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Traf2 and NCK-interacting protein kinase (EC 2 7 11 1)

 TNIK_MOUSE              Reviewed;        1323 AA.
P83510;
30-APR-2003, integrated into UniProtKB/Swiss-Prot.
24-JUL-2007, sequence version 2.
25-OCT-2017, entry version 145.
RecName: Full=Traf2 and NCK-interacting protein kinase;
EC=2.7.11.1;
Name=Tnik; Synonyms=Kiaa0551;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090 {ECO:0000312|EMBL:BAC40365.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-327 AND 735-1323 (ISOFORM
1).
STRAIN=C57BL/6J, and NOD; TISSUE=Hypothalamus, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-1323 (ISOFORM 1).
TISSUE=Embryo;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-842 (ISOFORM 2).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[4]
SEQUENCE REVISION.
Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH TCF7L2 AND CTNNB1, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-187; SER-324; SER-326;
SER-541; THR-552; SER-611; SER-659; SER-735 AND SER-740, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
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).
-!- 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
(By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000250|UniProtKB:Q9UKE5}.
-!- 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:19816403, ECO:0000269|PubMed:20159449}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19816403}.
Cytoplasm {ECO:0000269|PubMed:19816403}. Recycling endosome
{ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Note=Associated with recycling endosomes and the cytoskeletal
fraction upon RAP2A overexpression. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P83510-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=P83510-2; Sequence=VSP_007351;
Note=No experimental confirmation available.;
-!- PTM: Autophosphorylated. Autophosphorylation is activated by RAP2A
and induces association to the cytoskeletal fraction.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC65588.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK039113; BAC30241.1; -; mRNA.
EMBL; AK041777; BAC31061.2; -; mRNA.
EMBL; AK088459; BAC40365.1; -; mRNA.
EMBL; BC050866; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK122306; BAC65588.2; ALT_SEQ; Transcribed_RNA.
CCDS; CCDS50879.1; -. [P83510-1]
RefSeq; NP_001156480.1; NM_001163008.1. [P83510-1]
UniGene; Mm.126193; -.
UniGene; Mm.483052; -.
ProteinModelPortal; P83510; -.
SMR; P83510; -.
BioGrid; 576981; 4.
DIP; DIP-57467N; -.
IntAct; P83510; 4.
MINT; MINT-4138101; -.
STRING; 10090.ENSMUSP00000125081; -.
iPTMnet; P83510; -.
PhosphoSitePlus; P83510; -.
MaxQB; P83510; -.
PaxDb; P83510; -.
PeptideAtlas; P83510; -.
PRIDE; P83510; -.
Ensembl; ENSMUST00000159236; ENSMUSP00000124681; ENSMUSG00000027692. [P83510-1]
GeneID; 665113; -.
KEGG; mmu:665113; -.
UCSC; uc008oty.1; mouse. [P83510-1]
CTD; 23043; -.
MGI; MGI:1916264; Tnik.
eggNOG; KOG0587; Eukaryota.
eggNOG; ENOG410XPHR; LUCA.
GeneTree; ENSGT00900000140838; -.
HOGENOM; HOG000290708; -.
HOVERGEN; HBG036506; -.
InParanoid; P83510; -.
KO; K08840; -.
ChiTaRS; Tnik; mouse.
PRO; PR:P83510; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000027692; -.
CleanEx; MM_TNIK; -.
ExpressionAtlas; P83510; baseline and differential.
Genevisible; P83510; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0055037; C:recycling endosome; ISO:MGI.
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; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0007256; P:activation of JNKK activity; ISS:UniProtKB.
GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
GO; GO:0030033; P:microvillus assembly; ISO:MGI.
GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR001180; CNH_dom.
InterPro; IPR011009; Kinase-like_dom.
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;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Cytoskeleton; Endosome; Kinase; Neurogenesis; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
CHAIN 1 1323 Traf2 and NCK-interacting protein kinase.
/FTId=PRO_0000086762.
DOMAIN 25 289 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 1010 1297 CNH. {ECO:0000255|PROSITE-
ProRule:PRU00795}.
NP_BIND 31 39 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 290 1010 Mediates interaction with NEDD4.
{ECO:0000250}.
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:0000244|PubMed:21183079}.
MOD_RES 324 324 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 531 531 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKE5}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 552 552 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 571 571 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKE5}.
MOD_RES 579 579 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKE5}.
MOD_RES 581 581 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKE5}.
MOD_RES 611 611 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKE5}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKE5}.
MOD_RES 659 659 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 672 672 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKE5}.
MOD_RES 678 678 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKE5}.
MOD_RES 691 691 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKE5}.
MOD_RES 735 735 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 737 737 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKE5}.
MOD_RES 740 740 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 922 922 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UKE5}.
VAR_SEQ 926 962 YGIGSSTKASFTPFVDPRVYQTSPTDEDEEDDESSAA ->
SLK (in isoform 2).
{ECO:0000303|PubMed:12693553}.
/FTId=VSP_007351.
CONFLICT 735 735 S -> C (in Ref. 1; BAC40365).
{ECO:0000305}.
SEQUENCE 1323 AA; 150367 MW; B8289189530251D2 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 EHEQEYKRKQ LEEQRQAERL QRQLKQERDY LVSLQHQRQE
QRPLEKKPLY HYKEGMSPSE KPAWAKEVEE RSRLNRQSSP AMPHKVANRI SDPNLPPRSE
SFSISGVQPA RTPPMLRPVD PQIPQLVAVK SQGPALTASQ SVHEQPTKGL SGFQEALNVT
SHRVEMPRQN SDPTSENPPL PTRIEKFDRS SWLRQEEDIP PKVPQRTTSI SPALARKNSP
GNGSALGPRL GSQPIRASNP DLRRTEPVLE SSLQRTSSGS SSSSSTPSSQ PSSQGGSQPG
SQAGSSERSR VRANSKSEGS PVLPHEPSKV KPEESRDITR PSRPADLTAL AKELRELRIE
ETNRPLKKVT DYSSSSEESE SSEEEEEDGE SETHDGTVAV SDIPRLIPTG APGNNEQYNM
GMVGTHGLET SHADTFGGSI SREGTLMIRE TAEEKKRSGH SDSNGFAGHI NLPDLVQQSH
SPAGTPTEGL GRVSTHSQEM DSGAEYGIGS STKASFTPFV DPRVYQTSPT DEDEEDDESS
AAALFTSELL RQEQAKLNEA RKISVVNVNP TNIRPHSDTP EIRKYKKRFN SEILCAALWG
VNLLVGTENG LMLLDRSGQG KVYNLINRRR FQQMDVLEGL NVLVTISGKK NKLRVYYLSW
LRNRILHNDP EVEKKQGWIT VGDLEGCIHY KVVKYERIKF LVIALKNAVE IYAWAPKPYH
KFMAFKSFAD LQHKPLLVDL TVEEGQRLKV IFGSHTGFHV IDVDSGNSYD IYIPSHIQGN
ITPHAIVILP KTDGMEMLVC YEDEGVYVNT YGRITKDVVL QWGEMPTSVA YIHSNQIMGW
GEKAIEIRSV ETGHLDGVFM HKRAQRLKFL CERNDKVFFA SVRSGGSSQV FFMTLNRNSM
MNW


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