NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.274.14.9133; PubMed=10092583 [NCBI, ExPASy, EBI, Israel, Japan]
Brodbeck D., Cron P., Hemmings B.A.;
"A human protein kinase B gamma with regulatory phosphorylation sites in the activation loop and in the C-terminal hydrophobic domain.";
J. Biol. Chem. 274:9133-9136(1999).

[2]

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
DOI=10.1074/jbc.M104633200; PubMed=11387345 [NCBI, ExPASy, EBI, Israel, Japan]
Brodbeck D., Hill M.M., Hemmings B.A.;
"Two splice variants of PKB gamma have different regulatory capacity depending on the presence or absence of the regulatory phosphorylation site Ser-472 in the C-terminal hydrophobic domain.";
J. Biol. Chem. 276:29550-29558(2001).

Comments

FUNCTION: IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival. Capable of phosphorylating several known proteins. Truncated isoform 2/PKB gamma 1 without the second serine phosphorylation site could still be stimulated but to a lesser extent (By similarity).
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
ENZYME REGULATION: Two specific sites, one in the kinase domain (Thr-305) and the other in the C-terminal regulatory region (Ser-472), need to be phosphorylated for its full activation (By similarity).
SUBUNIT: Interacts (via PH domain) with TCL1A; this enhances AKT3 phosphorylation and activation (By similarity).
SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. Note=Membrane-associated after cell stimulation leading to its translocation.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	PKB gamma
Isoform ID	Q9WUA6-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	PKB gamma 1
Isoform ID	Q9WUA6-2
Features which should be applied to build the isoform sequence: VSP_004948.

TISSUE SPECIFICITY: Isoform 1 is expressed in prostate, testis, uterus and mammary gland and isoform 2 is expressed in prostate, testis and mammary gland.
DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI(3)K) results in its targeting to the plasma membrane.
PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By similarity).
SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.
SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
SIMILARITY: Contains 1 PH domain.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF124142; AAD29090.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Mm.235194

3D structure databases

HSSP

P31751; 1GZK. [HSSP ENTRY / PDB]

Q9WUA6; 1-115.

PTM databases

Q9WUA6; -.

Organism-specific databases

MGI

MGI:1345147; Akt3.

Gene expression databases

ArrayExpress

Q9WUA6; -.

CleanEx

MM_AKT3; -.

GermOnline

ENSMUSG00000019699; Mus musculus.

Family and domain databases

InterPro

IPR015744; 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 of domain structure.

Gene3D

G3DSA:2.30.29.30; PH_type; 1.

PANTHER

PTHR22985:SF69; Akt; 1.

Pfam

PF00169; PH; 1.
PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00233; PH; 1.
SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS51285; AGC_KINASE_CTER; 1.
PS50003; PH_DOMAIN; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q9WUA6.

Genome annotation databases

Ensembl

ENSMUSG00000019699; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

Q9WUA6; -.

HOVERGEN

Q9WUA6; -.

Other

Akt3; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; ATP-binding; Cytoplasm; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 479`	`479`	`RAC-gamma serine/threonine-protein kinase.`	`PRO_0000085612`
`DOMAIN`	`5 107`	`103`	`PH.`
`DOMAIN`	`148 405`	`258`	`Protein kinase.`
`DOMAIN`	`406 479`	`74`	`AGC-kinase C-terminal.`
`NP_BIND`	`154 162`	`9`	`ATP (By similarity).`
`ACT_SITE`	`271 271`		`Proton acceptor (By similarity).`
`BINDING`	`177 177`		`ATP (By similarity).`
`MOD_RES`	`120 120`		`Phosphoserine (By similarity).`
`MOD_RES`	`123 123`		`Phosphoserine (By similarity).`
`MOD_RES`	`305 305`		`Phosphothreonine; by PDPK1 (By similarity).`
`MOD_RES`	`472 472`		`Phosphoserine (By similarity).`
`VAR_SEQ`	`452 479`		`YDDDGMDGMDNERRPHFPQFSYSASGRE -> CQQSDCGMLGNWKKNDNKK (in isoform 2).`	`VSP_004948`

Sequence information

Length: 479 AA [This is the length of the unprocessed precursor]

Molecular weight: 55714 Da [This is the MW of the unprocessed precursor]

CRC64: F08ACDF75743B8FB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDVTIVKEG WVQKRGEYIK NWRPRYFLLK TDGSFIGYKE KPQDVDLPYP LNNFSVAKCQ 

        70         80         90        100        110        120 
LMKTERPKPN TFIIRCLQWT TVIERTFHVD TPEEREEWTE AIQAVADRLQ RQEEERMNCS 

       130        140        150        160        170        180 
PTSQIDNIGE EEMDASTTHH KRKTMNDFDY LKLLGKGTFG KVILVREKAS GKYYAMKILK 

       190        200        210        220        230        240 
KEVIIAKDEV AHTLTESRVL KNTRHPFLTS LKYSFQTKDR LCFVMEYVNG GELFFHLSRE 

       250        260        270        280        290        300 
RVFSEDRTRF YGAEIVSALD YLHSGKIVYR DLKLENLMLD KDGHIKITDF GLCKEGITDA 

       310        320        330        340        350        360 
ATMKTFCGTP EYLAPEVLED NDYGRAVDWW GLGVVMYEMM CGRLPFYNQD HEKLFELILM 

       370        380        390        400        410        420 
EDIKFPRTLS SDAKSLLSGL LIKDPNKRLG GGPDDAKEIM RHSFFSGVNW QDVYDKKLVP 

       430        440        450        460        470 
PFKPQVTSET DTRYFDEEFT AQTITITPPE KYDDDGMDGM DNERRPHFPQ FSYSASGRE

Q9WUA6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools