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Q9UKE5

- TNIK_HUMAN

UniProt

Q9UKE5 - TNIK_HUMAN

Protein

TRAF2 and NCK-interacting protein kinase

Gene

TNIK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase that acts as an essential activator of the Wnt signaling pathway. Recruited to promoters of Wnt target genes and required to activate their expression. May act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the JUN N-terminal pathway. May play a role in the response to environmental stress. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. More generally, it may play a role in cytoskeletal rearrangements and regulate cell spreading. Phosphorylates SMAD1 on Thr-322.6 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei54 – 541ATPPROSITE-ProRule annotation
    Active sitei153 – 1531Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi31 – 399ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein serine/threonine kinase activity Source: UniProtKB
    4. small GTPase regulator activity Source: InterPro

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. activation of JNKK activity Source: UniProtKB
    3. cytoskeleton organization Source: UniProtKB
    4. intracellular signal transduction Source: UniProtKB
    5. protein autophosphorylation Source: UniProtKB
    6. protein phosphorylation Source: UniProtKB
    7. regulation of dendrite morphogenesis Source: UniProtKB
    8. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Neurogenesis, Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
    SignaLinkiQ9UKE5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TRAF2 and NCK-interacting protein kinase (EC:2.7.11.1)
    Gene namesi
    Name:TNIK
    Synonyms:KIAA0551
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:30765. TNIK.

    Subcellular locationi

    Nucleus. Cytoplasm. Recycling endosome. Cytoplasmcytoskeleton
    Note: Associated with recycling endosomes and the cytoskeletal fraction upon RAP2A overexpression.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: UniProtKB
    5. recycling endosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Endosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi54 – 541K → A: Kinase dead. Loss of autophosphorylation and loss of function in cytoskeleton regulation. 2 Publications
    Mutagenesisi152 – 1532RD → AA: Loss of autophosphorylation.
    Mutagenesisi171 – 1722DF → AA: Loss of autophosphorylation.

    Organism-specific databases

    PharmGKBiPA134893180.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13601360TRAF2 and NCK-interacting protein kinasePRO_0000086761Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei326 – 3261Phosphoserine1 Publication
    Modified residuei560 – 5601Phosphoserine1 Publication
    Modified residuei640 – 6401Phosphoserine4 Publications
    Modified residuei678 – 6781Phosphoserine1 Publication
    Modified residuei680 – 6801Phosphoserine1 Publication
    Modified residuei688 – 6881Phosphoserine3 Publications
    Modified residuei707 – 7071Phosphoserine1 Publication
    Modified residuei720 – 7201Phosphoserine2 Publications
    Modified residuei766 – 7661Phosphoserine1 Publication
    Modified residuei769 – 7691Phosphoserine5 Publications

    Post-translational modificationi

    Autophosphorylated. Autophosphorylation is activated by RAP2A and induces association to the cytoskeletal fraction.6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UKE5.
    PaxDbiQ9UKE5.
    PRIDEiQ9UKE5.

    PTM databases

    PhosphoSiteiQ9UKE5.

    Miscellaneous databases

    PMAP-CutDBQ9UKE5.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously. Highest levels observed in heart, brain and skeletal muscle. Expressed in normal colonic epithelia and colorectal cancer tissues.2 Publications

    Gene expression databases

    ArrayExpressiQ9UKE5.
    BgeeiQ9UKE5.
    GenevestigatoriQ9UKE5.

    Organism-specific databases

    HPAiHPA012128.
    HPA012297.

    Interactioni

    Subunit structurei

    Interacts (via the CNH domain) with RAP2A (GTP-bound form preferentially); the interaction is direct and required for the activation of TNIK by RAP2A. Interacts with NEDD4; recruits RAP2A to NEDD4. Interacts with TRAF2 and NCK. Interacts with TCF7L2/TCF4 and CTNNB1; the interaction is direct. Interacts with TANC1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTNNB1P352223EBI-1051794,EBI-491549
    Tanc1Q6F6B32EBI-1051794,EBI-2133582From a different organism.
    TCF7L2Q9NQB03EBI-1051794,EBI-924724

    Protein-protein interaction databases

    BioGridi116682. 37 interactions.
    DIPiDIP-37562N.
    IntActiQ9UKE5. 21 interactions.
    MINTiMINT-7242209.

    Structurei

    Secondary structure

    1
    1360
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni22 – 243
    Beta strandi25 – 3410
    Beta strandi37 – 448
    Turni45 – 473
    Beta strandi50 – 578
    Helixi64 – 7613
    Beta strandi85 – 917
    Beta strandi100 – 1067
    Helixi113 – 1197
    Helixi121 – 1233
    Helixi127 – 14620
    Beta strandi158 – 1614
    Beta strandi167 – 1693
    Turni173 – 1753
    Helixi192 – 1943
    Helixi197 – 2004
    Helixi214 – 22815
    Turni232 – 2354
    Helixi238 – 24710
    Helixi260 – 26910
    Helixi274 – 2763
    Helixi280 – 2845
    Helixi287 – 2904
    Helixi295 – 31117

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2X7FX-ray2.80A/B/C/D/E1-325[»]
    ProteinModelPortaliQ9UKE5.
    SMRiQ9UKE5. Positions 13-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UKE5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 289265Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini1047 – 1334288CNHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni290 – 1047758Mediates interaction with NEDD4Add
    BLAST

    Sequence similaritiesi

    Contains 1 CNH domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG036506.
    InParanoidiQ9UKE5.
    KOiK08840.
    OMAiTEQYNVG.
    OrthoDBiEOG73803V.
    PhylomeDBiQ9UKE5.
    TreeFamiTF105138.

    Family and domain databases

    InterProiIPR001180. Citron.
    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]
    PfamiPF00780. CNH. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00036. CNH. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50219. CNH. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UKE5-1) [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

    MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL     50
    AAIKVMDVTG DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ 100
    LWLVMEFCGA GSVTDLIKNT KGNTLKEEWI AYICREILRG LSHLHQHKVI 150
    HRDIKGQNVL LTENAEVKLV DFGVSAQLDR TVGRRNTFIG TPYWMAPEVI 200
    ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR ALFLIPRNPA 250
    PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI 300
    QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL 350
    RRDFLRLQLA NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE 400
    QRRRLEEQQR REKELRKQQE REQRRHYEEQ MRREEERRRA EHEQEYIRRQ 450
    LEEEQRQLEI LQQQLLHEQA LLLEYKRKQL EEQRQAERLQ RQLKQERDYL 500
    VSLQHQRQEQ RPVEKKPLYH YKEGMSPSEK PAWAKEVEER SRLNRQSSPA 550
    MPHKVANRIS DPNLPPRSES FSISGVQPAR TPPMLRPVDP QIPHLVAVKS 600
    QGPALTASQS VHEQPTKGLS GFQEALNVTS HRVEMPRQNS DPTSENPPLP 650
    TRIEKFDRSS WLRQEEDIPP KVPQRTTSIS PALARKNSPG NGSALGPRLG 700
    SQPIRASNPD LRRTEPILES PLQRTSSGSS SSSSTPSSQP SSQGGSQPGS 750
    QAGSSERTRV RANSKSEGSP VLPHEPAKVK PEESRDITRP SRPASYKKAI 800
    DEDLTALAKE LRELRIEETN RPMKKVTDYS SSSEESESSE EEEEDGESET 850
    HDGTVAVSDI PRLIPTGAPG SNEQYNVGMV GTHGLETSHA DSFSGSISRE 900
    GTLMIRETSG EKKRSGHSDS NGFAGHINLP DLVQQSHSPA GTPTEGLGRV 950
    STHSQEMDSG TEYGMGSSTK ASFTPFVDPR VYQTSPTDED EEDEESSAAA 1000
    LFTSELLRQE QAKLNEARKI SVVNVNPTNI RPHSDTPEIR KYKKRFNSEI 1050
    LCAALWGVNL LVGTENGLML LDRSGQGKVY NLINRRRFQQ MDVLEGLNVL 1100
    VTISGKKNKL RVYYLSWLRN RILHNDPEVE KKQGWITVGD LEGCIHYKVV 1150
    KYERIKFLVI ALKNAVEIYA WAPKPYHKFM AFKSFADLQH KPLLVDLTVE 1200
    EGQRLKVIFG SHTGFHVIDV DSGNSYDIYI PSHIQGNITP HAIVILPKTD 1250
    GMEMLVCYED EGVYVNTYGR ITKDVVLQWG EMPTSVAYIH SNQIMGWGEK 1300
    AIEIRSVETG HLDGVFMHKR AQRLKFLCER NDKVFFASVR SGGSSQVFFM 1350
    TLNRNSMMNW 1360
    Length:1,360
    Mass (Da):154,943
    Last modified:May 1, 2000 - v1
    Checksum:i3590BC2905A72C3D
    GO
    Isoform 2 (identifier: Q9UKE5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         445-473: Missing.

    Show »
    Length:1,331
    Mass (Da):151,300
    Checksum:i85378CBC98631411
    GO
    Isoform 3 (identifier: Q9UKE5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         537-591: Missing.

    Show »
    Length:1,305
    Mass (Da):148,829
    Checksum:i209230BB15712DFC
    GO
    Isoform 4 (identifier: Q9UKE5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         795-802: Missing.

    Show »
    Length:1,352
    Mass (Da):154,008
    Checksum:iF4708A71FF26C54F
    GO
    Isoform 5 (identifier: Q9UKE5-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         445-473: Missing.
         537-591: Missing.

    Show »
    Length:1,276
    Mass (Da):145,186
    Checksum:i9B85E462E4FAE9F0
    GO
    Isoform 6 (identifier: Q9UKE5-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         445-473: Missing.
         795-802: Missing.

    Show »
    Length:1,323
    Mass (Da):150,365
    Checksum:i93B2E73EF75034B9
    GO
    Isoform 7 (identifier: Q9UKE5-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         537-591: Missing.
         795-802: Missing.

    Show »
    Length:1,297
    Mass (Da):147,894
    Checksum:iEED944B571948D3F
    GO
    Isoform 8 (identifier: Q9UKE5-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         445-473: Missing.
         537-591: Missing.
         795-802: Missing.

    Show »
    Length:1,268
    Mass (Da):144,251
    Checksum:i55AD5F59B7A08A2A
    GO

    Sequence cautioni

    The sequence BAA25477.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti778 – 7781K → E.1 Publication
    Corresponds to variant rs55778284 [ dbSNP | Ensembl ].
    VAR_041231
    Natural varianti910 – 9101G → E.1 Publication
    Corresponds to variant rs35090763 [ dbSNP | Ensembl ].
    VAR_041232
    Natural varianti999 – 9991A → T.1 Publication
    Corresponds to variant rs17857452 [ dbSNP | Ensembl ].
    VAR_041233

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei445 – 47329Missing in isoform 2, isoform 5, isoform 6 and isoform 8. 2 PublicationsVSP_004889Add
    BLAST
    Alternative sequencei537 – 59155Missing in isoform 3, isoform 5, isoform 7 and isoform 8. 2 PublicationsVSP_004890Add
    BLAST
    Alternative sequencei795 – 8028Missing in isoform 4, isoform 6, isoform 7 and isoform 8. 1 PublicationVSP_004891

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF172264 mRNA. Translation: AAF03782.1.
    AF172268 mRNA. Translation: AAF03786.1.
    AF172267 mRNA. Translation: AAF03785.1.
    AF172266 mRNA. Translation: AAF03784.1.
    AF172265 mRNA. Translation: AAF03783.1.
    AF172270 mRNA. Translation: AAF03788.1.
    AF172271 mRNA. Translation: AAF03789.1.
    AF172269 mRNA. Translation: AAF03787.1.
    AB011123 mRNA. Translation: BAA25477.2. Different initiation.
    AK291056 mRNA. Translation: BAF83745.1.
    AC026315 Genomic DNA. No translation available.
    AC078793 Genomic DNA. No translation available.
    AC092919 Genomic DNA. No translation available.
    AC137517 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78484.1.
    CH471052 Genomic DNA. Translation: EAW78489.1.
    CH471052 Genomic DNA. Translation: EAW78492.1.
    CH471052 Genomic DNA. Translation: EAW78493.1.
    BC019081 mRNA. Translation: AAH19081.2.
    BC150256 mRNA. Translation: AAI50257.1.
    CCDSiCCDS46956.1. [Q9UKE5-1]
    CCDS54673.1. [Q9UKE5-8]
    CCDS54674.1. [Q9UKE5-5]
    CCDS54675.1. [Q9UKE5-6]
    CCDS54676.1. [Q9UKE5-2]
    CCDS54677.1. [Q9UKE5-7]
    CCDS54678.1. [Q9UKE5-3]
    CCDS54679.1. [Q9UKE5-4]
    RefSeqiNP_001155032.1. NM_001161560.1. [Q9UKE5-4]
    NP_001155033.1. NM_001161561.1. [Q9UKE5-2]
    NP_001155034.1. NM_001161562.1. [Q9UKE5-6]
    NP_001155035.1. NM_001161563.1. [Q9UKE5-3]
    NP_001155036.1. NM_001161564.1. [Q9UKE5-7]
    NP_001155037.1. NM_001161565.1. [Q9UKE5-5]
    NP_001155038.1. NM_001161566.1. [Q9UKE5-8]
    NP_055843.1. NM_015028.2. [Q9UKE5-1]
    UniGeneiHs.34024.

    Genome annotation databases

    EnsembliENST00000284483; ENSP00000284483; ENSG00000154310. [Q9UKE5-4]
    ENST00000341852; ENSP00000345352; ENSG00000154310. [Q9UKE5-5]
    ENST00000357327; ENSP00000349880; ENSG00000154310. [Q9UKE5-2]
    ENST00000436636; ENSP00000399511; ENSG00000154310. [Q9UKE5-1]
    ENST00000460047; ENSP00000418916; ENSG00000154310. [Q9UKE5-7]
    ENST00000470834; ENSP00000419990; ENSG00000154310. [Q9UKE5-6]
    ENST00000475336; ENSP00000418156; ENSG00000154310. [Q9UKE5-8]
    ENST00000488470; ENSP00000418378; ENSG00000154310. [Q9UKE5-3]
    GeneIDi23043.
    KEGGihsa:23043.
    UCSCiuc003fhh.2. human. [Q9UKE5-1]
    uc003fhi.2. human. [Q9UKE5-3]
    uc003fhj.2. human. [Q9UKE5-2]
    uc003fhk.2. human. [Q9UKE5-4]
    uc003fhl.2. human. [Q9UKE5-5]
    uc003fhm.2. human. [Q9UKE5-7]
    uc003fhn.2. human. [Q9UKE5-6]
    uc003fho.2. human. [Q9UKE5-8]

    Polymorphism databases

    DMDMi29840818.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF172264 mRNA. Translation: AAF03782.1 .
    AF172268 mRNA. Translation: AAF03786.1 .
    AF172267 mRNA. Translation: AAF03785.1 .
    AF172266 mRNA. Translation: AAF03784.1 .
    AF172265 mRNA. Translation: AAF03783.1 .
    AF172270 mRNA. Translation: AAF03788.1 .
    AF172271 mRNA. Translation: AAF03789.1 .
    AF172269 mRNA. Translation: AAF03787.1 .
    AB011123 mRNA. Translation: BAA25477.2 . Different initiation.
    AK291056 mRNA. Translation: BAF83745.1 .
    AC026315 Genomic DNA. No translation available.
    AC078793 Genomic DNA. No translation available.
    AC092919 Genomic DNA. No translation available.
    AC137517 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78484.1 .
    CH471052 Genomic DNA. Translation: EAW78489.1 .
    CH471052 Genomic DNA. Translation: EAW78492.1 .
    CH471052 Genomic DNA. Translation: EAW78493.1 .
    BC019081 mRNA. Translation: AAH19081.2 .
    BC150256 mRNA. Translation: AAI50257.1 .
    CCDSi CCDS46956.1. [Q9UKE5-1 ]
    CCDS54673.1. [Q9UKE5-8 ]
    CCDS54674.1. [Q9UKE5-5 ]
    CCDS54675.1. [Q9UKE5-6 ]
    CCDS54676.1. [Q9UKE5-2 ]
    CCDS54677.1. [Q9UKE5-7 ]
    CCDS54678.1. [Q9UKE5-3 ]
    CCDS54679.1. [Q9UKE5-4 ]
    RefSeqi NP_001155032.1. NM_001161560.1. [Q9UKE5-4 ]
    NP_001155033.1. NM_001161561.1. [Q9UKE5-2 ]
    NP_001155034.1. NM_001161562.1. [Q9UKE5-6 ]
    NP_001155035.1. NM_001161563.1. [Q9UKE5-3 ]
    NP_001155036.1. NM_001161564.1. [Q9UKE5-7 ]
    NP_001155037.1. NM_001161565.1. [Q9UKE5-5 ]
    NP_001155038.1. NM_001161566.1. [Q9UKE5-8 ]
    NP_055843.1. NM_015028.2. [Q9UKE5-1 ]
    UniGenei Hs.34024.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2X7F X-ray 2.80 A/B/C/D/E 1-325 [» ]
    ProteinModelPortali Q9UKE5.
    SMRi Q9UKE5. Positions 13-313.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116682. 37 interactions.
    DIPi DIP-37562N.
    IntActi Q9UKE5. 21 interactions.
    MINTi MINT-7242209.

    Chemistry

    BindingDBi Q9UKE5.
    ChEMBLi CHEMBL4527.
    GuidetoPHARMACOLOGYi 2244.

    PTM databases

    PhosphoSitei Q9UKE5.

    Polymorphism databases

    DMDMi 29840818.

