Reviewed, UniProtKB/Swiss-Prot P47197 (AKT2_RAT)

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Interacts with TRAF6 By similarity.
Post-translational modification	Polyubiquitinated. TRAF6-induced 'Lys-63'-linked AKT2 ubiquitination 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.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	negative regulation of RNA splicing Inferred from mutant phenotype. Source: RGD negative regulation of apoptosis Inferred from mutant phenotype. Source: RGD negative regulation of caspase activity Inferred from mutant phenotype. Source: RGD positive regulation of cell migration Inferred from mutant phenotype. Source: RGD positive regulation of glucose import Inferred from mutant phenotype. Source: RGD positive regulation of nitric oxide biosynthetic process Inferred from mutant phenotype. Source: RGD positive regulation of peptidyl-serine phosphorylation Inferred from mutant phenotype. Source: RGD positive regulation of positive chemotaxis Inferred from direct assay. Source: RGD positive regulation of signal transduction Inferred from mutant phenotype. Source: RGD positive regulation of sodium ion transport Inferred from mutant phenotype. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: RGD protein amino acid phosphorylation Inferred from direct assay. Source: RGD protein kinase B signaling cascade Inferred from mutant phenotype. Source: RGD response to muscle activity Inferred from expression pattern. Source: RGD response to osmotic stress Inferred from expression pattern. Source: RGD
Cellular component	cytosol Inferred from direct assay. Source: RGD insulin-responsive compartment Inferred from direct assay. Source: RGD microsome Inferred from direct assay. Source: RGD mitochondrion Inferred from direct assay. Source: RGD nucleoplasm Inferred from Experiment. Source: Reactome plasma membrane Inferred from direct assay. Source: RGD soluble fraction Inferred from direct assay. Source: RGD
Molecular function	ATP binding Inferred from direct assay. Source: RGD protein binding Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 481	481	RAC-beta serine/threonine-protein kinase		PRO_0000085610
Regions
	Domain	5 – 108	104	PH
	Domain	152 – 409	258	Protein kinase
	Domain	410 – 481	72	AGC-kinase C-terminal
	Nucleotide binding	158 – 166	9	ATP By similarity
Sites
	Active site	275	1	Proton acceptor By similarity
	Binding site	181	1	ATP By similarity
Amino acid modifications
	Modified residue	126	1	Phosphoserine By similarity
	Modified residue	309	1	Phosphothreonine; by PDPK1 By similarity
	Modified residue	447	1	Phosphoserine By similarity
	Modified residue	451	1	Phosphothreonine By similarity
	Modified residue	474	1	Phosphoserine By similarity
	Modified residue	478	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P47197-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 3C4BE65B2F376F85	FASTA	481	55,543
	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

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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D30041 mRNA. Translation: BAA06280.1.
IPI	IPI00212846.
PIR	JC2438.
RefSeq	NP_058789.1.
UniGene	Rn.87066
3D structure databases
SMR	P47197. Positions 1-111, 146-479.
ModBase	Search...
Protein-protein interaction databases
STRING	P47197.
PTM databases
PhosphoSite	P47197.
Genome annotation databases
Ensembl	ENSRNOT00000025303; ENSRNOP00000025303; ENSRNOG00000018677; Rattus norvegicus. [Genome view]
GeneID	25233.
KEGG	rno:25233.
UCSC	NM_017093. rat.
Organism-specific databases
CTD	25233.
RGD	2082. Akt2.
Phylogenomic databases
eggNOG	roNOG14203.
HOVERGEN	P47197.
InParanoid	P47197.
PhylomeDB	P47197.
Enzyme and pathway databases
BRENDA	2.7.11.1. 248.
Gene expression databases
ArrayExpress	P47197.
Genevestigator	P47197.
GermOnline	ENSRNOG00000018677. Rattus norvegicus.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR011993. PH_type. IPR017892. Pkinase_C. IPR001849. Pleckstrin_homology. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. IPR015744. Serine/threonine_Kinase_Rac. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
PANTHER	PTHR22985:SF69. Akt. 1 hit.
Pfam	PF00169. PH. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
SMART	SM00233. PH. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	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]
ProtoNet	Search...
Other Resources
NextBio	605799.

Entry information

Entry name

AKT2_RAT

Accession

Primary (citable) accession number: P47197

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	February 9, 2010
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)