RAC-alpha serine/threonine-protein kinase

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Reviewed, UniProtKB/Swiss-Prot Q01314 (AKT1_BOVIN)

Last modified February 9, 2010. Version 94. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    RAC-alpha serine/threonine-protein kinase
    EC=2.7.11.1
Alternative name(s):
    RAC-PK-alpha
    Protein kinase B
      Short name=PKB

Gene names

Name:	AKT1
Synonyms:	PKB

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length	480 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI₃K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2, thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	The C-terminus interacts with the C-terminus of CCDC88A/GRDN and THEM4. Interacts with AKTIP. Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B. Interacts with TRAF6 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Cell membrane By similarity. Note: Nucleus after activation by integrin-linked protein kinase 1 (ILK1). Nuclear translocation is enhanced by interaction with TCL1A By similarity.
Domain	Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI₃K) results in its targeting to the plasma membrane. The AGC-kinase C-terminal mediates interaction with THEM4 By similarity.
Post-translational modification	Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required for full activity. Ser-473 phosphorylation by mTORC2 favors Thr-308 phosphorylation by PDPK1 By similarity. Ser-473 is dephosphorylated by PHLPP. Ref.4 Polyubiquitinated. TRAF6-induced 'Lys-63'-linked AKT1 ubiquitination is critical for phosphorylation and activation. When ubiquitinated, it translocates to the plasma membrane, where it becomes phosphorylated 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.

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Ontologies

Keywords
Biological process	Apoptosis Carbohydrate metabolism Glucose metabolism Glycogen biosynthesis Glycogen metabolism Sugar transport Translation regulation Transport
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW carbohydrate transport Inferred from electronic annotation. Source: UniProtKB-KW glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW glycogen biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ppl	Q9R269	1	EBI-368344,EBI-368293	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 480

480

RAC-alpha serine/threonine-protein kinase

PRO_0000085604

Regions

Domain

5 – 108

104

Domain

150 – 408

259

Protein kinase

Domain

409 – 480

AGC-kinase C-terminal

Nucleotide binding

156 – 164

ATP By similarity

Sites

Active site

274

Proton acceptor By similarity

Binding site

179

ATP By similarity

Amino acid modifications

Modified residue

124

Phosphoserine By similarity

Modified residue

129

Phosphoserine By similarity

Modified residue

308

Phosphothreonine By similarity

Modified residue

473

Phosphoserine Ref.4

Modified residue

474

Phosphotyrosine By similarity

Experimental info

Sequence conflict

149

D → E in CAA43371. Ref.1

Sequence conflict

153

L → V in CAA43371. Ref.1

Sequence conflict

173 – 174

GR → AA in CAA43371. Ref.1

Sequence conflict

209

F → S in CAA43371. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q01314-1 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: 152E6613C4E6ED5A
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FASTA

480

55,748

        10         20         30         40         50         60 
MNDVAIVKEG WLHKRGEYIK TWRPRYFLLK NDGTFIGYKE RPQDLEQRES PLNNFSVAQC 

        70         80         90        100        110        120 
QLMKTERPRP NTFIIRCLQW TTVIERTFHV ETPEEREEWT TAIQTVADGL KRQEEETMDF 

       130        140        150        160        170        180 
RSGSPGENSG AEEMEVSLAK PKHRVTMNDF EYLKLLGKGT FGKVILVKEK ATGRYYAMKI 

       190        200        210        220        230        240 
LKKEVIVAKD EVAHTLTENR VLQNSRHPFL TALKYSFQTH DRLCFVMEYA NGGELFFHLS 

       250        260        270        280        290        300 
RERVFSEDRA RFYGAEIVSA LDYLHSEKEV VYRDLKLENL MLDKDGHIKI TDFGLCKEGI 

       310        320        330        340        350        360 
KDGATMKTFC GTPEYLAPEV LEDNDYGRAV DWWGLGVVMY EMMCGRLPFY NQDHEKLFEL 

       370        380        390        400        410        420 
ILMEEIRFPR TLSPEAKSLL SGLLKKDPKQ RLGGGSEDAK EIMQHRFFAS IVWQDVYEKK 

       430        440        450        460        470        480 
LSPPFKPQVT SETDTRYFDE EFTAQMITIT PPDQDDSMEG VDSERRPHFP QFSYSASATA

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References

[1]	"Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families." Coffer P.J., Woodgett J.R. Eur. J. Biochem. 201:475-481(1991) [PubMed: 1718748] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	Erratum Coffer P.J., Woodgett J.R. Eur. J. Biochem. 205:1217-1218(1992) [PubMed: 1533586] [Abstract] Cited for: SEQUENCE REVISION.
[3]	"Complete sequence of the bovine AKT1 gene." Khatib H. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[4]	"PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth." Gao T., Furnari F., Newton A.C. Mol. Cell 18:13-24(2005) [PubMed: 15808505] [Abstract] Cited for: DEPHOSPHORYLATION AT SER-473 BY PHLPP.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	X61036 mRNA. Translation: CAA43371.1. AY781100 mRNA. Translation: AAW71957.1.
IPI	IPI00696205.
PIR	S62117.
RefSeq	NP_776411.1.
UniGene	Bt.4843
3D structure databases
SMR	Q01314. Positions 3-121, 144-478.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q01314. 1 interaction.
STRING	Q01314.
Genome annotation databases
Ensembl	ENSBTAT00000023461; ENSBTAP00000023461; ENSBTAG00000017636; Bos taurus. [Genome view]
GeneID	280991.
KEGG	bta:280991.
Organism-specific databases
CTD	280991.
Phylogenomic databases
eggNOG	maNOG18684.
HOVERGEN	Q01314.
PhylomeDB	Q01314.
Enzyme and pathway databases
BRENDA	2.7.11.1. 251.
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...

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Entry information

Entry name

AKT1_BOVIN

Accession

Primary (citable) accession number: Q01314
Secondary accession number(s): Q5ER96

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	July 25, 2006
Last modified:	February 9, 2010
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents