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Q60823

- AKT2_MOUSE

UniProt

Q60823 - AKT2_MOUSE

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Protein

RAC-beta serine/threonine-protein kinase

Gene

Akt2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinases, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI3P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.
One of the few specific substrates of AKT2 identified so far is PITX2. Phosphorylation of PITX2 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. AKT2 seems also to be the principal isoform responsible of the regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is also specifically involved in skeletal muscle differentiation, one of its substrates in this process being ANKRD2. Phosphorylates CLK2 on 'Thr-343'.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Two specific sites, one in the kinase domain (Thr-309) and the other in the C-terminal regulatory region (Ser-474), need to be phosphorylated for its full activation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei181 – 1811ATPPROSITE-ProRule annotation
Binding sitei181 – 1811InhibitorBy similarity
Binding sitei200 – 2001InhibitorBy similarity
Binding sitei232 – 2321Inhibitor; via amide nitrogenBy similarity
Binding sitei236 – 2361InhibitorBy similarity
Active sitei275 – 2751Proton acceptorPROSITE-ProRule annotation
Binding sitei279 – 2791Inhibitor; via carbonyl oxygenBy similarity
Binding sitei280 – 2801ManganeseBy similarity
Binding sitei293 – 2931InhibitorBy similarity
Binding sitei293 – 2931ManganeseBy similarity
Binding sitei294 – 2941Inhibitor; via amide nitrogenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 1669ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein kinase activity Source: MGI
  3. protein serine/threonine kinase activity Source: MGI

GO - Biological processi

  1. activation of Ral GTPase activity Source: MGI
  2. apoptotic process Source: UniProtKB-KW
  3. carbohydrate transport Source: UniProtKB-KW
  4. cellular response to insulin stimulus Source: UniProtKB
  5. glucose metabolic process Source: UniProtKB-KW
  6. glycogen biosynthetic process Source: UniProtKB-KW
  7. insulin receptor signaling pathway Source: MGI
  8. intracellular protein transmembrane transport Source: UniProtKB
  9. negative regulation of plasma membrane long-chain fatty acid transport Source: Ensembl
  10. peripheral nervous system myelin maintenance Source: MGI
  11. positive regulation of cell motility Source: Ensembl
  12. positive regulation of fatty acid beta-oxidation Source: Ensembl
  13. positive regulation of glucose import in response to insulin stimulus Source: MGI
  14. positive regulation of glycogen biosynthetic process Source: Ensembl
  15. positive regulation of protein phosphorylation Source: UniProtKB
  16. positive regulation of protein targeting to membrane Source: UniProtKB
  17. positive regulation of vesicle fusion Source: UniProtKB
  18. protein localization to plasma membrane Source: MGI
  19. protein phosphorylation Source: MGI
  20. regulation of translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Carbohydrate metabolism, Glucose metabolism, Glycogen biosynthesis, Glycogen metabolism, Sugar transport, Translation regulation, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.
ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_232427. Inhibition of TSC complex formation by PKB.
REACT_240075. Activation of PKB.

Names & Taxonomyi

Protein namesi
Recommended name:
RAC-beta serine/threonine-protein kinase (EC:2.7.11.1)
Alternative name(s):
Protein kinase Akt-2
Protein kinase B beta
Short name:
PKB beta
RAC-PK-beta
Gene namesi
Name:Akt2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:104874. Akt2.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity
Note: Localizes within both nucleus and cytoplasm of proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. By virtue of the N-terminal PH domain, is recruited to sites of the plasma membrane containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane targeting is also facilitared by interaction with CLIP3.By similarity

GO - Cellular componenti

  1. cell cortex Source: UniProtKB
  2. nucleus Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB
  4. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 481481RAC-beta serine/threonine-protein kinasePRO_0000085609Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Disulfide bondi60 ↔ 77By similarity
Modified residuei126 – 1261PhosphoserineBy similarity
Glycosylationi128 – 1281O-linked (GlcNAc)By similarity
Glycosylationi131 – 1311O-linked (GlcNAc)By similarity
Disulfide bondi297 ↔ 311By similarity
Glycosylationi306 – 3061O-linked (GlcNAc)By similarity
Modified residuei309 – 3091Phosphothreonine; by PDPK1By similarity
Glycosylationi313 – 3131O-linked (GlcNAc)By similarity
Modified residuei447 – 4471PhosphoserineBy similarity
Modified residuei451 – 4511PhosphothreonineBy similarity
Modified residuei474 – 4741PhosphoserineBy similarity
Modified residuei478 – 4781PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation on Thr-309 and Ser-474 is required for full activity.By similarity
Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT2 ubiquitination. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome (By similarity).By similarity
O-GlcNAcylation at Thr-306 and Thr-313 inhibits activating phosphorylation at Thr-309 via disrupting the interaction between AKT and PDK1.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ60823.
PaxDbiQ60823.
PRIDEiQ60823.

PTM databases

PhosphoSiteiQ60823.

Expressioni

Gene expression databases

BgeeiQ60823.
CleanExiMM_AKT2.
ExpressionAtlasiQ60823. baseline and differential.
GenevestigatoriQ60823.

Interactioni

Subunit structurei

Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B. Interacts with CLK2, PBH2 and TRAF6. Interacts (when phosphorylated) with CLIP3, the interaction promotes cell membrane localization (By similarity). Interacts with BTBD10 (PubMed:18160256). Interacts with KCTD20 (PubMed:24156551).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EEF2P136392EBI-400263,EBI-352560From a different organism.
ENO1P067332EBI-400263,EBI-353877From a different organism.
GAPDHP044062EBI-400263,EBI-354056From a different organism.

Protein-protein interaction databases

BioGridi198057. 4 interactions.
IntActiQ60823. 26 interactions.
MINTiMINT-1770302.

Structurei

3D structure databases

ProteinModelPortaliQ60823.
SMRiQ60823. Positions 1-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 108104PHPROSITE-ProRule annotationAdd
BLAST
Domaini152 – 409258Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini410 – 48172AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni230 – 2323Inhibitor bindingBy similarity
Regioni277 – 2793Inhibitor bindingBy similarity
Regioni292 – 2932Inhibitor bindingBy similarity

Domaini

Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PIK3CA) results in its targeting to the plasma membrane.By similarity

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120449.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ60823.
KOiK04456.
OMAiATGMYYA.
OrthoDBiEOG7Q5HCW.
PhylomeDBiQ60823.
TreeFamiTF102004.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60823-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP
60 70 80 90 100
PLNNFSVAEC QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWM
110 120 130 140 150
RAIQMVANSL KQRGPGEDAM DYKCGSPSDS STSEMMEVAV NKARAKVTMN
160 170 180 190 200
DFDYLKLLGK GTFGKVILVR EKATGRYYAM KILRKEVIIA KDEVAHTVTE
210 220 230 240 250
SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH LSRERVFTED
260 270 280 290 300
RARFYGAEIV SALEYLHSRD VVYRDIKLEN LMLDKDGHIK ITDFGLCKEG
310 320 330 340 350
ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF
360 370 380 390 400
YNQDHERLFE LILMEEIRFP RTLGPEAKSL LAGLLKKDPK QRLGGGPSDA
410 420 430 440 450
KEVMEHRFFL SINWQDVVQK KLLPPFKPQV TSEVDTRYFD DEFTAQSITI
460 470 480
TPPDRYDSLD PLELDQRTHF PQFSYSASIR E
Length:481
Mass (Da):55,742
Last modified:November 1, 1996 - v1
Checksum:i4AB4A9C4FB9CFA7D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22445 mRNA. Translation: AAA83557.1.
BC026151 mRNA. Translation: AAH26151.1.
BC040377 mRNA. Translation: AAH40377.1.
CCDSiCCDS21027.1.
RefSeqiNP_001103678.1. NM_001110208.1.
NP_031460.1. NM_007434.3.
XP_006539540.1. XM_006539477.1.
XP_006539541.1. XM_006539478.1.
XP_006539542.1. XM_006539479.1.
XP_006539543.1. XM_006539480.1.
XP_006539544.1. XM_006539481.1.
UniGeneiMm.177194.

Genome annotation databases

EnsembliENSMUST00000051356; ENSMUSP00000052103; ENSMUSG00000004056.
ENSMUST00000108343; ENSMUSP00000103980; ENSMUSG00000004056.
ENSMUST00000108344; ENSMUSP00000103981; ENSMUSG00000004056.
ENSMUST00000167435; ENSMUSP00000132141; ENSMUSG00000004056.
GeneIDi11652.
KEGGimmu:11652.
UCSCiuc009fwr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22445 mRNA. Translation: AAA83557.1 .
BC026151 mRNA. Translation: AAH26151.1 .
BC040377 mRNA. Translation: AAH40377.1 .
CCDSi CCDS21027.1.
RefSeqi NP_001103678.1. NM_001110208.1.
NP_031460.1. NM_007434.3.
XP_006539540.1. XM_006539477.1.
XP_006539541.1. XM_006539478.1.
XP_006539542.1. XM_006539479.1.
XP_006539543.1. XM_006539480.1.
XP_006539544.1. XM_006539481.1.
UniGenei Mm.177194.

3D structure databases

ProteinModelPortali Q60823.
SMRi Q60823. Positions 1-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198057. 4 interactions.
IntActi Q60823. 26 interactions.
MINTi MINT-1770302.

Chemistry

ChEMBLi CHEMBL5382.

PTM databases

PhosphoSitei Q60823.

Proteomic databases

MaxQBi Q60823.
PaxDbi Q60823.
PRIDEi Q60823.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000051356 ; ENSMUSP00000052103 ; ENSMUSG00000004056 .
ENSMUST00000108343 ; ENSMUSP00000103980 ; ENSMUSG00000004056 .
ENSMUST00000108344 ; ENSMUSP00000103981 ; ENSMUSG00000004056 .
ENSMUST00000167435 ; ENSMUSP00000132141 ; ENSMUSG00000004056 .
GeneIDi 11652.
KEGGi mmu:11652.
UCSCi uc009fwr.2. mouse.

Organism-specific databases

CTDi 208.
MGIi MGI:104874. Akt2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120449.
HOGENOMi HOG000233033.
HOVERGENi HBG108317.
InParanoidi Q60823.
KOi K04456.
OMAi ATGMYYA.
OrthoDBi EOG7Q5HCW.
PhylomeDBi Q60823.
TreeFami TF102004.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 3474.
Reactomei REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_232427. Inhibition of TSC complex formation by PKB.
REACT_240075. Activation of PKB.

Miscellaneous databases

NextBioi 279261.
PROi Q60823.
SOURCEi Search...

Gene expression databases

Bgeei Q60823.
CleanExi MM_AKT2.
ExpressionAtlasi Q60823. baseline and differential.
Genevestigatori Q60823.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
SMARTi SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, chromosomal localization and expression analysis of the mouse Akt2 oncogene."
    Altomare D.A., Guo K., Cheng J.Q., Sonoda G., Walsh K., Testa J.R.
    Oncogene 11:1055-1060(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
    Tissue: Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Retina and Salivary gland.
  3. "A novel Akt/PKB-interacting protein promotes cell adhesion and inhibits familial amyotrophic lateral sclerosis-linked mutant SOD1-induced neuronal death via inhibition of PP2A-mediated dephosphorylation of Akt/PKB."
    Nawa M., Kanekura K., Hashimoto Y., Aiso S., Matsuoka M.
    Cell. Signal. 20:493-505(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BTBD10.
  4. "Akt2-mediated phosphorylation of Pitx2 controls Ccnd1 mRNA decay during muscle cell differentiation."
    Gherzi R., Trabucchi M., Ponassi M., Gallouzi I.E., Rosenfeld M.G., Briata P.
    Cell Death Differ. 17:975-983(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PTIX2.
  5. "C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane."
    Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., Kruger M., Jiang Z.Y.
    Cell Metab. 14:378-389(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF C2CD5.
  6. Cited for: REVIEW ON FUNCTION.
  7. "Akt1 and Akt2: differentiating the aktion."
    Heron-Milhavet L., Khouya N., Fernandez A., Lamb N.J.
    Histol. Histopathol. 26:651-662(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  8. "KCTD20, a relative of BTBD10, is a positive regulator of Akt."
    Nawa M., Matsuoka M.
    BMC Biochem. 14:27-27(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCTD20.

Entry informationi

Entry nameiAKT2_MOUSE
AccessioniPrimary (citable) accession number: Q60823
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

In light of strong homologies in the primary amino acid sequence, the 3 AKT kinases were long surmised to play redundant and overlapping roles. More recent studies has brought into question the redundancy within AKT kinase isoforms and instead pointed to isoform specific functions in different cellular events and diseases. AKT1 is more specifically involved in cellular survival pathways, by inhibiting apoptotic processes; whereas AKT2 is more specific for the insulin receptor signaling pathway. Moreover, while AKT1 and AKT2 are often implicated in many aspects of cellular transformation, the 2 isoforms act in a complementary opposing manner. The role of AKT3 is less clear, though it appears to be predominantly expressed in brain.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3