NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
DOI=10.1006/bbrc.1994.2738; PubMed=7999118 [NCBI, ExPASy, EBI, Israel, Japan]
Konishi H., Shinomura T., Kuroda S.I., Ono Y., Kikkawa U.;
"Molecular cloning of rat RAC protein kinase alpha and beta and their association with protein kinase C zeta.";
Biochem. Biophys. Res. Commun. 205:817-825(1994).

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

D30041; BAA06280.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

JC2438; JC2438.

NP_058789.1; -.

3D structure databases

HSSP

P31751; 1GZK. [HSSP ENTRY / PDB]

P47197; 1-111.

PTM databases

P47197; -.

Organism-specific databases

RGD

2082; Akt2.

Gene expression databases

ArrayExpress

P47197; -.

GermOnline

ENSRNOG00000018677; Rattus norvegicus.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654;	Cellular component: nucleoplasm (inferred from experiment from Reactome).
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).

BLOCKS

P47197.

Genome annotation databases

Ensembl

ENSRNOG00000018677; Rattus norvegicus. [Contig view]

GeneID

25233; -.

KEGG

rno:25233; -.

Phylogenomic databases

HOVERGEN

P47197; -.

Other

ProtoNet

P47197.

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_0000085610`
`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`	`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: 55543 Da [This is the MW of the unprocessed precursor]

CRC64: 3C4BE65B2F376F85 [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 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

P47197 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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