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rac-beta serine/threonine kinase (AKT2 kinase, protein kinase B-beta, PKB beta, AKT2)

Function: - general protein kinase capable of phosphorylating several known proteins - 2 specific sites, one in the kinase domain (Thr-309) & the other in the C-terminal regulatory region (Ser-474), need to be phosphorylated for its full activation Structure: - belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family, RAC subfamily - contains 1 AGC-kinase C-terminal domain - contains 1 PH domain - contains 1 protein kinase domain Expression: - expressed in all human cell types so far analyzed - highly expressed in insulin responsive tissues Pathology: - alterations of AKT2 may contribute to the pathogenesis of ovarian carcinomas - mutation associated with severe insulin resistance & diabetes mellitus in one family [2]

General

rac S/T kinase; AKT kinase

Properties

SIZE: MW = 56 kD entity length = 481 aa STATE: active state MOTIF: PH domain {5-108} S/T phosphorylation site kinase domain SITE: 152-409 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 158-166 ATP-binding site NAME: ATP-binding site SITE: 181-181 aspartate residue {D275}

Database Correlations

OMIM 164731 MORBIDMAP 164731 UniProt P31751 PFAM correlations Entrez Gene 208 Kegg hsa:208 ENZYME 2.7.11.1

References

  1. UniProt :accession P31751
  2. George S, Rochford JJ, Wolfrum C, Gray SL, Schinner S et al A family with severe insulin resistance and diabetes due to a mutation in AKT2. Science. 2004 May 28;304(5675):1325-8. PMID: 15166380
  3. Atlas of genetics & cytogenetics in oncology & haematology http://atlasgeneticsoncology.org/genes/AKT2ID517ch19q13.html