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Q9UKE5 (TNIK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TRAF2 and NCK-interacting protein kinase

EC=2.7.11.1
Gene names
Name:TNIK
Synonyms:KIAA0551
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1360 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.9 Ref.15 Ref.16 Ref.18 Ref.20

Catalytic activity

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

Subunit structure

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. Ref.1 Ref.9 Ref.10 Ref.16 Ref.18

Subcellular location

Nucleus. Cytoplasm. Recycling endosome. Cytoplasmcytoskeleton. Note: Associated with recycling endosomes and the cytoskeletal fraction upon RAP2A overexpression. Ref.9 Ref.15 Ref.16

Tissue specificity

Expressed ubiquitously. Highest levels observed in heart, brain and skeletal muscle. Expressed in normal colonic epithelia and colorectal cancer tissues. Ref.1 Ref.16

Post-translational modification

Autophosphorylated. Autophosphorylation is activated by RAP2A and induces association to the cytoskeletal fraction. Ref.1 Ref.9 Ref.16

Sequence similarities

Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.

Contains 1 CNH domain.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Biological processNeurogenesis
Wnt signaling pathway
   Cellular componentCytoplasm
Cytoskeleton
Endosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

actin cytoskeleton reorganization

Inferred from direct assay Ref.9. Source: UniProtKB

activation of JNKK activity

Inferred from direct assay Ref.9. Source: UniProtKB

cytoskeleton organization

Inferred from mutant phenotype Ref.1. Source: UniProtKB

intracellular signal transduction

Inferred from direct assay Ref.1. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.1Ref.9. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.1Ref.9. Source: UniProtKB

regulation of dendrite morphogenesis

Inferred from direct assay Ref.18. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.9Ref.15. Source: UniProtKB

cytoskeleton

Inferred from direct assay Ref.9. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

recycling endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from direct assay Ref.1Ref.9. Source: UniProtKB

receptor signaling protein serine/threonine kinase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

small GTPase regulator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTNNB1P352223EBI-1051794,EBI-491549
Tanc1Q6F6B32EBI-1051794,EBI-2133582From a different organism.
TCF7L2Q9NQB03EBI-1051794,EBI-924724

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UKE5-1)

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.
Isoform 2 (identifier: Q9UKE5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     445-473: Missing.
Isoform 3 (identifier: Q9UKE5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     537-591: Missing.
Isoform 4 (identifier: Q9UKE5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     795-802: Missing.
Isoform 5 (identifier: Q9UKE5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     445-473: Missing.
     537-591: Missing.
Isoform 6 (identifier: Q9UKE5-6)

The sequence of this isoform differs from the canonical sequence as follows:
     445-473: Missing.
     795-802: Missing.
Isoform 7 (identifier: Q9UKE5-7)

The sequence of this isoform differs from the canonical sequence as follows:
     537-591: Missing.
     795-802: Missing.
Isoform 8 (identifier: Q9UKE5-8)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13601360TRAF2 and NCK-interacting protein kinase
PRO_0000086761

Regions

Domain25 – 289265Protein kinase
Domain1047 – 1334288CNH
Nucleotide binding31 – 399ATP By similarity UniProtKB O00506
Region290 – 1047758Mediates interaction with NEDD4

Sites

Active site1531Proton acceptor By similarity UniProtKB O00506
Binding site541ATP By similarity UniProtKB O00506

Amino acid modifications

Modified residue3261Phosphoserine Ref.21
Modified residue5601Phosphoserine Ref.17
Modified residue6401Phosphoserine Ref.11 Ref.12 Ref.17 Ref.21
Modified residue6781Phosphoserine Ref.13
Modified residue6801Phosphoserine Ref.13
Modified residue6881Phosphoserine Ref.12 Ref.17 Ref.21
Modified residue7071Phosphoserine Ref.17
Modified residue7201Phosphoserine Ref.12 Ref.17
Modified residue7661Phosphoserine Ref.17
Modified residue7691Phosphoserine Ref.8 Ref.11 Ref.12 Ref.17 Ref.21

Natural variations

Alternative sequence445 – 47329Missing in isoform 2, isoform 5, isoform 6 and isoform 8. Ref.1
VSP_004889
Alternative sequence537 – 59155Missing in isoform 3, isoform 5, isoform 7 and isoform 8. Ref.1
VSP_004890
Alternative sequence795 – 8028Missing in isoform 4, isoform 6, isoform 7 and isoform 8. Ref.1
VSP_004891
Natural variant7781K → E. Ref.22
Corresponds to variant rs55778284 [ dbSNP | Ensembl ].
VAR_041231
Natural variant9101G → E. Ref.22
Corresponds to variant rs35090763 [ dbSNP | Ensembl ].
VAR_041232
Natural variant9991A → T. Ref.22
Corresponds to variant rs17857452 [ dbSNP | Ensembl ].
VAR_041233

Experimental info

Mutagenesis541K → A: Kinase dead. Loss of autophosphorylation and loss of function in cytoskeleton regulation. Ref.9 Ref.16
Mutagenesis152 – 1532RD → AA: Loss of autophosphorylation.
Mutagenesis171 – 1722DF → AA: Loss of autophosphorylation.

Secondary structure

............................................... 1360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 3590BC2905A72C3D

FASTA1,360154,943
        10         20         30         40         50         60 
MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL AAIKVMDVTG 

        70         80         90        100        110        120 
DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ LWLVMEFCGA GSVTDLIKNT 

       130        140        150        160        170        180 
KGNTLKEEWI AYICREILRG LSHLHQHKVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR 

       190        200        210        220        230        240 
TVGRRNTFIG TPYWMAPEVI ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR 

       250        260        270        280        290        300 
ALFLIPRNPA PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI 

       310        320        330        340        350        360 
QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL RRDFLRLQLA 

       370        380        390        400        410        420 
NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE QRRRLEEQQR REKELRKQQE 

       430        440        450        460        470        480 
REQRRHYEEQ MRREEERRRA EHEQEYIRRQ LEEEQRQLEI LQQQLLHEQA LLLEYKRKQL 

       490        500        510        520        530        540 
EEQRQAERLQ RQLKQERDYL VSLQHQRQEQ RPVEKKPLYH YKEGMSPSEK PAWAKEVEER 

       550        560        570        580        590        600 
SRLNRQSSPA MPHKVANRIS DPNLPPRSES FSISGVQPAR TPPMLRPVDP QIPHLVAVKS 

       610        620        630        640        650        660 
QGPALTASQS VHEQPTKGLS GFQEALNVTS HRVEMPRQNS DPTSENPPLP TRIEKFDRSS 

       670        680        690        700        710        720 
WLRQEEDIPP KVPQRTTSIS PALARKNSPG NGSALGPRLG SQPIRASNPD LRRTEPILES 

       730        740        750        760        770        780 
PLQRTSSGSS SSSSTPSSQP SSQGGSQPGS QAGSSERTRV RANSKSEGSP VLPHEPAKVK 

       790        800        810        820        830        840 
PEESRDITRP SRPASYKKAI DEDLTALAKE LRELRIEETN RPMKKVTDYS SSSEESESSE 

       850        860        870        880        890        900 
EEEEDGESET HDGTVAVSDI PRLIPTGAPG SNEQYNVGMV GTHGLETSHA DSFSGSISRE 

       910        920        930        940        950        960 
GTLMIRETSG EKKRSGHSDS NGFAGHINLP DLVQQSHSPA GTPTEGLGRV STHSQEMDSG 

       970        980        990       1000       1010       1020 
TEYGMGSSTK ASFTPFVDPR VYQTSPTDED EEDEESSAAA LFTSELLRQE QAKLNEARKI 

      1030       1040       1050       1060       1070       1080 
SVVNVNPTNI RPHSDTPEIR KYKKRFNSEI LCAALWGVNL LVGTENGLML LDRSGQGKVY 

      1090       1100       1110       1120       1130       1140 
NLINRRRFQQ MDVLEGLNVL VTISGKKNKL RVYYLSWLRN RILHNDPEVE KKQGWITVGD 

      1150       1160       1170       1180       1190       1200 
LEGCIHYKVV KYERIKFLVI ALKNAVEIYA WAPKPYHKFM AFKSFADLQH KPLLVDLTVE 

      1210       1220       1230       1240       1250       1260 
EGQRLKVIFG SHTGFHVIDV DSGNSYDIYI PSHIQGNITP HAIVILPKTD GMEMLVCYED 

      1270       1280       1290       1300       1310       1320 
EGVYVNTYGR ITKDVVLQWG EMPTSVAYIH SNQIMGWGEK AIEIRSVETG HLDGVFMHKR 

      1330       1340       1350       1360 
AQRLKFLCER NDKVFFASVR SGGSSQVFFM TLNRNSMMNW 

« Hide

Isoform 2 [UniParc].

Checksum: 85378CBC98631411
Show »

FASTA1,331151,300
Isoform 3 [UniParc].

Checksum: 209230BB15712DFC
Show »

FASTA1,305148,829
Isoform 4 [UniParc].

Checksum: F4708A71FF26C54F
Show »

FASTA1,352154,008
Isoform 5 [UniParc].

Checksum: 9B85E462E4FAE9F0
Show »

FASTA1,276145,186
Isoform 6 [UniParc].

Checksum: 93B2E73EF75034B9
Show »

FASTA1,323150,365
Isoform 7 [UniParc].

Checksum: EED944B571948D3F
Show »

FASTA1,297147,894
Isoform 8 [UniParc].

Checksum: 55AD5F59B7A08A2A
Show »

FASTA1,268144,251

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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
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]"MINK is a Rap2 effector for phosphorylation of the postsynaptic scaffold protein TANC1."
Nonaka H., Takei K., Umikawa M., Oshiro M., Kuninaka K., Bayarjargal M., Asato T., Yamashiro Y., Uechi Y., Endo S., Suzuki T., Kariya K.
Biochem. Biophys. Res. Commun. 377:573-578(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TANC1.
[11]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Rap2 function requires palmitoylation and recycling endosome localization."
Uechi Y., Bayarjargal M., Umikawa M., Oshiro M., Takei K., Yamashiro Y., Asato T., Endo S., Misaki R., Taguchi T., Kariya K.
Biochem. Biophys. Res. Commun. 378:732-737(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite development."
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.
Neuron 65:358-372(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NEDD4 AND RAP2A.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Smad inhibition by the Ste20 kinase Misshapen."
Kaneko S., Chen X., Lu P., Yao X., Wright T.G., Rajurkar M., Kariya K., Mao J., Ip Y.T., Xu L.
Proc. Natl. Acad. Sci. U.S.A. 108:11127-11132(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001155032.1. NM_001161560.1.
NP_001155033.1. NM_001161561.1.
NP_001155034.1. NM_001161562.1.
NP_001155035.1. NM_001161563.1.
NP_001155036.1. NM_001161564.1.
NP_001155037.1. NM_001161565.1.
NP_001155038.1. NM_001161566.1.
NP_055843.1. NM_015028.2.
UniGeneHs.34024.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2X7FX-ray2.80A/B/C/D/E1-325[»]
ProteinModelPortalQ9UKE5.
SMRQ9UKE5. Positions 13-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116682. 37 interactions.
DIPDIP-37562N.
IntActQ9UKE5. 21 interactions.
MINTMINT-7242209.

Chemistry

BindingDBQ9UKE5.
ChEMBLCHEMBL4527.
GuidetoPHARMACOLOGY2244.

PTM databases

PhosphoSiteQ9UKE5.

Polymorphism databases

DMDM29840818.

Proteomic databases

PaxDbQ9UKE5.
PRIDEQ9UKE5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000284483; 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]
GeneID23043.
KEGGhsa:23043.
UCSCuc003fhh.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

CTD23043.
GeneCardsGC03M170779.
HGNCHGNC:30765. TNIK.
HPAHPA012128.
HPA012297.
MIM610005. gene.
neXtProtNX_Q9UKE5.
PharmGKBPA134893180.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG036506.
InParanoidQ9UKE5.
KOK08840.
OMATEQYNVG.
OrthoDBEOG73803V.
PhylomeDBQ9UKE5.
TreeFamTF105138.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
SignaLinkQ9UKE5.

Gene expression databases

ArrayExpressQ9UKE5.
BgeeQ9UKE5.
GenevestigatorQ9UKE5.

Family and domain databases

InterProIPR001180. 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.
IPR028560. TNIK.
[Graphical view]
PANTHERPTHR24361:SF27. PTHR24361:SF27. 1 hit.
PfamPF00780. CNH. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00036. CNH. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50219. CNH. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UKE5.
GeneWikiTNIK.
GenomeRNAi23043.
NextBio44076.
PMAP-CutDBQ9UKE5.
PROQ9UKE5.
SOURCESearch...

Entry information

Entry nameTNIK_HUMAN
AccessionPrimary (citable) accession number: Q9UKE5
Secondary accession number(s): A7E2A3 expand/collapse secondary AC list , A8K4U1, D3DNQ6, O60298, Q8WUY7, Q9UKD8, Q9UKD9, Q9UKE0, Q9UKE1, Q9UKE2, Q9UKE3, Q9UKE4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM