Q9UKE5 (TNIK_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 125.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: TRAF2 and NCK-interacting protein kinase EC=2.7.11.1 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1360 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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.14 Ref.15 Ref.17 Ref.19 |
| 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.15 Ref.17 |
| Subcellular location | Nucleus. Cytoplasm. Recycling endosome. Cytoplasm › cytoskeleton. Note: Associated with recycling endosomes and the cytoskeletal fraction upon RAP2A overexpression. Ref.9 Ref.14 Ref.15 |
| 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.15 |
| Post-translational modification | Autophosphorylated. Autophosphorylation is activated by RAP2A and induces association to the cytoskeletal fraction. Ref.1 Ref.9 Ref.15 |
| 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
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Tanc1 | Q6F6B3 | 2 | EBI-1051794,EBI-2133582 | From a different organism. |
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1360 | 1360 | TRAF2 and NCK-interacting protein kinase | PRO_0000086761 | |||||||||||||||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 25 – 289 | 265 | Protein kinase | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Domain | 1047 – 1334 | 288 | CNH | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Nucleotide binding | 31 – 39 | 9 | ATP By similarity UniProtKB O00506 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Region | 290 – 1047 | 758 | Mediates interaction with NEDD4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 153 | 1 | Proton acceptor By similarity UniProtKB O00506 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 54 | 1 | ATP By similarity UniProtKB O00506 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 326 | 1 | Phosphoserine Ref.20 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 560 | 1 | Phosphoserine Ref.16 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 640 | 1 | Phosphoserine Ref.11 Ref.12 Ref.16 Ref.20 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 678 | 1 | Phosphoserine Ref.13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 680 | 1 | Phosphoserine Ref.13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 688 | 1 | Phosphoserine Ref.12 Ref.16 Ref.20 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 707 | 1 | Phosphoserine Ref.16 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 720 | 1 | Phosphoserine Ref.12 Ref.16 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 766 | 1 | Phosphoserine Ref.16 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 769 | 1 | Phosphoserine Ref.8 Ref.11 Ref.12 Ref.16 Ref.20 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 987 | 1 | Phosphothreonine By similarity | ||||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 445 – 473 | 29 | Missing in isoform 2, isoform 5, isoform 6 and isoform 8. Ref.1 | VSP_004889 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 537 – 591 | 55 | Missing in isoform 3, isoform 5, isoform 7 and isoform 8. Ref.1 | VSP_004890 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Alternative sequence | 795 – 802 | 8 | Missing in isoform 4, isoform 6, isoform 7 and isoform 8. Ref.1 | VSP_004891 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 778 | 1 | K → E. Ref.21 Corresponds to variant rs55778284 [ dbSNP | Ensembl ]. | VAR_041231 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 910 | 1 | G → E. Ref.21 Corresponds to variant rs35090763 [ dbSNP | Ensembl ]. | VAR_041232 | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 999 | 1 | A → T. Ref.21 Corresponds to variant rs17857452 [ dbSNP | Ensembl ]. | VAR_041233 | |||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 54 | 1 | K → A: Kinase dead. Loss of autophosphorylation and loss of function in cytoskeleton regulation. Ref.9 Ref.15 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 152 – 153 | 2 | RD → AA: Loss of autophosphorylation. | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Mutagenesis | 171 – 172 | 2 | DF → AA: Loss of autophosphorylation. | ||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 22 – 24 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 25 – 34 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 37 – 44 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 45 – 47 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 50 – 57 | 8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 64 – 76 | 13 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 85 – 91 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 100 – 106 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 113 – 119 | 7 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 121 – 123 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 127 – 146 | 20 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 158 – 161 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 167 – 169 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 173 – 175 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 192 – 194 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 197 – 200 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 214 – 228 | 15 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 232 – 235 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 238 – 247 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 260 – 269 | 10 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 274 – 276 | 3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 280 – 284 | 5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 287 – 290 | 4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 295 – 311 | 17 | |||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
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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. 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. 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. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [14] | "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. |
| [15] | "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. |
| [16] | "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, MASS SPECTROMETRY. |
| [17] | "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. |
| [18] | "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]. |
| [19] | "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. |
| [20] | "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, MASS SPECTROMETRY. |
| [21] | "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. 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. | ||||||||||||
| IPI | IPI00145805. IPI00218901. IPI00218902. IPI00218904. IPI00218906. IPI00218907. IPI00514275. IPI00943704. | ||||||||||||
| RefSeq | NP_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. | ||||||||||||
| UniGene | Hs.34024. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q9UKE5. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q9UKE5. 18 interactions. | ||||||||||||
| MINT | MINT-7242209. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q9UKE5. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 29840818. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | Q9UKE5. | ||||||||||||
| PRIDE | Q9UKE5. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000284483; ENSP00000284483; ENSG00000154310. ENST00000341852; ENSP00000345352; ENSG00000154310. ENST00000357327; ENSP00000349880; ENSG00000154310. ENST00000436636; ENSP00000399511; ENSG00000154310. ENST00000460047; ENSP00000418916; ENSG00000154310. ENST00000470834; ENSP00000419990; ENSG00000154310. ENST00000475336; ENSP00000418156; ENSG00000154310. ENST00000488470; ENSP00000418378; ENSG00000154310. | ||||||||||||
| GeneID | 23043. | ||||||||||||
| KEGG | hsa:23043. | ||||||||||||
| UCSC | uc003fhh.2. human. uc003fhi.2. human. uc003fhj.2. human. uc003fhk.2. human. uc003fhl.2. human. uc003fhm.2. human. uc003fhn.2. human. uc003fho.2. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 23043. | ||||||||||||
| GeneCards | GC03M170779. | ||||||||||||
| HGNC | HGNC:30765. TNIK. | ||||||||||||
| HPA | HPA012128. HPA012297. | ||||||||||||
| MIM | 610005. gene. | ||||||||||||
| neXtProt | NX_Q9UKE5. | ||||||||||||
| PharmGKB | PA134893180. | ||||||||||||
| HUGE | Search... | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0515. | ||||||||||||
| HOVERGEN | HBG036506. | ||||||||||||
| InParanoid | Q9UKE5. | ||||||||||||
| KO | K08840. | ||||||||||||
| OMA | TALFTSE. | ||||||||||||
| OrthoDB | EOG444KJG. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| Pathway_Interaction_DB | tnfpathway. TNF receptor signaling pathway. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q9UKE5. | ||||||||||||
| Bgee | Q9UKE5. | ||||||||||||
| Genevestigator | Q9UKE5. | ||||||||||||
| GermOnline | ENSG00000154310. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001180. Citron. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view] | ||||||||||||
| Pfam | PF00780. CNH. 1 hit. PF00069. Pkinase. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00036. CNH. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF56112. Kinase_like. 1 hit. | ||||||||||||
| PROSITE | PS50219. CNH. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| BindingDB | Q9UKE5. | ||||||||||||
| ChEMBL | CHEMBL4527. | ||||||||||||
| EvolutionaryTrace | Q9UKE5. | ||||||||||||
| GenomeRNAi | 23043. | ||||||||||||
| NextBio | 44076. | ||||||||||||
| PMAP-CutDB | Q9UKE5. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | TNIK_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q9UKE5 Secondary accession number(s): A7E2A3 Q9UKE4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| Human and mouse protein kinases Human and mouse protein kinases: classification and index |
| Human chromosome 3 Human chromosome 3: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
