HHP2_SCHPO
ID HHP2_SCHPO Reviewed; 400 AA.
AC P40236;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Casein kinase I homolog hhp2;
DE EC=2.7.11.1;
GN Name=hhp2; ORFNames=SPAC23C4.12;
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. May regulate the activity of
CC protein(s) involved in 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; U10864; AAA21545.1; -; mRNA.
DR EMBL; X78872; CAA55474.1; -; mRNA.
DR EMBL; CU329670; CAB16883.1; -; Genomic_DNA.
DR PIR; S46358; S46358.
DR RefSeq; NP_593184.1; NM_001018580.2.
DR AlphaFoldDB; P40236; -.
DR SMR; P40236; -.
DR BioGRID; 278417; 59.
DR STRING; 4896.SPAC23C4.12.1; -.
DR iPTMnet; P40236; -.
DR MaxQB; P40236; -.
DR PaxDb; P40236; -.
DR PRIDE; P40236; -.
DR EnsemblFungi; SPAC23C4.12.1; SPAC23C4.12.1:pep; SPAC23C4.12.
DR GeneID; 2541929; -.
DR KEGG; spo:SPAC23C4.12; -.
DR PomBase; SPAC23C4.12; hhp2.
DR VEuPathDB; FungiDB:SPAC23C4.12; -.
DR eggNOG; KOG1164; Eukaryota.
DR HOGENOM; CLU_019279_2_0_1; -.
DR InParanoid; P40236; -.
DR OMA; RDTKINT; -.
DR PhylomeDB; P40236; -.
DR BRENDA; 2.7.11.1; 5613.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P40236; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0035838; C:growing cell tip; IDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; 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; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM: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; IMP:PomBase.
DR GO; GO:0010895; P:negative regulation of ergosterol biosynthetic process; IMP:PomBase.
DR GO; GO:0010620; P:negative regulation of transcription by transcription factor catabolism; IMP: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 GO; GO:0032933; P:SREBP signaling pathway; IMP:PomBase.
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..400
FT /note="Casein kinase I homolog hhp2"
FT /id="PRO_0000192865"
FT DOMAIN 12..278
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 330..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 18..26
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 4
FT /note="Missing (in Ref. 1; AAA21545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 45832 MW; CCE6DD85444D0EA9 CRC64;
MTVVDIKIGN KYRIGRKIGS GSFGQIYLGL NTVNGEQVAV KLEPLKARHH QLEYEFRVYN
ILKGNIGIPT IRWFGVTNSY NAMVMDLLGP SLEDLFCYCG RKFTLKTVLL LADQLISRIE
YVHSKSFLHR DIKPDNFLMK KHSNVVTMID FGLAKKYRDF KTHVHIPYRD NKNLTGTARY
ASINTHIGIE QSRRDDLESL GYVLLYFCRG SLPWQGLQAD TKEQKYQRIR DTKIGTPLEV
LCKGLPEEFI TYMCYTRQLS FTEKPNYAYL RKLFRDLLIR KGYQYDYVFD WMILKYQKRA
AAAAAASATA PPQVTSPMVS QTQPVNPITP NYSSIPLPAE RNPKTPQSFS TNIVQCASPS
PLPLSFRSPV PNKDYEYIPS SLQPQYSAQL RRVLDEEPAP
