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Q9UKI8

- TLK1_HUMAN

UniProt

Q9UKI8 - TLK1_HUMAN

Protein

Serine/threonine-protein kinase tousled-like 1

Gene

TLK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (22 Aug 2003)
      Previous versions | rss
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    Functioni

    Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase. This is cell cycle checkpoint and ATM-pathway dependent and appears to regulate processes involved in chromatin assembly. Isoform 3 phosphorylates and enhances the stability of the t-SNARE SNAP23, augmenting its assembly with syntaxin. Isoform 3 protects the cells from the ionizing radiation by facilitating the repair of DSBs. In vitro, phosphorylates histone H3 at 'Ser-10'.6 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.3 Publications

    Cofactori

    Magnesium.3 Publications

    Enzyme regulationi

    Cell-cycle regulated, maximal activity in S-phase. Inactivated by phosphorylation at Ser-743, potentially by CHEK1.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei485 – 4851ATPPROSITE-ProRule annotation
    Active sitei586 – 5861Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi462 – 4709ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cellular response to DNA damage stimulus Source: UniProtKB-KW
    3. chromatin modification Source: UniProtKB-KW
    4. intracellular protein transport Source: UniProtKB
    5. intracellular signal transduction Source: UniProtKB
    6. protein phosphorylation Source: UniProtKB
    7. regulation of chromatin assembly or disassembly Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, DNA damage

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9UKI8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase tousled-like 1 (EC:2.7.11.1)
    Alternative name(s):
    PKU-beta
    Tousled-like kinase 1
    Gene namesi
    Name:TLK1
    Synonyms:KIAA0137
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11841. TLK1.

    Subcellular locationi

    Nucleus 4 Publications

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi607 – 6071D → A: Loss of kinase activity. 2 Publications
    Mutagenesisi743 – 7431S → A: Loss of kinase inhibition in response to DNA damage. 1 Publication
    Mutagenesisi743 – 7431S → D: Loss of kinase inhibition in response to DNA damage. 1 Publication
    Mutagenesisi743 – 7431S → E: Loss of kinase inhibition in response to DNA damage. 1 Publication

    Organism-specific databases

    PharmGKBiPA36543.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 766766Serine/threonine-protein kinase tousled-like 1PRO_0000086752Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei159 – 1591Phosphoserine3 Publications
    Modified residuei743 – 7431Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UKI8.
    PaxDbiQ9UKI8.
    PRIDEiQ9UKI8.

    Expressioni

    Tissue specificityi

    Widely expressed. Present in fetal placenta, liver, kidney and pancreas but not heart or skeletal muscle. Also found in adult cell lines. Isoform 3 is ubiquitously expressed in all tissues examined.2 Publications

    Gene expression databases

    ArrayExpressiQ9UKI8.
    BgeeiQ9UKI8.
    CleanExiHS_TLK1.
    GenevestigatoriQ9UKI8.

    Organism-specific databases

    HPAiHPA016043.

    Interactioni

    Subunit structurei

    Heterodimerizes with TLK2. Interacts with ASF1A and ASF1B.2 Publications

    Protein-protein interaction databases

    BioGridi115206. 15 interactions.
    IntActiQ9UKI8. 7 interactions.
    MINTiMINT-112025.
    STRINGi9606.ENSP00000411099.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UKI8.
    SMRiQ9UKI8. Positions 427-764.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini456 – 734279Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili230 – 28152Sequence AnalysisAdd
    BLAST
    Coiled coili397 – 44549Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000259522.
    HOVERGENiHBG007938.
    KOiK08864.
    OMAiDVQFPVK.
    OrthoDBiEOG78H3SF.
    PhylomeDBiQ9UKI8.
    TreeFamiTF315233.

