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Q86UE8

- TLK2_HUMAN

UniProt

Q86UE8 - TLK2_HUMAN

Protein

Serine/threonine-protein kinase tousled-like 2

Gene

TLK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (22 Aug 2003)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation. Phosphorylates the chromatin assembly factors ASF1A AND ASF1B. Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly. Negative regulator of amino acid starvation-induced autophagy.7 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium.3 Publications

    Enzyme regulationi

    Cell cycle-regulated, with maximal activity in the S-phase. Rapidly and transiently inhibited by phosphorylation following the generation of DNA double-stranded breaks during S-phase, probably by CHEK1, possibly at Ser-750. This inhibition is cell cycle checkpoint- and ATM-dependent.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei491 – 4911ATPPROSITE-ProRule annotation
    Active sitei592 – 5921Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi468 – 4769ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. 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
    3. cellular response to gamma radiation Source: UniProtKB
    4. chromatin modification Source: UniProtKB-KW
    5. chromosome segregation Source: UniProtKB
    6. intracellular signal transduction Source: UniProtKB
    7. negative regulation of autophagy Source: BHF-UCL
    8. negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    9. peptidyl-serine phosphorylation Source: UniProtKB
    10. protein phosphorylation Source: UniProtKB
    11. 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

    SignaLinkiQ86UE8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase tousled-like 2 (EC:2.7.11.1)
    Alternative name(s):
    HsHPK
    PKU-alpha
    Tousled-like kinase 2
    Gene namesi
    Name:TLK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:11842. TLK2.

    Subcellular locationi

    Nucleus. Cytoplasmperinuclear region. Cytoplasmcytoskeleton
    Note: Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle. Present in the perinuclear region at S phase and in the nucleus at late G2.

    GO - Cellular componenti

    1. intermediate filament Source: UniProtKB
    2. nucleolus Source: HPA
    3. nucleus Source: UniProtKB
    4. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi613 – 6131D → A: Loss of kinase activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA36544.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 772772Serine/threonine-protein kinase tousled-like 2PRO_0000086754Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei94 – 941Phosphoserine1 Publication
    Modified residuei99 – 991Phosphoserine2 Publications
    Modified residuei134 – 1341Phosphoserine1 Publication
    Modified residuei750 – 7501Phosphoserine; by CHEK11 Publication

    Post-translational modificationi

    Phosphorylated at Ser-750, probably by CHEK1.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ86UE8.
    PaxDbiQ86UE8.
    PRIDEiQ86UE8.

    PTM databases

    PhosphoSiteiQ86UE8.

    Expressioni

    Tissue specificityi

    Ubiquitous. Detected in placenta, fetal liver, kidney, pancreas, heart and skeletal muscle. Highly expressed in testis. Detected in spleen, thymus, colon, ovary, small intestine, prostate and peripheral blood leukocytes.2 Publications

    Gene expression databases

    ArrayExpressiQ86UE8.
    BgeeiQ86UE8.
    CleanExiHS_TLK2.
    GenevestigatoriQ86UE8.

    Organism-specific databases

    HPAiHPA056342.

    Interactioni

    Subunit structurei

    Monomer and heterodimer with TLK1. Interacts with ASF1A and ASF1B. Association with 14-3-3 proteins such as YWHAZ regulates subcellular location. May also interact with FEZ1/LZTS1 and FEZ2.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IRF4Q153062EBI-1047967,EBI-751345
    IRF7Q929852EBI-1047967,EBI-968267

    Protein-protein interaction databases

    BioGridi116201. 14 interactions.
    IntActiQ86UE8. 3 interactions.
    MINTiMINT-5006424.
    STRINGi9606.ENSP00000275780.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86UE8.
    SMRiQ86UE8. Positions 458-769.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini462 – 741280Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili225 – 27652Sequence AnalysisAdd
    BLAST
    Coiled coili317 – 34731Sequence AnalysisAdd
    BLAST
    Coiled coili403 – 45149Sequence 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.
    InParanoidiQ86UE8.
    KOiK08864.
    OMAiLVYRKED.
    PhylomeDBiQ86UE8.
    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.
    IPR027086. TLK2.
    [Graphical view]
    PANTHERiPTHR22974:SF20. PTHR22974:SF20. 1 hit.
    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 1Curated (identifier: Q86UE8-1) [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

