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Q8BVP5 (KC1G2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity. 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.2 Ref.3

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Stimulated by estrogen. Ref.2

Subunit structure

Monomer. Interacts with MTA1 (short isoform) in the cytoplasm. Interacts with SMAD3. Ref.2

Subcellular location

Cytoplasm By similarity Ref.2.

Tissue specificity

Expressed in both the striatum and the neocortex. Ref.3

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 processWnt signaling pathway
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   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 – 415415Casein kinase I isoform gamma-2
PRO_0000192843

Regions

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

Sites

Active site1651Proton acceptor By similarity
Binding site751ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BVP5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C5EE5AFCF2F44677

FASTA41547,582
        10         20         30         40         50         60 
MDFDKKGGKG ELEEGRRMSK TGTSRSNHGV RSSGTSSGVL MVGPNFRVGK KIGCGNFGEL 

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

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

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

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

       310        320        330        340        350        360 
EKPDYDYLRK LFTDLFDRSG YVFDYEYDWA GKPLPTPIGT VHPDVPSQPP HRDKAQLHTK 

       370        380        390        400        410 
NQALNSTNGE LNTDDPTAGH SNAPIAAPAE VEVADETKCC CFFKRRKRKS LQRHK 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[2]"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.
[3]"Physiological role for casein kinase 1 in glutamatergic synaptic transmission."
Chergui K., Svenningsson P., Greengard P.
J. Neurosci. 25:6601-6609(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SYNAPTIC TRANSMISSION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK077076 mRNA. Translation: BAC36596.1.
AK132871 mRNA. Translation: BAE21399.1.
CCDSCCDS48638.1.
RefSeqNP_001153063.1. NM_001159591.1.
NP_598763.1. NM_134002.2.
XP_006513074.1. XM_006513011.1.
UniGeneMm.29873.

3D structure databases

ProteinModelPortalQ8BVP5.
SMRQ8BVP5. Positions 44-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000078706.

PTM databases

PhosphoSiteQ8BVP5.

Proteomic databases

PaxDbQ8BVP5.
PRIDEQ8BVP5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000085435; ENSMUSP00000082560; ENSMUSG00000003345.
GeneID103236.
KEGGmmu:103236.
UCSCuc007geb.2. mouse.

Organism-specific databases

CTD1455.
MGIMGI:1920014. Csnk1g2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110718.
HOGENOMHOG000182054.
HOVERGENHBG000176.
KOK08958.
PhylomeDBQ8BVP5.

Gene expression databases

ArrayExpressQ8BVP5.
BgeeQ8BVP5.
CleanExMM_CSNK1G2.
GenevestigatorQ8BVP5.

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. mouse.
NextBio355866.
PROQ8BVP5.
SOURCESearch...

Entry information

Entry nameKC1G2_MOUSE
AccessionPrimary (citable) accession number: Q8BVP5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot