TNIK

From Wikipedia, the free encyclopedia

TRAF2 and NCK interacting kinase

Identifiers

TNIK; AD 2

External IDs

Gene ontology
Molecular Function:	• nucleotide binding • protein serine/threonine kinase activity • small GTPase regulator activity • ATP binding • transferase activity
Cellular Component:	• cellular_component
Biological Process:	• protein amino acid phosphorylation • response to stress • protein kinase cascade • JNK cascade

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_015028 (mRNA)
NP_055843 (protein)

XM_976612 (mRNA)
XP_981706 (protein)

Location

Chr 3: 172.26 - 172.66 Mb

n/a

Pubmed search

[1]

[2]

TRAF2 and NCK interacting kinase, also known as TNIK, is a human gene.^[1]

Germinal center kinases (GCKs), such as TNIK, are characterized by an N-terminal kinase domain and a C-terminal GCK domain that serves a regulatory function (Fu et al., 1999).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: TNIK TRAF2 and NCK interacting kinase.

[edit] Further reading

Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.". DNA Res. 9 (3): 99–106. PMID 12168954.
Nagase T, Ishikawa K, Miyajima N, et al. (1998). "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 (1): 31–9. PMID 9628581.
Yonekura H, Migita H, Sakurai S, et al. (1999). "Antisense display--a method for functional gene screening: evaluation in a cell-free system and isolation of angiogenesis-related genes.". Nucleic Acids Res. 27 (13): 2591–600. PMID 10373574.
Fu CA, Shen M, Huang BC, et al. (1999). "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 (43): 30729–37. PMID 10521462.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
Taira K, Umikawa M, Takei K, et al. (2005). "The Traf2- and Nck-interacting kinase as a putative effector of Rap2 to regulate actin cytoskeleton.". J. Biol. Chem. 279 (47): 49488–96. doi:10.1074/jbc.M406370200. PMID 15342639.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Wissing J, Jänsch L, Nimtz M, et al. (2007). "Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.". Mol. Cell Proteomics 6 (3): 537–47. doi:10.1074/mcp.T600062-MCP200. PMID 17192257.