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Casein kinase I isoform gamma-2 (CKI-gamma 2) (EC 2.7.11.1)

 KC1G2_HUMAN             Reviewed;         415 AA.
P78368; B5BU42; O00704; Q8WUB1;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
28-MAR-2018, entry version 180.
RecName: Full=Casein kinase I isoform gamma-2;
Short=CKI-gamma 2;
EC=2.7.11.1;
Name=CSNK1G2; Synonyms=CK1G2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=9403068; DOI=10.1006/geno.1997.4991;
Kitabayashi A.N., Kusuda J., Hirai M., Hashimoto K.;
"Cloning and chromosomal mapping of human casein kinase I gamma 2
(CSNK1G2).";
Genomics 46:133-137(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
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.,
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.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
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., 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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION IN BRAIN DEVELOPMENT.
PubMed=15342122; DOI=10.1016/j.neulet.2004.06.054;
Yinan M., Yu Q., Zhiyue C., Jianjun L., Lie H., Liping Z., Jianhui Z.,
Fang S., Dingfang B., Qing L., Xiru W.;
"Polymorphisms of casein kinase I gamma 2 gene associated with simple
febrile seizures in Chinese Han population.";
Neurosci. Lett. 368:2-6(2004).
[8]
FUNCTION AS MTA1 KINASE, INTERACTION WITH MTA1, SUBCELLULAR LOCATION,
AND ENZYME REGULATION.
PubMed=15077195; DOI=10.1038/sj.onc.1207569;
Mishra S.K., Yang Z., Mazumdar A., Talukder A.H., Larose L., Kumar R.;
"Metastatic tumor antigen 1 short form (MTA1s) associates with casein
kinase I-gamma2, an estrogen-responsive kinase.";
Oncogene 23:4422-4429(2004).
[9]
FUNCTION IN PER1 STABILITY.
PubMed=15917222; DOI=10.1074/jbc.M502862200;
Shirogane T., Jin J., Ang X.L., Harper J.W.;
"SCFbeta-TRCP controls clock-dependent transcription via casein kinase
1-dependent degradation of the mammalian period-1 (Per1) protein.";
J. Biol. Chem. 280:26863-26872(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
FUNCTION AS SMAD3 KINASE, AND INTERACTION WITH SMAD3.
PubMed=18794808; DOI=10.1038/onc.2008.337;
Guo X., Waddell D.S., Wang W., Wang Z., Liberati N.T., Yong S.,
Liu X., Wang X.-F.;
"Ligand-dependent ubiquitination of Smad3 is regulated by casein
kinase 1 gamma 2, an inhibitor of TGF-beta signaling.";
Oncogene 27:7235-7247(2008).
[12]
FUNCTION AS COL4A3BP/CERT KINASE.
PubMed=19005213; DOI=10.1091/mbc.E08-07-0669;
Tomishige N., Kumagai K., Kusuda J., Nishijima M., Hanada K.;
"Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the
synthesis of sphingomyelin.";
Mol. Biol. Cell 20:348-357(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 43-353 IN COMPLEX WITH
5-IODOTUBERCIDIN.
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.;
"The structure of casein kinase 1 gamma 2.";
Submitted (JUL-2011) to the PDB data bank.
[17]
VARIANTS [LARGE SCALE ANALYSIS] LEU-189; GLY-194; THR-196; CYS-206;
HIS-206; SER-207; GLN-208; CYS-217 AND MET-223.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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. {ECO:0000269|PubMed:15077195,
ECO:0000269|PubMed:15342122, ECO:0000269|PubMed:15917222,
ECO:0000269|PubMed:18794808, ECO:0000269|PubMed:19005213}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Stimulated by estrogen. Repressed by 5-
iodotubercidin (DB04604). {ECO:0000269|PubMed:15077195}.
-!- SUBUNIT: Monomer (By similarity). Interacts with MTA1 (short
isoform) in the cytoplasm. Interacts with SMAD3. {ECO:0000250,
ECO:0000269|PubMed:15077195, ECO:0000269|PubMed:18794808,
ECO:0000269|Ref.16}.
-!- INTERACTION:
Q92624:APPBP2; NbExp=3; IntAct=EBI-748380, EBI-743771;
Q9Y5P4:COL4A3BP; NbExp=4; IntAct=EBI-748380, EBI-739994;
Q9Y5P4-2:COL4A3BP; NbExp=4; IntAct=EBI-748380, EBI-11156432;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-748380, EBI-10172290;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15077195}.
-!- TISSUE SPECIFICITY: Testis.
-!- PTM: Autophosphorylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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EMBL; U89896; AAB88627.1; -; mRNA.
