ORC1_HUMAN
ID ORC1_HUMAN Reviewed; 861 AA.
AC Q13415; D3DQ34; Q13471; Q5T0F5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Origin recognition complex subunit 1;
DE AltName: Full=Replication control protein 1;
GN Name=ORC1; Synonyms=ORC1L, PARC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7502077; DOI=10.1126/science.270.5242.1667;
RA Gavin K.A., Hidaka M., Stillman B.D.;
RT "Conserved initiator proteins in eukaryotes.";
RL Science 270:1667-1671(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wolf D.A., McKeon F.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH CDC6.
RX PubMed=9566895; DOI=10.1128/mcb.18.5.2758;
RA Saha P., Chen J., Thome K.C., Lawlis S.J., Hou Z.H., Hendricks M.,
RA Parvin J.D., Dutta A.;
RT "Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively
RT eliminated from the nucleus at the onset of S phase.";
RL Mol. Cell. Biol. 18:2758-2767(1998).
RN [6]
RP INTERACTION WITH KAT7.
RX PubMed=10438470; DOI=10.1074/jbc.274.33.23027;
RA Iizuka M., Stillman B.;
RT "Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the
RT human initiator protein.";
RL J. Biol. Chem. 274:23027-23034(1999).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=12909627; DOI=10.1074/jbc.m307534200;
RA Tatsumi Y., Ohta S., Kimura H., Tsurimoto T., Obuse C.;
RT "The ORC1 cycle in human cells: I. cell cycle-regulated oscillation of
RT human ORC1.";
RL J. Biol. Chem. 278:41528-41534(2003).
RN [8]
RP IDENTIFICATION IN THE ORC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP ASSEMBLY OF THE ORC COMPLEX.
RX PubMed=12909626; DOI=10.1074/jbc.m307535200;
RA Ohta S., Tatsumi Y., Fujita M., Tsurimoto T., Obuse C.;
RT "The ORC1 cycle in human cells: II. Dynamic changes in the human ORC
RT complex during the cell cycle.";
RL J. Biol. Chem. 278:41535-41540(2003).
RN [9]
RP RECONSTITUTION OF THE ORC COMPLEX, AND DISASSEMBLY OF THE ORC COMPLEX.
RX PubMed=17716973; DOI=10.1074/jbc.m705905200;
RA Siddiqui K., Stillman B.;
RT "ATP-dependent assembly of the human origin recognition complex.";
RL J. Biol. Chem. 282:32370-32383(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203; THR-337; SER-340;
RP SER-417; SER-420 AND SER-478, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-326, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203; SER-273 AND SER-287, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP INTERACTION WITH LRWD1, AND PHOSPHORYLATION DURING MITOSIS.
RX PubMed=22645314; DOI=10.1128/mcb.00362-12;
RA Shen Z., Chakraborty A., Jain A., Giri S., Ha T., Prasanth K.V.,
RA Prasanth S.G.;
RT "Dynamic association of ORCA with prereplicative complex components
RT regulates DNA replication initiation.";
RL Mol. Cell. Biol. 32:3107-3120(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-273; SER-287 AND
RP SER-478, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP VARIANTS MGORS1 SER-89; GLN-105; GLY-127 AND GLN-720.
RX PubMed=21358633; DOI=10.1038/ng.776;
RA Bicknell L.S., Walker S., Klingseisen A., Stiff T., Leitch A.,
RA Kerzendorfer C., Martin C.A., Yeyati P., Al Sanna N., Bober M., Johnson D.,
RA Wise C., Jackson A.P., O'Driscoll M., Jeggo P.A.;
RT "Mutations in ORC1, encoding the largest subunit of the origin recognition
RT complex, cause microcephalic primordial dwarfism resembling Meier-Gorlin
RT syndrome.";
RL Nat. Genet. 43:350-355(2011).
RN [18]
RP VARIANT MGORS1 GLN-105.
RX PubMed=21358632; DOI=10.1038/ng.775;
RA Bicknell L.S., Bongers E.M., Leitch A., Brown S., Schoots J., Harley M.E.,
RA Aftimos S., Al-Aama J.Y., Bober M., Brown P.A., van Bokhoven H., Dean J.,
RA Edrees A.Y., Feingold M., Fryer A., Hoefsloot L.H., Kau N., Knoers N.V.,
RA Mackenzie J., Opitz J.M., Sarda P., Ross A., Temple I.K., Toutain A.,
RA Wise C.A., Wright M., Jackson A.P.;
RT "Mutations in the pre-replication complex cause Meier-Gorlin syndrome.";
RL Nat. Genet. 43:356-359(2011).
RN [19]
RP VARIANTS MGORS1 GLN-105 AND TRP-666.
RX PubMed=21358631; DOI=10.1038/ng.777;
RA Guernsey D.L., Matsuoka M., Jiang H., Evans S., Macgillivray C.,
RA Nightingale M., Perry S., Ferguson M., LeBlanc M., Paquette J., Patry L.,
RA Rideout A.L., Thomas A., Orr A., McMaster C.R., Michaud J.L., Deal C.,
RA Langlois S., Superneau D.W., Parkash S., Ludman M., Skidmore D.L.,
RA Samuels M.E.;
RT "Mutations in origin recognition complex gene ORC4 cause Meier-Gorlin
RT syndrome.";
RL Nat. Genet. 43:360-364(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.39 ANGSTROMS) OF 471-861 IN COMPLEX WITH ATP AND
RP MAGNESIUM, AND MUTAGENESIS OF ASP-620 AND ARG-720.
RX PubMed=28112645; DOI=10.7554/elife.20818;
RA Tocilj A., On K.F., Yuan Z., Sun J., Elkayam E., Li H., Stillman B.,
RA Joshua-Tor L.;
RT "Structure of the active form of human origin recognition complex and its
RT ATPase motor module.";
RL Elife 6:E20818-E20818(2017).
CC -!- FUNCTION: Component of the origin recognition complex (ORC) that binds
CC origins of replication. DNA-binding is ATP-dependent. The DNA sequences
CC that define origins of replication have not been identified yet. ORC is
CC required to assemble the pre-replication complex necessary to initiate
CC DNA replication.
CC -!- SUBUNIT: Component of ORC, a complex composed of at least 6 subunits:
CC ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle
CC dependent manner. It is sequentially assembled at the exit from
CC anaphase of mitosis and disassembled as cells enter S phase. Interacts
CC with CDC6 and KAT7/HBO1. Interacts with LRWD1 predominantly during the
CC G1 phase and with less affinity during mitosis, when phosphorylated.
CC {ECO:0000269|PubMed:10438470, ECO:0000269|PubMed:12909626,
CC ECO:0000269|PubMed:22645314, ECO:0000269|PubMed:9566895}.
CC -!- INTERACTION:
CC Q13415; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-374847, EBI-5916454;
CC Q13415; Q13416: ORC2; NbExp=14; IntAct=EBI-374847, EBI-374957;
CC Q13415; Q9UBD5: ORC3; NbExp=16; IntAct=EBI-374847, EBI-374916;
CC Q13415; O43913: ORC5; NbExp=11; IntAct=EBI-374847, EBI-374928;
CC Q13415; Q13309: SKP2; NbExp=2; IntAct=EBI-374847, EBI-456291;
CC Q13415; Q15554: TERF2; NbExp=2; IntAct=EBI-374847, EBI-706637;
CC Q13415; P03211: EBNA1; Xeno; NbExp=2; IntAct=EBI-374847, EBI-996522;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: Expression is cell-cycle regulated, it starts to
CC accumulate in mid-G1 phase, reaches a peak at the G1/S boundary, and
CC decreases to a basal level in S phase (at protein level).
CC {ECO:0000269|PubMed:12909627}.
CC -!- DOMAIN: The BAH domain mediates binding to dimethylated histone H4
CC 'Lys-20' (H4K20me2), which is enriched at replication origins.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000269|PubMed:22645314}.
