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P49761

- CLK3_HUMAN

UniProt

P49761 - CLK3_HUMAN

Protein

Dual specificity protein kinase CLK3

Gene

CLK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (12 Jun 2007)
      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. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Leucettine L41 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei334 – 3341ATPPROSITE-ProRule annotation
    Active sitei431 – 4311Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi310 – 3189ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
    5. protein serine/threonine kinase activity Source: UniProtKB
    6. protein tyrosine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. protein autophosphorylation Source: Ensembl
    2. protein phosphorylation Source: UniProtKB
    3. regulation of RNA splicing Source: UniProtKB

    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.
    SignaLinkiP49761.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein kinase CLK3 (EC:2.7.12.1)
    Alternative name(s):
    CDC-like kinase 3
    Gene namesi
    Name:CLK3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:2071. CLK3.

    Subcellular locationi

    Isoform 2 : Nucleus speckle
    Note: Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles.

    GO - Cellular componenti

    1. acrosomal vesicle Source: UniProtKB-SubCell
    2. intermediate filament cytoskeleton Source: HPA
    3. membrane Source: UniProtKB
    4. nuclear speck Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26597.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 638638Dual specificity protein kinase CLK3PRO_0000085870Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei155 – 1551Phosphotyrosine2 Publications
    Modified residuei157 – 1571Phosphoserine3 Publications
    Modified residuei215 – 2151Phosphoserine2 Publications
    Modified residuei224 – 2241Phosphoserine3 Publications
    Modified residuei226 – 2261Phosphoserine3 Publications
    Modified residuei283 – 2831Phosphoserine2 Publications

    Post-translational modificationi

    Autophosphorylates on all three types of residues.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP49761.
    PaxDbiP49761.
    PRIDEiP49761.

    PTM databases

    PhosphoSiteiP49761.

    Expressioni

    Tissue specificityi

    Endothelial cells.1 Publication

    Gene expression databases

    ArrayExpressiP49761.
    BgeeiP49761.
    CleanExiHS_CLK3.
    GenevestigatoriP49761.

    Organism-specific databases

    HPAiHPA046817.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CLK2P497603EBI-745579,EBI-750020
    SUV39H1O434632EBI-745579,EBI-349968

    Protein-protein interaction databases

    BioGridi107609. 47 interactions.
    IntActiP49761. 33 interactions.
    MINTiMINT-1448658.
    STRINGi9606.ENSP00000391518.

    Structurei

    Secondary structure

    1
    638
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni301 – 3033
    Beta strandi304 – 31310
    Beta strandi316 – 3238
    Turni324 – 3285
    Beta strandi330 – 3367
    Helixi340 – 35920
    Beta strandi370 – 3767
    Beta strandi379 – 3857
    Helixi391 – 3977
    Turni398 – 4003
    Helixi405 – 42319
    Turni424 – 4263
    Helixi434 – 4363
    Beta strandi437 – 4404
    Beta strandi444 – 4485
    Turni450 – 4534
    Beta strandi456 – 4605
    Beta strandi464 – 4663
    Helixi469 – 4713
    Helixi486 – 4883
    Helixi491 – 4944
    Helixi502 – 51716
    Helixi527 – 53812
    Helixi543 – 5486
    Helixi552 – 5543
    Helixi567 – 5759
    Helixi579 – 5824
    Helixi588 – 60013
    Turni605 – 6073
    Helixi611 – 6144
    Helixi618 – 6225
    Helixi625 – 6284

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EU9X-ray1.53A284-638[»]
    2EXEX-ray2.35A275-631[»]
    2WU6X-ray1.92A275-632[»]
    2WU7X-ray2.25A275-632[»]
    3RAWX-ray2.09A/B275-632[»]
    ProteinModelPortaliP49761.
    SMRiP49761. Positions 284-629.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49761.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini304 – 620317Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi167 – 26498Arg-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000203417.
    HOVERGENiHBG107720.
    KOiK08823.
    OMAiNENKSCE.
    OrthoDBiEOG7TBC1V.
    PhylomeDBiP49761.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 4 (identifier: P49761-4) [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

    MPVLSARRRE LADHAGSGRR SGPSPTARSG PHLSALRAQP ARAAHLSGRG    50
    TYVRRDTAGG GPGQARPLGP PGTSLLGRGA RRSGEGWCPG AFESGARAAR 100
    PPSRVEPRLA TAASREGAGL PRAEVAAGSG RGARSGEWGL AAAGAWETMH 150
    HCKRYRSPEP DPYLSYRWKR RRSYSREHEG RLRYPSRREP PPRRSRSRSH 200
    DRLPYQRRYR ERRDSDTYRC EERSPSFGED YYGPSRSRHR RRSRERGPYR 250
    TRKHAHHCHK RRTRSCSSAS SRSQQSSKRS SRSVEDDKEG HLVCRIGDWL 300
    QERYEIVGNL GEGTFGKVVE CLDHARGKSQ VALKIIRNVG KYREAARLEI 350
    NVLKKIKEKD KENKFLCVLM SDWFNFHGHM CIAFELLGKN TFEFLKENNF 400
    QPYPLPHVRH MAYQLCHALR FLHENQLTHT DLKPENILFV NSEFETLYNE 450
    HKSCEEKSVK NTSIRVADFG SATFDHEHHT TIVATRHYRP PEVILELGWA 500
    QPCDVWSIGC ILFEYYRGFT LFQTHENREH LVMMEKILGP IPSHMIHRTR 550
    KQKYFYKGGL VWDENSSDGR YVKENCKPLK SYMLQDSLEH VQLFDLMRRM 600
    LEFDPAQRIT LAEALLHPFF AGLTPEERSF HTSRNPSR 638
    Length:638
    Mass (Da):73,515
    Last modified:June 12, 2007 - v3
    Checksum:iD3B60A9DB4ECEC94
    GO
    Isoform 1 (identifier: P49761-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    The sequence of this isoform differs from the canonical sequence as follows:
         1-148: Missing.

    Show »
    Length:490
    Mass (Da):58,588
    Checksum:i86A342ABB8AB24CA
    GO
    Isoform 2 (identifier: P49761-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         1-148: Missing.
         272-300: RSQQSSKRSSRSVEDDKEGHLVCRIGDWL → MRLWGTWVKAPLARWWSAWTMPEGSLRLP
         301-638: 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:152
    Mass (Da):18,971
    Checksum:i5BABA6574A0E9801
    GO
    Isoform 3 (identifier: P49761-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-148: Missing.
         306-328: Missing.

    Show »
    Length:467
    Mass (Da):56,207
    Checksum:i2890E88AE23AE7BC
    GO

    Sequence cautioni

    The sequence AAH02555.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH19881.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti280 – 2812SS → TG in AAA61484. (PubMed:7990150)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti486 – 4861R → C.1 Publication
    VAR_040413
    Natural varianti607 – 6071Q → R.1 Publication
    VAR_045579
    Natural varianti628 – 6281R → W.1 Publication
    VAR_045580

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 148148Missing in isoform 1, isoform 2 and isoform 3. 3 PublicationsVSP_026138Add
    BLAST
    Alternative sequencei272 – 30029RSQQS…IGDWL → MRLWGTWVKAPLARWWSAWT MPEGSLRLP in isoform 2. 1 PublicationVSP_004858Add
    BLAST
    Alternative sequencei301 – 638338Missing in isoform 2. 1 PublicationVSP_004859Add
    BLAST
    Alternative sequencei306 – 32823Missing in isoform 3. 1 PublicationVSP_004860Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29220 mRNA. Translation: AAA61483.1.
    L29217 mRNA. Translation: AAA61484.1.
    BT006993 mRNA. Translation: AAP35639.1.
    AC100835 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99321.1.
    CH471136 Genomic DNA. Translation: EAW99322.1.
    BC002555 mRNA. Translation: AAH02555.1. Different initiation.
    BC006103 mRNA. Translation: AAH06103.1.
    BC019881 mRNA. Translation: AAH19881.1. Different initiation.
    CCDSiCCDS10265.1. [P49761-1]
    CCDS45304.1. [P49761-4]
    PIRiS53639.
    S53640.
    RefSeqiNP_001123500.1. NM_001130028.1. [P49761-4]
    NP_003983.2. NM_003992.4. [P49761-1]
    XP_005254210.1. XM_005254153.2. [P49761-1]
    UniGeneiHs.584748.

    Genome annotation databases

    EnsembliENST00000345005; ENSP00000344112; ENSG00000179335. [P49761-1]
    ENST00000395066; ENSP00000378505; ENSG00000179335. [P49761-4]
    ENST00000483723; ENSP00000431825; ENSG00000179335. [P49761-2]
    GeneIDi1198.
    KEGGihsa:1198.
    UCSCiuc002ayg.4. human. [P49761-4]

    Polymorphism databases

    DMDMi148887358.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29220 mRNA. Translation: AAA61483.1 .
    L29217 mRNA. Translation: AAA61484.1 .
    BT006993 mRNA. Translation: AAP35639.1 .
    AC100835 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99321.1 .
    CH471136 Genomic DNA. Translation: EAW99322.1 .
    BC002555 mRNA. Translation: AAH02555.1 . Different initiation.
    BC006103 mRNA. Translation: AAH06103.1 .
    BC019881 mRNA. Translation: AAH19881.1 . Different initiation.
    CCDSi CCDS10265.1. [P49761-1 ]
    CCDS45304.1. [P49761-4 ]
    PIRi S53639.
    S53640.
    RefSeqi NP_001123500.1. NM_001130028.1. [P49761-4 ]
    NP_003983.2. NM_003992.4. [P49761-1 ]
    XP_005254210.1. XM_005254153.2. [P49761-1 ]
    UniGenei Hs.584748.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EU9 X-ray 1.53 A 284-638 [» ]
    2EXE X-ray 2.35 A 275-631 [» ]
    2WU6 X-ray 1.92 A 275-632 [» ]
    2WU7 X-ray 2.25 A 275-632 [» ]
    3RAW X-ray 2.09 A/B 275-632 [» ]
    ProteinModelPortali P49761.
    SMRi P49761. Positions 284-629.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107609. 47 interactions.
    IntActi P49761. 33 interactions.
    MINTi MINT-1448658.
    STRINGi 9606.ENSP00000391518.

    Chemistry

    BindingDBi P49761.
    ChEMBLi CHEMBL4226.
    GuidetoPHARMACOLOGYi 1992.

    PTM databases

    PhosphoSitei P49761.

    Polymorphism databases

    DMDMi 148887358.

    Proteomic databases

    MaxQBi P49761.
    PaxDbi P49761.
    PRIDEi P49761.

    Protocols and materials databases

    DNASUi 1198.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345005 ; ENSP00000344112 ; ENSG00000179335 . [P49761-1 ]
    ENST00000395066 ; ENSP00000378505 ; ENSG00000179335 . [P49761-4 ]
    ENST00000483723 ; ENSP00000431825 ; ENSG00000179335 . [P49761-2 ]
    GeneIDi 1198.
    KEGGi hsa:1198.
    UCSCi uc002ayg.4. human. [P49761-4 ]

    Organism-specific databases

    CTDi 1198.
    GeneCardsi GC15P074900.
    HGNCi HGNC:2071. CLK3.
    HPAi HPA046817.
    MIMi 602990. gene.
    neXtProti NX_P49761.
    PharmGKBi PA26597.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000203417.
    HOVERGENi HBG107720.
    KOi K08823.
    OMAi NENKSCE.
    OrthoDBi EOG7TBC1V.
    PhylomeDBi P49761.
    TreeFami TF101041.

    Enzyme and pathway databases

    BRENDAi 2.7.12.1. 2681.
    SignaLinki P49761.

    Miscellaneous databases

    EvolutionaryTracei P49761.
    GeneWikii CLK3_(gene).
    GenomeRNAii 1198.
    NextBioi 4949.
    PROi P49761.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49761.
    Bgeei P49761.
    CleanExi HS_CLK3.
    Genevestigatori P49761.

    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. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-638 (ISOFORM 4).
      Tissue: Cervix and Placenta.
    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. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-155; SER-157; SER-224 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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.
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-224 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 284-638.
    15. "Crystal structure of the phosphorylated clk3."
      Structural genomics consortium (SGC)
      Submitted (APR-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 275-627.
    16. "Leucettines, a class of potent inhibitors of cdc2-like kinases and dual specificity, tyrosine phosphorylation regulated kinases derived from the marine sponge leucettamine B: modulation of alternative pre-RNA splicing."
      Debdab M., Carreaux F., Renault S., Soundararajan M., Fedorov O., Filippakopoulos P., Lozach O., Babault L., Tahtouh T., Baratte B., Ogawa Y., Hagiwara M., Eisenreich A., Rauch U., Knapp S., Meijer L., Bazureau J.P.
      J. Med. Chem. 54:4172-4186(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 275-632 IN COMPLEX WITH LEUCETTINE L41.
    17. "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] CYS-486; ARG-607 AND TRP-628.

    Entry informationi

    Entry nameiCLK3_HUMAN
    AccessioniPrimary (citable) accession number: P49761
    Secondary accession number(s): D3DW59
    , Q53Y48, Q9BRS3, Q9BUJ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 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 15
      Human chromosome 15: 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