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P49760

- CLK2_HUMAN

UniProt

P49760 - CLK2_HUMAN

Protein

Dual specificity protein kinase CLK2

Gene

CLK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    5,6-dichloro-1-b-D-ribofuranosylbenzimidazole (DRB) inhibits autophosphorylation. TG003 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei193 – 1931ATPPROSITE-ProRule annotation
    Active sitei290 – 2901Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi169 – 1779ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. negative regulation of gluconeogenesis Source: UniProtKB
    2. protein autophosphorylation Source: UniProtKB
    3. protein phosphorylation Source: UniProtKB
    4. regulation of RNA splicing Source: UniProtKB
    5. response to ionizing radiation Source: UniProtKB
    6. response to retinoic acid Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.12.1. 2681.
    SignaLinkiP49760.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein kinase CLK2 (EC:2.7.12.1)
    Alternative name(s):
    CDC-like kinase 2
    Gene namesi
    Name:CLK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:2069. CLK2.

    Subcellular locationi

    Isoform 1 : Nucleus. Nucleus speckle
    Note: Inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle.By similarity
    Isoform 2 : Nucleus speckle
    Note: Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles.

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26595.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 499499Dual specificity protein kinase CLK2PRO_0000085868Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei34 – 341Phosphoserine; by PKB/AKT12 Publications
    Modified residuei98 – 981Phosphoserine; by autocatalysisBy similarity
    Modified residuei99 – 991Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei127 – 1271Phosphothreonine; by PKB/AKT12 Publications
    Modified residuei142 – 1421Phosphoserine; by autocatalysis4 Publications
    Modified residuei153 – 1531Phosphotyrosine2 Publications
    Modified residuei344 – 3441Phosphothreonine; by PKB/AKT2By similarity

    Post-translational modificationi

    Autophosphorylates on all three types of residues. Phosphorylation on Ser-34 and Thr-127 by AKT1 is induced by ionizing radiation or insulin. Phosphorylation plays a critical role in cell proliferation following low dose radiation and prevents cell death following high dose radiation. Phosphorylation at Thr-344 by PKB/AKT2 induces its kinase activity which is required for its stability. The phosphorylation status at Ser-142 influences its subnuclear localization; inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP49760.
    PaxDbiP49760.
    PRIDEiP49760.

    PTM databases

    PhosphoSiteiP49760.

    Expressioni

    Tissue specificityi

    Endothelial cells.1 Publication

    Gene expression databases

    ArrayExpressiP49760.
    BgeeiP49760.
    CleanExiHS_CLK2.
    GenevestigatoriP49760.

    Organism-specific databases

    HPAiHPA055366.

    Interactioni

    Subunit structurei

    Interacts with RBMX. Interacts with AKT1 and UBL5.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CLK3P497613EBI-750020,EBI-745579
    SNRNP70P086212EBI-750020,EBI-1049228

    Protein-protein interaction databases

    BioGridi107607. 40 interactions.
    IntActiP49760. 30 interactions.
    MINTiMINT-1683264.
    STRINGi9606.ENSP00000354856.

    Structurei

    Secondary structure

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni146 – 1494
    Turni160 – 1623
    Beta strandi163 – 17210
    Beta strandi175 – 1828
    Turni183 – 1875
    Beta strandi189 – 1957
    Helixi199 – 21820
    Beta strandi229 – 2357
    Beta strandi238 – 2447
    Helixi250 – 2567
    Turni257 – 2593
    Helixi264 – 28320
    Helixi293 – 2953
    Beta strandi296 – 2994
    Beta strandi317 – 3193
    Beta strandi323 – 3253
    Beta strandi332 – 3365
    Helixi345 – 3473
    Helixi350 – 3534
    Helixi361 – 37616
    Helixi386 – 39712
    Helixi402 – 4076
    Helixi411 – 4133
    Helixi426 – 4349
    Helixi438 – 4414
    Helixi447 – 45913
    Turni464 – 4663
    Helixi470 – 4756
    Helixi477 – 4793
    Helixi480 – 4834