CC -!- DISEASE: Meier-Gorlin syndrome 1 (MGORS1) [MIM:224690]: A syndrome
CC characterized by bilateral microtia, aplasia/hypoplasia of the
CC patellae, and severe intrauterine and postnatal growth retardation with
CC short stature and poor weight gain. Additional clinical findings
CC include anomalies of cranial sutures, microcephaly, apparently low-set
CC and simple ears, microstomia, full lips, highly arched or cleft palate,
CC micrognathia, genitourinary tract anomalies, and various skeletal
CC anomalies. While almost all cases have primordial dwarfism with
CC substantial prenatal and postnatal growth retardation, not all cases
CC have microcephaly, and microtia and absent/hypoplastic patella are
CC absent in some. Despite the presence of microcephaly, intellect is
CC usually normal. {ECO:0000269|PubMed:21358631,
CC ECO:0000269|PubMed:21358632, ECO:0000269|PubMed:21358633}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ORC1 family. {ECO:0000305}.
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DR EMBL; U40152; AAC50325.1; -; mRNA.
DR EMBL; U43416; AAA86260.1; -; mRNA.
DR EMBL; AL513218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06783.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06784.1; -; Genomic_DNA.
DR CCDS; CCDS566.1; -.
DR PIR; G02329; G02329.
DR RefSeq; NP_001177747.1; NM_001190818.1.
DR RefSeq; NP_001177748.1; NM_001190819.1.
DR RefSeq; NP_004144.2; NM_004153.3.
DR PDB; 5UJ7; X-ray; 3.39 A; A/B=471-861.
DR PDB; 5UJM; EM; 18.00 A; A=471-861.
DR PDB; 6P3W; X-ray; 2.54 A; E/F=233-239.
DR PDB; 7CTF; EM; 4.80 A; A=1-861.
DR PDB; 7CTG; EM; 5.00 A; A=1-861.
DR PDB; 7JPO; EM; 3.20 A; A=471-861.
DR PDB; 7JPP; EM; 3.70 A; A=471-861.
DR PDB; 7JPR; EM; 4.00 A; A=471-861.
DR PDB; 7JPS; EM; 4.40 A; A=471-861.
DR PDBsum; 5UJ7; -.
DR PDBsum; 5UJM; -.
DR PDBsum; 6P3W; -.
DR PDBsum; 7CTF; -.
DR PDBsum; 7CTG; -.
DR PDBsum; 7JPO; -.
DR PDBsum; 7JPP; -.
DR PDBsum; 7JPR; -.
DR PDBsum; 7JPS; -.
DR AlphaFoldDB; Q13415; -.
DR SMR; Q13415; -.
DR BioGRID; 111040; 81.
DR ComplexPortal; CPX-1880; Nuclear origin of replication recognition complex.
DR CORUM; Q13415; -.
DR DIP; DIP-29688N; -.
DR IntAct; Q13415; 50.
DR MINT; Q13415; -.
DR STRING; 9606.ENSP00000360623; -.
DR iPTMnet; Q13415; -.
DR PhosphoSitePlus; Q13415; -.
DR BioMuta; ORC1; -.
DR DMDM; 76803807; -.
DR EPD; Q13415; -.
DR jPOST; Q13415; -.
DR MassIVE; Q13415; -.
DR MaxQB; Q13415; -.
DR PaxDb; Q13415; -.
DR PeptideAtlas; Q13415; -.
DR PRIDE; Q13415; -.
DR ProteomicsDB; 59394; -.
DR Antibodypedia; 19104; 221 antibodies from 32 providers.
DR DNASU; 4998; -.
DR Ensembl; ENST00000371566.1; ENSP00000360621.1; ENSG00000085840.13.
DR Ensembl; ENST00000371568.8; ENSP00000360623.3; ENSG00000085840.13.
DR GeneID; 4998; -.
DR KEGG; hsa:4998; -.
DR MANE-Select; ENST00000371568.8; ENSP00000360623.3; NM_004153.4; NP_004144.2.
DR UCSC; uc001ctt.4; human.
DR CTD; 4998; -.
DR DisGeNET; 4998; -.
DR GeneCards; ORC1; -.
DR HGNC; HGNC:8487; ORC1.
DR HPA; ENSG00000085840; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; ORC1; -.
DR MIM; 224690; phenotype.
DR MIM; 601902; gene.
DR neXtProt; NX_Q13415; -.
DR OpenTargets; ENSG00000085840; -.
DR Orphanet; 2554; Ear-patella-short stature syndrome.
DR PharmGKB; PA32808; -.
