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P78368

- KC1G2_HUMAN

UniProt

P78368 - KC1G2_HUMAN

Protein

Casein kinase I isoform gamma-2

Gene

CSNK1G2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    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.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Stimulated by estrogen. Repressed by 5-iodotubercidin (DB04604).1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei75 – 751ATPPROSITE-ProRule annotation
    Active sitei165 – 1651Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi52 – 609ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. magnesium ion binding Source: Ensembl
    3. peptide binding Source: Ensembl
    4. protein binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. protein autophosphorylation Source: Ensembl
    2. protein phosphorylation Source: ProtInc
    3. signal transduction Source: ProtInc
    4. small molecule metabolic process Source: Reactome
    5. sphingolipid biosynthetic process Source: Reactome
    6. sphingolipid metabolic process Source: Reactome
    7. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_115810. Sphingolipid de novo biosynthesis.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    SignaLinkiP78368.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Casein kinase I isoform gamma-2 (EC:2.7.11.1)
    Short name:
    CKI-gamma 2
    Gene namesi
    Name:CSNK1G2
    Synonyms:CK1G2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:2455. CSNK1G2.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26955.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 415415Casein kinase I isoform gamma-2PRO_0000192842Add
    BLAST

    Post-translational modificationi

    Autophosphorylated.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP78368.
    PaxDbiP78368.
    PRIDEiP78368.

    PTM databases

    PhosphoSiteiP78368.

    Expressioni

    Tissue specificityi

    Testis.

    Gene expression databases

    ArrayExpressiP78368.
    BgeeiP78368.
    CleanExiHS_CSNK1G2.
    GenevestigatoriP78368.

    Organism-specific databases

    HPAiHPA034868.

    Interactioni

    Subunit structurei

    Monomer By similarity. Interacts with MTA1 (short isoform) in the cytoplasm. Interacts with SMAD3.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi107839. 12 interactions.
    IntActiP78368. 5 interactions.
    MINTiMINT-1473562.
    STRINGi9606.ENSP00000255641.

    Structurei

    Secondary structure

    1
    415
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi46 – 516
    Beta strandi60 – 656
    Turni66 – 683
    Beta strandi71 – 788
    Helixi86 – 9510
    Turni96 – 983
    Beta strandi105 – 1117
    Beta strandi114 – 1207
    Helixi126 – 1327
    Turni133 – 1353
    Helixi139 – 15820
    Helixi168 – 1703
    Beta strandi171 – 1733
    Turni179 – 1824
    Beta strandi183 – 1864
    Beta strandi193 – 1964
    Turni198 – 2003
    Turni216 – 2183
    Helixi221 – 2244
    Helixi231 – 24717
    Turni251 – 2544
    Beta strandi257 – 2593
    Helixi260 – 27213
    Helixi276 – 2794
    Turni280 – 2823
    Helixi285 – 29511
    Helixi305 – 31814
    Turni328 – 3314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C47X-ray2.40A/B/C/D43-353[»]
    ProteinModelPortaliP78368.
    SMRiP78368. Positions 17-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP78368.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 316271Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000182054.
    HOVERGENiHBG000176.
    InParanoidiP78368.
    KOiK08958.
    OMAiHTKHQVM.
    OrthoDBiEOG7G1V66.
    PhylomeDBiP78368.
    TreeFamiTF313349.

    Family and domain databases

    InterProiIPR022247. 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]
    PfamiPF12605. CK1gamma_C. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P78368-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDFDKKGGKG ETEEGRRMSK AGGGRSSHGI RSSGTSSGVL MVGPNFRVGK    50
    KIGCGNFGEL RLGKNLYTNE YVAIKLEPIK SRAPQLHLEY RFYKQLSATE 100
    GVPQVYYFGP CGKYNAMVLE LLGPSLEDLF DLCDRTFTLK TVLMIAIQLI 150
    TRMEYVHTKS LIYRDVKPEN FLVGRPGTKR QHAIHIIDFG LAKEYIDPET 200
    KKHIPYREHK SLTGTARYMS INTHLGKEQS RRDDLEALGH MFMYFLRGSL 250
    PWQGLKADTL KERYQKIGDT KRATPIEVLC ENFPEEMATY LRYVRRLDFF 300
    EKPDYDYLRK LFTDLFDRSG FVFDYEYDWA GKPLPTPIGT VHTDLPSQPQ 350
    LRDKTQPHSK NQALNSTNGE LNADDPTAGH SNAPITAPAE VEVADETKCC 400
    CFFKRRKRKS LQRHK 415
    Length:415
    Mass (Da):47,457
    Last modified:May 1, 1997 - v1
    Checksum:i036A39148A1DA038
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti113 – 1131K → N in AAP88924. 1 PublicationCurated
    Sequence conflicti113 – 1131K → N in AAH20972. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti189 – 1891F → L.1 Publication
    VAR_042086
    Natural varianti194 – 1941E → G.1 Publication
    VAR_042087
    Natural varianti196 – 1961I → T.1 Publication
    VAR_042088
    Natural varianti206 – 2061Y → C.1 Publication
    VAR_042089
    Natural varianti206 – 2061Y → H.1 Publication
    VAR_042090
    Natural varianti207 – 2071R → S.1 Publication
    VAR_042091
    Natural varianti208 – 2081E → Q.1 Publication
    VAR_042092
    Natural varianti217 – 2171R → C.1 Publication
    VAR_042093
    Natural varianti223 – 2231T → M.1 Publication
    VAR_042094

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS12077.1.
    RefSeqiNP_001310.3. NM_001319.6.
    UniGeneiHs.651905.

    Genome annotation databases

    EnsembliENST00000255641; ENSP00000255641; ENSG00000133275.
    GeneIDi1455.
    KEGGihsa:1455.
    UCSCiuc002lul.4. human.

    Polymorphism databases

    DMDMi3024060.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS12077.1.
    RefSeqi NP_001310.3. NM_001319.6.
    UniGenei Hs.651905.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C47 X-ray 2.40 A/B/C/D 43-353 [» ]
    ProteinModelPortali P78368.
    SMRi P78368. Positions 17-338.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107839. 12 interactions.
    IntActi P78368. 5 interactions.
    MINTi MINT-1473562.
    STRINGi 9606.ENSP00000255641.

    Chemistry

    BindingDBi P78368.
    ChEMBLi CHEMBL2543.
    GuidetoPHARMACOLOGYi 2000.

    PTM databases

    PhosphoSitei P78368.

    Polymorphism databases

    DMDMi 3024060.

    Proteomic databases

    MaxQBi P78368.
    PaxDbi P78368.
    PRIDEi P78368.

    Protocols and materials databases

    DNASUi 1455.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000255641 ; ENSP00000255641 ; ENSG00000133275 .
    GeneIDi 1455.
    KEGGi hsa:1455.
    UCSCi uc002lul.4. human.

    Organism-specific databases

    CTDi 1455.
    GeneCardsi GC19P001941.
    HGNCi HGNC:2455. CSNK1G2.
    HPAi HPA034868.
    MIMi 602214. gene.
    neXtProti NX_P78368.
    PharmGKBi PA26955.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000182054.
    HOVERGENi HBG000176.
    InParanoidi P78368.
    KOi K08958.
    OMAi HTKHQVM.
    OrthoDBi EOG7G1V66.
    PhylomeDBi P78368.
    TreeFami TF313349.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_115810. Sphingolipid de novo biosynthesis.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    SignaLinki P78368.

    Miscellaneous databases

    ChiTaRSi CSNK1G2. human.
    EvolutionaryTracei P78368.
    GenomeRNAii 1455.
    NextBioi 5975.
    PROi P78368.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78368.
    Bgeei P78368.
    CleanExi HS_CSNK1G2.
    Genevestigatori P78368.

    Family and domain databases

    InterProi IPR022247. 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 ]
    Pfami PF12605. CK1gamma_C. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiKC1G2_HUMAN
    AccessioniPrimary (citable) accession number: P78368
    Secondary accession number(s): B5BU42, O00704, Q8WUB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 146 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3