MAST2

In today's world, MAST2 remains a topic of constant interest and debate. With the advancement of technology and globalization, MAST2 has acquired unprecedented relevance in modern society. From its impact on the economy to its influence on culture and politics, MAST2 has become a phenomenon that cuts across all spheres of contemporary life. In this article, we will explore the various facets of MAST2 and analyze its reach and impact in today's world.

Protein-coding gene in the species Homo sapiens

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)[1] Band 1p34.1 Start 45,786,987 bp[1] End 46,036,122 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4|4 D1 Start 116,306,762 bp[2] End 116,464,183 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) 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 BioGPS 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 Species Human Mouse Entrez 23139 17776 Ensembl ENSG00000086015 ENSMUSG00000003810 UniProt Q6P0Q8 Q60592 RefSeq (mRNA) NM_015112 NM_001319245 NM_001324320 NM_001324321 NM_001042743 NM_008641 NM_001369061 NM_001369062 RefSeq (protein) NP_001306174 NP_001311249 NP_001311250 NP_055927 NP_001036208 NP_032667 NP_001355990 NP_001355991 Location (UCSC) Chr 1: 45.79 – 46.04 Mb Chr 4: 116.31 – 116.46 Mb PubMed search [3] [4]
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

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000086015 – Ensembl, May 2017
2. ^ ^{a b c} 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.
5. ^ "Entrez Gene: MAST2 microtubule associated serine/threonine kinase 2".
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.
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.

Further reading

• 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.