Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P48729

- KC1A_HUMAN

UniProt

P48729 - KC1A_HUMAN

Protein

Casein kinase I isoform alpha

Gene

CSNK1A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (23 May 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 CTNNB1 at 'Ser-45'. May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei46 – 461ATPPROSITE-ProRule annotation
    Active sitei136 – 1361Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi23 – 319ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein kinase activity Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. mitotic nuclear division Source: UniProtKB-KW
    3. protein phosphorylation Source: UniProtKB
    4. signal transduction Source: ProtInc
    5. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    SignaLinkiP48729.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Casein kinase I isoform alpha (EC:2.7.11.1)
    Short name:
    CKI-alpha
    Alternative name(s):
    CK1
    Gene namesi
    Name:CSNK1A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:2451. CSNK1A1.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosomecentromerekinetochore. Nucleus speckle
    Note: Localizes to the centrosome in interphase cells, and to kinetochore fibers during mitosis.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. condensed chromosome kinetochore Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. membrane Source: UniProtKB
    5. nuclear speck Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26951.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 337336Casein kinase I isoform alphaPRO_0000192822Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei8 – 81N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP48729.
    PaxDbiP48729.
    PRIDEiP48729.

    PTM databases

    PhosphoSiteiP48729.

    Expressioni

    Gene expression databases

    ArrayExpressiP48729.
    BgeeiP48729.
    CleanExiHS_CSNK1A1.
    GenevestigatoriP48729.

    Organism-specific databases

    HPAiCAB016680.

    Interactioni

    Subunit structurei

    Monomer. Interacts with the Axin complex. Interacts with TUT1, leading to TUT1 phosphorylation.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MDM2Q009873EBI-1383726,EBI-389668
    MDM4O151512EBI-1383726,EBI-398437
    RIPK1Q135465EBI-1383726,EBI-358507

    Protein-protein interaction databases

    BioGridi107836. 74 interactions.
    DIPiDIP-40367N.
    IntActiP48729. 39 interactions.
    MINTiMINT-193806.
    STRINGi9606.ENSP00000261798.

    Structurei

    3D structure databases

    ProteinModelPortaliP48729.
    SMRiP48729. Positions 17-302.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 285269Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG000176.
    KOiK08957.
    OMAiYKILHGG.
    OrthoDBiEOG7CZK5W.
    PhylomeDBiP48729.
    TreeFamiTF354246.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. 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]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P48729-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ    50
    KARHPQLLYE SKLYKILQGG VGIPHIRWYG QEKDYNVLVM DLLGPSLEDL 100
    FNFCSRRFTM KTVLMLADQM ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC 150
    NKLFLIDFGL AKKYRDNRTR QHIPYREDKN LTGTARYASI NAHLGIEQSR 200
    RDDMESLGYV LMYFNRTSLP WQGLKAATKK QKYEKISEKK MSTPVEVLCK 250
    GFPAEFAMYL NYCRGLRFEE APDYMYLRQL FRILFRTLNH QYDYTFDWTM 300
    LKQKAAQQAA SSSGQGQQAQ TPTGKQTDKT KSNMKGF 337
    Length:337
    Mass (Da):38,915
    Last modified:May 23, 2003 - v2
    Checksum:i1B2085AE33CAFAC2
    GO
    Isoform 2 (identifier: P48729-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         152-152: K → KCLESPVGKRKRSMTVSTSQDPSFSGLNQ

    Note: Contains a phosphoserine at position 156.

    Show »
    Length:365
    Mass (Da):41,937
    Checksum:i11756FB15947D9F5
    GO
    Isoform 3 (identifier: P48729-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         324-335: Missing.

