HHP1_SCHPO
ID HHP1_SCHPO Reviewed; 365 AA.
AC P40235;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Casein kinase I homolog hhp1;
DE EC=2.7.11.1;
GN Name=hhp1; ORFNames=SPBC3H7.15;
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 [MRNA].
RC STRAIN=SP66;
RX PubMed=8074660; DOI=10.1006/bbrc.1994.2172;
RA Kearney P., Ebert M., Kuret J.;
RT "Molecular cloning and sequence analysis of two novel fission yeast casein
RT kinase-1 isoforms.";
RL Biochem. Biophys. Res. Commun. 203:231-236(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8026462; DOI=10.1002/j.1460-2075.1994.tb06571.x;
RA Dhillon N., Hoekstra M.F.;
RT "Characterization of two protein kinases from Schizosaccharomyces pombe
RT involved in the regulation of DNA repair.";
RL EMBO J. 13:2777-2788(1994).
RN [3]
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).
CC -!- FUNCTION: Involved in DNA repair. Has a probable role in repairing
CC alkylated DNA and may regulate the activity of protein(s) involved in
CC double strand break repair caused by gamma rays.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR EMBL; U10863; AAA21544.1; -; mRNA.
DR EMBL; X78871; CAA55473.1; -; mRNA.
DR EMBL; CU329671; CAA20311.1; -; Genomic_DNA.
DR PIR; S46357; S46357.
DR RefSeq; NP_595760.1; NM_001021661.2.
DR AlphaFoldDB; P40235; -.
DR SMR; P40235; -.
DR BioGRID; 277241; 30.
DR STRING; 4896.SPBC3H7.15.1; -.
DR iPTMnet; P40235; -.
DR SwissPalm; P40235; -.
DR MaxQB; P40235; -.
DR PaxDb; P40235; -.
DR PRIDE; P40235; -.
DR EnsemblFungi; SPBC3H7.15.1; SPBC3H7.15.1:pep; SPBC3H7.15.
DR GeneID; 2540718; -.
DR KEGG; spo:SPBC3H7.15; -.
DR PomBase; SPBC3H7.15; hhp1.
DR VEuPathDB; FungiDB:SPBC3H7.15; -.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_2_7_1; -.
DR InParanoid; P40235; -.
DR OMA; IFDWTFL; -.
DR PhylomeDB; P40235; -.
DR BRENDA; 2.7.11.1; 5613.
DR Reactome; R-SPO-204005; COPII-mediated vesicle transport.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P40235; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0000228; C:nuclear chromosome; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
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:0004713; F:protein tyrosine kinase activity; IDA:PomBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0045143; P:homologous chromosome segregation; IGI:PomBase.
DR GO; GO:0030999; P:linear element assembly; IMP:PomBase.
DR GO; GO:0051755; P:meiotic sister chromatid arm separation; EXP:PomBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0010845; P:positive regulation of reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:0006282; P:regulation of DNA repair; IMP:PomBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR030509; CK1.
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; PTHR11909:SF409; PTHR11909:SF409; 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 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA repair; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..365
FT /note="Casein kinase I homolog hhp1"
FT /id="PRO_0000192864"
FT DOMAIN 11..279
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 301..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 365 AA; 42450 MW; D637C950555F1339 CRC64;
MALDLRIGNK YRIGRKIGSG SFGDIYLGTN VVSGEEVAIK LESTRAKHPQ LEYEYRVYRI
LSGGVGIPFV RWFGVECDYN AMVMDLLGPS LEDLFNFCNR KFSLKTVLLL ADQLISRIEF
IHSKSFLHRD IKPDNFLMGI GKRGNQVNII DFGLAKKYRD HKTHLHIPYR ENKNLTGTAR
YASINTHLGI EQSRRDDLES LGYVLVYFCR GSLPWQGLKA TTKKQKYEKI MEKKISTPTE
VLCRGFPQEF SIYLNYTRSL RFDDKPDYAY LRKLFRDLFC RQSYEFDYMF DWTLKRKTQQ
DQQHQQQLQQ QLSATPQAIN PPPERSSFRN YQKQNFDEKG GDINTTVPVI NDPSATGAQY
INRPN
