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TRAF2 and NCK-interacting protein kinase (EC 2.7.11.1)

 TNIK_HUMAN              Reviewed;        1360 AA.
Q9UKE5; A7E2A3; A8K4U1; D3DNQ6; O60298; Q8WUY7; Q9UKD8; Q9UKD9;
Q9UKE0; Q9UKE1; Q9UKE2; Q9UKE3; Q9UKE4;
28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 173.
RecName: Full=TRAF2 and NCK-interacting protein kinase;
EC=2.7.11.1;
Name=TNIK; Synonyms=KIAA0551;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAF03782.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8),
FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRAF2 AND NCK, AND
AUTOPHOSPHORYLATION.
PubMed=10521462; DOI=10.1074/jbc.274.43.30729;
Fu C.A., Shen M., Huang B.C., Lasaga J., Payan D.G., Luo Y.;
"TNIK, a novel member of the germinal center kinase family that
activates the c-Jun N-terminal kinase pathway and regulates the
cytoskeleton.";
J. Biol. Chem. 274:30729-30737(1999).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"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.";
DNA Res. 5:31-39(1998).
[3] {ECO:0000305}
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
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.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[9]
FUNCTION, INTERACTION WITH RAP2A, SUBCELLULAR LOCATION,
AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-54.
PubMed=15342639; DOI=10.1074/jbc.M406370200;
Taira K., Umikawa M., Takei K., Myagmar B.-E., Shinzato M.,
Machida N., Uezato H., Nonaka S., Kariya K.;
"The Traf2- and Nck-interacting kinase as a putative effector of Rap2
to regulate actin cytoskeleton.";
J. Biol. Chem. 279:49488-49496(2004).
[10]
INTERACTION WITH TANC1.
PubMed=18930710; DOI=10.1016/j.bbrc.2008.10.038;
Nonaka H., Takei K., Umikawa M., Oshiro M., Kuninaka K.,
Bayarjargal M., Asato T., Yamashiro Y., Uechi Y., Endo S., Suzuki T.,
Kariya K.;
"MINK is a Rap2 effector for phosphorylation of the postsynaptic
scaffold protein TANC1.";
Biochem. Biophys. Res. Commun. 377:573-578(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-769, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640; SER-688; SER-720
AND SER-769, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678 AND SER-680, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19061864; DOI=10.1016/j.bbrc.2008.11.107;
Uechi Y., Bayarjargal M., Umikawa M., Oshiro M., Takei K.,
Yamashiro Y., Asato T., Endo S., Misaki R., Taguchi T., Kariya K.;
"Rap2 function requires palmitoylation and recycling endosome
localization.";
Biochem. Biophys. Res. Commun. 378:732-737(2009).
[16]
SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54;
152-ARG-ASP-153 AND 171-ASP-PHE-172, INTERACTION WITH TCF7L2 AND
CTNNB1, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=19816403; DOI=10.1038/emboj.2009.285;
Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J.,
Mohammed S., Heck A.J., Clevers H.;
"The kinase TNIK is an essential activator of Wnt target genes.";
EMBO J. 28:3329-3340(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560; SER-640; SER-688;
SER-707; SER-720; SER-766 AND SER-769, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[18]
FUNCTION, AND INTERACTION WITH NEDD4 AND RAP2A.
PubMed=20159449; DOI=10.1016/j.neuron.2010.01.007;
Kawabe H., Neeb A., Dimova K., Young S.M. Jr., Takeda M.,
Katsurabayashi S., Mitkovski M., Malakhova O.A., Zhang D.E.,
Umikawa M., Kariya K., Goebbels S., Nave K.A., Rosenmund C., Jahn O.,
Rhee J., Brose N.;
"Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite
development.";
Neuron 65:358-372(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
FUNCTION.
PubMed=21690388; DOI=10.1073/pnas.1104128108;
Kaneko S., Chen X., Lu P., Yao X., Wright T.G., Rajurkar M.,
Kariya K., Mao J., Ip Y.T., Xu L.;
"Smad inhibition by the Ste20 kinase Misshapen.";
Proc. Natl. Acad. Sci. U.S.A. 108:11127-11132(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-688 AND
SER-769, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; SER-600; SER-608;
SER-610; SER-640; SER-678; SER-680; SER-688; SER-701; SER-707;
SER-720; SER-764; SER-769 AND SER-959, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-680, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
POSSIBLE INVOLVEMENT IN MRT54.
PubMed=27106596; DOI=10.1007/s00439-016-1671-9;
Anazi S., Shamseldin H.E., AlNaqeb D., Abouelhoda M., Monies D.,
Salih M.A., Al-Rubeaan K., Alkuraya F.S.;
"A null mutation in TNIK defines a novel locus for intellectual
disability.";
Hum. Genet. 135:773-778(2016).
[25]
VARIANTS [LARGE SCALE ANALYSIS] GLU-778; GLU-910 AND THR-999.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10521462,
ECO:0000269|PubMed:15342639, ECO:0000269|PubMed:19061864,
ECO:0000269|PubMed:19816403, ECO:0000269|PubMed:20159449,
ECO:0000269|PubMed:21690388}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:10521462}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:10521462, ECO:0000269|PubMed:15342639,
ECO:0000269|PubMed:18930710, ECO:0000269|PubMed:19816403,
ECO:0000269|PubMed:20159449}.
-!- INTERACTION:
P35222:CTNNB1; NbExp=3; IntAct=EBI-1051794, EBI-491549;
O14920:IKBKB; NbExp=2; IntAct=EBI-1051794, EBI-81266;
P03230:LMP1 (xeno); NbExp=7; IntAct=EBI-1051794, EBI-6973030;
O43318:MAP3K7; NbExp=3; IntAct=EBI-1051794, EBI-358684;
Q9NYJ8:TAB2; NbExp=3; IntAct=EBI-1051794, EBI-358708;
Q6F6B3:Tanc1 (xeno); NbExp=2; IntAct=EBI-1051794, EBI-2133582;
Q9NQB0:TCF7L2; NbExp=3; IntAct=EBI-1051794, EBI-924724;
Q12933:TRAF2; NbExp=2; IntAct=EBI-1051794, EBI-355744;
Q9Y4K3:TRAF6; NbExp=3; IntAct=EBI-1051794, EBI-359276;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Recycling endosome.
Cytoplasm, cytoskeleton. Note=Associated with recycling endosomes
and the cytoskeletal fraction upon RAP2A overexpression.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1;
IsoId=Q9UKE5-1; Sequence=Displayed;
Name=2;
IsoId=Q9UKE5-2; Sequence=VSP_004889;
Name=3;
IsoId=Q9UKE5-3; Sequence=VSP_004890;
Name=4;
IsoId=Q9UKE5-4; Sequence=VSP_004891;
Name=5;
IsoId=Q9UKE5-5; Sequence=VSP_004889, VSP_004890;
Name=6;
IsoId=Q9UKE5-6; Sequence=VSP_004889, VSP_004891;
Name=7;
IsoId=Q9UKE5-7; Sequence=VSP_004890, VSP_004891;
Name=8;
IsoId=Q9UKE5-8; Sequence=VSP_004889, VSP_004890, VSP_004891;
-!- TISSUE SPECIFICITY: Expressed ubiquitously. Highest levels
observed in heart, brain and skeletal muscle. Expressed in normal
colonic epithelia and colorectal cancer tissues.
{ECO:0000269|PubMed:10521462, ECO:0000269|PubMed:19816403}.
-!- PTM: Autophosphorylated. Autophosphorylation is activated by RAP2A
and induces association to the cytoskeletal fraction.
-!- DISEASE: Mental retardation, autosomal recessive 54 (MRT54)
[MIM:617028]: A form of mental retardation, a disorder
characterized by significantly below average general intellectual
functioning associated with impairments in adaptive behavior and
manifested during the developmental period. MRT54 patients
manifest intellectual disability, delayed speech and
hyperactivity. {ECO:0000269|PubMed:27106596}. Note=The disease may
be caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA25477.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF172264; AAF03782.1; -; mRNA.
EMBL; AF172268; AAF03786.1; -; mRNA.
EMBL; AF172267; AAF03785.1; -; mRNA.
EMBL; AF172266; AAF03784.1; -; mRNA.
EMBL; AF172265; AAF03783.1; -; mRNA.
EMBL; AF172270; AAF03788.1; -; mRNA.
EMBL; AF172271; AAF03789.1; -; mRNA.
EMBL; AF172269; AAF03787.1; -; mRNA.
EMBL; AB011123; BAA25477.2; ALT_INIT; mRNA.
