[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1833819 [NCBI, ExPASy, EBI, Israel, Japan] Bellacosa A., Testa J.R., Staal S.P., Tsichlis P.N.; "A retroviral oncogene, akt, encoding a serine-threonine kinase containing an SH2-like region."; Science 254:274-277(1991).
[2]	INTERACTION WITH THEM4. DOI=10.1126/science.1062030; PubMed=11598301 [NCBI, ExPASy, EBI, Israel, Japan] Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.; "Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane."; Science 294:374-380(2001).

Comments

CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
SUBUNIT: Interacts with mouse THEM4.
DOMAIN: The AGC-kinase C-terminal mediates interaction with THEM4.
PTM: Autophosphorylated on threonine and serine residues.
MISCELLANEOUS: This protein is synthesized as a Gag-Akt polyprotein.
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

M80675; AAA42545.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P31749; 1H10. [HSSP ENTRY / PDB]

SMR

P31748; 24-142.

ModBase

P31748.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004674;	Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from InterPro).
GO:0044419;	Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
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

P31748.

Other

UniRef

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

Keywords

ATP-binding; Host-virus interaction; Kinase; Nucleotide-binding; Oncogene; Phosphoprotein; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 501`	`501`	`AKT kinase-transforming protein.`	`PRO_0000085614`
`DOMAIN`	`26 129`	`104`	`PH.`
`DOMAIN`	`171 429`	`259`	`Protein kinase.`
`DOMAIN`	`430 501`	`72`	`AGC-kinase C-terminal.`
`NP_BIND`	`177 185`	`9`	`ATP (By similarity).`
`ACT_SITE`	`295 295`		`Proton acceptor (By similarity).`
`BINDING`	`200 200`		`ATP (By similarity).`
`MOD_RES`	`347 347`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 501 AA [This is the length of the unprocessed precursor]

Molecular weight: 57870 Da [This is the MW of the unprocessed precursor]

CRC64: 5AEFDE58CD42F773 [This is a checksum on the sequence]

        10         20         30         40         50         60 
AREETLIIIP GLPLSLGATD TMNDVAIVKE GWLHKRGEYI KTWRPRYFLL KNDGTFIGYK 

        70         80         90        100        110        120 
ERPQDVDQRE SPLNNFSVAQ CQLMKTERPR PNTFIIRCLQ WTTVIERTFH VETPEEREEW 

       130        140        150        160        170        180 
ATAIQTVADG LKRQEEETMD FRSGSPSDNS GAEEMEVSLA KPKHRVTMNE FEYLKLLGKG 

       190        200        210        220        230        240 
TFGKVILVKE KATGRYYAMK ILKKEVIVAK DEVAHTLTEN RVLQNSRHPF LTALKYSFQT 

       250        260        270        280        290        300 
HDRLCFVMEY ANGGELFFHL SRERVFSEDR ARFYGAEIVS ALDYLHSEKN VVYRDLKLEN 

       310        320        330        340        350        360 
LMLDKDGHIK ITDFGLCKEG IKDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM 

       370        380        390        400        410        420 
YEMMCGRLPF YNQDHEKLFE LILMEEIRFP RTLGPEAKSL LSGLLKKDPT QRLGGGSEDA 

       430        440        450        460        470        480 
KEIMQHRFFA NIVWQDVYEK KLSPPFKPQV TSETDTRYFD EEFTAQMITI TPPDQDDSME 

       490        500 
CVDSERRPHF PQFSYSASGT A

P31748 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