[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=C57BL/6 X CBA; TISSUE=Thymus; PubMed=7566964 [NCBI, ExPASy, EBI, Israel, Japan] Altomare D.A., Guo K., Cheng J.Q., Sonoda G., Walsh K., Testa J.R.; "Cloning, chromosomal localization and expression analysis of the mouse Akt2 oncogene."; Oncogene 11:1055-1060(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Retina, and Salivary gland; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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: Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B (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

U22445; AAA83557.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC026151; AAH26151.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC040377; AAH40377.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001103678.1; -.
NP_031460.1; -.
XP_001479789.1; -.
XP_001479797.1; -.
XP_001479802.1; -.

UniGene

Mm.177194

3D structure databases

HSSP

P31751; 1GZK. [HSSP ENTRY / PDB]

SMR

Q60823; 1-111.

ModBase

Q60823.

Protein-protein interaction databases

IntAct

Q60823; -.

PTM databases

PhosphoSite

Q60823; -.

Organism-specific databases

MGI

MGI:104874; Akt2.

Gene expression databases

ArrayExpress

Q60823; -.

CleanEx

MM_AKT2; -.

GermOnline

ENSMUSG00000004056; Mus musculus.

Ontologies

GO:0030027;	Cellular component: lamellipodium (inferred from direct assay from MGI).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004674;	Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from InterPro).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0046328;	Biological process: regulation of JNK cascade (inferred from direct assay from MGI).
QuickGo view.

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).

ProtoNet

Q60823.

Genome annotation databases

Ensembl

ENSMUSG00000004056; Mus musculus. [Contig view]

GeneID

100048123; -.
11652; -.

KEGG

mmu:100048123; -.
mmu:11652; -.

Phylogenomic databases

HOGENOM

Q60823; -.

HOVERGEN

Q60823; -.

Other

NextBio

461547; -.

SOURCE

Akt2; Mus musculus.

UniRef

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

Keywords

ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 481`	`481`	`RAC-beta serine/threonine-protein kinase.`	`PRO_0000085609`
`DOMAIN`	`5 108`	`104`	`PH.`
`DOMAIN`	`152 409`	`258`	`Protein kinase.`
`DOMAIN`	`410 481`	`72`	`AGC-kinase C-terminal.`
`NP_BIND`	`158 166`	`9`	`ATP (By similarity).`
`ACT_SITE`	`275 275`		`Proton acceptor (By similarity).`
`BINDING`	`181 181`		`ATP (By similarity).`
`MOD_RES`	`126 126`		`Phosphoserine (By similarity).`
`MOD_RES`	`309 309`		`Phosphothreonine; by PDPK1 (By similarity).`
`MOD_RES`	`474 474`		`Phosphoserine (By similarity).`

Sequence information

Length: 481 AA [This is the length of the unprocessed precursor]

Molecular weight: 55742 Da [This is the MW of the unprocessed precursor]

CRC64: 4AB4A9C4FB9CFA7D [This is a checksum on the sequence]

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

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

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

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

       250        260        270        280        290        300 
LSRERVFTED RARFYGAEIV SALEYLHSRD VVYRDIKLEN LMLDKDGHIK ITDFGLCKEG 

       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 TPPDRYDSLD PLELDQRTHF PQFSYSASIR 


E

Q60823 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