DR VEuPathDB; HostDB:ENSG00000085840; -.
DR eggNOG; KOG1514; Eukaryota.
DR GeneTree; ENSGT00530000063498; -.
DR HOGENOM; CLU_012774_0_1_1; -.
DR InParanoid; Q13415; -.
DR OMA; ICEFSCQ; -.
DR OrthoDB; 935804at2759; -.
DR PhylomeDB; Q13415; -.
DR TreeFam; TF313743; -.
DR BRENDA; 3.6.4.B8; 2681.
DR PathwayCommons; Q13415; -.
DR Reactome; R-HSA-113507; E2F-enabled inhibition of pre-replication complex formation.
DR Reactome; R-HSA-176187; Activation of ATR in response to replication stress.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-68689; CDC6 association with the ORC:origin complex.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR SignaLink; Q13415; -.
DR SIGNOR; Q13415; -.
DR BioGRID-ORCS; 4998; 700 hits in 1088 CRISPR screens.
DR GeneWiki; ORC1; -.
DR GenomeRNAi; 4998; -.
DR Pharos; Q13415; Tbio.
DR PRO; PR:Q13415; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13415; protein.
DR Bgee; ENSG00000085840; Expressed in ventricular zone and 92 other tissues.
DR Genevisible; Q13415; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005664; C:nuclear origin of replication recognition complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0000808; C:origin recognition complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR CDD; cd08768; Cdc6_C; 1.
DR DisProt; DP02072; -.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR015163; Cdc6_C.
DR InterPro; IPR020793; ORC1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10763:SF23; PTHR10763:SF23; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17872; AAA_lid_10; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF09079; Cdc6_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM01074; Cdc6_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51038; BAH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Disease variant; DNA replication;
KW DNA-binding; Dwarfism; Magnesium; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..861
FT /note="Origin recognition complex subunit 1"
FT /id="PRO_0000127067"
FT DOMAIN 45..171
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 183..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..861
FT /note="Necessary and sufficient for ORC complex assembly"
FT COMPBIAS 271..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28112645,
FT ECO:0007744|PDB:5UJ7"
FT BINDING 534..542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28112645,
FT ECO:0007744|PDB:5UJ7, ECO:0007744|PDB:5UJM"
FT BINDING 620
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:28112645,
FT ECO:0007744|PDB:5UJ7, ECO:0007744|PDB:5UJM"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28112645,
FT ECO:0007744|PDB:5UJ7"
FT BINDING 621
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:28112645,
FT ECO:0007744|PDB:5UJ7, ECO:0007744|PDB:5UJM"
FT BINDING 654
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28112645,
FT ECO:0007744|PDB:5UJ7"
FT BINDING 720
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:28112645,
FT ECO:0007744|PDB:5UJ7"
FT SITE 94
FT /note="Histone H4K20me2 binding"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N2"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N2"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1N2"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 19
FT /note="R -> S (in dbSNP:rs3087473)"
FT /id="VAR_014507"
FT VARIANT 89
FT /note="F -> S (in MGORS1; dbSNP:rs387906827)"
FT /evidence="ECO:0000269|PubMed:21358633"
FT /id="VAR_065481"
FT VARIANT 105
FT /note="R -> Q (in MGORS1; dbSNP:rs143141689)"
FT /evidence="ECO:0000269|PubMed:21358631,
FT ECO:0000269|PubMed:21358632, ECO:0000269|PubMed:21358633"
FT /id="VAR_065482"
FT VARIANT 127
FT /note="E -> G (in MGORS1; dbSNP:rs387906826)"
FT /evidence="ECO:0000269|PubMed:21358633"
FT /id="VAR_065483"
FT VARIANT 180
FT /note="Q -> H (in dbSNP:rs3087482)"
FT /id="VAR_014508"
FT VARIANT 190
FT /note="V -> M (in dbSNP:rs3087477)"
FT /id="VAR_014509"
FT VARIANT 372
FT /note="A -> V (in dbSNP:rs3087476)"
FT /id="VAR_014510"
FT VARIANT 441
FT /note="R -> M (in dbSNP:rs3087472)"
FT /id="VAR_014511"
FT VARIANT 456
FT /note="K -> E (in dbSNP:rs3087470)"
FT /id="VAR_014512"
FT VARIANT 466
FT /note="T -> M (in dbSNP:rs3087481)"
FT /id="VAR_014513"
FT VARIANT 469
FT /note="C -> Y (in dbSNP:rs3087483)"
FT /id="VAR_014514"
FT VARIANT 666
FT /note="R -> W (in MGORS1; dbSNP:rs201253919)"
FT /evidence="ECO:0000269|PubMed:21358631"
FT /id="VAR_065484"
FT VARIANT 720
FT /note="R -> Q (in MGORS1; dbSNP:rs387906828)"
FT /evidence="ECO:0000269|PubMed:21358633"
FT /id="VAR_065485"
FT VARIANT 816
FT /note="M -> T (in dbSNP:rs34521609)"
FT /id="VAR_050426"
FT MUTAGEN 620
FT /note="D->A: Abolished ATPase activity."
FT /evidence="ECO:0000269|PubMed:28112645"
FT MUTAGEN 720
FT /note="R->Q: Abolished ATPase activity."
FT /evidence="ECO:0000269|PubMed:28112645"
FT CONFLICT 582
FT /note="Q -> H (in Ref. 1; AAC50325)"
FT /evidence="ECO:0000305"
FT HELIX 488..495
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 508..522
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 528..533
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 540..556
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 565..570
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 578..587
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 594..604
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 616..620
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 622..625
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 631..638
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 639..642
FT /evidence="ECO:0007829|PDB:7JPO"
FT TURN 643..645
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 658..660
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 674..677
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 683..693
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 702..715
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 719..735
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 748..759
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 763..768
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 772..788
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 795..809
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 816..828
FT /evidence="ECO:0007829|PDB:7JPO"
FT STRAND 831..833
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 837..842
FT /evidence="ECO:0007829|PDB:5UJ7"
FT STRAND 844..849
FT /evidence="ECO:0007829|PDB:7JPO"
FT HELIX 851..858
FT /evidence="ECO:0007829|PDB:7JPO"
SQ SEQUENCE 861 AA; 97350 MW; 5C594553F7F808E2 CRC64;
MAHYPTRLKT RKTYSWVGRP LLDRKLHYQT YREMCVKTEG CSTEIHIQIG QFVLIEGDDD
ENPYVAKLLE LFEDDSDPPP KKRARVQWFV RFCEVPACKR HLLGRKPGAQ EIFWYDYPAC
DSNINAETII GLVRVIPLAP KDVVPTNLKN EKTLFVKLSW NEKKFRPLSS ELFAELNKPQ
ESAAKCQKPV RAKSKSAESP SWTPAEHVAK RIESRHSASK SRQTPTHPLT PRARKRLELG
NLGNPQMSQQ TSCASLDSPG RIKRKVAFSE ITSPSKRSQP DKLQTLSPAL KAPEKTRETG
LSYTEDDKKA SPEHRIILRT RIAASKTIDI REERTLTPIS GGQRSSVVPS VILKPENIKK
RDAKEAKAQN EATSTPHRIR RKSSVLTMNR IRQQLRFLGN SKSDQEEKEI LPAAEISDSS
SDEEEASTPP LPRRAPRTVS RNLRSSLKSS LHTLTKVPKK SLKPRTPRCA APQIRSRSLA
AQEPASVLEE ARLRLHVSAV PESLPCREQE FQDIYNFVES KLLDHTGGCM YISGVPGTGK
TATVHEVIRC LQQAAQANDV PPFQYIEVNG MKLTEPHQVY VQILQKLTGQ KATANHAAEL
LAKQFCTRGS PQETTVLLVD ELDLLWTHKQ DIMYNLFDWP THKEARLVVL AIANTMDLPE
RIMMNRVSSR LGLTRMCFQP YTYSQLQQIL RSRLKHLKAF EDDAIQLVAR KVAALSGDAR
RCLDICRRAT EICEFSQQKP DSPGLVTIAH SMEAVDEMFS SSYITAIKNS SVLEQSFLRA
ILAEFRRSGL EEATFQQIYS QHVALCRMEG LPYPTMSETM AVCSHLGSCR LLLVEPSRND
LLLRVRLNVS QDDVLYALKD E