    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9UKI8-1) [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

    MSVQSSSGSL EGPPSWSQLS TSPTPGSAAA ARSLLNHTPP SGRPREGAMD    50
    ELHSLDPRRQ ELLEARFTGV ASGSTGSTGS CSVGAKASTN NESSNHSFGS 100
    LGSLSDKESE TPEKKQSESS RGRKRKAENQ NESSQGKSIG GRGHKISDYF 150
    EYQGGNGSSP VRGIPPAIRS PQNSHSHSTP SSSVRPNSPS PTALAFGDHP 200
    IVQPKQLSFK IIQTDLTMLK LAALESNKIQ DLEKKEGRID DLLRANCDLR 250
    RQIDEQQKLL EKYKERLNKC ISMSKKLLIE KSTQEKLSSR EKSMQDRLRL 300
    GHFTTVRHGA SFTEQWTDGF AFQNLVKQQE WVNQQREDIE RQRKLLAKRK 350
    PPTANNSQAP STNSEPKQRK NKAVNGAEND PFVRPNLPQL LTLAEYHEQE 400
    EIFKLRLGHL KKEEAEIQAE LERLERVRNL HIRELKRINN EDNSQFKDHP 450
    TLNERYLLLH LLGRGGFSEV YKAFDLYEQR YAAVKIHQLN KSWRDEKKEN 500
    YHKHACREYR IHKELDHPRI VKLYDYFSLD TDTFCTVLEY CEGNDLDFYL 550
    KQHKLMSEKE ARSIVMQIVN ALRYLNEIKP PIIHYDLKPG NILLVDGTAC 600
    GEIKITDFGL SKIMDDDSYG VDGMDLTSQG AGTYWYLPPE CFVVGKEPPK 650
    ISNKVDVWSV GVIFFQCLYG RKPFGHNQSQ QDILQENTIL KATEVQFPVK 700
    PVVSSEAKAF IRRCLAYRKE DRFDVHQLAN DPYLLPHMRR SNSSGNLHMA 750
    GLTASPTPPS SSIITY 766
    Length:766
    Mass (Da):86,700
    Last modified:August 22, 2003 - v2
    Checksum:iA65AE0A2A7C7FF2F
    GO
    Isoform 21 Publication (identifier: Q9UKI8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         136-136: G → GFPNLPVFQSLAYWEMGRTAGG

    Show »
    Length:787
    Mass (Da):89,023
    Checksum:i87275865796F5A54
    GO
    Isoform 31 Publication (identifier: Q9UKI8-3) [UniParc]FASTAAdd to Basket

    Also known as: SNAK1 Publication

    , TLK1B

    The sequence of this isoform differs from the canonical sequence as follows:
         1-217: Missing.

    Show »
    Length:549
    Mass (Da):63,994
    Checksum:iED6FBF1F77E7E90F
    GO
    Isoform 4 (identifier: Q9UKI8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: MSVQSSSGSLEGPP → MAVLFLYDLKTTGK
         15-110: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:670
    Mass (Da):77,110
    Checksum:iBFA0D9CF3CEFB7C1
    GO
    Isoform 5 (identifier: Q9UKI8-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-48: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:718
    Mass (Da):81,927
    Checksum:i73E77AF8D34C531D
    GO

    Sequence cautioni

    The sequence AAF03094.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA09486.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti88 – 881S → T in AAF03094. (PubMed:10523312)Curated
    Sequence conflicti102 – 1021G → E in BAA20562. (PubMed:9427565)Curated
    Sequence conflicti230 – 2301Q → L in BAA20562. (PubMed:9427565)Curated
    Sequence conflicti261 – 2611E → D in BAA20562. (PubMed:9427565)Curated
    Sequence conflicti416 – 4161E → G in BAA20562. (PubMed:9427565)Curated
    Sequence conflicti439 – 4391N → H in BAA20562. (PubMed:9427565)Curated
    Sequence conflicti471 – 4711Y → D in BAA20562. (PubMed:9427565)Curated
    Sequence conflicti477 – 4771Y → S in BAA20562. (PubMed:9427565)Curated
    Sequence conflicti625 – 6251D → V in BAA20562. (PubMed:9427565)Curated
    Sequence conflicti665 – 6651F → Y in BAA20562. (PubMed:9427565)Curated
    Sequence conflicti730 – 7301N → C in BAA20562. (PubMed:9427565)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti121 – 1211R → C.1 Publication
    VAR_041215

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 217217Missing in isoform 3. 1 PublicationVSP_050570Add
    BLAST
    Alternative sequencei1 – 4848Missing in isoform 5. 1 PublicationVSP_043504Add
    BLAST
    Alternative sequencei1 – 1414MSVQS…LEGPP → MAVLFLYDLKTTGK in isoform 4. 1 PublicationVSP_043505Add
    BLAST
    Alternative sequencei15 – 11096Missing in isoform 4. 1 PublicationVSP_043506Add
    BLAST
    Alternative sequencei136 – 1361G → GFPNLPVFQSLAYWEMGRTA GG in isoform 2. 1 PublicationVSP_050571

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004885 mRNA. Translation: BAA20562.1.
    AF162666 mRNA. Translation: AAF03094.1. Different initiation.
    AF246219 mRNA. Translation: AAF71263.1.
    D50927 mRNA. Translation: BAA09486.2. Different initiation.
    AK090779 mRNA. Translation: BAG52227.1.
    AK301857 mRNA. Translation: BAG63299.1.
    AC007739 Genomic DNA. No translation available.
    AC009953 Genomic DNA. No translation available.
    AC010092 Genomic DNA. No translation available.
    BC032657 mRNA. Translation: AAH32657.1.
    CCDSiCCDS2241.1. [Q9UKI8-1]
    CCDS46447.1. [Q9UKI8-5]
    CCDS46448.1. [Q9UKI8-4]
    RefSeqiNP_001130026.1. NM_001136554.1. [Q9UKI8-5]
    NP_001130027.1. NM_001136555.1. [Q9UKI8-4]
    NP_036422.3. NM_012290.4. [Q9UKI8-1]
    XP_005247038.1. XM_005246981.1. [Q9UKI8-3]
    UniGeneiHs.744917.

    Genome annotation databases

    EnsembliENST00000360843; ENSP00000354089; ENSG00000198586. [Q9UKI8-2]
    ENST00000431350; ENSP00000411099; ENSG00000198586. [Q9UKI8-1]
    ENST00000434911; ENSP00000409222; ENSG00000198586. [Q9UKI8-4]
    ENST00000521943; ENSP00000428113; ENSG00000198586. [Q9UKI8-5]
    GeneIDi9874.
    KEGGihsa:9874.
    UCSCiuc002ugn.2. human. [Q9UKI8-1]
    uc002ugo.2. human. [Q9UKI8-2]
    uc010zdn.1. human. [Q9UKI8-4]

    Polymorphism databases

    DMDMi34223086.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004885 mRNA. Translation: BAA20562.1 .
    AF162666 mRNA. Translation: AAF03094.1 . Different initiation.
    AF246219 mRNA. Translation: AAF71263.1 .
    D50927 mRNA. Translation: BAA09486.2 . Different initiation.
    AK090779 mRNA. Translation: BAG52227.1 .
    AK301857 mRNA. Translation: BAG63299.1 .
    AC007739 Genomic DNA. No translation available.
    AC009953 Genomic DNA. No translation available.
    AC010092 Genomic DNA. No translation available.
    BC032657 mRNA. Translation: AAH32657.1 .
    CCDSi CCDS2241.1. [Q9UKI8-1 ]
    CCDS46447.1. [Q9UKI8-5 ]
    CCDS46448.1. [Q9UKI8-4 ]
    RefSeqi NP_001130026.1. NM_001136554.1. [Q9UKI8-5 ]
    NP_001130027.1. NM_001136555.1. [Q9UKI8-4 ]
    NP_036422.3. NM_012290.4. [Q9UKI8-1 ]
    XP_005247038.1. XM_005246981.1. [Q9UKI8-3 ]
    UniGenei Hs.744917.

    3D structure databases

    ProteinModelPortali Q9UKI8.
    SMRi Q9UKI8. Positions 427-764.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115206. 15 interactions.
    IntActi Q9UKI8. 7 interactions.
    MINTi MINT-112025.
    STRINGi 9606.ENSP00000411099.

    Chemistry

    BindingDBi Q9UKI8.
    ChEMBLi CHEMBL5388.
    GuidetoPHARMACOLOGYi 2242.

    Polymorphism databases

    DMDMi 34223086.

    Proteomic databases

    MaxQBi Q9UKI8.
    PaxDbi Q9UKI8.
    PRIDEi Q9UKI8.

