RAC-alpha serine/threonine-protein kinase - Xenopus laevis (African clawed frog)

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Reviewed, UniProtKB/Swiss-Prot Q98TY9 (AKT1_XENLA)

Last modified September 22, 2009. Version 57. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · 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 Akt-1
      Short name=xAkt
    Protein kinase B, alpha
      Short name=PKB alpha

Gene names

Name:

akt1

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

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Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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General annotation (Comments)

Function	General protein kinase capable of phosphorylating several known proteins. 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, partly by playing a role in both insulin-induced phosphorylation of 4E-BP1 and in insulin-induced activation of p70 S6 kinase. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase By similarity. Required for insulin-stimulated meiotic reinitiation during oocyte maturation. Ref.1 UniProtKB P31750 UniProtKB P47196
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. UniProtKB P31750
Enzyme regulation	Activated in response to insulin. Three specific sites, one in the kinase domain (Thr-309) and the two other ones in the C-terminal regulatory region (Ser-474 and Tyr-475), need to be phosphorylated for its full activation. Ref.1
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Nucleus after activation by integrin-linked protein kinase 1 (ILK1) By similarity.
Tissue specificity	Expressed in the oocyte. Ref.1
Domain	Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI₃K) results in its targeting to the plasma membrane.
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	Carbohydrate metabolism Glucose metabolism Glycogen biosynthesis Sugar transport Transport
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW glucose transport Inferred from sequence or structural similarity. Source: UniProtKB glycogen biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW insulin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB insulin-like growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB protein amino acid phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 481

481

RAC-alpha serine/threonine-protein kinase

PRO_0000223507

Regions

Domain

5 – 108

104

Domain

151 – 409

259

Protein kinase

Domain

410 – 481

AGC-kinase C-terminal

Nucleotide binding

157 – 165

ATP By similarity

Sites

Active site

275

Proton acceptor By similarity

Binding site

180

ATP By similarity

Amino acid modifications

Modified residue

309

Phosphothreonine; by PDPK1 By similarity

Modified residue

474

Phosphoserine By similarity

Modified residue

475

Phosphotyrosine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q98TY9-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: FF56CFB9A6454303
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FASTA

481

56,042

        10         20         30         40         50         60 
MNEVAIVKEG WLHKRGEYIK TWRPRYFLLK SDGTFIGYKE RPQDVDQLET PLNNFSVAKC 

        70         80         90        100        110        120 
QLMKTERPKP NTFIIRCLQW TTVIERTFHV DSPEEREEWI QVIQHVADNL KKQEEEMMEV 

       130        140        150        160        170        180 
RSGDSPSDNS GAEEMEVSHS KPKHKVTMNE FEYLKLLGKG TFGKVILVKE KATGRYYAMK 

       190        200        210        220        230        240 
ILKKEVIVAK DEVAHTLTEN RVLQNSRHPF LTALKYSFQT HDRLCFVMEY ANGGELFFHL 

       250        260        270        280        290        300 
SRERIFSEDR ARFYGAEIVS ALDYLHSEKN VVYRDLKLEN LMLDKDGHIK ITDFGLCKEG 

       310        320        330        340        350        360 
IKDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF YNQDHEKLFE 

       370        380        390        400        410        420 
LILMEEIRFP RTLLPEAKSL LSGLLKKDPK QRLGGGPDDA KEIMQHKFFA GIVWQDVYEK 

       430        440        450        460        470        480 
KLVPPFKPQV TSETDTRYFD EEFTAQMITI TPPDQDDNFE FVDNERRPHF PQFSYSASGN 


A

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References

[1]

"Protein kinase B/Akt is essential for the insulin- but not progesterone-stimulated resumption of meiosis in Xenopus oocytes."
Andersen C.B., Sakaue H., Nedachi T., Kovacina K.S., Clayberger C., Conti M., Roth R.A.
Biochem. J. 369:227-238(2003) [PubMed: 12374568] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
Tissue: Oocyte.

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Cross-references

Sequence databases
	AF317656 mRNA. Translation: AAG59601.1.
RefSeq	NP_001083878.1.
UniGene	Xl.738
3D structure databases
HSSP	HSSP built from PDB template 1MRY based on UniProtKB P31751.
SMR	Q98TY9. Positions 1-116.
ModBase	Search...
Genome annotation databases
GeneID	399170.
KEGG	xla:399170.
Organism-specific databases
CTD	399170.
Xenbase	XB-FEAT-484952. akt1.
Phylogenomic databases
HOVERGEN	Q98TY9.
Enzyme and pathway databases
BRENDA	2.7.11.1. 648.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011993. PH_type. IPR017892. Pkinase_C. IPR001849. Pleckstrin_homology. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. 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]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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_XENLA

Accession

Primary (citable) accession number: Q98TY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	June 1, 2001
Last modified:	September 22, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents