MAST2

MAST2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2KQF, 2KYL
Identifiers
Aliases	MAST2, MAST205, MTSSK, microtubule associated serine/threonine kinase 2
External IDs	OMIM: 612257; MGI: 894676; HomoloGene: 7428; GeneCards: MAST2; OMA:MAST2 - orthologs
Gene location (Human)
Chr.	Chromosome 1 (human)
End	46,036,122 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	116,464,183 bp
RNA expression pattern
	Top expressed in
	gastrocnemius muscle; ; muscle of thigh; ; apex of heart; ; gastric mucosa; ; glutes; ; stromal cell of endometrium; ; pancreatic ductal cell; ; skeletal muscle tissue; ; left ventricle; ; left testis;
	Top expressed in
	neural layer of retina; ; muscle of thigh; ; internal carotid artery; ; right ventricle; ; ankle joint; ; cardiac muscle tissue of left ventricle; ; external carotid artery; ; ankle; ; digastric muscle; ; soleus muscle;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	transferase activity; nucleotide binding; protein kinase activity; phosphatase binding; microtubule binding; metal ion binding; kinase activity; protein serine/threonine kinase activity; protein binding; ATP binding; magnesium ion binding;
Cellular component	membrane; microtubule cytoskeleton; plasma membrane; cytoskeleton; cytoplasm;
Biological process	intracellular signal transduction; phosphorylation; spermatid differentiation; protein phosphorylation; cytoskeleton organization; peptidyl-serine phosphorylation;
	Sources:Amigo / QuickGO
Orthologs
	23139
	17776
	ENSG00000086015
	ENSMUSG00000003810
	Q6P0Q8
	Q60592
	NM_015112; NM_001319245; NM_001324320; NM_001324321
	NM_001042743; NM_008641; NM_001369061; NM_001369062
	NP_001306174; NP_001311249; NP_001311250; NP_055927
	NP_001036208; NP_032667; NP_001355990; NP_001355991
	Wikidata
View/Edit Human	View/Edit Mouse

Microtubule-associated serine/threonine-protein kinase 2 is an enzyme that in humans is encoded by the MAST2 gene.^[5] The protein encoded by this gene controls TRAF6 and NF-kappaB activity.^[6]

Interactions

MAST2 has been shown to interact with PCLKC.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000086015 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000003810 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: MAST2 microtubule associated serine/threonine kinase 2".
^ Xiong H, Li H, Chen Y, Zhao J, Unkeless JC (2004). "Interaction of TRAF6 with MAST205 regulates NF-kappaB activation and MAST205 stability". J. Biol. Chem. 279 (42): 43675–83. doi:10.1074/jbc.M404328200. PMID 15308666.
^ Okazaki N, Takahashi N, Kojima S, Masuho Y, Koga H (July 2002). "Protocadherin LKC, a new candidate for a tumor suppressor of colon and liver cancers, its association with contact inhibition of cell proliferation". Carcinogenesis. 23 (7): 1139–48. doi:10.1093/carcin/23.7.1139. PMID 12117771.

Walden PD, Cowan NJ (1993). "A novel 205-kilodalton testis-specific serine/threonine protein kinase associated with microtubules of the spermatid manchette". Mol. Cell. Biol. 13 (12): 7625–35. doi:10.1128/mcb.13.12.7625. PMC 364834. PMID 8246979.
Bonaldo MF, Lennon G, Soares MB (1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Walden PD, Millette CF (1996). "Increased activity associated with the MAST205 protein kinase complex during mammalian spermiogenesis". Biol. Reprod. 55 (5): 1039–44. doi:10.1095/biolreprod55.5.1039. PMID 8902215.
Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (1998). "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (5): 277–86. doi:10.1093/dnares/5.5.277. PMID 9872452.
Lumeng C, Phelps S, Crawford GE, Walden PD, Barald K, Chamberlain JS (1999). "Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases". Nat. Neurosci. 2 (7): 611–7. doi:10.1038/10165. PMID 10404183. S2CID 20910888.
Adey NB, Huang L, Ormonde PA, Baumgard ML, Pero R, Byreddy DV, Tavtigian SV, Bartel PL (2000). "Threonine phosphorylation of the MMAC1/PTEN PDZ binding domain both inhibits and stimulates PDZ binding". Cancer Res. 60 (1): 35–7. PMID 10646847.
Gisler SM, Stagljar I, Traebert M, Bacic D, Biber J, Murer H (2001). "Interaction of the type IIa Na/Pi cotransporter with PDZ proteins". J. Biol. Chem. 276 (12): 9206–13. doi:10.1074/jbc.M008745200. PMID 11099500.
Okazaki N, Takahashi N, Kojima S, Masuho Y, Koga H (2002). "Protocadherin LKC, a new candidate for a tumor suppressor of colon and liver cancers, its association with contact inhibition of cell proliferation". Carcinogenesis. 23 (7): 1139–48. doi:10.1093/carcin/23.7.1139. PMID 12117771.
Nakayama M, Kikuno R, Ohara O (2002). "Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs". Genome Res. 12 (11): 1773–84. doi:10.1101/gr.406902. PMC 187542. PMID 12421765.
Navarro-Lérida I, Martínez Moreno M, Roncal F, Gavilanes F, Albar JP, Rodríguez-Crespo I (2004). "Proteomic identification of brain proteins that interact with dynein light chain LC8". Proteomics. 4 (2): 339–46. doi:10.1002/pmic.200300528. PMID 14760703. S2CID 8868600.
Zhou H, Xiong H, Li H, Plevy SE, Walden PD, Sassaroli M, Prestwich GD, Unkeless JC (2004). "Microtubule-associated serine/threonine kinase-205 kDa and Fc gamma receptor control IL-12 p40 synthesis and NF-kappa B activation". J. Immunol. 172 (4): 2559–68. doi:10.4049/jimmunol.172.4.2559. PMID 14764729. S2CID 85692192.
Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
Xiong H, Li H, Chen Y, Zhao J, Unkeless JC (2004). "Interaction of TRAF6 with MAST205 regulates NF-kappaB activation and MAST205 stability". J. Biol. Chem. 279 (42): 43675–83. doi:10.1074/jbc.M404328200. PMID 15308666.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000086015 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000003810 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez_23139-5] "Entrez Gene: MAST2 microtubule associated serine/threonine kinase 2".

[pmid_15308666-6] Xiong H, Li H, Chen Y, Zhao J, Unkeless JC (2004). "Interaction of TRAF6 with MAST205 regulates NF-kappaB activation and MAST205 stability". J. Biol. Chem. 279 (42): 43675–83. doi:10.1074/jbc.M404328200. PMID 15308666.

[pmid12117771-7] Okazaki N, Takahashi N, Kojima S, Masuho Y, Koga H (July 2002). "Protocadherin LKC, a new candidate for a tumor suppressor of colon and liver cancers, its association with contact inhibition of cell proliferation". Carcinogenesis. 23 (7): 1139–48. doi:10.1093/carcin/23.7.1139. PMID 12117771.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Interactions

References

Further reading