    Protocols and materials databases

    DNASUi 9874.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360843 ; ENSP00000354089 ; ENSG00000198586 . [Q9UKI8-2 ]
    ENST00000431350 ; ENSP00000411099 ; ENSG00000198586 . [Q9UKI8-1 ]
    ENST00000434911 ; ENSP00000409222 ; ENSG00000198586 . [Q9UKI8-4 ]
    ENST00000521943 ; ENSP00000428113 ; ENSG00000198586 . [Q9UKI8-5 ]
    GeneIDi 9874.
    KEGGi hsa:9874.
    UCSCi uc002ugn.2. human. [Q9UKI8-1 ]
    uc002ugo.2. human. [Q9UKI8-2 ]
    uc010zdn.1. human. [Q9UKI8-4 ]

    Organism-specific databases

    CTDi 9874.
    GeneCardsi GC02M171812.
    HGNCi HGNC:11841. TLK1.
    HPAi HPA016043.
    MIMi 608438. gene.
    neXtProti NX_Q9UKI8.
    PharmGKBi PA36543.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000259522.
    HOVERGENi HBG007938.
    KOi K08864.
    OMAi DVQFPVK.
    OrthoDBi EOG78H3SF.
    PhylomeDBi Q9UKI8.
    TreeFami TF315233.

    Enzyme and pathway databases

    SignaLinki Q9UKI8.

    Miscellaneous databases

    ChiTaRSi TLK1. human.
    GeneWikii TLK1.
    GenomeRNAii 9874.
    NextBioi 37219.
    PROi Q9UKI8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKI8.
    Bgeei Q9UKI8.
    CleanExi HS_TLK1.
    Genevestigatori Q9UKI8.

    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. "cDNA cloning and chromosomal mapping of genes encoding novel protein kinases termed PKU-alpha and PKU-beta, which have nuclear localization signal."
      Yamakawa A., Kameoka Y., Hashimoto K., Yoshitake Y., Nishikawa K., Tanihara K., Date T.
      Gene 202:193-201(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Placenta1 Publication and Testis1 Publication.
    2. "Mammalian homologues of the plant tousled gene code for cell-cycle-regulated kinases with maximal activities linked to ongoing DNA replication."
      Sillje H.H.W., Takahashi K., Tanaka K., Van Houwe G., Nigg E.A.
      EMBO J. 18:5691-5702(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF ASP-607, SUBCELLULAR LOCATION, INTERACTION WITH TLK2, ENZYME REGULATION.
      Tissue: PlacentaImported.
    3. "Phosphorylation of SNAP-23 by the novel kinase SNAK regulates t-SNARE complex assembly."
      Cabaniols J.-P., Ravichandran V., Roche P.A.
      Mol. Biol. Cell 10:4033-4041(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Placenta1 Publication.
    4. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
      DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow1 Publication.
    5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    6. "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 4 AND 5).
      Tissue: Amygdala and Testis.
    7. "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].
    8. "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: UterusImported.
    9. "Identification of human Asf1 chromatin assembly factors as substrates of Tousled-like kinases."
      Sillje H.H.W., Nigg E.A.
      Curr. Biol. 11:1068-1073(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ASF1A AND ASF1B, MUTAGENESIS OF ASP-607.
    10. "A translationally regulated Tousled kinase phosphorylates histone H3 and confers radioresistance when overexpressed."
      Li Y., DeFatta R., Anthony C., Sunavala G., De Benedetti A.
      Oncogene 20:726-738(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION OF HISTONE H3.
    11. "Human tousled like kinases are targeted by an ATM- and Chk1-dependent DNA damage checkpoint."
      Groth A., Lukas J., Nigg E.A., Sillje H.H.W., Wernstedt C., Bartek J., Hansen K.
      EMBO J. 22:1676-1687(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-743, PHOSPHORYLATION AT SER-743, ENZYME REGULATION.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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] CYS-121.

    Entry informationi

    Entry nameiTLK1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKI8
    Secondary accession number(s): B3KR15
    , B4DX87, Q14150, Q8N591, Q9NYH2, Q9Y4F6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 22, 2003
    Last sequence update: August 22, 2003
    Last modified: October 1, 2014
    This is version 139 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, 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. 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