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P49759

- CLK1_HUMAN

UniProt

P49759 - CLK1_HUMAN

Protein

Dual specificity protein kinase CLK1

Gene

CLK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (23 Sep 2008)
      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 and may be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Regulates splicing of its own pre-mRNA according to its kinase activity; increased expression of the catalytically active form influences splicing to generate the catalytically inactive splicing variant lacking the kinase domain. Leucettine L41 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 sitei191 – 1911ATPPROSITE-ProRule annotation
    Active sitei288 – 2881Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi167 – 1759ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. peptidyl-serine phosphorylation Source: Ensembl
    3. peptidyl-threonine phosphorylation Source: Ensembl
    4. protein autophosphorylation Source: Ensembl
    5. 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.
    SignaLinkiP49759.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein kinase CLK1 (EC:2.7.12.1)
    Alternative name(s):
    CDC-like kinase 1
    Gene namesi
    Name:CLK1
    Synonyms:CLK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2068. CLK1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26594.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 484484Dual specificity protein kinase CLK1PRO_0000085866Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei61 – 611Phosphoserine1 Publication
    Modified residuei138 – 1381Phosphothreonine1 Publication
    Modified residuei140 – 1401Phosphoserine4 Publications

    Post-translational modificationi

    Autophosphorylates on all three types of residues.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP49759.
    PaxDbiP49759.
    PRIDEiP49759.

    PTM databases

    PhosphoSiteiP49759.

    Expressioni

    Tissue specificityi

    Endothelial cells.1 Publication

    Gene expression databases

    ArrayExpressiP49759.
    BgeeiP49759.
    CleanExiHS_CLK1.
    GenevestigatoriP49759.

    Organism-specific databases

    HPAiCAB033141.

    Interactioni

    Subunit structurei

    Interacts with PPIG and UBL5.1 Publication

    Protein-protein interaction databases

    BioGridi107606. 17 interactions.
    IntActiP49759. 9 interactions.
    MINTiMINT-8417657.
    STRINGi9606.ENSP00000326830.

    Structurei

    Secondary structure

    1
    484
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi148 – 1503
    Turni158 – 1603
    Beta strandi161 – 17010
    Beta strandi173 – 1808
    Turni181 – 1855
    Beta strandi187 – 1937
    Helixi197 – 21620
    Beta strandi227 – 2337
    Beta strandi236 – 2427
    Helixi248 – 2547
    Turni255 – 2573
    Helixi262 – 28120
    Helixi291 – 2933
    Beta strandi294 – 2974
    Beta strandi301 – 3055
    Beta strandi312 – 3176
    Beta strandi321 – 3233
    Helixi343 – 3453
    Helixi348 – 3514
    Helixi359 – 37416
    Helixi384 – 39512
    Helixi400 – 4056
    Helixi409 – 4113
    Helixi424 – 4329
    Helixi436 – 4394
    Helixi445 – 45713
    Turni462 – 4643
    Helixi468 – 4714
    Helixi475 – 4817

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z57X-ray1.70A148-484[»]
    2VAGX-ray1.80A148-484[»]
    ProteinModelPortaliP49759.
    SMRiP49759. Positions 97-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49759.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini161 – 477317Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000203417.
    HOVERGENiHBG107720.
    InParanoidiP49759.
    KOiK08823.
    OMAiMLSQDVE.
    OrthoDBiEOG7TBC1V.
    PhylomeDBiP49759.
    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: P49759-1) [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

    MRHSKRTYCP DWDDKDWDYG KWRSSSSHKR RKRSHSSAQE NKRCKYNHSK    50
    MCDSHYLESR SINEKDYHSR RYIDEYRNDY TQGCEPGHRQ RDHESRYQNH 100
    SSKSSGRSGR SSYKSKHRIH HSTSHRRSHG KSHRRKRTRS VEDDEEGHLI 150
    CQSGDVLSAR YEIVDTLGEG AFGKVVECID HKAGGRHVAV KIVKNVDRYC 200
    EAARSEIQVL EHLNTTDPNS TFRCVQMLEW FEHHGHICIV FELLGLSTYD 250
    FIKENGFLPF RLDHIRKMAY QICKSVNFLH SNKLTHTDLK PENILFVQSD 300
    YTEAYNPKIK RDERTLINPD IKVVDFGSAT YDDEHHSTLV STRHYRAPEV 350
    ILALGWSQPC DVWSIGCILI EYYLGFTVFP THDSKEHLAM MERILGPLPK 400
    HMIQKTRKRK YFHHDRLDWD EHSSAGRYVS RRCKPLKEFM LSQDVEHERL 450
    FDLIQKMLEY DPAKRITLRE ALKHPFFDLL KKSI 484
    Length:484
    Mass (Da):57,291
    Last modified:September 23, 2008 - v2
    Checksum:iF34B5B44988BD118
    GO
    Isoform 2 (identifier: P49759-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         131-136: KSHRRK → MKLLIL
         137-484: 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:136
    Mass (Da):16,570
    Checksum:i3A1B92FD19E2A521
    GO
    Isoform 3 (identifier: P49759-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAAGRRPASALWPERRGSPLRGDLLGFQNVREPSSCGETLSGM

    Note: No experimental confirmation available.

    Show »
    Length:526
    Mass (Da):61,757
    Checksum:i8514814549CC0655
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti432 – 4321R → A in AAA61480. (PubMed:1704889)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti61 – 611S → F.1 Publication
    Corresponds to variant rs55989135 [ dbSNP | Ensembl ].
    VAR_040409
    Natural varianti99 – 991N → D.
    Corresponds to variant rs6735666 [ dbSNP | Ensembl ].
    VAR_046551
    Natural varianti118 – 1181R → G.1 Publication
    Corresponds to variant rs56135616 [ dbSNP | Ensembl ].
    VAR_040410
    Natural varianti307 – 3071P → S.1 Publication
    Corresponds to variant rs35412475 [ dbSNP | Ensembl ].
    VAR_040411
    Natural varianti440 – 4401M → T.1 Publication
    Corresponds to variant rs35393352 [ dbSNP | Ensembl ].
    VAR_040412
    Natural varianti459 – 4591E → G.
    Corresponds to variant rs12709 [ dbSNP | Ensembl ].
    VAR_051620

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MAAGRRPASALWPERRGSPL RGDLLGFQNVREPSSCGETL SGM in isoform 3. 1 PublicationVSP_043578
    Alternative sequencei131 – 1366KSHRRK → MKLLIL in isoform 2. 3 PublicationsVSP_004852
    Alternative sequencei137 – 484348Missing in isoform 2. 3 PublicationsVSP_004853Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29219 mRNA. Translation: AAA61480.1.
    L29222 mRNA. Translation: AAB59459.1.
    AK289365 mRNA. Translation: BAF82054.1.
    AK294295 mRNA. Translation: BAG57578.1.
    AC005037 Genomic DNA. Translation: AAY14722.1.
    CH471063 Genomic DNA. Translation: EAW70217.1.
    BC028149 mRNA. Translation: AAH28149.1.
    BC031549 mRNA. Translation: AAH31549.1.
    CCDSiCCDS2331.1. [P49759-1]
    CCDS54427.1. [P49759-3]
    PIRiS53641.
    RefSeqiNP_001155879.1. NM_001162407.1. [P49759-3]
    NP_004062.2. NM_004071.3. [P49759-1]
    UniGeneiHs.433732.

