Aurora kinase A-A - Xenopus laevis (African clawed frog)

Contribute

Send feedback

Read comments (?) or add your own

Q91820 (AURAA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aurora kinase A-A
EC=2.7.11.1

Alternative name(s):
Aurora/IPL1-related kinase 1
Short name=ARK-1
Short name=Aurora-related kinase 1
Serine/threonine-protein kinase 6-A
Serine/threonine-protein kinase Eg2-A
Short name=pEg2
Serine/threonine-protein kinase aurora-A
p46Eg265

Gene names

Name:	aurka-a
Synonyms:	aurka, eg2, stk6

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mitotic serine/threonine kinases that contributes to the regulation of cell cycle progression. Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis. Phosphorylates numerous target proteins. Important for microtubule formation and/or stabilization. Ref.1 Ref.3 Ref.4
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.1 Ref.3
Subunit structure	Interacts with kif2c and kif11. Ref.3 Ref.4
Subcellular location	Cytoplasm › cytoskeleton › spindle. Cytoplasm › cytoskeleton › centrosome. Note: Localizes to the spindle pole during mitosis especially from prophase through anaphase. Partially colocalized with gamma tubulin in the centrosome, from S to M phase. Ref.1 Ref.3
Tissue specificity	Highly expressed in ovary and testis. Ref.1
Developmental stage	Expressed maternally in oocytes, unfertilized eggs and embryos up to the mid-blastula transition (MBT). Ref.1
Post-translational modification	Phosphorylated. Autophosphorylated on a serine residue. Ref.1
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-serine phosphorylation Inferred from mutant phenotype Ref.3 Ref.1. Source: UniProtKB protein autophosphorylation Inferred from mutant phenotype Ref.1. Source: UniProtKB spindle assembly involved in mitosis Inferred from mutant phenotype Ref.1. Source: UniProtKB
Cellular_component	centrosome Inferred from direct assay Ref.3 Ref.1. Source: UniProtKB cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB spindle microtubule Inferred from direct assay Ref.1. Source: UniProtKB spindle pole Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule binding Inferred from direct assay Ref.1. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.3 Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 407

407

Aurora kinase A-A

PRO_0000086695

Regions

Domain

140 – 390

251

Protein kinase

Nucleotide binding

217 – 220

ATP By similarity

Region

287 – 300

Activation segment By similarity

Sites

Active site

263

Proton acceptor By similarity

Binding site

150

ATP; via amide nitrogen By similarity

Binding site

169

ATP Probable

Binding site

281

ATP By similarity

Experimental info

Mutagenesis

169

K → R: Lacks kinase activity. Disrupts mitotic spindle assembly. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q91820 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: DE1628A2C6D11277
Show »

FASTA

407

46,372

        10         20         30         40         50         60 
MERAVKENHK PSNVKIFHPM TEGAKRIPVN QPQSTQFRPP GTAVSAQRIL GPSNVPQRVL 

        70         80         90        100        110        120 
AQAQKPILSS QKPTTQIPLR PATQGHQSSK PQGPNENRNP QQTSHSSTPN VEKKGSTDQG 

       130        140        150        160        170        180 
KTSAVPKEEG KKKQWCLEDF EIGRPLGKGK FGNVYLARER ESKFILALKV LFKSQLEKAG 

       190        200        210        220        230        240 
VEHQLRREVE IQSHLRHPNI LRLYGYFHDA SRVYLILDYA PGGELFRELQ KCTRFDDQRS 

       250        260        270        280        290        300 
AMYIKQLAEA LLYCHSKKVI HRDIKPENLL LGSNGELKIA DFGWSVHAPS SRRTTLCGTL 

       310        320        330        340        350        360 
DYLPPEMIEG RMHDETVDLW SLGVLCYEFL VGKPPFETDT HQETYRRISK VEFQYPPYVS 

       370        380        390        400 
EEARDLVSKL LKHNPNHRLP LKGVLEHPWI IKNSQLKKKD EPLPGAQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Xenopus protein kinase pEg2 associates with the centrosome in a cell cycle-dependent manner, binds to the spindle microtubules and is involved in bipolar mitotic spindle assembly." Roghi C., Giet R., Uzbekov R., Morin N., Chartrain I., Le Guellec R., Couturier A., Doree M., Phillippe M., Prigent C. J. Cell Sci. 111:557-572(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF LYS-169. Tissue: Egg.
[2]	NIH - Xenopus Gene Collection (XGC) project Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[3]	"The Xenopus laevis aurora-related protein kinase pEg2 associates with and phosphorylates the kinesin-related protein XlEg5." Giet R., Uzbekov R., Cubizolles F., Le Guellec K., Prigent C. J. Biol. Chem. 274:15005-15013(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH KIF11, SUBCELLULAR LOCATION.
[4]	"Aurora A phosphorylates MCAK to control ran-dependent spindle bipolarity." Zhang X., Ems-McClung S.C., Walczak C.E. Mol. Biol. Cell 19:2752-2765(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH KIF2C.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z17207 mRNA. Translation: CAA78915.1. BC072133 mRNA. Translation: AAH72133.1.
PIR	S52243.
RefSeq	NP_001081565.1. NM_001088096.1.
UniGene	Xl.124.
3D structure databases
ProteinModelPortal	Q91820.
SMR	Q91820. Positions 131-394.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q91820. 2 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	397925.
KEGG	xla:397925.
Organism-specific databases
CTD	6790.
Xenbase	XB-GENE-866460. aurka.
Phylogenomic databases
HOVERGEN	HBG108519.
KO	K11481.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AURAA_XENLA

Accession

Primary (citable) accession number: Q91820
Secondary accession number(s): Q6INY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents