ARK1_SCHPO
ID ARK1_SCHPO Reviewed; 355 AA.
AC O59790;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Serine/threonine-protein kinase ark1;
DE EC=2.7.11.1;
DE AltName: Full=Aurora-related kinase 1;
GN Name=ark1; Synonyms=sex1; ORFNames=SPCC320.13c, SPCC330.16;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Gwilliam R., Barrell B.G., Rajandream M.A., Wedler H., Wambutt R.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=11792803; DOI=10.1242/jcs.114.24.4371;
RA Petersen J., Paris J., Willer M., Philippe M., Hagan I.M.;
RT "The S. pombe aurora-related kinase Ark1 associates with mitotic structures
RT in a stage dependent manner and is required for chromosome segregation.";
RL J. Cell Sci. 114:4371-4384(2001).
RN [4]
RP FUNCTION, INTERACTION WITH PIC1, AND MUTAGENESIS OF LYS-118.
RX PubMed=11950927; DOI=10.1091/mbc.01-07-0330;
RA Leverson J.D., Huang H.-K., Forsburg S.L., Hunter T.;
RT "The Schizosaccharomyces pombe aurora-related kinase Ark1 interacts with
RT the inner centromere protein Pic1 and mediates chromosome segregation and
RT cytokinesis.";
RL Mol. Biol. Cell 13:1132-1143(2002).
RN [5]
RP FUNCTION, INTERACTION WITH BIR1 AND MAD3, AND IDENTIFICATION OF THE
RP TRANSLATION INITIATION CODON.
RX PubMed=12676091; DOI=10.1016/s0960-9822(03)00205-7;
RA Petersen J., Hagan I.M.;
RT "S. pombe aurora kinase/survivin is required for chromosome condensation
RT and the spindle checkpoint attachment response.";
RL Curr. Biol. 13:590-597(2003).
RN [6]
RP INTERACTION WITH PIC1.
RX PubMed=16199877; DOI=10.1128/mcb.25.20.9000-9015.2005;
RA Huang H.-K., Bailis J.M., Leverson J.D., Gomez E.B., Forsburg S.L.,
RA Hunter T.;
RT "Suppressors of Bir1p (Survivin) identify roles for the chromosomal
RT passenger protein Pic1p (INCENP) and the replication initiation factor
RT Psf2p in chromosome segregation.";
RL Mol. Cell. Biol. 25:9000-9015(2005).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Required for the spindle checkpoint attachment response
CC during spindle formation, kinetochore microtubule interactions and
CC chromosome segregation during anaphase. Ark1 activity depends upon
CC cut17 function and phosphorylation. Ark1 with bir1 is required for
CC full-scale association with kinetochores and formation of a complex
CC with mad3. Ark1 is also required for phosphorylation of histone H3 that
CC accompanies chromosome condensation and condensin recruitment to
CC mitotic chromatin. Ark1 with pic1 is required for the execution of
CC cytokinesis. {ECO:0000269|PubMed:11792803, ECO:0000269|PubMed:11950927,
CC ECO:0000269|PubMed:12676091}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with bir1 and mad3 to form part of the mad2 complex
CC involved in checkpoint activation. Interacts with pic1.
CC {ECO:0000269|PubMed:11950927, ECO:0000269|PubMed:12676091,
CC ECO:0000269|PubMed:16199877}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:16823372}. Note=Associates
CC with the elongating spindle during anaphase.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; CU329672; CAD88263.1; -; Genomic_DNA.
DR PIR; T41298; T41298.
DR RefSeq; NP_001018849.1; NM_001022711.2.
DR AlphaFoldDB; O59790; -.
DR SMR; O59790; -.
DR BioGRID; 280112; 49.
DR DIP; DIP-44220N; -.
DR IntAct; O59790; 4.
DR MINT; O59790; -.
DR STRING; 4896.SPCC320.13c.1; -.
DR SwissPalm; O59790; -.
DR MaxQB; O59790; -.
DR PaxDb; O59790; -.
DR EnsemblFungi; SPCC320.13c.1; SPCC320.13c.1:pep; SPCC320.13c.
DR GeneID; 3361036; -.
DR KEGG; spo:SPCC320.13c; -.
DR PomBase; SPCC320.13c; ark1.
DR VEuPathDB; FungiDB:SPCC320.13c; -.
DR eggNOG; KOG0580; Eukaryota.
DR HOGENOM; CLU_000288_63_6_1; -.
DR InParanoid; O59790; -.
DR OMA; PYGRQTT; -.
DR PhylomeDB; O59790; -.
DR BRENDA; 2.7.11.1; 5613.
DR Reactome; R-SPO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR PRO; PR:O59790; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032133; C:chromosome passenger complex; IDA:PomBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000939; C:inner kinetochore; IDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0072687; C:meiotic spindle; IDA:PomBase.
DR GO; GO:1990385; C:meiotic spindle midzone; IDA:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035175; F:histone kinase activity (H3-S10 specific); IDA:PomBase.
DR GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0051316; P:attachment of spindle microtubules to kinetochore involved in meiotic chromosome segregation; IMP:PomBase.
DR GO; GO:0120110; P:interphase mitotic telomere clustering; IMP:PomBase.
DR GO; GO:0033316; P:meiotic spindle assembly checkpoint signaling; IMP:PomBase.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IMP:PomBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IDA:PomBase.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:PomBase.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:1905561; P:positive regulation of kinetochore assembly; EXP:PomBase.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IMP:PomBase.
DR GO; GO:1903380; P:positive regulation of mitotic chromosome condensation; IMP:PomBase.
DR GO; GO:1905824; P:positive regulation of mitotic sister chromatid arm separation; IMP:PomBase.
DR GO; GO:0140429; P:positive regulation of mitotic sister chromatid biorientation; IGI:PomBase.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:PomBase.
DR GO; GO:0034503; P:protein localization to nucleolar rDNA repeats; IMP:PomBase.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IMP:PomBase.
DR GO; GO:1904967; P:regulation of monopolar spindle attachment to meiosis I kinetochore; IMP:PomBase.
DR GO; GO:0140273; P:repair of mitotic kinetochore microtubule attachment defect; EXP:PomBase.
DR InterPro; IPR030616; Aur.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24350; PTHR24350; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..355
FT /note="Serine/threonine-protein kinase ark1"
FT /id="PRO_0000085634"
FT DOMAIN 89..340
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 212
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 95..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 118
FT /note="K->R: No phosphorylation of bir1; inhibits
FT cytokinesis in a dominant negative manner."
FT /evidence="ECO:0000269|PubMed:11950927"
SQ SEQUENCE 355 AA; 40597 MW; BF15AC7B7571A301 CRC64;
MSDSKLADSL NCLSVSTPST TANPGRQQLL RLAVSNQRQV NNVSLANGKE NKRTSNSKFN
SSLRKIEEPI AGVPSSAGPQ WREFHIGMFE IGKPLGKGKF GRVYLAKEKK TGFIVALKTL
HKSELVQSKI EKQVRREIEI QSNLRHKNIL RLYGHFHDEK RIYLILEFAG RGELYQHLRR
AKRFSEEVAS KYIFQMANAL SYLHKKHVIH RDIKPENILL GIDGEIKLSD FGWSVHAPSN
RRTTLCGTLD YLPPEMVEGK EHTEKVDLWS LGVLTYEFLV GAPPFEDMSG HSATYKRIAK
VDLKIPSFVP PDARDLISRL LQHNPEKRMS LEQVMRHPWI VKYKDSWTRK SSESS
