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MAST2

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From Wikipedia, the free encyclopedia

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	45,786,987bp^[1]
Band	1p34.1	End	46,036,122bp^[1]

Gene location (Mouse)

Chr.	Chromosome 4 (mouse)^[2]

Band	4\|4 D1	Start	116,306,762bp^[2]
Band	4\|4 D1	End	116,464,183bp^[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 anenzyme that in humans is encoded by theMAST2gene.^[5] Theprotein encoded by this gene controlsTRAF6 andNF-kappaB activity.^[6]

Interactions

[edit]

MAST2 has been shown tointeract withPCLKC.^[7]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000086015 –Ensembl, May 2017
^^a ^b ^cGRCm38: 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.

Kinases:Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4
Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase Aurora C kinase
Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-
IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP
cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY
cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1
Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3
Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase
Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2
G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6
Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1
Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4
Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2
Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19
Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4
Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1
Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14
MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14
Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-
Tropomyosin kinase (EC 2.7.11.28)	-
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-
Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

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	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

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