KC1G2_MOUSE
ID KC1G2_MOUSE Reviewed; 415 AA.
AC Q8BVP5;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Casein kinase I isoform gamma-2;
DE Short=CKI-gamma 2;
DE EC=2.7.11.1;
GN Name=Csnk1g2; Synonyms=Ck1g2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP FUNCTION AS MTA1 KINASE, INTERACTION WITH MTA1, SUBCELLULAR LOCATION, AND
RP ACTIVITY REGULATION.
RX PubMed=15077195; DOI=10.1038/sj.onc.1207569;
RA Mishra S.K., Yang Z., Mazumdar A., Talukder A.H., Larose L., Kumar R.;
RT "Metastatic tumor antigen 1 short form (MTA1s) associates with casein
RT kinase I-gamma2, an estrogen-responsive kinase.";
RL Oncogene 23:4422-4429(2004).
RN [3]
RP FUNCTION IN SYNAPTIC TRANSMISSION, AND TISSUE SPECIFICITY.
RX PubMed=16014721; DOI=10.1523/jneurosci.1082-05.2005;
RA Chergui K., Svenningsson P., Greengard P.;
RT "Physiological role for casein kinase 1 in glutamatergic synaptic
RT transmission.";
RL J. Neurosci. 25:6601-6609(2005).
CC -!- FUNCTION: Serine/threonine-protein kinase. Casein kinases are
CC operationally defined by their preferential utilization of acidic
CC proteins such as caseins as substrates. It can phosphorylate a large
CC number of proteins. Participates in Wnt signaling (By similarity).
CC Phosphorylates COL4A3BP/CERT, MTA1 and SMAD3. Involved in brain
CC development and vesicular trafficking and neurotransmitter releasing
CC from small synaptic vesicles. Regulates fast synaptic transmission
CC mediated by glutamate. SMAD3 phosphorylation promotes its ligand-
CC dependent ubiquitination and subsequent proteasome degradation, thus
CC inhibiting SMAD3-mediated TGF-beta responses. Hyperphosphorylation of
CC the serine-repeat motif of COL4A3BP/CERT leads to its inactivation by
CC dissociation from the Golgi complex, thus down-regulating ER-to-Golgi
CC transport of ceramide and sphingomyelin synthesis. Triggers PER1
CC proteasomal degradation probably through phosphorylation. {ECO:0000250,
CC ECO:0000269|PubMed:15077195, ECO:0000269|PubMed:16014721}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Stimulated by estrogen.
CC {ECO:0000269|PubMed:15077195}.
CC -!- SUBUNIT: Monomer. Interacts with MTA1 (short isoform) in the cytoplasm.
CC Interacts with SMAD3. {ECO:0000269|PubMed:15077195}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:P78368}. Cytoplasm
CC {ECO:0000250|UniProtKB:P78368}.
CC -!- TISSUE SPECIFICITY: Expressed in both the striatum and the neocortex.
CC {ECO:0000269|PubMed:16014721}.
CC -!- DOMAIN: The phospho-regulated basic and hydrophobic (PRBH) motif is
CC sufficient and important for interaction with phospholipids permitting
CC cortical localization (By similarity). Phosphorylation of the PRBH
CC motif by aPKC inhibits the association of the protein with the cortical
CC membrane (By similarity). {ECO:0000250|UniProtKB:P78368}.
CC -!- PTM: Autophosphorylated. Phosphorylated by aPKC which promotes
CC dissociation from the cell cortex. {ECO:0000250|UniProtKB:P78368}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR EMBL; AK077076; BAC36596.1; -; mRNA.
DR EMBL; AK132871; BAE21399.1; -; mRNA.
DR CCDS; CCDS48638.1; -.
DR RefSeq; NP_001153063.1; NM_001159591.1.
DR RefSeq; NP_598763.1; NM_134002.2.
DR RefSeq; XP_006513074.1; XM_006513011.1.
DR AlphaFoldDB; Q8BVP5; -.
DR SMR; Q8BVP5; -.
DR STRING; 10090.ENSMUSP00000078706; -.
DR iPTMnet; Q8BVP5; -.
DR PhosphoSitePlus; Q8BVP5; -.
DR SwissPalm; Q8BVP5; -.
DR EPD; Q8BVP5; -.
DR MaxQB; Q8BVP5; -.
DR PeptideAtlas; Q8BVP5; -.
DR PRIDE; Q8BVP5; -.
DR ProteomicsDB; 269243; -.
DR Antibodypedia; 22865; 488 antibodies from 31 providers.
DR DNASU; 103236; -.
DR Ensembl; ENSMUST00000085435; ENSMUSP00000082560; ENSMUSG00000003345.
DR GeneID; 103236; -.
DR KEGG; mmu:103236; -.
DR UCSC; uc007geb.2; mouse.
DR CTD; 1455; -.
DR MGI; MGI:1920014; Csnk1g2.
DR VEuPathDB; HostDB:ENSMUSG00000003345; -.
DR eggNOG; KOG1165; Eukaryota.
DR GeneTree; ENSGT00940000156470; -.
DR HOGENOM; CLU_019279_2_0_1; -.
DR InParanoid; Q8BVP5; -.
DR OMA; HANMIHI; -.
DR OrthoDB; 889559at2759; -.
DR PhylomeDB; Q8BVP5; -.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR BioGRID-ORCS; 103236; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Csnk1g2; mouse.
DR PRO; PR:Q8BVP5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BVP5; protein.
DR Bgee; ENSMUSG00000003345; Expressed in seminiferous tubule of testis and 269 other tissues.
DR ExpressionAtlas; Q8BVP5; baseline and differential.
DR Genevisible; Q8BVP5; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR022247; Casein_kinase-1_gamma_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12605; CK1gamma_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Wnt signaling pathway.
FT CHAIN 1..415
FT /note="Casein kinase I isoform gamma-2"
FT /id="PRO_0000192843"
FT DOMAIN 46..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..415
FT /note="Phospho-regulated basic and hydrophobic (PRBH)
FT motif"
FT /evidence="ECO:0000250|UniProtKB:P78368"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 52..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 415 AA; 47582 MW; C5EE5AFCF2F44677 CRC64;
MDFDKKGGKG ELEEGRRMSK TGTSRSNHGV RSSGTSSGVL MVGPNFRVGK KIGCGNFGEL
RLGKNLYTNE YVAIKLEPIK SRAPQLHLEY RFYKQLSTTE GVPQVYYFGP CGKYNAMVLE
LLGPSLEDLF DLCDRTFTLK TVLMIAIQLI TRMEYVHTKS LIYRDVKPEN FLVGRPGSKR
QHSIHIIDFG LAKEYIDPET KKHIPYREHK SLTGTARYMS INTHLGKEQS RRDDLEALGH
MFMYFLRGSL PWQGLKADTL KERYQKIGDT KRATPIEVLC ESFPEEMATY LRYVRRLDFF
EKPDYDYLRK LFTDLFDRSG YVFDYEYDWA GKPLPTPIGT VHPDVPSQPP HRDKAQLHTK
NQALNSTNGE LNTDDPTAGH SNAPIAAPAE VEVADETKCC CFFKRRKRKS LQRHK
