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

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Q91819 (AURAB_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 87. History...

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

Documents (1) |

Third-party data

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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-B
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-B
Serine/threonine-protein kinase Eg2-B
Serine/threonine-protein kinase aurora-A
p46XlEg22

Gene names

Name:	aurka-b
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 › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with kif2c and kif11 By similarity.
Subcellular location	Cytoplasm › cytoskeleton › spindle pole By similarity. Cytoplasm › cytoskeleton › centrosome By similarity. 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 By similarity.
Post-translational modification	Phosphorylated. Autophosphorylated on a serine residue By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence CAA78914.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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 sequence or structural similarity. Source: UniProtKB protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB spindle assembly involved in mitosis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	centrosome Inferred from sequence or structural similarity. Source: UniProtKB spindle microtubule Inferred from sequence or structural similarity. Source: UniProtKB spindle pole Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW kinesin binding Inferred from sequence or structural similarity. Source: UniProtKB microtubule binding Inferred from sequence or structural similarity. Source: UniProtKB protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 408

408

Aurora kinase A-B

PRO_0000086696

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 By similarity

Binding site

281

ATP By similarity

Experimental info

Sequence conflict

211

C → S in CAA78914. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q91819 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: FD4855CC6708E5E7
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FASTA

408

46,477

        10         20         30         40         50         60 
MERAVKENHK PSNVKVFHPM TEGPKRIPVS QPPSTQVRPP VTGVSAQRIL GPSNVPQRVM 

        70         80         90        100        110        120 
MQAQKPVLSN QKPTAQGLLR PATHGHQTSK PQGPNENRNP QQTSHSSTPN MEKKGSTDQG 

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

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

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

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

       370        380        390        400 
EEAKDLVSKL LKHNPNHRLP LKGVLEHPWI VKNSQQPKKK DEPLAGAQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Eg2, selected by differential screening encodes a new Xenopus protein kinase family." Roghi C., Le Guellec R., Paris J., Couturier A., Philippe M. Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: Kidney.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z17206 mRNA. Translation: CAA78914.1. Different initiation. BC075177 mRNA. Translation: AAH75177.1.
RefSeq	NP_001082272.1. NM_001088803.1.
UniGene	Xl.4421.
3D structure databases
ProteinModelPortal	Q91819.
SMR	Q91819. Positions 131-394.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	398349.
KEGG	xla:398349.
Organism-specific databases
CTD	398349.
Phylogenomic databases
HOVERGEN	HBG108519.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K11481.
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

AURAB_XENLA

Accession

Primary (citable) accession number: Q91819
Secondary accession number(s): Q6DJK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	October 5, 2010
Last modified:	November 16, 2011
This is version 87 of the entry and version 3 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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents