLE 

       130        140        150        160        170        180 
LLGPSLEDLF DLCDRTFTLK TVLMIAIQLI TRMEYVHTKS LIYRDVKPEN FLVGRPGTKR 

       190        200        210        220        230        240 
QHAIHIIDFG LAKEYIDPET KKHIPYREHK SLTGTARYMS INTHLGKEQS RRDDLEALGH 

       250        260        270        280        290        300 
MFMYFLRGSL PWQGLKADTL KERYQKIGDT KRATPIEVLC ENFPEEMATY LRYVRRLDFF 

       310        320        330        340        350        360 
EKPDYDYLRK LFTDLFDRSG FVFDYEYDWA GKPLPTPIGT VHTDLPSQPQ LRDKTQPHSK 

       370        380        390        400        410 
NQALNSTNGE LNADDPTAGH SNAPITAPAE VEVADETKCC CFFKRRKRKS LQRHK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and chromosomal mapping of human casein kinase I gamma 2 (CSNK1G2)."
Kitabayashi A.N., Kusuda J., Hirai M., Hashimoto K.
Genomics 46:133-137(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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].
Tissue: Colon and Muscle.
[7]"Polymorphisms of casein kinase I gamma 2 gene associated with simple febrile seizures in Chinese Han population."
Yinan M., Yu Q., Zhiyue C., Jianjun L., Lie H., Liping Z., Jianhui Z., Fang S., Dingfang B., Qing L., Xiru W.
Neurosci. Lett. 368:2-6(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN BRAIN DEVELOPMENT.
[8]"Metastatic tumor antigen 1 short form (MTA1s) associates with casein kinase I-gamma2, an estrogen-responsive kinase."
Mishra S.K., Yang Z., Mazumdar A., Talukder A.H., Larose L., Kumar R.
Oncogene 23:4422-4429(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS MTA1 KINASE, INTERACTION WITH MTA1, SUBCELLULAR LOCATION, ENZYME REGULATION.
[9]"SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein."
Shirogane T., Jin J., Ang X.L., Harper J.W.
J. Biol. Chem. 280:26863-26872(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PER1 STABILITY.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Ligand-dependent ubiquitination of Smad3 is regulated by casein kinase 1 gamma 2, an inhibitor of TGF-beta signaling."
Guo X., Waddell D.S., Wang W., Wang Z., Liberati N.T., Yong S., Liu X., Wang X.-F.
Oncogene 27:7235-7247(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS SMAD3 KINASE, INTERACTION WITH SMAD3.
[12]"Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the synthesis of sphingomyelin."
Tomishige N., Kumagai K., Kusuda J., Nishijima M., Hanada K.
Mol. Biol. Cell 20:348-357(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS COL4A3BP/CERT KINASE.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"The structure of casein kinase 1 gamma 2."
Bunkoczi G., Rellos P., Das S., Ugochukwu E., Fedorov O., Sobott F., Eswaran J., Amos A., Ball L., Von Delft F., Bullock A., Debreczeni J., Turnbull A., Sundstrom M., Weigelt J., Arrowsmith C., Edwards A., Knapp S.
Submitted (JUL-2011) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 43-353 IN COMPLEX WITH 5-IODOTUBERCIDIN.
[16]"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] LEU-189; GLY-194; THR-196; CYS-206; HIS-206; SER-207; GLN-208; CYS-217 AND MET-223.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U89896 mRNA. Translation: AAB88627.1.
BT009922 mRNA. Translation: AAP88924.1.
AF001177 Transcribed RNA. Translation: AAC00212.1.
AB451278 mRNA. Translation: BAG70092.1.
AB451410 mRNA. Translation: BAG70224.1.
AC005306 Genomic DNA. Translation: AAC26983.1.
CH471139 Genomic DNA. Translation: EAW69430.1.
BC018693 mRNA. Translation: AAH18693.1.
BC018699 mRNA. Translation: AAH18699.1.
BC020972 mRNA. Translation: AAH20972.1.
CCDSCCDS12077.1.
RefSeqNP_001310.3. NM_001319.6.
UniGeneHs.651905.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C47X-ray2.40A/B/C/D43-353[»]
ProteinModelPortalP78368.
SMRP78368. Positions 17-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107839. 12 interactions.
IntActP78368. 5 interactions.
MINTMINT-1473562.
STRING9606.ENSP00000255641.

Chemistry

BindingDBP78368.
ChEMBLCHEMBL2543.
GuidetoPHARMACOLOGY2000.

PTM databases

PhosphoSiteP78368.

Polymorphism databases

DMDM3024060.

Proteomic databases

MaxQBP78368.
PaxDbP78368.
PRIDEP78368.

Protocols and materials databases

DNASU1455.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255641; ENSP00000255641; ENSG00000133275.
GeneID1455.
KEGGhsa:1455.
UCSCuc002lul.4. human.

Organism-specific databases

CTD1455.
GeneCardsGC19P001941.
HGNCHGNC:2455. CSNK1G2.
HPAHPA034868.
MIM602214. gene.
neXtProtNX_P78368.
PharmGKBPA26955.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000182054.
HOVERGENHBG000176.
InParanoidP78368.
KOK08958.
OMAHTKHQVM.
OrthoDBEOG7G1V66.
PhylomeDBP78368.
TreeFamTF313349.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
SignaLinkP78368.

Gene expression databases

ArrayExpressP78368.
BgeeP78368.
CleanExHS_CSNK1G2.
GenevestigatorP78368.

Family and domain databases

InterProIPR022247. Casein_kinase-1_gamma_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF12605. CK1gamma_C. 1 hit.
PF00069. 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

ChiTaRSCSNK1G2. human.
EvolutionaryTraceP78368.
GenomeRNAi1455.
NextBio5975.
PROP78368.
SOURCESearch...

Entry information

Entry nameKC1G2_HUMAN
AccessionPrimary (citable) accession number: P78368
Secondary accession number(s): B5BU42, O00704, Q8WUB1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 144 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

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 19

Human chromosome 19: entries, gene names and cross-references to MIM