EMBL; AK291056; BAF83745.1; -; mRNA.
EMBL; AC026315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC078793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC137517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW78484.1; -; Genomic_DNA.
EMBL; CH471052; EAW78489.1; -; Genomic_DNA.
EMBL; CH471052; EAW78492.1; -; Genomic_DNA.
EMBL; CH471052; EAW78493.1; -; Genomic_DNA.
EMBL; BC019081; AAH19081.2; -; mRNA.
EMBL; BC150256; AAI50257.1; -; mRNA.
CCDS; CCDS46956.1; -. [Q9UKE5-1]
CCDS; CCDS54673.1; -. [Q9UKE5-8]
CCDS; CCDS54674.1; -. [Q9UKE5-5]
CCDS; CCDS54675.1; -. [Q9UKE5-6]
CCDS; CCDS54676.1; -. [Q9UKE5-2]
CCDS; CCDS54677.1; -. [Q9UKE5-7]
CCDS; CCDS54678.1; -. [Q9UKE5-3]
CCDS; CCDS54679.1; -. [Q9UKE5-4]
RefSeq; NP_001155032.1; NM_001161560.2. [Q9UKE5-4]
RefSeq; NP_001155033.1; NM_001161561.2. [Q9UKE5-2]
RefSeq; NP_001155034.1; NM_001161562.2. [Q9UKE5-6]
RefSeq; NP_001155035.1; NM_001161563.2. [Q9UKE5-3]
RefSeq; NP_001155036.1; NM_001161564.2. [Q9UKE5-7]
RefSeq; NP_001155037.1; NM_001161565.2. [Q9UKE5-5]
RefSeq; NP_001155038.1; NM_001161566.2. [Q9UKE5-8]
RefSeq; NP_055843.1; NM_015028.3. [Q9UKE5-1]
UniGene; Hs.34024; -.
UniGene; Hs.723245; -.
PDB; 2X7F; X-ray; 2.80 A; A/B/C/D/E=1-325.
PDB; 5AX9; X-ray; 2.40 A; A/B/C=11-314.
PDB; 5CWZ; X-ray; 2.90 A; A/B/C=11-314.
PDB; 5D7A; X-ray; 2.90 A; A/B/C=11-314.
PDBsum; 2X7F; -.
PDBsum; 5AX9; -.
PDBsum; 5CWZ; -.
PDBsum; 5D7A; -.
ProteinModelPortal; Q9UKE5; -.
SMR; Q9UKE5; -.
BioGrid; 116682; 46.
DIP; DIP-37562N; -.
IntAct; Q9UKE5; 30.
MINT; MINT-7242209; -.
STRING; 9606.ENSP00000399511; -.
BindingDB; Q9UKE5; -.
ChEMBL; CHEMBL4527; -.
GuidetoPHARMACOLOGY; 2244; -.
iPTMnet; Q9UKE5; -.
PhosphoSitePlus; Q9UKE5; -.
BioMuta; TNIK; -.
DMDM; 29840818; -.
EPD; Q9UKE5; -.
PaxDb; Q9UKE5; -.
PeptideAtlas; Q9UKE5; -.
PRIDE; Q9UKE5; -.
Ensembl; ENST00000284483; ENSP00000284483; ENSG00000154310. [Q9UKE5-4]
Ensembl; ENST00000341852; ENSP00000345352; ENSG00000154310. [Q9UKE5-5]
Ensembl; ENST00000357327; ENSP00000349880; ENSG00000154310. [Q9UKE5-2]
Ensembl; ENST00000436636; ENSP00000399511; ENSG00000154310. [Q9UKE5-1]
Ensembl; ENST00000460047; ENSP00000418916; ENSG00000154310. [Q9UKE5-7]
Ensembl; ENST00000470834; ENSP00000419990; ENSG00000154310. [Q9UKE5-6]
Ensembl; ENST00000475336; ENSP00000418156; ENSG00000154310. [Q9UKE5-8]
Ensembl; ENST00000488470; ENSP00000418378; ENSG00000154310. [Q9UKE5-3]
GeneID; 23043; -.
KEGG; hsa:23043; -.
UCSC; uc003fhh.3; human. [Q9UKE5-1]
CTD; 23043; -.
DisGeNET; 23043; -.
EuPathDB; HostDB:ENSG00000154310.16; -.
GeneCards; TNIK; -.
HGNC; HGNC:30765; TNIK.
HPA; HPA012128; -.
HPA; HPA012297; -.
MalaCards; TNIK; -.
MIM; 610005; gene.
MIM; 617028; phenotype.
neXtProt; NX_Q9UKE5; -.
OpenTargets; ENSG00000154310; -.
PharmGKB; PA134893180; -.
eggNOG; KOG0587; Eukaryota.
eggNOG; ENOG410XPHR; LUCA.
GeneTree; ENSGT00900000140838; -.
HOVERGEN; HBG036506; -.
InParanoid; Q9UKE5; -.
KO; K08840; -.
OMA; KHTQGAI; -.
OrthoDB; EOG091G018A; -.
PhylomeDB; Q9UKE5; -.
TreeFam; TF105138; -.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
SignaLink; Q9UKE5; -.
SIGNOR; Q9UKE5; -.
ChiTaRS; TNIK; human.
EvolutionaryTrace; Q9UKE5; -.
GeneWiki; TNIK; -.
GenomeRNAi; 23043; -.
PMAP-CutDB; Q9UKE5; -.
PRO; PR:Q9UKE5; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000154310; -.
ExpressionAtlas; Q9UKE5; baseline and differential.
Genevisible; Q9UKE5; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008349; F:MAP kinase kinase kinase kinase activity; IBA:GO_Central.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
GO; GO:0007256; P:activation of JNKK activity; IDA:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0030033; P:microvillus assembly; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IDA:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR001180; CNH_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00780; CNH; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00036; CNH; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50219; CNH; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Cytoskeleton; Endosome; Kinase; Mental retardation;
Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transferase; Wnt signaling pathway.
CHAIN 1 1360 TRAF2 and NCK-interacting protein kinase.
/FTId=PRO_0000086761.
DOMAIN 25 289 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 1047 1334 CNH. {ECO:0000255|PROSITE-
ProRule:PRU00795}.
NP_BIND 31 39 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 290 1047 Mediates interaction with NEDD4.
{ECO:0000269|PubMed:20159449}.
ACT_SITE 153 153 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 54 54 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 187 187 Phosphothreonine.
{ECO:0000250|UniProtKB:P83510}.
MOD_RES 324 324 Phosphoserine.
{ECO:0000250|UniProtKB:P83510}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 560 560 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 581 581 Phosphothreonine.
{ECO:0000250|UniProtKB:P83510}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 608 608 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 610 610 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 678 678 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 680 680 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 701 701 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 707 707 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 720 720 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:23186163}.
MOD_RES 764 764 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 766 766 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 769 769 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 959 959 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 445 473 Missing (in isoform 2, isoform 5, isoform
6 and isoform 8).
{ECO:0000303|PubMed:10521462,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_004889.
VAR_SEQ 537 591 Missing (in isoform 3, isoform 5, isoform
7 and isoform 8).
{ECO:0000303|PubMed:10521462,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_004890.
VAR_SEQ 795 802 Missing (in isoform 4, isoform 6, isoform
7 and isoform 8).
{ECO:0000303|PubMed:10521462}.
/FTId=VSP_004891.
VARIANT 778 778 K -> E (in dbSNP:rs55778284).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041231.
VARIANT 910 910 G -> E (in dbSNP:rs35090763).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041232.
VARIANT 999 999 A -> T (in dbSNP:rs17857452).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041233.
MUTAGEN 54 54 K->A: Kinase dead. Loss of
autophosphorylation and loss of function
in cytoskeleton regulation.
{ECO:0000269|PubMed:15342639,
ECO:0000269|PubMed:19816403}.
MUTAGEN 152 153 RD->AA: Loss of autophosphorylation.
{ECO:0000269|PubMed:19816403}.
MUTAGEN 171 172 DF->AA: Loss of autophosphorylation.
{ECO:0000269|PubMed:19816403}.
HELIX 15 17 {ECO:0000244|PDB:5AX9}.
TURN 22 24 {ECO:0000244|PDB:5AX9}.
STRAND 25 34 {ECO:0000244|PDB:5AX9}.
STRAND 37 44 {ECO:0000244|PDB:5AX9}.
TURN 45 47 {ECO:0000244|PDB:5AX9}.
STRAND 50 58 {ECO:0000244|PDB:5AX9}.
TURN 60 62 {ECO:0000244|PDB:5AX9}.
HELIX 63 76 {ECO:0000244|PDB:5AX9}.
STRAND 85 91 {ECO:0000244|PDB:5AX9}.
STRAND 95 97 {ECO:0000244|PDB:5AX9}.
STRAND 99 106 {ECO:0000244|PDB:5AX9}.
HELIX 113 118 {ECO:0000244|PDB:5AX9}.
HELIX 121 123 {ECO:0000244|PDB:5AX9}.
HELIX 127 146 {ECO:0000244|PDB:5AX9}.
HELIX 156 158 {ECO:0000244|PDB:5AX9}.
STRAND 159 161 {ECO:0000244|PDB:5AX9}.
STRAND 167 169 {ECO:0000244|PDB:5AX9}.
TURN 173 175 {ECO:0000244|PDB:2X7F}.
HELIX 192 194 {ECO:0000244|PDB:2X7F}.
HELIX 197 199 {ECO:0000244|PDB:5AX9}.
STRAND 203 207 {ECO:0000244|PDB:5CWZ}.
HELIX 212 228 {ECO:0000244|PDB:5AX9}.
TURN 232 235 {ECO:0000244|PDB:5AX9}.
HELIX 238 247 {ECO:0000244|PDB:5AX9}.
HELIX 260 269 {ECO:0000244|PDB:5AX9}.
HELIX 274 276 {ECO:0000244|PDB:5AX9}.
HELIX 280 283 {ECO:0000244|PDB:5AX9}.
HELIX 287 290 {ECO:0000244|PDB:5AX9}.
HELIX 295 306 {ECO:0000244|PDB:5AX9}.
SEQUENCE 1360 AA; 154943 MW; 3590BC2905A72C3D CRC64;
MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL AAIKVMDVTG
DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ LWLVMEFCGA GSVTDLIKNT
KGNTLKEEWI AYICREILRG LSHLHQHKVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
TVGRRNTFIG TPYWMAPEVI ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR
ALFLIPRNPA PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL RRDFLRLQLA
NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE QRRRLEEQQR REKELRKQQE
REQRRHYEEQ MRREEERRRA EHEQEYIRRQ LEEEQRQLEI LQQQLLHEQA LLLEYKRKQL
EEQRQAERLQ RQLKQERDYL VSLQHQRQEQ RPVEKKPLYH YKEGMSPSEK PAWAKEVEER
SRLNRQSSPA MPHKVANRIS DPNLPPRSES FSISGVQPAR TPPMLRPVDP QIPHLVAVKS
QGPALTASQS VHEQPTKGLS GFQEALNVTS HRVEMPRQNS DPTSENPPLP TRIEKFDRSS
WLRQEEDIPP KVPQRTTSIS PALARKNSPG NGSALGPRLG SQPIRASNPD LRRTEPILES
PLQRTSSGSS SSSSTPSSQP SSQGGSQPGS QAGSSERTRV RANSKSEGSP VLPHEPAKVK
PEESRDITRP SRPASYKKAI DEDLTALAKE LRELRIEETN RPMKKVTDYS SSSEESESSE
EEEEDGESET HDGTVAVSDI PRLIPTGAPG SNEQYNVGMV GTHGLETSHA DSFSGSISRE
GTLMIRETSG EKKRSGHSDS NGFAGHINLP DLVQQSHSPA GTPTEGLGRV STHSQEMDSG
TEYGMGSSTK ASFTPFVDPR VYQTSPTDED EEDEESSAAA LFTSELLRQE QAKLNEARKI
SVVNVNPTNI RPHSDTPEIR KYKKRFNSEI LCAALWGVNL LVGTENGLML LDRSGQGKVY
NLINRRRFQQ MDVLEGLNVL VTISGKKNKL RVYYLSWLRN RILHNDPEVE KKQGWITVGD
LEGCIHYKVV KYERIKFLVI ALKNAVEIYA WAPKPYHKFM AFKSFADLQH KPLLVDLTVE
EGQRLKVIFG SHTGFHVIDV DSGNSYDIYI PSHIQGNITP HAIVILPKTD GMEMLVCYED
EGVYVNTYGR ITKDVVLQWG EMPTSVAYIH SNQIMGWGEK AIEIRSVETG HLDGVFMHKR
AQRLKFLCER NDKVFFASVR SGGSSQVFFM TLNRNSMMNW


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