HASP_SCHPO
ID HASP_SCHPO Reviewed; 488 AA.
AC O13924;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Serine/threonine-protein kinase haspin homolog hrk1;
DE EC=2.7.11.1;
GN Name=hrk1; ORFNames=SPAC23C4.03;
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 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).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PDS5 AND SWI6.
RX PubMed=20929775; DOI=10.1126/science.1194498;
RA Yamagishi Y., Honda T., Tanno Y., Watanabe Y.;
RT "Two histone marks establish the inner centromere and chromosome bi-
RT orientation.";
RL Science 330:239-243(2010).
CC -!- FUNCTION: Serine/threonine haspin-like protein kinase involved in cell
CC cycle regulation. Acts in chromosomal passenger complex (CPC) targeting
CC to centromeres by phosphorylating histone H3 at 'Thr3' (H3T3ph).
CC {ECO:0000269|PubMed:20929775}.
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 pds5 and swi6. {ECO:0000269|PubMed:20929775}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Chromosome.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Haspin subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; CU329670; CAB16874.1; -; Genomic_DNA.
DR PIR; T38259; T38259.
DR RefSeq; NP_593176.1; NM_001018572.2.
DR AlphaFoldDB; O13924; -.
DR SMR; O13924; -.
DR BioGRID; 278446; 17.
DR STRING; 4896.SPAC23C4.03.1; -.
DR iPTMnet; O13924; -.
DR MaxQB; O13924; -.
DR PaxDb; O13924; -.
DR EnsemblFungi; SPAC23C4.03.1; SPAC23C4.03.1:pep; SPAC23C4.03.
DR GeneID; 2541959; -.
DR KEGG; spo:SPAC23C4.03; -.
DR PomBase; SPAC23C4.03; hrk1.
DR VEuPathDB; FungiDB:SPAC23C4.03; -.
DR eggNOG; KOG2464; Eukaryota.
DR HOGENOM; CLU_559165_0_0_1; -.
DR InParanoid; O13924; -.
DR OMA; SENDHPM; -.
DR PhylomeDB; O13924; -.
DR Reactome; R-SPO-9020702; Interleukin-1 signaling.
DR PRO; PR:O13924; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031934; C:mating-type region heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0072354; F:histone kinase activity (H3-T3 specific); IDA:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0051456; P:attachment of spindle microtubules to kinetochore involved in meiotic sister chromatid segregation; IMP:PomBase.
DR GO; GO:0072356; P:chromosome passenger complex localization to kinetochore; IC:GOC-OWL.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IMP:PomBase.
DR InterPro; IPR024604; GSG2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR SMART; SM01331; DUF3635; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Chromosome; Cytoplasm; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..488
FT /note="Serine/threonine-protein kinase haspin homolog hrk1"
FT /id="PRO_0000352813"
FT DOMAIN 156..488
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 305
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 162..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 488 AA; 56521 MW; E5576EFAF5B3025A CRC64;
MESRSKVKTY GKNRRYINKD IEIWASLDER PCALKPRNIE NFNNQERSDL EHIHSKPKKD
SLLSWNILLK KGSYKENELL AKRNQNLVPT VIIPASPRDN ASKSVVSKKE VVNLSSSVAL
SGKPANNSKL DPLHRLLQIV AQEDALPFSQ FVKSQTFEIQ KIGEASYSEV YQASNADDVP
VVWKVIPFGE DGQAQYADVL NEVQISQWIK VDGFANLHQV VVVKGTYPSL LLEEWDRYLM
QNGSENDRPD SYSSTQLYCV LCLDHSGTDL EHFELRSWRE CWSVFYETLK ILSLVETRYE
FEHRDLHWGN ILIRKADRSE EEVSFLLNEI SLDDIESVDF PGSQDKADDF DNILQVTLID
FTLARASYSQ GIISYNEFND PDLFNGVDDY QFDIYRLMSR VTKGRWAQFF PITNVLWLHY
LIHQLLHKKN LSSPLTETET LMRSRLKQIF RLIDPVKTMQ FQQAEDSIRS KSTVTSATSL
LNWVRQKY
