Reviewed, UniProtKB/Swiss-Prot O59790 (ARK1_SCHPO)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase ark1
    EC=2.7.11.1
Alternative name(s):
    Aurora-related kinase 1

Gene names

Name:	ark1
Synonyms:	sex1
ORF Names:	SPCC320.13c, SPCC330.16

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for the spindle checkpoint attachment response during spindle formation, kinetochore microtubule interactions and chromosome segregation during anaphase. Ark1 activity depends upon cut17 function and phosphorylation. Ark1 with bir1 is required for full-scale association with kinetochores and formation of a complex with mad3. Ark1 is also required for phosphorylation of histone H3 that accompanies chromosome condensation and condensin recruitment to mitotic chromatin. Ark1 with pic1 is required for the execution of cytokinesis.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with bir1 and mad3 to form part of the mad2 complex involved in checkpoint activation. Interacts with pic1.
Subcellular location	Nucleus. Note= Associates with the elongating spindle during anaphase.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	attachment of spindle microtubules to kinetochore during mitosis Traceable author statement. Source: GeneDB_SPombe cytokinesis Ref.4 Inferred from mutant phenotype. Source: GeneDB_SPombe mitotic cell cycle spindle assembly checkpoint Ref.5 Inferred from mutant phenotype. Source: GeneDB_SPombe protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro protein localization to kinetochore Inferred from genetic interaction. Source: GeneDB_SPombe protein localization to nucleolar rDNA repeats Inferred from genetic interaction. Source: GeneDB_SPombe sister chromatid biorientation Ref.6 Traceable author statement. Source: GeneDB_SPombe
Cellular component	chromosome passenger complex Non-traceable author statement. Source: GeneDB_SPombe condensed chromosome kinetochore Ref.3 Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from electronic annotation. Source: UniProtKB-KW spindle midzone Ref.3 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro protein binding Ref.3 Ref.4 Inferred from physical interaction. Source: GeneDB_SPombe protein serine/threonine kinase activity Ref.3 Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 355	355	Serine/threonine-protein kinase ark1		PRO_0000085634
Regions
	Domain	89 – 340	252	Protein kinase
	Nucleotide binding	95 – 103	9	ATP By similarity
Sites
	Active site	212	1	Proton acceptor By similarity
	Binding site	118	1	ATP By similarity
Experimental info
	Mutagenesis	147	1	K → R: No phosphorylation of bir1; inhibits cytokinesis in a dominant negative manner

Sequences

	Sequence		Length	Mass (Da)
	O59790-1 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: BF15AC7B7571A301	FASTA	355	40,597
	10 20 30 40 50 60 MSDSKLADSL NCLSVSTPST TANPGRQQLL RLAVSNQRQV NNVSLANGKE NKRTSNSKFN 70 80 90 100 110 120 SSLRKIEEPI AGVPSSAGPQ WREFHIGMFE IGKPLGKGKF GRVYLAKEKK TGFIVALKTL 130 140 150 160 170 180 HKSELVQSKI EKQVRREIEI QSNLRHKNIL RLYGHFHDEK RIYLILEFAG RGELYQHLRR 190 200 210 220 230 240 AKRFSEEVAS KYIFQMANAL SYLHKKHVIH RDIKPENILL GIDGEIKLSD FGWSVHAPSN 250 260 270 280 290 300 RRTTLCGTLD YLPPEMVEGK EHTEKVDLWS LGVLTYEFLV GAPPFEDMSG HSATYKRIAK 310 320 330 340 350 VDLKIPSFVP PDARDLISRL LQHNPEKRMS LEQVMRHPWI VKYKDSWTRK SSESS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	Gwilliam R., Barrell B.G., Rajandream M.A., Wedler H., Wambutt R. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO N-TERMINUS.
[3]	"The S. pombe aurora-related kinase Ark1 associates with mitotic structures in a stage dependent manner and is required for chromosome segregation." Petersen J., Paris J., Willer M., Philippe M., Hagan I.M. J. Cell Sci. 114:4371-4384(2001) [PubMed: 11792803] [Abstract] Cited for: FUNCTION.
[4]	"The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts with the inner centromere protein Pic1 and mediates chromosome segregation and cytokinesis." Leverson J.D., Huang H.-K., Forsburg S.L., Hunter T. Mol. Biol. Cell 13:1132-1143(2002) [PubMed: 11950927] [Abstract] Cited for: FUNCTION, INTERACTION WITH PIC1, MUTAGENESIS OF LYS-147.
[5]	"S. pombe aurora kinase/survivin is required for chromosome condensation and the spindle checkpoint attachment response." Petersen J., Hagan I.M. Curr. Biol. 13:590-597(2003) [PubMed: 12676091] [Abstract] Cited for: FUNCTION, INTERACTION WITH BIR1 AND MAD3, IDENTIFICATION OF THE TRANSLATION INITIATION CODON.
[6]	"Suppressors of Bir1p (Survivin) identify roles for the chromosomal passenger protein Pic1p (INCENP) and the replication initiation factor Psf2p in chromosome segregation." Huang H.-K., Bailis J.M., Leverson J.D., Gomez E.B., Forsburg S.L., Hunter T. Mol. Cell. Biol. 25:9000-9015(2005) [PubMed: 16199877] [Abstract] Cited for: INTERACTION WITH PIC1.
[7]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329672 Genomic DNA. Translation: CAD88263.1.
PIR	T41298.
RefSeq	NP_001018849.1.
3D structure databases
HSSP	HSSP built from PDB template 1GZK based on UniProtKB P31751.
ModBase	Search...
Genome annotation databases
GeneID	3361036.
KEGG	spo:SPCC320.13c.
NMPDR	fig|4896.1.peg.54.
Organism-specific databases
GeneDB_Spombe	SPCC320.13c.
Gene expression databases
ArrayExpress	O59790.
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]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
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

ARK1_SCHPO

Accession

Primary (citable) accession number: O59790

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	April 13, 2004
Last modified:	November 25, 2008
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)