EMBL; BT009922; AAP88924.1; -; mRNA.
EMBL; AF001177; AAC00212.1; -; Transcribed_RNA.
EMBL; AB451278; BAG70092.1; -; mRNA.
EMBL; AB451410; BAG70224.1; -; mRNA.
EMBL; AC005306; AAC26983.1; -; Genomic_DNA.
EMBL; CH471139; EAW69430.1; -; Genomic_DNA.
EMBL; BC018693; AAH18693.1; -; mRNA.
EMBL; BC018699; AAH18699.1; -; mRNA.
EMBL; BC020972; AAH20972.1; -; mRNA.
CCDS; CCDS12077.1; -.
RefSeq; NP_001310.3; NM_001319.6.
UniGene; Hs.651905; -.
PDB; 2C47; X-ray; 2.40 A; A/B/C/D=43-353.
PDBsum; 2C47; -.
ProteinModelPortal; P78368; -.
SMR; P78368; -.
BioGrid; 107839; 35.
IntAct; P78368; 13.
MINT; P78368; -.
STRING; 9606.ENSP00000255641; -.
BindingDB; P78368; -.
ChEMBL; CHEMBL2543; -.
DrugBank; DB04604; 5-iodotubercidin.
DrugBank; DB03083; IC261.
DrugBank; DB03693; N-(2-Aminoethyl)-5-Chloroisoquinoline-8-Sulfonamide.
GuidetoPHARMACOLOGY; 2000; -.
iPTMnet; P78368; -.
PhosphoSitePlus; P78368; -.
SwissPalm; P78368; -.
BioMuta; CSNK1G2; -.
DMDM; 3024060; -.
EPD; P78368; -.
MaxQB; P78368; -.
PaxDb; P78368; -.
PeptideAtlas; P78368; -.
PRIDE; P78368; -.
DNASU; 1455; -.
Ensembl; ENST00000255641; ENSP00000255641; ENSG00000133275.
GeneID; 1455; -.
KEGG; hsa:1455; -.
UCSC; uc002lul.5; human.
CTD; 1455; -.
DisGeNET; 1455; -.
EuPathDB; HostDB:ENSG00000133275.15; -.
GeneCards; CSNK1G2; -.
HGNC; HGNC:2455; CSNK1G2.
HPA; HPA034868; -.
HPA; HPA056572; -.
MIM; 602214; gene.
neXtProt; NX_P78368; -.
OpenTargets; ENSG00000133275; -.
PharmGKB; PA26955; -.
eggNOG; KOG1165; Eukaryota.
eggNOG; ENOG410XNXP; LUCA.
GeneTree; ENSGT00760000119040; -.
HOGENOM; HOG000182054; -.
HOVERGEN; HBG000176; -.
InParanoid; P78368; -.
KO; K08958; -.
OMA; NAPITAN; -.
OrthoDB; EOG091G0F3Z; -.
PhylomeDB; P78368; -.
TreeFam; TF313349; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-1660661; Sphingolipid de novo biosynthesis.
Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
SignaLink; P78368; -.
SIGNOR; P78368; -.
ChiTaRS; CSNK1G2; human.
EvolutionaryTrace; P78368; -.
GenomeRNAi; 1455; -.
PRO; PR:P78368; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000133275; -.
CleanEx; HS_CSNK1G2; -.
ExpressionAtlas; P78368; baseline and differential.
Genevisible; P78368; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
GO; GO:0042277; F:peptide binding; IEA:Ensembl.
GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0006897; P:endocytosis; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
GO; GO:0016055; P:Wnt signaling pathway; IBA:GO_Central.
InterPro; IPR022247; Casein_kinase-1_gamma_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF12605; CK1gamma_C; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm; Kinase;
Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
CHAIN 1 415 Casein kinase I isoform gamma-2.
/FTId=PRO_0000192842.
DOMAIN 46 316 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 52 60 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 165 165 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 75 75 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
VARIANT 189 189 F -> L (in dbSNP:rs55702630).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042086.
VARIANT 194 194 E -> G (in dbSNP:rs55780547).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042087.
VARIANT 196 196 I -> T (in dbSNP:rs55923222).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042088.
VARIANT 206 206 Y -> C (in dbSNP:rs56264133).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042089.
VARIANT 206 206 Y -> H (in dbSNP:rs56108438).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042090.
VARIANT 207 207 R -> S (in dbSNP:rs56340103).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042091.
VARIANT 208 208 E -> Q (in dbSNP:rs55818316).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042092.
VARIANT 217 217 R -> C (in dbSNP:rs55754218).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042093.
VARIANT 223 223 T -> M (in dbSNP:rs56038081).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042094.
CONFLICT 113 113 K -> N (in Ref. 2; AAP88924 and 6;
AAH20972). {ECO:0000305}.
STRAND 46 51 {ECO:0000244|PDB:2C47}.
STRAND 60 65 {ECO:0000244|PDB:2C47}.
TURN 66 68 {ECO:0000244|PDB:2C47}.
STRAND 71 78 {ECO:0000244|PDB:2C47}.
HELIX 86 95 {ECO:0000244|PDB:2C47}.
TURN 96 98 {ECO:0000244|PDB:2C47}.
STRAND 105 111 {ECO:0000244|PDB:2C47}.
STRAND 114 120 {ECO:0000244|PDB:2C47}.
HELIX 126 132 {ECO:0000244|PDB:2C47}.
TURN 133 135 {ECO:0000244|PDB:2C47}.
HELIX 139 158 {ECO:0000244|PDB:2C47}.
HELIX 168 170 {ECO:0000244|PDB:2C47}.
STRAND 171 173 {ECO:0000244|PDB:2C47}.
TURN 179 182 {ECO:0000244|PDB:2C47}.
STRAND 183 186 {ECO:0000244|PDB:2C47}.
STRAND 193 196 {ECO:0000244|PDB:2C47}.
TURN 198 200 {ECO:0000244|PDB:2C47}.
TURN 216 218 {ECO:0000244|PDB:2C47}.
HELIX 221 224 {ECO:0000244|PDB:2C47}.
HELIX 231 247 {ECO:0000244|PDB:2C47}.
TURN 251 254 {ECO:0000244|PDB:2C47}.
STRAND 257 259 {ECO:0000244|PDB:2C47}.
HELIX 260 272 {ECO:0000244|PDB:2C47}.
HELIX 276 279 {ECO:0000244|PDB:2C47}.
TURN 280 282 {ECO:0000244|PDB:2C47}.
HELIX 285 295 {ECO:0000244|PDB:2C47}.
HELIX 305 318 {ECO:0000244|PDB:2C47}.
TURN 328 331 {ECO:0000244|PDB:2C47}.
SEQUENCE 415 AA; 47457 MW; 036A39148A1DA038 CRC64;
MDFDKKGGKG ETEEGRRMSK AGGGRSSHGI RSSGTSSGVL MVGPNFRVGK KIGCGNFGEL
RLGKNLYTNE YVAIKLEPIK SRAPQLHLEY RFYKQLSATE GVPQVYYFGP CGKYNAMVLE
LLGPSLEDLF DLCDRTFTLK TVLMIAIQLI TRMEYVHTKS LIYRDVKPEN FLVGRPGTKR
QHAIHIIDFG LAKEYIDPET KKHIPYREHK SLTGTARYMS INTHLGKEQS RRDDLEALGH
MFMYFLRGSL PWQGLKADTL KERYQKIGDT KRATPIEVLC ENFPEEMATY LRYVRRLDFF
EKPDYDYLRK LFTDLFDRSG FVFDYEYDWA GKPLPTPIGT VHTDLPSQPQ LRDKTQPHSK
NQALNSTNGE LNADDPTAGH SNAPITAPAE VEVADETKCC CFFKRRKRKS LQRHK


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CSB-EL006071RA Rat Casein kinase I isoform gamma-3(CSNK1G3) ELISA kit SpeciesRat 96T
CSB-EL006069BO Bovine Casein kinase I isoform gamma-1(CSNK1G1) ELISA kit 96T
CSB-EL006070MO Mouse Casein kinase I isoform gamma-2(CSNK1G2) ELISA kit 96T
CSB-EL006071MO Mouse Casein kinase I isoform gamma-3(CSNK1G3) ELISA kit 96T
CG70 Recombinant Human Casein kinase I isoform gamma-2_CSNK1G2 10 ug
CSB-EL006069HU Human Casein kinase I isoform gamma-1(CSNK1G1) ELISA kit 96T
CSB-EL006070HU Human Casein kinase I isoform gamma-2(CSNK1G2) ELISA kit 96T
CSB-EL006071HU Human Casein kinase I isoform gamma-3(CSNK1G3) ELISA kit 96T
EIAAB30892 Homo sapiens,Human,PHKG2,PHK-gamma-T,Phosphorylase b kinase gamma catalytic chain, testis_liver isoform,Phosphorylase kinase subunit gamma-2,PSK-C3,Serine_threonine-protein kinase PHKG2
CSB-EL006071MO Mouse Casein kinase I isoform gamma-3(CSNK1G3) ELISA kit SpeciesMouse 96T


 

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