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NR9X-ray2.89A/B/C135-496[»]
    ProteinModelPortaliP49760.
    SMRiP49760. Positions 136-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49760.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini163 – 479317Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000203417.
    HOVERGENiHBG107720.
    InParanoidiP49760.
    KOiK08823.
    OMAiGHLIYRV.
    PhylomeDBiP49760.
    TreeFamiTF101041.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 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.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49760-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MPHPRRYHSS ERGSRGSYRE HYRSRKHKRR RSRSWSSSSD RTRRRRREDS    50
    YHVRSRSSYD DRSSDRRVYD RRYCGSYRRN DYSRDRGDAY YDTDYRHSYE 100
    YQRENSSYRS QRSSRRKHRR RRRRSRTFSR SSSQHSSRRA KSVEDDAEGH 150
    LIYHVGDWLQ ERYEIVSTLG EGTFGRVVQC VDHRRGGARV ALKIIKNVEK 200
    YKEAARLEIN VLEKINEKDP DNKNLCVQMF DWFDYHGHMC ISFELLGLST 250
    FDFLKDNNYL PYPIHQVRHM AFQLCQAVKF LHDNKLTHTD LKPENILFVN 300
    SDYELTYNLE KKRDERSVKS TAVRVVDFGS ATFDHEHHST IVSTRHYRAP 350
    EVILELGWSQ PCDVWSIGCI IFEYYVGFTL FQTHDNREHL AMMERILGPI 400
    PSRMIRKTRK QKYFYRGRLD WDENTSAGRY VRENCKPLRR YLTSEAEEHH 450
    QLFDLIESML EYEPAKRLTL GEALQHPFFA RLRAEPPNKL WDSSRDISR 499
    Length:499
    Mass (Da):60,090
    Last modified:October 1, 1996 - v1
    Checksum:iE43BBF3BAD6EF991
    GO
    Isoform 2 (identifier: P49760-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         134-139: QHSSRR → MKSLAP
         140-499: Missing.

    Note: Lacks the kinase domain. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:139
    Mass (Da):17,569
    Checksum:iCC9C9C63B3B07667
    GO
    Isoform 3 (identifier: P49760-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         134-134: Missing.

    Show »
    Length:498
    Mass (Da):59,962
    Checksum:i0A21FC66FD22DBC6
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei134 – 1396QHSSRR → MKSLAP in isoform 2. 1 PublicationVSP_004856
    Alternative sequencei134 – 1341Missing in isoform 3. 1 PublicationVSP_038744
    Alternative sequencei140 – 499360Missing in isoform 2. 1 PublicationVSP_004857Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29218 mRNA. Translation: AAA61482.1.
    L29216 mRNA. Translation: AAA61481.1.
    AF023268 Genomic DNA. Translation: AAC51817.1.
    AL713999 Genomic DNA. Translation: CAI95098.1.
    BC014067 mRNA. Translation: AAH14067.1.
    BC053603 mRNA. Translation: AAH53603.1.
    CCDSiCCDS1107.1. [P49760-3]
    PIRiS53637.
    S53638.
    RefSeqiNP_003984.2. NM_003993.2. [P49760-3]
    XP_005244933.1. XM_005244876.1. [P49760-1]
    XP_005276799.1. XM_005276742.1. [P49760-1]
    UniGeneiHs.73986.

    Genome annotation databases

    EnsembliENST00000361168; ENSP00000354856; ENSG00000176444. [P49760-3]
    ENST00000368361; ENSP00000357345; ENSG00000176444. [P49760-1]
    ENST00000572269; ENSP00000459461; ENSG00000261893. [P49760-3]
    ENST00000574445; ENSP00000460443; ENSG00000261893. [P49760-1]
    GeneIDi1196.
    KEGGihsa:1196.
    UCSCiuc001fjw.3. human. [P49760-3]
    uc001fjx.3. human. [P49760-1]

    Polymorphism databases

    DMDMi1705919.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29218 mRNA. Translation: AAA61482.1 .
    L29216 mRNA. Translation: AAA61481.1 .
    AF023268 Genomic DNA. Translation: AAC51817.1 .
    AL713999 Genomic DNA. Translation: CAI95098.1 .
    BC014067 mRNA. Translation: AAH14067.1 .
    BC053603 mRNA. Translation: AAH53603.1 .
    CCDSi CCDS1107.1. [P49760-3 ]
    PIRi S53637.
    S53638.
    RefSeqi NP_003984.2. NM_003993.2. [P49760-3 ]
    XP_005244933.1. XM_005244876.1. [P49760-1 ]
    XP_005276799.1. XM_005276742.1. [P49760-1 ]
    UniGenei Hs.73986.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3NR9 X-ray 2.89 A/B/C 135-496 [» ]
    ProteinModelPortali P49760.
    SMRi P49760. Positions 136-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107607. 40 interactions.
    IntActi P49760. 30 interactions.
    MINTi MINT-1683264.
    STRINGi 9606.ENSP00000354856.

    Chemistry

    BindingDBi P49760.
    ChEMBLi CHEMBL4225.
    GuidetoPHARMACOLOGYi 1991.

    PTM databases

    PhosphoSitei P49760.

    Polymorphism databases

    DMDMi 1705919.

    Proteomic databases

    MaxQBi P49760.
    PaxDbi P49760.
    PRIDEi P49760.

    Protocols and materials databases

    DNASUi 1196.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361168 ; ENSP00000354856 ; ENSG00000176444 . [P49760-3 ]
    ENST00000368361 ; ENSP00000357345 ; ENSG00000176444 . [P49760-1 ]
    ENST00000572269 ; ENSP00000459461 ; ENSG00000261893 . [P49760-3 ]
    ENST00000574445 ; ENSP00000460443 ; ENSG00000261893 . [P49760-1 ]
    GeneIDi 1196.
    KEGGi hsa:1196.
    UCSCi uc001fjw.3. human. [P49760-3 ]
    uc001fjx.3. human. [P49760-1 ]

    Organism-specific databases

    CTDi 1196.
    GeneCardsi GC01M155232.
    H-InvDB HIX0001112.
    HGNCi HGNC:2069. CLK2.
    HPAi HPA055366.
    MIMi 602989. gene.
    neXtProti NX_P49760.
    PharmGKBi PA26595.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000203417.
    HOVERGENi HBG107720.
    InParanoidi P49760.
    KOi K08823.
    OMAi GHLIYRV.
    PhylomeDBi P49760.
    TreeFami TF101041.

    Enzyme and pathway databases

    BRENDAi 2.7.12.1. 2681.
    SignaLinki P49760.

    Miscellaneous databases

    ChiTaRSi CLK2. human.
    EvolutionaryTracei P49760.
    GeneWikii CLK2.
    GenomeRNAii 1196.
    NextBioi 4940.
    PROi P49760.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49760.
    Bgeei P49760.
    CleanExi HS_CLK2.
    Genevestigatori P49760.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 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. "Characterization by cDNA cloning of two new human protein kinases. Evidence by sequence comparison of a new family of mammalian protein kinases."
      Hanes J.J., der Kammer H., Klaudiny J.J., Scheit K.H.
      J. Mol. Biol. 244:665-672(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. "Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease."
      Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.
      Genome Res. 7:1020-1026(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 3).
      Tissue: Lung and Ovary.
    5. "Activity and autophosphorylation of LAMMER protein kinases."
      Lee K., Du C., Horn M., Rabinow L.
      J. Biol. Chem. 271:27299-27303(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing."
      Duncan P.I., Stojdl D.F., Marius R.M., Scheit K.H., Bell J.C.
      Exp. Cell Res. 241:300-308(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    7. "The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B."
      Moeslein F.M., Myers M.P., Landreth G.E.
      J. Biol. Chem. 274:26697-26704(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: INTERACTION WITH UBL5.
    9. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Cdc2-like kinases and DNA topoisomerase I regulate alternative splicing of tissue factor in human endothelial cells."
      Eisenreich A., Bogdanov V.Y., Zakrzewicz A., Pries A., Antoniak S., Poller W., Schultheiss H.P., Rauch U.
      Circ. Res. 104:589-599(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    13. "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regions in pre-mRNA."
      Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M., Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R., Stamm S.
      J. Biol. Chem. 284:14303-14315(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBMX.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND TYR-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Phosphorylation of CLK2 at serine 34 and threonine 127 by AKT controls cell survival after ionizing radiation."
      Nam S.Y., Seo H.H., Park H.S., An S., Kim J.Y., Yang K.H., Kim C.S., Jeong M., Jin Y.W.
      J. Biol. Chem. 285:31157-31163(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-34 AND THR-127, INTERACTION WITH AKT1.
    16. "Structure of human cdc2-like kinase 2 (clk2)."
      Structural genomics consortium (SGC)
      Submitted (AUG-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 135-496.

    Entry informationi

    Entry nameiCLK2_HUMAN
    AccessioniPrimary (citable) accession number: P49760
    Secondary accession number(s): B1AVS9, B5MBX6, Q96CQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 150 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 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3