    MMEELHSLDP RRQELLEARF TGVGVSKGPL NSESSNQSLC SVGSLSDKEV    50
    ETPEKKQNDQ RNRKRKAEPY ETSQGKGTPR GHKISDYFEF AGGSAPGTSP 100
    GRSVPPVARS SPQHSLSNPL PRRVEQPLYG LDGSAAKEAT EEQSALPTLM 150
    SVMLAKPRLD TEQLAQRGAG LCFTFVSAQQ NSPSSTGSGN TEHSCSSQKQ 200
    ISIQHRQTQS DLTIEKISAL ENSKNSDLEK KEGRIDDLLR ANCDLRRQID 250
    EQQKMLEKYK ERLNRCVTMS KKLLIEKSKQ EKMACRDKSM QDRLRLGHFT 300
    TVRHGASFTE QWTDGYAFQN LIKQQERINS QREEIERQRK MLAKRKPPAM 350
    GQAPPATNEQ KQRKSKTNGA ENETPSSGNT ELKDTAPALG AHSLLRLTLA 400
    EYHEQEEIFK LRLGHLKKEE AEIQAELERL ERVRNLHIRE LKRIHNEDNS 450
    QFKDHPTLND RYLLLHLLGR GGFSEVYKAF DLTEQRYVAV KIHQLNKNWR 500
    DEKKENYHKH ACREYRIHKE LDHPRIVKLY DYFSLDTDSF CTVLEYCEGN 550
    DLDFYLKQHK LMSEKEARSI IMQIVNALKY LNEIKPPIIH YDLKPGNILL 600
    VNGTACGEIK ITDFGLSKIM DDDSYNSVDG MELTSQGAGT YWYLPPECFV 650
    VGKEPPKISN KVDVWSVGVI FYQCLYGRKP FGHNQSQQDI LQENTILKAT 700
    EVQFPPKPVV TPEAKAFIRR CLAYRKEDRI DVQQLACDPY LLPHIRKSVS 750
    TSSPAGAAIA STSGASNNSS SN 772

    Note: No experimental confirmation available.Curated

    Length:772
    Mass (Da):87,661
    Last modified:August 22, 2003 - v2
    Checksum:i765EE37ED4A4ADEC
    GO
    Isoform 21 Publication (identifier: Q86UE8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         375-396: Missing.

    Show »
    Length:750
    Mass (Da):85,444
    Checksum:iDECCDBF95115C286
    GO
    Isoform 31 Publication (identifier: Q86UE8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         90-121: Missing.
         375-396: Missing.

    Show »
    Length:718
    Mass (Da):82,348
    Checksum:i60E703322E8F2D2D
    GO

    Sequence cautioni

    The sequence AAF03095.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH44925.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA20561.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → I in BAA20561. (PubMed:9427565)Curated
    Sequence conflicti161 – 1611T → P in BAA20561. (PubMed:9427565)Curated
    Sequence conflicti207 – 2071Q → R in AAF03095. (PubMed:10523312)Curated
    Sequence conflicti562 – 5621M → I in BAA20561. (PubMed:9427565)Curated
    Sequence conflicti727 – 7271E → R in AAF03095. (PubMed:10523312)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61H → R.2 Publications
    Corresponds to variant rs45550140 [ dbSNP | Ensembl ].
    VAR_041216
    Natural varianti54 – 541E → D.1 Publication
    VAR_041217
    Natural varianti95 – 951A → G.1 Publication
    VAR_041218
    Natural varianti108 – 1081A → G.1 Publication
    VAR_041219
    Natural varianti109 – 1091R → L.1 Publication
    VAR_041220
    Natural varianti173 – 1731F → L in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041221
    Natural varianti262 – 2621R → Q.1 Publication
    VAR_041222

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei90 – 12132Missing in isoform 3. 1 PublicationVSP_050572Add
    BLAST
    Alternative sequencei375 – 39622Missing in isoform 2 and isoform 3. 2 PublicationsVSP_050573Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004884 mRNA. Translation: BAA20561.1. Different initiation.
    AF162667 mRNA. Translation: AAF03095.1. Different initiation.
    CH471109 Genomic DNA. Translation: EAW94346.1.
    CH471109 Genomic DNA. Translation: EAW94348.1.
    BC044925 mRNA. Translation: AAH44925.2. Different initiation.
    CCDSiCCDS11633.1. [Q86UE8-2]
    CCDS45753.1. [Q86UE8-3]
    CCDS62283.1. [Q86UE8-1]
    RefSeqiNP_001271262.1. NM_001284333.1. [Q86UE8-1]
    NP_001271292.1. NM_001284363.1. [Q86UE8-3]
    NP_006843.2. NM_006852.3. [Q86UE8-2]
    XP_005257026.1. XM_005256969.1. [Q86UE8-2]
    XP_005257027.1. XM_005256970.2. [Q86UE8-2]
    XP_005257028.1. XM_005256971.2. [Q86UE8-3]
    XP_006721710.1. XM_006721647.1. [Q86UE8-2]
    XP_006721711.1. XM_006721648.1. [Q86UE8-3]
    UniGeneiHs.445078.

    Genome annotation databases

    EnsembliENST00000326270; ENSP00000316512; ENSG00000146872. [Q86UE8-1]
    ENST00000343388; ENSP00000340800; ENSG00000146872. [Q86UE8-3]
    ENST00000346027; ENSP00000275780; ENSG00000146872. [Q86UE8-2]
    ENST00000542523; ENSP00000442311; ENSG00000146872. [Q86UE8-3]
    GeneIDi11011.
    KEGGihsa:11011.
    UCSCiuc002izz.4. human. [Q86UE8-2]
    uc002jaa.4. human. [Q86UE8-3]
    uc010ddp.3. human. [Q86UE8-1]

    Polymorphism databases

    DMDMi34222826.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB004884 mRNA. Translation: BAA20561.1 . Different initiation.
    AF162667 mRNA. Translation: AAF03095.1 . Different initiation.
    CH471109 Genomic DNA. Translation: EAW94346.1 .
    CH471109 Genomic DNA. Translation: EAW94348.1 .
    BC044925 mRNA. Translation: AAH44925.2 . Different initiation.
    CCDSi CCDS11633.1. [Q86UE8-2 ]
    CCDS45753.1. [Q86UE8-3 ]
    CCDS62283.1. [Q86UE8-1 ]
    RefSeqi NP_001271262.1. NM_001284333.1. [Q86UE8-1 ]
    NP_001271292.1. NM_001284363.1. [Q86UE8-3 ]
    NP_006843.2. NM_006852.3. [Q86UE8-2 ]
    XP_005257026.1. XM_005256969.1. [Q86UE8-2 ]
    XP_005257027.1. XM_005256970.2. [Q86UE8-2 ]
    XP_005257028.1. XM_005256971.2. [Q86UE8-3 ]
    XP_006721710.1. XM_006721647.1. [Q86UE8-2 ]
    XP_006721711.1. XM_006721648.1. [Q86UE8-3 ]
    UniGenei Hs.445078.

    3D structure databases

    ProteinModelPortali Q86UE8.
    SMRi Q86UE8. Positions 458-769.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116201. 14 interactions.
    IntActi Q86UE8. 3 interactions.
    MINTi MINT-5006424.
    STRINGi 9606.ENSP00000275780.

    Chemistry

    BindingDBi Q86UE8.
    ChEMBLi CHEMBL5404.
    GuidetoPHARMACOLOGYi 2243.

    PTM databases

    PhosphoSitei Q86UE8.

    Polymorphism databases

    DMDMi 34222826.

    Proteomic databases

    MaxQBi Q86UE8.
    PaxDbi Q86UE8.
    PRIDEi Q86UE8.

    Protocols and materials databases

    DNASUi 11011.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000326270 ; ENSP00000316512 ; ENSG00000146872 . [Q86UE8-1 ]
    ENST00000343388 ; ENSP00000340800 ; ENSG00000146872 . [Q86UE8-3 ]
    ENST00000346027 ; ENSP00000275780 ; ENSG00000146872 . [Q86UE8-2 ]
    ENST00000542523 ; ENSP00000442311 ; ENSG00000146872 . [Q86UE8-3 ]
    GeneIDi 11011.
    KEGGi hsa:11011.
    UCSCi uc002izz.4. human. [Q86UE8-2 ]
    uc002jaa.4. human. [Q86UE8-3 ]
    uc010ddp.3. human. [Q86UE8-1 ]

    Organism-specific databases

    CTDi 11011.
    GeneCardsi GC17P060556.
    H-InvDB HIX0027107.
    HGNCi HGNC:11842. TLK2.
    HPAi HPA056342.
    MIMi 608439. gene.
    neXtProti NX_Q86UE8.
    PharmGKBi PA36544.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000259522.
    HOVERGENi HBG007938.
    InParanoidi Q86UE8.
    KOi K08864.
    OMAi LVYRKED.
    PhylomeDBi Q86UE8.
    TreeFami TF315233.

    Enzyme and pathway databases

    SignaLinki Q86UE8.

    Miscellaneous databases

    ChiTaRSi TLK2. human.
    GeneWikii TLK2.
    GenomeRNAii 11011.
    NextBioi 41827.
    PROi Q86UE8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86UE8.
    Bgeei Q86UE8.
    CleanExi HS_TLK2.
    Genevestigatori Q86UE8.

    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.
    IPR027086. TLK2.
    [Graphical view ]
    PANTHERi PTHR22974:SF20. PTHR22974:SF20. 1 hit.
    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 3), VARIANT ARG-6, 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 2), FUNCTION, MUTAGENESIS OF ASP-613, SUBCELLULAR LOCATION, INTERACTION WITH TLK1, ENZYME REGULATION.
      Tissue: Placenta1 Publication.
    3. 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] (ISOFORM 1).
      Tissue: Testis.
    5. "From mosquito to man: identification of a novel protein kinase, HsHPK, which is highly expressed in human hepatoma tissues."
      Huang A.M., Chang T.J., Cho W.L., Chou C.K.
      J. Biomed. Sci. 5:135-140(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 189-772 (ISOFORM 2/3), TISSUE SPECIFICITY.
    6. "Nuclear localization of protein kinase U-alpha is regulated by 14-3-3."
      Zhang S., Xing H., Muslin A.J.
      J. Biol. Chem. 274:24865-24872(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH YWHAZ.
    7. "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-613.
    8. "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, ENZYME REGULATION.
    9. "Suppression of tousled-like kinase activity after DNA damage or replication block requires ATM, NBS1 and Chk1."
      Krause D.R., Jonnalagadda J.C., Gatei M.H., Sillje H.H.W., Zhou B.-B., Nigg E.A., Khanna K.
      Oncogene 22:5927-5937(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-750, FUNCTION, ENZYME REGULATION.
    10. "FEZ1 dimerization and interaction with transcription regulatory proteins involves its coiled-coil region."
      Assmann E.M., Alborghetti M.R., Camargo M.E.R., Kobarg J.
      J. Biol. Chem. 281:9869-9881(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FEZ1 AND FEZ2.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-134, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Phosphorylation-mediated control of histone chaperone ASF1 levels by Tousled-like kinases."
      Pilyugin M., Demmers J., Verrijzer C.P., Karch F., Moshkin Y.M.
      PLoS ONE 4:E8328-E8328(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS ASF1A AND ASF1B KINASE, ENZYME REGULATION.
    16. "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-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Genome-wide siRNA screen reveals amino acid starvation-induced autophagy requires SCOC and WAC."
      McKnight N.C., Jefferies H.B., Alemu E.A., Saunders R.E., Howell M., Johansen T., Tooze S.A.
      EMBO J. 31:1931-1946(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "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] ARG-6; ASP-54; GLY-95; GLY-108; LEU-109; LEU-173 AND GLN-262.

    Entry informationi

    Entry nameiTLK2_HUMAN
    AccessioniPrimary (citable) accession number: Q86UE8
    Secondary accession number(s): D3DU07, Q9UKI7, Q9Y4F7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 22, 2003
    Last sequence update: August 22, 2003
    Last modified: October 1, 2014
    This is version 126 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 17
      Human chromosome 17: 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