    Proteomic databases

    MaxQBi Q9UKE5.
    PaxDbi Q9UKE5.
    PRIDEi Q9UKE5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284483 ; ENSP00000284483 ; ENSG00000154310 . [Q9UKE5-4 ]
    ENST00000341852 ; ENSP00000345352 ; ENSG00000154310 . [Q9UKE5-5 ]
    ENST00000357327 ; ENSP00000349880 ; ENSG00000154310 . [Q9UKE5-2 ]
    ENST00000436636 ; ENSP00000399511 ; ENSG00000154310 . [Q9UKE5-1 ]
    ENST00000460047 ; ENSP00000418916 ; ENSG00000154310 . [Q9UKE5-7 ]
    ENST00000470834 ; ENSP00000419990 ; ENSG00000154310 . [Q9UKE5-6 ]
    ENST00000475336 ; ENSP00000418156 ; ENSG00000154310 . [Q9UKE5-8 ]
    ENST00000488470 ; ENSP00000418378 ; ENSG00000154310 . [Q9UKE5-3 ]
    GeneIDi 23043.
    KEGGi hsa:23043.
    UCSCi uc003fhh.2. human. [Q9UKE5-1 ]
    uc003fhi.2. human. [Q9UKE5-3 ]
    uc003fhj.2. human. [Q9UKE5-2 ]
    uc003fhk.2. human. [Q9UKE5-4 ]
    uc003fhl.2. human. [Q9UKE5-5 ]
    uc003fhm.2. human. [Q9UKE5-7 ]
    uc003fhn.2. human. [Q9UKE5-6 ]
    uc003fho.2. human. [Q9UKE5-8 ]

    Organism-specific databases

    CTDi 23043.
    GeneCardsi GC03M170779.
    HGNCi HGNC:30765. TNIK.
    HPAi HPA012128.
    HPA012297.
    MIMi 610005. gene.
    neXtProti NX_Q9UKE5.
    PharmGKBi PA134893180.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG036506.
    InParanoidi Q9UKE5.
    KOi K08840.
    OMAi TEQYNVG.
    OrthoDBi EOG73803V.
    PhylomeDBi Q9UKE5.
    TreeFami TF105138.

    Enzyme and pathway databases

    Reactomei REACT_169436. Oxidative Stress Induced Senescence.
    SignaLinki Q9UKE5.

    Miscellaneous databases

    EvolutionaryTracei Q9UKE5.
    GeneWikii TNIK.
    GenomeRNAii 23043.
    NextBioi 44076.
    PMAP-CutDB Q9UKE5.
    PROi Q9UKE5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKE5.
    Bgeei Q9UKE5.
    Genevestigatori Q9UKE5.

    Family and domain databases

    InterProi IPR001180. Citron.
    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 PF00780. CNH. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00036. CNH. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50219. CNH. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "TNIK, a novel member of the germinal center kinase family that activates the c-Jun N-terminal kinase pathway and regulates the cytoskeleton."
      Fu C.A., Shen M., Huang B.C., Lasaga J., Payan D.G., Luo Y.
      J. Biol. Chem. 274:30729-30737(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRAF2 AND NCK, AUTOPHOSPHORYLATION.
    2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "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.
    4. "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] (ISOFORM 5).
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Placenta.
    8. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "The Traf2- and Nck-interacting kinase as a putative effector of Rap2 to regulate actin cytoskeleton."
      Taira K., Umikawa M., Takei K., Myagmar B.-E., Shinzato M., Machida N., Uezato H., Nonaka S., Kariya K.
      J. Biol. Chem. 279:49488-49496(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAP2A, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54.
    10. Cited for: INTERACTION WITH TANC1.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    12. "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-640; SER-688; SER-720 AND SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678 AND SER-680, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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].
    15. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    16. "The kinase TNIK is an essential activator of Wnt target genes."
      Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J., Mohammed S., Heck A.J., Clevers H.
      EMBO J. 28:3329-3340(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54; 152-ARG-ASP-153 AND 171-ASP-PHE-172, INTERACTION WITH TCF7L2 AND CTNNB1, TISSUE SPECIFICITY, FUNCTION.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560; SER-640; SER-688; SER-707; SER-720; SER-766 AND SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: FUNCTION, INTERACTION WITH NEDD4 AND RAP2A.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: FUNCTION.
    21. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-640; SER-688 AND SER-769, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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] GLU-778; GLU-910 AND THR-999.

    Entry informationi

    Entry nameiTNIK_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKE5
    Secondary accession number(s): A7E2A3
    , A8K4U1, D3DNQ6, O60298, Q8WUY7, Q9UKD8, Q9UKD9, Q9UKE0, Q9UKE1, Q9UKE2, Q9UKE3, Q9UKE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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