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Reviewed, UniProtKB/Swiss-Prot P47197 (AKT2_RAT)

Last modified November 25, 2008. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    RAC-beta serine/threonine-protein kinase
    EC=2.7.11.1
Alternative name(s):
    RAC-PK-beta
    Protein kinase Akt-2
    Protein kinase B, beta
      Short name=PKB beta
Gene names
Name: Akt2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

General protein kinase capable of phosphorylating several known proteins.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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.

Subunit structure

Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B By similarity.

Sequence similarities

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481RAC-beta serine/threonine-protein kinase
PRO_0000085610

Regions

Domain5 – 108104PH
Domain152 – 409258Protein kinase
Domain410 – 48172AGC-kinase C-terminal
Nucleotide binding158 – 1669ATP By similarity

Sites

Active site2751Proton acceptor By similarity
Binding site1811ATP By similarity

Amino acid modifications

Modified residue1261Phosphoserine By similarity
Modified residue3091Phosphothreonine; by PDPK1 By similarity
Modified residue4741Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P47197-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 3C4BE65B2F376F85

FASTA48155,543
        10         20         30         40         50         60 
MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP PLNNFSVAEC 

        70         80         90        100        110        120 
QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWI RAIQMVANSL KQRGPGEDAM 

       130        140        150        160        170        180 
DYKCGSPSDS STSEMMEVAV SKARAKVTMN DFDYLKLLGK GTFGKVILVR EKATGRYYAM 

       190        200        210        220        230        240 
KILRKEVIIA KDEVAHTVTE SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGDLFFH 

       250        260        270        280        290        300 
LSRERVFTED RARFYGAEIV SALEYLHSTD VVYRDIKLEN LMLDKDGHIK ITDFGLSKEG 

       310        320        330        340        350        360 
ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF YNQDHERLFE 

       370        380        390        400        410        420 
LILMEEIRFP RTLGPEAKSL LAGLLKKDPK QRLGGGPSDA KEVMEHRFFL SINWQDVVQK 

       430        440        450        460        470        480 
KLLPPFKPQV TSEVDTRYFD DEFTAQSITI TPPDRYDSLG SLELDQRTHF PQFSYSASIR 


E 

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References

[1]"Molecular cloning of rat RAC protein kinase alpha and beta and their association with protein kinase C zeta."
Konishi H., Shinomura T., Kuroda S.I., Ono Y., Kikkawa U.
Biochem. Biophys. Res. Commun. 205:817-825(1994) [PubMed: 7999118] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.

Cross-references

Sequence databases

D30041 mRNA. Translation: BAA06280.1.
PIRJC2438.
RefSeqNP_058789.1.
UniGeneRn.87066

3D structure databases

HSSPHSSP built from PDB template 1GZK based on UniProtKB P31751.
SMRP47197. Positions 1-111.
ModBaseSearch...

PTM databases

PhosphoSiteP47197.

Genome annotation databases

EnsemblENSRNOG00000018677. Rattus norvegicus. [Contig view]
GeneID25233.
KEGGrno:25233.

Organism-specific databases

RGD2082. Akt2.

Phylogenomic databases

HOVERGENP47197.

Gene expression databases

ArrayExpressP47197.
GermOnlineENSRNOG00000018677. Rattus norvegicus.

Family and domain databases

InterProIPR015744. Akt.
IPR001849. PH.
IPR011993. PH_type.
IPR000961. Pkinase_C.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
PANTHERPTHR22985:SF69. Akt. 1 hit.
PfamPF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. 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]
ProtoNetSearch...

Other Resources

NextBio605799.

Entry information

Entry nameAKT2_RAT
AccessionPrimary (citable) accession number: P47197
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 25, 2008
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents