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UniProtKB/Swiss-Prot entry O59790


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARK1_SCHPO
Primary accession number O59790
Secondary accession numbers None
Integrated into Swiss-Prot on June 20, 2002
Sequence was last modified on April 13, 2004 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 70)
Name and origin of the protein
Protein name Serine/threonine-protein kinase ark1
Synonyms EC 2.7.11.1
Aurora-related kinase 1
Gene name
Name: ark1
Synonyms: sex1
ORFNames: SPCC320.13c, SPCC330.16
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
SEQUENCE REVISION TO N-TERMINUS.
Gwilliam R., Barrell B.G., Rajandream M.A., Wedler H., Wambutt R.;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION.
PubMed=11792803 [NCBI, ExPASy, EBI, Israel, Japan]
Petersen J., Paris J., Willer M., Philippe M., Hagan I.M.;
"The S. pombe aurora-related kinase Ark1 associates with mitotic structures in a stage dependent manner and is required for chromosome segregation.";
J. Cell Sci. 114:4371-4384(2001).
[4]
FUNCTION, INTERACTION WITH PIC1, AND MUTAGENESIS OF LYS-147.
DOI=10.1091/mbc.01-07-0330; PubMed=11950927 [NCBI, ExPASy, EBI, Israel, Japan]
Leverson J.D., Huang H.-K., Forsburg S.L., Hunter T.;
"The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts with the inner centromere protein Pic1 and mediates chromosome segregation and cytokinesis.";
Mol. Biol. Cell 13:1132-1143(2002).
[5]
FUNCTION, INTERACTION WITH BIR1 AND MAD3, AND IDENTIFICATION OF THE TRANSLATION INITIATION CODON.
DOI=10.1016/S0960-9822(03)00205-7; PubMed=12676091 [NCBI, ExPASy, EBI, Israel, Japan]
Petersen J., Hagan I.M.;
"S. pombe aurora kinase/survivin is required for chromosome condensation and the spindle checkpoint attachment response.";
Curr. Biol. 13:590-597(2003).
[6]
INTERACTION WITH PIC1.
DOI=10.1128/MCB.25.20.9000-9015.2005; PubMed=16199877 [NCBI, ExPASy, EBI, Israel, Japan]
Huang H.-K., Bailis J.M., Leverson J.D., Gomez E.B., Forsburg S.L., Hunter T.;
"Suppressors of Bir1p (Survivin) identify roles for the chromosomal passenger protein Pic1p (INCENP) and the replication initiation factor Psf2p in chromosome segregation.";
Mol. Cell. Biol. 25:9000-9015(2005).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nbt1222; PubMed=16823372 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
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: 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.
  • 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
CU329672; CAD88263.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T41298; T41298.
RefSeq NP_001018849.1; -.
3D structure databases
HSSP P31751; 1GZK. [HSSP ENTRY / PDB]
ModBase O59790.
Organism-specific databases
GeneDB_Spombe SPCC320.13c; -.
Gene expression databases
ArrayExpress O59790; -.
Ontologies
GO
GO:0032133; Cellular component: chromosome passenger complex (non-traceable author statement from GeneDB_SPombe).
GO:0000777; Cellular component: condensed chromosome kinetochore (inferred from direct assay from GeneDB_SPombe).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0051233; Cellular component: spindle midzone (inferred from direct assay from GeneDB_SPombe).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from GeneDB_SPombe).
GO:0004674; Molecular function: protein serine/threonine kinase activity (inferred from electronic annotation from InterPro).
GO:0051315; Biological process: attachment of spindle microtubules to kinetochore during mitosis (traceable author statement from GeneDB_SPombe).
GO:0000910; Biological process: cytokinesis (inferred from mutant phenotype from GeneDB_SPombe).
GO:0007094; Biological process: mitotic cell cycle spindle assembly checkpoint (inferred from mutant phenotype from GeneDB_SPombe).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0034501; Biological process: protein localization to kinetochore (inferred from genetic interaction from GeneDB_SPombe).
GO:0034503; Biological process: protein localization to nucleolar rDNA repeats (inferred from genetic interaction from GeneDB_SPombe).
GO:0031134; Biological process: sister chromatid biorientation (traceable author statement from GeneDB_SPombe).
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
GeneID 3361036; -.
KEGG spo:SPCC320.13c; -.
NMPDR fig|4896.1.peg.54; -.
Other
ProtoNet O59790.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Nucleus; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   355  355     Serine/threonine-protein kinase ark1. PRO_0000085634
DOMAIN   89   340  252     Protein kinase. 
NP_BIND   95   103  9     ATP (By similarity). 
ACT_SITE   212   212        Proton acceptor (By similarity). 
BINDING   118   118        ATP (By similarity). 
MUTAGEN   147   147        K->R: No phosphorylation of bir1; inhibits cytokinesis in a dominant negative manner. 
Sequence information
Length: 355 AA [This is the length of the unprocessed precursor] Molecular weight: 40597 Da [This is the MW of the unprocessed precursor] CRC64: BF15AC7B7571A301 [This is a checksum on the sequence]
        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 

O59790 in FASTA format

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View entry in raw text format (no links)
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