    Genome annotation databases

    EnsembliENST00000321356; ENSP00000326830; ENSG00000013441. [P49759-1]
    ENST00000432425; ENSP00000400487; ENSG00000013441. [P49759-2]
    ENST00000434813; ENSP00000394734; ENSG00000013441. [P49759-3]
    GeneIDi1195.
    KEGGihsa:1195.
    UCSCiuc002uwe.2. human. [P49759-1]
    uc010zhi.1. human. [P49759-3]

    Polymorphism databases

    DMDMi206729857.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L29219 mRNA. Translation: AAA61480.1 .
    L29222 mRNA. Translation: AAB59459.1 .
    AK289365 mRNA. Translation: BAF82054.1 .
    AK294295 mRNA. Translation: BAG57578.1 .
    AC005037 Genomic DNA. Translation: AAY14722.1 .
    CH471063 Genomic DNA. Translation: EAW70217.1 .
    BC028149 mRNA. Translation: AAH28149.1 .
    BC031549 mRNA. Translation: AAH31549.1 .
    CCDSi CCDS2331.1. [P49759-1 ]
    CCDS54427.1. [P49759-3 ]
    PIRi S53641.
    RefSeqi NP_001155879.1. NM_001162407.1. [P49759-3 ]
    NP_004062.2. NM_004071.3. [P49759-1 ]
    UniGenei Hs.433732.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z57 X-ray 1.70 A 148-484 [» ]
    2VAG X-ray 1.80 A 148-484 [» ]
    ProteinModelPortali P49759.
    SMRi P49759. Positions 97-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107606. 17 interactions.
    IntActi P49759. 9 interactions.
    MINTi MINT-8417657.
    STRINGi 9606.ENSP00000326830.

    Chemistry

    BindingDBi P49759.
    ChEMBLi CHEMBL4224.
    GuidetoPHARMACOLOGYi 1990.

    PTM databases

    PhosphoSitei P49759.

    Polymorphism databases

    DMDMi 206729857.

    Proteomic databases

    MaxQBi P49759.
    PaxDbi P49759.
    PRIDEi P49759.

    Protocols and materials databases

    DNASUi 1195.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321356 ; ENSP00000326830 ; ENSG00000013441 . [P49759-1 ]
    ENST00000432425 ; ENSP00000400487 ; ENSG00000013441 . [P49759-2 ]
    ENST00000434813 ; ENSP00000394734 ; ENSG00000013441 . [P49759-3 ]
    GeneIDi 1195.
    KEGGi hsa:1195.
    UCSCi uc002uwe.2. human. [P49759-1 ]
    uc010zhi.1. human. [P49759-3 ]

    Organism-specific databases

    CTDi 1195.
    GeneCardsi GC02M201717.
    HGNCi HGNC:2068. CLK1.
    HPAi CAB033141.
    MIMi 601951. gene.
    neXtProti NX_P49759.
    PharmGKBi PA26594.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000203417.
    HOVERGENi HBG107720.
    InParanoidi P49759.
    KOi K08823.
    OMAi MLSQDVE.
    OrthoDBi EOG7TBC1V.
    PhylomeDBi P49759.
    TreeFami TF101041.

    Enzyme and pathway databases

    BRENDAi 2.7.12.1. 2681.
    SignaLinki P49759.

    Miscellaneous databases

    ChiTaRSi CLK1. human.
    EvolutionaryTracei P49759.
    GeneWikii CLK1.
    GenomeRNAii 1195.
    NextBioi 4936.
    PROi P49759.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49759.
    Bgeei P49759.
    CleanExi HS_CLK1.
    Genevestigatori P49759.

    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. "Molecular cloning of a novel human cdc2/CDC28-like protein kinase."
      Johnson K.W., Smith K.A.
      J. Biol. Chem. 266:3402-3407(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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] (ISOFORM 2).
    3. "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] (ISOFORMS 2 AND 3).
      Tissue: Amygdala.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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] (ISOFORMS 1 AND 2).
      Tissue: Blood and Bone.
    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. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-61 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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] PHE-61; GLY-118; SER-307 AND THR-440.

    Entry informationi

    Entry nameiCLK1_HUMAN
    AccessioniPrimary (citable) accession number: P49759
    Secondary accession number(s): B4DFW7, Q0P694, Q8N5V8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: September 23, 2008
    Last modified: October 1, 2014
    This is version 143 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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