HIM1_SCHPO
ID HIM1_SCHPO Reviewed; 545 AA.
AC O59836;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Hsk1-interacting molecule 1;
DE AltName: Full=DNA repair protein rad35;
GN Name=him1; Synonyms=dfp1, rad35; ORFNames=SPCC550.13;
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 [GENOMIC DNA / MRNA], FUNCTION, INTERACTION WITH HSK1,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=10409743; DOI=10.1128/mcb.19.8.5535;
RA Takeda T., Ogino K., Matsui E., Cho M.K., Kumagai H., Miyake T., Arai K.,
RA Masai H.;
RT "A fission yeast gene, him1(+)/dfp1(+), encoding a regulatory subunit for
RT Hsk1 kinase, plays essential roles in S-phase initiation as well as in S-
RT phase checkpoint control and recovery from DNA damage.";
RL Mol. Cell. Biol. 19:5535-5547(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RA Struck C., Schmidt H.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
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).
RN [4]
RP INTERACTION WITH MCM10.
RX PubMed=12604790; DOI=10.1073/pnas.0237384100;
RA Lee J.-K., Seo Y.-S., Hurwitz J.;
RT "The Cdc23 (Mcm10) protein is required for the phosphorylation of
RT minichromosome maintenance complex by the Dfp1-Hsk1 kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2334-2339(2003).
CC -!- FUNCTION: Activates hsk1 kinase and is essential for G1/S transition.
CC Has a role in S-phase checkpoint control induced by replication fork
CC blocks after nucleotide deprivation and DNA damage.
CC {ECO:0000269|PubMed:10409743}.
CC -!- SUBUNIT: Associates with hsk1. Interacts with mcm10.
CC {ECO:0000269|PubMed:10409743, ECO:0000269|PubMed:12604790}.
CC -!- INTERACTION:
CC O59836; P40381: swi6; NbExp=2; IntAct=EBI-908382, EBI-926939;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10409743}.
CC -!- PTM: Hyperphosphorylated at the G1/S and S-phases of the cell cycle.
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DR EMBL; AF110398; AAD03738.1; -; Genomic_DNA.
DR EMBL; AB028068; BAA78328.1; -; mRNA.
DR EMBL; Y17146; CAA76653.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA19117.1; -; Genomic_DNA.
DR PIR; T43513; T43513.
DR RefSeq; NP_588105.1; NM_001023096.2.
DR AlphaFoldDB; O59836; -.
DR SMR; O59836; -.
DR BioGRID; 275964; 19.
DR IntAct; O59836; 5.
DR STRING; 4896.SPCC550.13.1; -.
DR iPTMnet; O59836; -.
DR MaxQB; O59836; -.
DR PaxDb; O59836; -.
DR PRIDE; O59836; -.
DR EnsemblFungi; SPCC550.13.1; SPCC550.13.1:pep; SPCC550.13.
DR GeneID; 2539399; -.
DR KEGG; spo:SPCC550.13; -.
DR PomBase; SPCC550.13; -.
DR VEuPathDB; FungiDB:SPCC550.13; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_023948_0_0_1; -.
DR InParanoid; O59836; -.
DR OMA; RELTYFK; -.
DR PhylomeDB; O59836; -.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR PRO; PR:O59836; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:PomBase.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; EXP:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:PomBase.
DR GO; GO:0043392; P:negative regulation of DNA binding; IMP:PomBase.
DR GO; GO:1903468; P:positive regulation of DNA replication initiation; IDA:PomBase.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IBA:GO_Central.
DR GO; GO:1901987; P:regulation of cell cycle phase transition; IBA:GO_Central.
DR Gene3D; 3.40.50.10190; -; 1.
DR Gene3D; 6.10.250.3410; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR013939; Regulatory_Dfp1/Him1.
DR InterPro; IPR006572; Znf_DBF.
DR InterPro; IPR038545; Znf_DBF_sf.
DR Pfam; PF08630; Dfp1_Him1_M; 1.
DR Pfam; PF07535; zf-DBF; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00586; ZnF_DBF; 1.
DR PROSITE; PS51265; ZF_DBF4; 1.
PE 1: Evidence at protein level;
KW Cell cycle; DNA damage; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..545
FT /note="Hsk1-interacting molecule 1"
FT /id="PRO_0000083978"
FT ZN_FING 492..541
FT /note="DBF4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 518
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
SQ SEQUENCE 545 AA; 61860 MW; 96F90243322AFD8D CRC64;
MNLGRCPLAP RSANIVLPKH DAVSKQKEYR IEEKTNEAQR EEIITWKDNR EDEGEVKTDF
EVVNNENIIT TTPKHQTVIT PKSYRKSVKR IKHDAPQNED IPVMKGLAPI NADTESKAES
MAAGKVLGSK NSSQKARLQE WKRQYKKAFP HFRFYLDGCD PSVAHRVKKQ IQQLGGHVET
FFSGNVTHVA TVRAIQDVSV KYAKQDVITK ARQLNMKIWS MEKLCNRVLK TLMENDQCTT
NAPTKQGNDL SYLLYVEKVQ GTNERDLSVP RQDFVHFRGP YLYVHDIANI YKPILLREWQ
KPLPDRDVPW PTFRATSIGR CPFVPETKYR LSTSKSLVAK NDQQLLQRQS QEPSLILRAN
SMKASLPDIS NTGISGMNTN TTYNTNINNT PQTAISGITQ DTSPSIRTNC HHCLDDGMQA
SGIVQSNLTS AAMSNNSAIR SGSAASVPVV TINGRDIAEL KKRIIQQKSG MIGKDYSYKA
MLHNTSQRKI RVDAKPGYCE NCREKFDNFE SHIRSSRHRR FAENNDNFKD LDELFALVQR
PLRPD