    Show »
    Length:325
    Mass (Da):37,567
    Checksum:iB84DC84BDDC17854
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451V → L in CAA56710. (PubMed:8050587)Curated
    Sequence conflicti74 – 741P → T in AAV38633. 1 PublicationCurated
    Sequence conflicti122 – 1221S → A AA sequence (PubMed:1409656)Curated
    Sequence conflicti129 – 1291T → TK AA sequence (PubMed:1409656)Curated
    Sequence conflicti231 – 2311Q → K in AAH08717. (PubMed:15489334)Curated
    Sequence conflicti250 – 2501K → E in AAY84562. 1 PublicationCurated
    Sequence conflicti330 – 3301T → S in CAA56710. (PubMed:8050587)Curated
    Sequence conflicti330 – 3301T → S in AAV38632. 1 PublicationCurated
    Sequence conflicti330 – 3301T → S in AAV38633. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti297 – 2971D → H in a breast pleomorphic lobular carcinoma sample; somatic mutation. 1 Publication
    VAR_042073

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei152 – 1521K → KCLESPVGKRKRSMTVSTSQ DPSFSGLNQ in isoform 2. 1 PublicationVSP_035455
    Alternative sequencei324 – 33512Missing in isoform 3. 2 PublicationsVSP_055131Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80693 mRNA. Translation: CAA56710.1.
    L37042 mRNA. Translation: AAC41760.1.
    AF218004 mRNA. Translation: AAG17246.1.
    AK294942 mRNA. Translation: BAG58018.1.
    CR542206 mRNA. Translation: CAG47002.1.
    BT019829 mRNA. Translation: AAV38632.1.
    BT019830 mRNA. Translation: AAV38633.1.
    DQ082865 mRNA. Translation: AAY84562.1.
    AC021078 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61767.1.
    CH471062 Genomic DNA. Translation: EAW61769.1.
    CH471062 Genomic DNA. Translation: EAW61773.1.
    CH471062 Genomic DNA. Translation: EAW61774.1.
    CH471062 Genomic DNA. Translation: EAW61776.1.
    BC008717 mRNA. Translation: AAH08717.1.
    CCDSiCCDS47303.1. [P48729-1]
    CCDS47304.1. [P48729-2]
    CCDS64291.1. [P48729-3]
    PIRiA57011.
    S46254.
    RefSeqiNP_001020276.1. NM_001025105.2. [P48729-2]
    NP_001258670.1. NM_001271741.1.
    NP_001258671.1. NM_001271742.1.
    NP_001883.4. NM_001892.5. [P48729-1]
    UniGeneiHs.529862.
    Hs.712555.

    Genome annotation databases

    EnsembliENST00000261798; ENSP00000261798; ENSG00000113712. [P48729-3]
    ENST00000377843; ENSP00000367074; ENSG00000113712. [P48729-1]
    ENST00000515768; ENSP00000421689; ENSG00000113712. [P48729-2]
    GeneIDi1452.
    KEGGihsa:1452.
    UCSCiuc003lqw.2. human. [P48729-2]
    uc003lqx.2. human. [P48729-1]

    Polymorphism databases

    DMDMi31077177.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80693 mRNA. Translation: CAA56710.1 .
    L37042 mRNA. Translation: AAC41760.1 .
    AF218004 mRNA. Translation: AAG17246.1 .
    AK294942 mRNA. Translation: BAG58018.1 .
    CR542206 mRNA. Translation: CAG47002.1 .
    BT019829 mRNA. Translation: AAV38632.1 .
    BT019830 mRNA. Translation: AAV38633.1 .
    DQ082865 mRNA. Translation: AAY84562.1 .
    AC021078 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61767.1 .
    CH471062 Genomic DNA. Translation: EAW61769.1 .
    CH471062 Genomic DNA. Translation: EAW61773.1 .
    CH471062 Genomic DNA. Translation: EAW61774.1 .
    CH471062 Genomic DNA. Translation: EAW61776.1 .
    BC008717 mRNA. Translation: AAH08717.1 .
    CCDSi CCDS47303.1. [P48729-1 ]
    CCDS47304.1. [P48729-2 ]
    CCDS64291.1. [P48729-3 ]
    PIRi A57011.
    S46254.
    RefSeqi NP_001020276.1. NM_001025105.2. [P48729-2 ]
    NP_001258670.1. NM_001271741.1.
    NP_001258671.1. NM_001271742.1.
    NP_001883.4. NM_001892.5. [P48729-1 ]
    UniGenei Hs.529862.
    Hs.712555.

    3D structure databases

    ProteinModelPortali P48729.
    SMRi P48729. Positions 17-302.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107836. 74 interactions.
    DIPi DIP-40367N.
    IntActi P48729. 39 interactions.
    MINTi MINT-193806.
    STRINGi 9606.ENSP00000261798.

    Chemistry

    BindingDBi P48729.
    ChEMBLi CHEMBL3038493.
    GuidetoPHARMACOLOGYi 1995.

    PTM databases

    PhosphoSitei P48729.

    Polymorphism databases

    DMDMi 31077177.

    Proteomic databases

    MaxQBi P48729.
    PaxDbi P48729.
    PRIDEi P48729.

    Protocols and materials databases

    DNASUi 1452.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261798 ; ENSP00000261798 ; ENSG00000113712 . [P48729-3 ]
    ENST00000377843 ; ENSP00000367074 ; ENSG00000113712 . [P48729-1 ]
    ENST00000515768 ; ENSP00000421689 ; ENSG00000113712 . [P48729-2 ]
    GeneIDi 1452.
    KEGGi hsa:1452.
    UCSCi uc003lqw.2. human. [P48729-2 ]
    uc003lqx.2. human. [P48729-1 ]

    Organism-specific databases

    CTDi 1452.
    GeneCardsi GC05M148854.
    HGNCi HGNC:2451. CSNK1A1.
    HPAi CAB016680.
    MIMi 600505. gene.
    neXtProti NX_P48729.
    PharmGKBi PA26951.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG000176.
    KOi K08957.
    OMAi YKILHGG.
    OrthoDBi EOG7CZK5W.
    PhylomeDBi P48729.
    TreeFami TF354246.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 2681.
    Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    SignaLinki P48729.

    Miscellaneous databases

    ChiTaRSi CSNK1A1. human.
    GeneWikii Casein_kinase_1,_alpha_1.
    GenomeRNAii 1452.
    NextBioi 5955.
    PROi P48729.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48729.
    Bgeei P48729.
    CleanExi HS_CSNK1A1.
    Genevestigatori P48729.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami 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 localization of the gene coding for human protein kinase CK1."
      Tapia C., Featherstone T., Gomez C., Taillon-Miller P., Allende C.C., Allende J.E.
      FEBS Lett. 349:307-312(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family."
      Fish K.J., Cegielska A., Getman M.E., Landes G.M., Virshup D.M.
      J. Biol. Chem. 270:14875-14883(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Huang B., Li H., Yang S.
      Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    8. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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] (ISOFORM 1).
      Tissue: Lung.
    11. "Cell cycle-dependent localization of casein kinase I to mitotic spindles."
      Brockman J.L., Gross S.D., Sussman M.R., Anderson R.A.
      Proc. Natl. Acad. Sci. U.S.A. 89:9454-9458(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 65-83; 111-152 AND 179-204, FUNCTION, SUBCELLULAR LOCATION.
    12. "Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism."
      Liu C., Li Y., Semenov M., Han C., Baeg G.-H., Tan Y., Zhang Z., Lin X., He X.
      Cell 108:837-847(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN WNT SIGNALING.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "CKIalpha is associated with and phosphorylates star-PAP and is also required for expression of select star-PAP target messenger RNAs."
      Gonzales M.L., Mellman D.L., Anderson R.A.
      J. Biol. Chem. 283:12665-12673(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TUT1, SUBCELLULAR LOCATION.
    15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    18. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 AND LYS-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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: VARIANT [LARGE SCALE ANALYSIS] HIS-297.

    Entry informationi

    Entry nameiKC1A_HUMAN
    AccessioniPrimary (citable) accession number: P48729
    Secondary accession number(s): D3DQG0
    , D3DQG1, Q4JJA0, Q5U046, Q5U047, Q6FGA2, Q71TU5, Q96HD2, Q9UDK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: May 23, 2003
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3