[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. STRAIN=Bristol N2; DOI=10.1083/jcb.143.6.1635; PubMed=9852156 [NCBI, ExPASy, EBI, Israel, Japan] Schumacher J.M., Golden A., Donovan P.J.; "AIR-2: an Aurora/Ipl1-related protein kinase associated with chromosomes and midbody microtubules is required for polar body extrusion and cytokinesis in Caenorhabditis elegans embryos."; J. Cell Biol. 143:1635-1646(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Bristol N2; DOI=10.1126/science.282.5396.2012; PubMed=9851916 [NCBI, ExPASy, EBI, Israel, Japan] The C. elegans sequencing consortium; "Genome sequence of the nematode C. elegans: a platform for investigating biology."; Science 282:2012-2018(1998).
[3]	IDENTIFICATION, AND FUNCTION. DOI=10.1016/S0925-4773(99)00020-9; PubMed=10354474 [NCBI, ExPASy, EBI, Israel, Japan] Woollard A., Hodgkin J.; "Stu-7/air-2 is a C. elegans aurora homologue essential for chromosome segregation during embryonic and post-embryonic development."; Mech. Dev. 82:95-108(1999).
[4]	FUNCTION. DOI=10.1016/S0092-8674(00)00034-9; PubMed=10975519 [NCBI, ExPASy, EBI, Israel, Japan] Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K., Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M., Allis C.D.; "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes."; Cell 102:279-291(2000).
[5]	FUNCTION, AND INTERACTION WITH ZEN-4. DOI=10.1016/S0960-9822(00)00715-6; PubMed=11050384 [NCBI, ExPASy, EBI, Israel, Japan] Severson A.F., Hamill D.R., Carter J.C., Schumacher J., Bowerman B.; "The aurora-related kinase AIR-2 recruits ZEN-4/CeMKLP1 to the mitotic spindle at metaphase and is required for cytokinesis."; Curr. Biol. 10:1162-1171(2000).
[6]	FUNCTION, AND INTERACTION WITH ICP-1. DOI=10.1016/S0960-9822(00)00721-1; PubMed=11050385 [NCBI, ExPASy, EBI, Israel, Japan] Kaitna S., Mendoza M., Jantsch-Plunger V., Glotzer M.; "Incenp and an aurora-like kinase form a complex essential for chromosome segregation and efficient completion of cytokinesis."; Curr. Biol. 10:1172-1181(2000).
[7]	FUNCTION. DOI=10.1016/S1097-2765(00)00023-X; PubMed=10983970 [NCBI, ExPASy, EBI, Israel, Japan] Speliotes E.K., Uren A., Vaux D., Horvitz H.R.; "The survivin-like C. elegans BIR-1 protein acts with the Aurora-like kinase AIR-2 to affect chromosomes and the spindle midzone."; Mol. Cell 6:211-223(2000).
[8]	FUNCTION. DOI=10.1016/S0960-9822(02)00820-5; PubMed=12015116 [NCBI, ExPASy, EBI, Israel, Japan] Kaitna S., Pasierbek P., Jantsch M., Loidl J., Glotzer M.; "The aurora B kinase AIR-2 regulates kinetochores during mitosis and is required for separation of homologous Chromosomes during meiosis."; Curr. Biol. 12:798-812(2002).
[9]	FUNCTION. DOI=10.1083/jcb.200110045; PubMed=11940606 [NCBI, ExPASy, EBI, Israel, Japan] Rogers E., Bishop J.D., Waddle J.A., Schumacher J.M., Lin R.; "The aurora kinase AIR-2 functions in the release of chromosome cohesion in Caenorhabditis elegans meiosis."; J. Cell Biol. 157:219-229(2002).
[10]	IDENTIFICATION IN A COMPLEX WITH ICP-1; CSC-1 AND BIR-1. DOI=10.1083/jcb.200207117; PubMed=12707312 [NCBI, ExPASy, EBI, Israel, Japan] Romano A., Guse A., Krascenicova I., Schnabel H., Schnabel R., Glotzer M.; "CSC-1: a subunit of the Aurora B kinase complex that binds to the survivin-like protein BIR-1 and the incenp-like protein ICP-1."; J. Cell Biol. 161:229-236(2003).
[11]	FUNCTION. DOI=10.1016/j.cub.2005.03.041; PubMed=15854913 [NCBI, ExPASy, EBI, Israel, Japan] Guse A., Mishima M., Glotzer M.; "Phosphorylation of ZEN-4/MKLP1 by aurora B regulates completion of cytokinesis."; Curr. Biol. 15:778-786(2005).
[12]	FUNCTION, AND INTERACTION WITH TLK-1. DOI=10.1016/j.cub.2005.04.019; PubMed=15916946 [NCBI, ExPASy, EBI, Israel, Japan] Han Z., Riefler G.M., Saam J.R., Mango S.E., Schumacher J.M.; "The C. elegans Tousled-like kinase contributes to chromosome segregation as a substrate and regulator of the Aurora B kinase."; Curr. Biol. 15:894-904(2005).
[13]	INTERACTION WITH BMK-1. DOI=10.1091/mbc.E04-08-0682; PubMed=15548597 [NCBI, ExPASy, EBI, Israel, Japan] Bishop J.D., Han Z., Schumacher J.M.; "The Caenorhabditis elegans Aurora B kinase AIR-2 phosphorylates and is required for the localization of a BimC kinesin to meiotic and mitotic spindles."; Mol. Biol. Cell 16:742-756(2005).

Comments

FUNCTION: Serine/threonine-protein kinase which mediates both meiotic and mitotic chromosome segregation. Required for histone H3 'Ser-10' phosphorylation. Phosphorylates tlk-1 at 'Ser-634', which enhances its activity. Phosphorylates zen-4 at 'Ser-680'.
CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
SUBUNIT: Interacts with zen-4 and icp-1. Part of a complex containing at least air-2; icp-1; csc-1 and bir-1. Interacts with tlk-1 and bmk-1.
INTERACTION:
Q9GSQ0:icp-1; NbExp=1; IntAct=EBI-312947, EBI-312981;
SUBCELLULAR LOCATION: Note=Meiotic and mitotic chromosomes. During each division, relocates to the midbody microtubules.
DEVELOPMENTAL STAGE: Present during gametogenesis and throughout embryogenesis (at protein level).
SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.
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

AF071207; AAC70945.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U97196; AAB52459.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B87790; B87790.
T43221; T43221.

RefSeq

NP_491714.1; -.

UniGene

Cel.6613

3D structure databases

HSSP

O14965; 1OL6. [HSSP ENTRY / PDB]

ModBase

O01427.

Protein-protein interaction databases

DIP

DIP:25477N; -.

IntAct

O01427; 5.

Organism-specific databases

WormBase

WBGene00000099; air-2.

WormPep

B0207.4; CE24761. [WormPep / WorfDB]

Gene expression databases

ArrayExpress

O01427; -.

Ontologies

GO:0005694;	Cellular component: chromosome (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004674;	Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from InterPro).
GO:0051301;	Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0016568;	Biological process: chromatin modification (inferred from electronic annotation from UniProtKB-KW).
GO:0007059;	Biological process: chromosome segregation (inferred from electronic annotation from UniProtKB-KW).
GO:0009792;	Biological process: embryonic development ending in birth or egg hatching (inferred from mutant phenotype from WormBase).
GO:0040035;	Biological process: hermaphrodite genitalia development (inferred from mutant phenotype from WormBase).
GO:0007126;	Biological process: meiosis (inferred from electronic annotation from UniProtKB-KW).
GO:0007067;	Biological process: mitosis (inferred from electronic annotation from UniProtKB-KW).
GO:0007052;	Biological process: mitotic spindle organization (inferred from mutant phenotype from WormBase).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

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.

Pfam

PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

B0207.4; Caenorhabditis elegans. [Contig view]

GeneID

172268; -.

KEGG

cel:B0207.4; -.

NMPDR

fig|6239.3.peg.1382; -.

Other

874753; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell cycle; Cell division; Chromatin regulator; Chromosomal protein; Chromosome partition; Complete proteome; Developmental protein; Kinase; Meiosis; Mitosis; Nucleotide-binding; Serine/threonine-protein kinase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 305`	`305`	`Aurora/Ipl1-related protein kinase 2.`	`PRO_0000268640`
`DOMAIN`	`30 280`	`251`	`Protein kinase.`
`NP_BIND`	`36 44`	`9`	`ATP (By similarity).`
`ACT_SITE`	`153 153`		`Proton acceptor (By similarity).`
`BINDING`	`59 59`		`ATP (By similarity).`

Sequence information

Length: 305 AA [This is the length of the unprocessed precursor]

Molecular weight: 34749 Da [This is the MW of the unprocessed precursor]

CRC64: 1635EB60D2E14011 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MENKPPVINL PEKETVNTPQ KGGKFTINDF EIGRPLGKGK FGSVYLARTK TGHFHVAIKV 

        70         80         90        100        110        120 
LFKSQLISGG VEHQLEREIE IQSHLNHPNI IKLYTYFWDA KKIYLVLEYA PGGEMYKQLT 

       130        140        150        160        170        180 
VSKRFSEPTA AKYMYEIADA LSYCHRKNVI HRDIKPENLL IGSQGELKIG DFGWSVHAPS 

       190        200        210        220        230        240 
NKRQTMCGTM DYLPPEMVNG ADHSDAVDLW AIGVLCYEFL VGKPPFEHED QSKTYAAIKA 

       250        260        270        280        290        300 
ARFTYPDSVK KGARDLIGRL LVVDPKARCT LEQVKEHYWI QGMMEAKIRA EKQQKIEKEA 


SLRNH

O01427 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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