GSK3B

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes

1GNG, 1H8F, 1I09, 1J1B, 1J1C, 1O6K, 1O6L, 1O9U, 1PYX, 1Q3D, 1Q3W, 1Q41, 1Q4L, 1Q5K, 1R0E, 1UV5, 2JDO, 2JDR, 2JLD, 2O5K, 2OW3, 2UW9, 2X39, 2XH5, 3CQU, 3CQW, 3DU8, 3E87, 3E88, 3E8D, 3F7Z, 3F88, 3GB2, 3I4B, 3L1S, 3M1S, 3MV5, 3OW4, 3PUP, 3Q3B, 3QKK, 3SAY, 3SD0, 3ZDI, 3ZRK, 3ZRL, 3ZRM, 4ACC, 4ACD, 4ACG, 4ACH, 4AFJ, 4B7T, 4DIT, 4EKK, 4IQ6, 4J1R, 4J71, 4NM0, 4NM3, 4NM5, 4NM7, 4PTC, 4PTE, 4PTG, 5F94, 5F95, 5HLP, 5HLN

Identifiers

Aliases

GSK3B, Gsk3b, 7330414F15Rik, 8430431H08Rik, C86142, GSK-3, GSK-3beta, GSK3

External IDs

MGI: 1861437 HomoloGene: 55629 GeneCards: GSK3B

EC number

2.7.11.1

Targeted by Drug

tideglusib^[1]

Gene ontology
Molecular function	• kinase activity • ionotropic glutamate receptor binding • ATP binding • protein kinase activity • protein kinase A catalytic subunit binding • transcription factor binding • protein serine/threonine kinase activity • transferase activity • beta-catenin binding • RNA polymerase II transcription factor binding • NF-kappaB binding • integrin binding • tau-protein kinase activity • protein binding • tau protein binding • protein kinase binding • nucleotide binding • p53 binding • ubiquitin protein ligase binding
Cellular component	• cytoplasm • cytosol • membrane • mitochondrion • perinuclear region of cytoplasm • nucleus • centrosome • dendritic spine • dendritic shaft • membrane-bounded organelle • membrane raft • Wnt signalosome • growth cone • plasma membrane • protein complex • axon • neuronal cell body • beta-catenin destruction complex • cell body • intracellular ribonucleoprotein complex • dendrite • postsynapse
Biological process	• myotube differentiation • regulation of neuron projection development • positive regulation of protein catabolic process • regulation of axon extension • negative regulation of cardiac muscle hypertrophy • rhythmic process • negative regulation of type B pancreatic cell development • negative regulation of protein binding • cellular response to iron(II) ion • response to insulin-like growth factor stimulus • protein phosphorylation • cellular response to mechanical stimulus • positive regulation of neuron apoptotic process • negative regulation of glycogen (starch) synthase activity • circadian rhythm • response to L-glutamate • positive regulation of excitatory postsynaptic potential • animal organ morphogenesis • glycogen metabolic process • superior temporal gyrus development • positive regulation of mitochondrial membrane potential • negative regulation of canonical Wnt signaling pathway • hypermethylation of CpG island • regulation of gene expression by genetic imprinting • chemical synaptic transmission, postsynaptic • negative regulation of protein complex assembly • negative regulation of dopaminergic neuron differentiation • response to epinephrine • positive regulation of peptidyl-serine phosphorylation • ER overload response • response to lithium ion • establishment or maintenance of cell polarity • response to insulin • regulation of axonogenesis • positive regulation of protein export from nucleus • positive regulation of GTPase activity • response to angiotensin • negative regulation of MAP kinase activity • protein export from nucleus • positive regulation of DNA biosynthetic process • establishment of cell polarity • regulation of neuronal synaptic plasticity • protein autophosphorylation • cellular response to interleukin-3 • positive regulation of axon extension • positive regulation of proteasomal ubiquitin-dependent protein catabolic process • cell differentiation • negative regulation of protein localization to nucleus • negative regulation of neuron projection development • positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway • cellular response to lithium ion • phosphorylation • carbohydrate metabolic process • positive regulation of cell-matrix adhesion • cellular response to hepatocyte growth factor stimulus • canonical Wnt signaling pathway involved in positive regulation of apoptotic process • positive regulation of stem cell differentiation • negative regulation of apoptotic process • nervous system development • dopamine receptor signaling pathway • regulation of microtubule-based process • epithelial to mesenchymal transition • canonical Wnt signaling pathway • response to ultrasound • positive regulation of protein binding • myoblast fusion • peptidyl-threonine phosphorylation • fat cell differentiation • positive regulation of smooth muscle cell proliferation • negative regulation of neuron migration • response to estradiol • intracellular signal transduction • negative regulation of nitric-oxide synthase activity • positive regulation of protein complex assembly • axonogenesis • cellular response to dopamine • aging • re-entry into mitotic cell cycle • positive regulation of neuron death • negative regulation of glycogen biosynthetic process • response to activity • negative regulation of dendrite development • regulation of dendrite morphogenesis • multicellular organism development • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress • cellular response to erythropoietin • negative regulation of NFAT protein import into nucleus • protein localization to microtubule • negative regulation of dendrite morphogenesis • positive regulation of peptidyl-threonine phosphorylation • peptidyl-serine phosphorylation • extrinsic apoptotic signaling pathway in absence of ligand • positive regulation of apoptotic process • regulation of cellular response to heat • negative regulation of signal transduction • negative regulation of neuron maturation • cell migration • hippocampus development • negative regulation of smooth muscle cell apoptotic process • response to drug • positive regulation of transcription from RNA polymerase II promoter • cellular response to hydrogen peroxide • beta-catenin destruction complex disassembly • proteasome-mediated ubiquitin-dependent protein catabolic process • Wnt signaling pathway • beta-catenin destruction complex assembly
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


2932


56637

Ensembl


ENSG00000082701


ENSMUSG00000022812

UniProt


P49841


Q9WV60

RefSeq (mRNA)


NM_001146156 NM_002093


NM_019827

RefSeq (protein)


NP_001139628.1 NP_002084.2


NP_062801.1

Location (UCSC)

Chr 3: 119.82 – 120.09 Mb

Chr 16: 38.09 – 38.25 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Glycogen synthase kinase 3 beta, also known as GSK3B, is an enzyme that in humans is encoded by the GSK3B gene.^[4]^[5] In mice, the enzyme is encoded by the GSK-3β gene.^[6] Abnormal regulation and expression of GSK3β is associated with an increased susceptibility towards bipolar disorder.^[7]

Function

Glycogen synthase kinase-3 (GSK-3) is a proline-directed serine-threonine kinase that was initially identified as a phosphorylating and an inactivating agent of glycogen synthase. Two isoforms, alpha (GSK3A) and beta, show a high degree of amino acid homology.^[4] GSK3B is involved in energy metabolism, neuronal cell development, and body pattern formation.^[8]^[9]

Loss of function mutations

Homozygous disruption of the GSK-3β locus in mice results in embryonic lethality during mid-gestation.^[6] This lethality phenotype could be rescued by inhibition of tumor necrosis factor.^[6]

Interactions

GSK3B has been shown to interact with:

Overview of signal transduction pathways involved in apoptosis.

References

↑ "Drugs that physically interact with Glycogen synthase kinase-3 beta view/edit references on wikidata".
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 Stambolic V, Woodgett JR (Nov 1994). "Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation". The Biochemical Journal. 303 (Pt 3): 701–4. doi:10.1042/bj3030701. PMC 1137602. PMID 7980435.
↑ Lau KF, Miller CC, Anderton BH, Shaw PC (Sep 1999). "Molecular cloning and characterization of the human glycogen synthase kinase-3beta promoter". Genomics. 60 (2): 121–8. doi:10.1006/geno.1999.5875. PMID 10486203.
1 2 3 Hoeflich KP, Luo J, Rubie EA, Tsao MS, Jin O, Woodgett JR (2000). "Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation". Nature. 406 (6791): 86–90. doi:10.1038/35017574. PMID 10894547.
↑ Luykx JJ, Boks MP, Terwindt AP, Bakker S, Kahn RS, Ophoff RA (Jun 2010). "The involvement of GSK3beta in bipolar disorder: integrating evidence from multiple types of genetic studies". European Neuropsychopharmacology. 20 (6): 357–68. doi:10.1016/j.euroneuro.2010.02.008. PMID 20226637.
↑ Plyte SE, Hughes K, Nikolakaki E, Pulverer BJ, Woodgett JR (Dec 1992). "Glycogen synthase kinase-3: functions in oncogenesis and development". Biochimica et Biophysica Acta. 1114 (2-3): 147–62. doi:10.1016/0304-419X(92)90012-N. PMID 1333807.
↑ "Entrez Gene: GSK3B glycogen synthase kinase 3 beta".
1 2 Tanji C, Yamamoto H, Yorioka N, Kohno N, Kikuchi K, Kikuchi A (Oct 2002). "A-kinase anchoring protein AKAP220 binds to glycogen synthase kinase-3beta (GSK-3beta ) and mediates protein kinase A-dependent inhibition of GSK-3beta". The Journal of Biological Chemistry. 277 (40): 36955–61. doi:10.1074/jbc.M206210200. PMID 12147701.
1 2 Mak BC, Takemaru K, Kenerson HL, Moon RT, Yeung RS (Feb 2003). "The tuberin-hamartin complex negatively regulates beta-catenin signaling activity". The Journal of Biological Chemistry. 278 (8): 5947–51. doi:10.1074/jbc.C200473200. PMID 12511557.
↑ Nakamura T, Hamada F, Ishidate T, Anai K, Kawahara K, Toyoshima K, Akiyama T (Jun 1998). "Axin, an inhibitor of the Wnt signalling pathway, interacts with beta-catenin, GSK-3beta and APC and reduces the beta-catenin level". Genes to Cells. 3 (6): 395–403. doi:10.1046/j.1365-2443.1998.00198.x. PMID 9734785.
↑ von Kries JP, Winbeck G, Asbrand C, Schwarz-Romond T, Sochnikova N, Dell'Oro A, Behrens J, Birchmeier W (Sep 2000). "Hot spots in beta-catenin for interactions with LEF-1, conductin and APC". Nature Structural Biology. 7 (9): 800–7. doi:10.1038/79039. PMID 10966653.
↑ Schwarz-Romond T, Asbrand C, Bakkers J, Kühl M, Schaeffer HJ, Huelsken J, Behrens J, Hammerschmidt M, Birchmeier W (Aug 2002). "The ankyrin repeat protein Diversin recruits Casein kinase Iepsilon to the beta-catenin degradation complex and acts in both canonical Wnt and Wnt/JNK signaling". Genes & Development. 16 (16): 2073–84. doi:10.1101/gad.230402. PMC 186448. PMID 12183362.
↑ Wang L, Lin HK, Hu YC, Xie S, Yang L, Chang C (Jul 2004). "Suppression of androgen receptor-mediated transactivation and cell growth by the glycogen synthase kinase 3 beta in prostate cells". The Journal of Biological Chemistry. 279 (31): 32444–52. doi:10.1074/jbc.M313963200. PMID 15178691.
↑ Davies G, Jiang WG, Mason MD (Apr 2001). "The interaction between beta-catenin, GSK3beta and APC after motogen induced cell-cell dissociation, and their involvement in signal transduction pathways in prostate cancer". International Journal of Oncology. 18 (4): 843–7. doi:10.3892/ijo.18.4.843. PMID 11251183.
↑ Kishida S, Yamamoto H, Hino S, Ikeda S, Kishida M, Kikuchi A (Jun 1999). "DIX domains of Dvl and axin are necessary for protein interactions and their ability to regulate beta-catenin stability". Molecular and Cellular Biology. 19 (6): 4414–22. doi:10.1128/mcb.19.6.4414. PMC 104400. PMID 10330181.
↑ Hong YR, Chen CH, Cheng DS, Howng SL, Chow CC (Aug 1998). "Human dynamin-like protein interacts with the glycogen synthase kinase 3beta". Biochemical and Biophysical Research Communications. 249 (3): 697–703. doi:10.1006/bbrc.1998.9253. PMID 9731200.
↑ Wu X, Shen QT, Oristian DS, Lu CP, Zheng Q, Wang HW, Fuchs E (Feb 2011). "Skin stem cells orchestrate directional migration by regulating microtubule-ACF7 connections through GSK3β". Cell. 144 (3): 341–52. doi:10.1016/j.cell.2010.12.033. PMID 21295697.
↑ Li Y, Bharti A, Chen D, Gong J, Kufe D (Dec 1998). "Interaction of glycogen synthase kinase 3beta with the DF3/MUC1 carcinoma-associated antigen and beta-catenin". Molecular and Cellular Biology. 18 (12): 7216–24. doi:10.1128/mcb.18.12.7216. PMC 109303. PMID 9819408.
↑ Li Y, Kuwahara H, Ren J, Wen G, Kufe D (Mar 2001). "The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1 carcinoma-associated antigen with GSK3 beta and beta-catenin". The Journal of Biological Chemistry. 276 (9): 6061–4. doi:10.1074/jbc.C000754200. PMID 11152665.
↑ Guo X, Ramirez A, Waddell DS, Li Z, Liu X, Wang XF (Jan 2008). "Axin and GSK3- control Smad3 protein stability and modulate TGF- signaling". Genes & Development. 22 (1): 106–20. doi:10.1101/gad.1590908. PMC 2151009. PMID 18172167.
↑ Foltz DR, Santiago MC, Berechid BE, Nye JS (Jun 2002). "Glycogen synthase kinase-3beta modulates notch signaling and stability". Current Biology. 12 (12): 1006–11. doi:10.1016/S0960-9822(02)00888-6. PMID 12123574.
↑ Espinosa L, Inglés-Esteve J, Aguilera C, Bigas A (Aug 2003). "Phosphorylation by glycogen synthase kinase-3 beta down-regulates Notch activity, a link for Notch and Wnt pathways". The Journal of Biological Chemistry. 278 (34): 32227–35. doi:10.1074/jbc.M304001200. PMID 12794074.
↑ Watcharasit P, Bijur GN, Zmijewski JW, Song L, Zmijewska A, Chen X, Johnson GV, Jope RS (Jun 2002). "Direct, activating interaction between glycogen synthase kinase-3beta and p53 after DNA damage". Proceedings of the National Academy of Sciences of the United States of America. 99 (12): 7951–5. doi:10.1073/pnas.122062299. PMC 123001. PMID 12048243.
↑ Dai F, Yu L, He H, Chen Y, Yu J, Yang Y, Xu Y, Ling W, Zhao S (May 2002). "Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction". Biochemical and Biophysical Research Communications. 293 (4): 1191–6. doi:10.1016/S0006-291X(02)00349-2. PMID 12054501.
↑ Inoki K, Ouyang H, Zhu T, Lindvall C, Wang Y, Zhang X, Yang Q, Bennett C, Harada Y, Stankunas K, Wang CY, He X, MacDougald OA, You M, Williams BO, Guan KL (Sep 2006). "TSC2 integrates Wnt and energy signals via a coordinated phosphorylation by AMPK and GSK3 to regulate cell growth". Cell. 126 (5): 955–68. doi:10.1016/j.cell.2006.06.055. PMID 16959574.

Turenne GA, Price BD (2001). "Glycogen synthase kinase3 beta phosphorylates serine 33 of p53 and activates p53's transcriptional activity". BMC Cell Biology. 2: 12. doi:10.1186/1471-2121-2-12. PMC 35361. PMID 11483158.
Plyte SE, Hughes K, Nikolakaki E, Pulverer BJ, Woodgett JR (Dec 1992). "Glycogen synthase kinase-3: functions in oncogenesis and development". Biochimica et Biophysica Acta. 1114 (2-3): 147–62. doi:10.1016/0304-419X(92)90012-N. PMID 1333807.
Morishima-Kawashima M, Hasegawa M, Takio K, Suzuki M, Yoshida H, Watanabe A, Titani K, Ihara Y (1995). "Hyperphosphorylation of tau in PHF". Neurobiology of Aging. 16 (3): 365–71; discussion 371–80. doi:10.1016/0197-4580(95)00027-C. PMID 7566346.
Jope RS, Bijur GN (2002). "Mood stabilizers, glycogen synthase kinase-3beta and cell survival". Molecular Psychiatry. 7 Suppl 1: S35–45. doi:10.1038/sj.mp.4001017. PMID 11986994.
Bhat RV, Budd SL (2003). "GSK3beta signalling: casting a wide net in Alzheimer's disease". Neuro-Signals. 11 (5): 251–61. doi:10.1159/000067423. PMID 12566926.
Nadri C, Kozlovsky N, Agam G (Sep 2003). "[Schizophrenia, neurodevelopment and glycogen synthase kinase-3]". Harefuah. 142 (8-9): 636–42, 644. PMID 14518171.
Mulholland DJ, Dedhar S, Wu H, Nelson CC (Jan 2006). "PTEN and GSK3beta: key regulators of progression to androgen-independent prostate cancer". Oncogene. 25 (3): 329–37. doi:10.1038/sj.onc.1209020. PMID 16421604.

PDB gallery

1gng: GLYCOGEN SYNTHASE KINASE-3 BETA (GSK3) COMPLEX WITH FRATTIDE PEPTIDE

1h8f: GLYCOGEN SYNTHASE KINASE 3 BETA.

1i09: STRUCTURE OF GLYCOGEN SYNTHASE KINASE-3 (GSK3B)

1j1b: Binary complex structure of human tau protein kinase I with AMPPNP

1j1c: Binary complex structure of human tau protein kinase I with ADP

1o9u: GLYCOGEN SYNTHASE KINASE 3 BETA COMPLEXED WITH AXIN PEPTIDE

1pyx: GSK-3 Beta complexed with AMP-PNP

1q3d: GSK-3 Beta complexed with Staurosporine

1q3w: GSK-3 Beta complexed with Alsterpaullone

1q41: GSK-3 Beta complexed with Indirubin-3'-monoxime

1q4l: GSK-3 Beta complexed with Inhibitor I-5

1q5k: crystal structure of Glycogen synthase kinase 3 in complexed with inhibitor

1r0e: Glycogen synthase kinase-3 beta in complex with 3-indolyl-4-arylmaleimide inhibitor

1uv5: GLYCOGEN SYNTHASE KINASE 3 BETA COMPLEXED WITH 6-BROMOINDIRUBIN-3'-OXIME

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 Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

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

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 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

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

This article is issued from Wikipedia - version of the 11/8/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

GSK3B

Function

Loss of function mutations

Interactions

See also

References

Further reading