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Q13415

- ORC1_HUMAN

UniProt

Q13415 - ORC1_HUMAN

Protein

Origin recognition complex subunit 1

Gene

ORC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (27 Sep 2005)
      Previous versions | rss
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    Functioni

    Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei93 – 931Histone H4K20me2By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi534 – 5418ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: InterPro
    3. DNA binding Source: ProtInc
    4. nucleoside-triphosphatase activity Source: InterPro
    5. protein binding Source: IntAct

    GO - Biological processi

    1. DNA replication Source: Reactome
    2. DNA replication initiation Source: ProtInc
    3. G1/S transition of mitotic cell cycle Source: Reactome
    4. mitotic cell cycle Source: Reactome
    5. regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1095. Activation of the pre-replicative complex.
    REACT_1156. Orc1 removal from chromatin.
    REACT_1181. Association of licensing factors with the pre-replicative complex.
    REACT_1321. E2F-enabled inhibition of pre-replication complex formation.
    REACT_1707. CDC6 association with the ORC:origin complex.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_207. Removal of licensing factors from origins.
    REACT_2243. Assembly of the pre-replicative complex.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_567. Assembly of the ORC complex at the origin of replication.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_683. G1/S-Specific Transcription.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Origin recognition complex subunit 1
    Alternative name(s):
    Replication control protein 1
    Gene namesi
    Name:ORC1
    Synonyms:ORC1L, PARC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8487. ORC1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nuclear origin of replication recognition complex Source: UniProtKB
    4. nucleolus Source: HPA
    5. nucleoplasm Source: Reactome
    6. nucleus Source: HPA
    7. origin recognition complex Source: UniProtKB
    8. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Meier-Gorlin syndrome 1 (MGORS1) [MIM:224690]: A syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891F → S in MGORS1. 1 Publication
    VAR_065481
    Natural varianti105 – 1051R → Q in MGORS1. 3 Publications
    VAR_065482
    Natural varianti127 – 1271E → G in MGORS1. 1 Publication
    VAR_065483
    Natural varianti666 – 6661R → W in MGORS1. 1 Publication
    Corresponds to variant rs201253919 [ dbSNP | Ensembl ].
    VAR_065484
    Natural varianti720 – 7201R → Q in MGORS1. 1 Publication
    VAR_065485

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi224690. phenotype.
    Orphaneti2554. Ear-patella-short stature syndrome.
    PharmGKBiPA32808.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 861861Origin recognition complex subunit 1PRO_0000127067Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei203 – 2031Phosphothreonine3 Publications
    Modified residuei273 – 2731Phosphoserine3 Publications
    Modified residuei287 – 2871Phosphoserine2 Publications
    Modified residuei326 – 3261N6-acetyllysine1 Publication
    Modified residuei337 – 3371Phosphothreonine2 Publications
    Modified residuei340 – 3401Phosphoserine2 Publications
    Modified residuei417 – 4171Phosphoserine2 Publications
    Modified residuei420 – 4201Phosphoserine2 Publications
    Modified residuei478 – 4781Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated during mitosis.4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13415.
    PaxDbiQ13415.
    PRIDEiQ13415.

    PTM databases

    PhosphoSiteiQ13415.

    Expressioni

    Developmental stagei

    Expression is cell-cycle regulated, it starts to accumulate in mid-G1 phase, reaches a peak at the G1/S boundary, and decreases to a basal level in S phase (at protein level).1 Publication

    Gene expression databases

    BgeeiQ13415.
    CleanExiHS_ORC1L.
    GenevestigatoriQ13415.

    Organism-specific databases

    HPAiHPA027450.

    Interactioni

    Subunit structurei

    Component of ORC, a complex composed of at least 6 subunits: ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. ORC is regulated in a cell-cycle dependent manner. It is sequentially assembled at the exit from anaphase of mitosis and disassembled as cells enter S phase. Interacts with CDC6 and KAT7/HBO1. Interacts with LRWD1 predominantly during the G1 phase and with less affinity during mitosis, when phosphorylated.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EBNA1P032112EBI-374847,EBI-996522From a different organism.
    ORC2Q134166EBI-374847,EBI-374957
    ORC3Q9UBD512EBI-374847,EBI-374916
    ORC5O439135EBI-374847,EBI-374928
    SKP2Q133092EBI-374847,EBI-456291
    TERF2Q155542EBI-374847,EBI-706637

    Protein-protein interaction databases

    BioGridi111040. 25 interactions.
    DIPiDIP-29688N.
    IntActiQ13415. 19 interactions.
    MINTiMINT-1201992.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13415.
    SMRiQ13415. Positions 12-168, 500-732.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 171127BAHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni501 – 861361Necessary and sufficient for ORC complex assemblyAdd
    BLAST

    Domaini

    The BAH domain mediates binding to dimethylated histone H4 'Lys-20' (H4K20me2), which is enriched at replication origins.By similarity

    Sequence similaritiesi

    Belongs to the ORC1 family.Curated
    Contains 1 BAH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1474.
    HOGENOMiHOG000231132.
    HOVERGENiHBG007873.
    InParanoidiQ13415.
    KOiK02603.
    OMAiIYSQHVA.
    OrthoDBiEOG7QG44J.
    PhylomeDBiQ13415.
    TreeFamiTF313743.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR001025. BAH_dom.
    IPR015163. Cdc6_C_dom.
    IPR027417. P-loop_NTPase.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    PF01426. BAH. 1 hit.
    PF09079. Cdc6_C. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00439. BAH. 1 hit.
    SM01074. Cdc6_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS51038. BAH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q13415-1 [UniParc]FASTAAdd to Basket

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    MAHYPTRLKT RKTYSWVGRP LLDRKLHYQT YREMCVKTEG CSTEIHIQIG    50
    QFVLIEGDDD ENPYVAKLLE LFEDDSDPPP KKRARVQWFV RFCEVPACKR 100
    HLLGRKPGAQ EIFWYDYPAC DSNINAETII GLVRVIPLAP KDVVPTNLKN 150
    EKTLFVKLSW NEKKFRPLSS ELFAELNKPQ ESAAKCQKPV RAKSKSAESP 200
    SWTPAEHVAK RIESRHSASK SRQTPTHPLT PRARKRLELG NLGNPQMSQQ 250
    TSCASLDSPG RIKRKVAFSE ITSPSKRSQP DKLQTLSPAL KAPEKTRETG 300
    LSYTEDDKKA SPEHRIILRT RIAASKTIDI REERTLTPIS GGQRSSVVPS 350
    VILKPENIKK RDAKEAKAQN EATSTPHRIR RKSSVLTMNR IRQQLRFLGN 400
    SKSDQEEKEI LPAAEISDSS SDEEEASTPP LPRRAPRTVS RNLRSSLKSS 450
    LHTLTKVPKK SLKPRTPRCA APQIRSRSLA AQEPASVLEE ARLRLHVSAV 500
    PESLPCREQE FQDIYNFVES KLLDHTGGCM YISGVPGTGK TATVHEVIRC 550
    LQQAAQANDV PPFQYIEVNG MKLTEPHQVY VQILQKLTGQ KATANHAAEL 600
    LAKQFCTRGS PQETTVLLVD ELDLLWTHKQ DIMYNLFDWP THKEARLVVL 650
    AIANTMDLPE RIMMNRVSSR LGLTRMCFQP YTYSQLQQIL RSRLKHLKAF 700
    EDDAIQLVAR KVAALSGDAR RCLDICRRAT EICEFSQQKP DSPGLVTIAH 750
    SMEAVDEMFS SSYITAIKNS SVLEQSFLRA ILAEFRRSGL EEATFQQIYS 800
    QHVALCRMEG LPYPTMSETM AVCSHLGSCR LLLVEPSRND LLLRVRLNVS 850
    QDDVLYALKD E 861
    Length:861
    Mass (Da):97,350
    Last modified:September 27, 2005 - v2
    Checksum:i5C594553F7F808E2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti582 – 5821Q → H in AAC50325. (PubMed:7502077)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191R → S.
    Corresponds to variant rs3087473 [ dbSNP | Ensembl ].
    VAR_014507
    Natural varianti89 – 891F → S in MGORS1. 1 Publication
    VAR_065481
    Natural varianti105 – 1051R → Q in MGORS1. 3 Publications
    VAR_065482
    Natural varianti127 – 1271E → G in MGORS1. 1 Publication
    VAR_065483
    Natural varianti180 – 1801Q → H.
    Corresponds to variant rs3087482 [ dbSNP | Ensembl ].
    VAR_014508
    Natural varianti190 – 1901V → M.
    Corresponds to variant rs3087477 [ dbSNP | Ensembl ].
    VAR_014509
    Natural varianti372 – 3721A → V.
    Corresponds to variant rs3087476 [ dbSNP | Ensembl ].
    VAR_014510
    Natural varianti441 – 4411R → M.
    Corresponds to variant rs3087472 [ dbSNP | Ensembl ].
    VAR_014511
    Natural varianti456 – 4561K → E.
    Corresponds to variant rs3087470 [ dbSNP | Ensembl ].
    VAR_014512
    Natural varianti466 – 4661T → M.
    Corresponds to variant rs3087481 [ dbSNP | Ensembl ].
    VAR_014513
    Natural varianti469 – 4691C → Y.
    Corresponds to variant rs3087483 [ dbSNP | Ensembl ].
    VAR_014514
    Natural varianti666 – 6661R → W in MGORS1. 1 Publication
    Corresponds to variant rs201253919 [ dbSNP | Ensembl ].
    VAR_065484
    Natural varianti720 – 7201R → Q in MGORS1. 1 Publication
    VAR_065485
    Natural varianti816 – 8161M → T.
    Corresponds to variant rs34521609 [ dbSNP | Ensembl ].
    VAR_050426

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40152 mRNA. Translation: AAC50325.1.
    U43416 mRNA. Translation: AAA86260.1.
    AL513218 Genomic DNA. Translation: CAI12288.1.
    CH471059 Genomic DNA. Translation: EAX06783.1.
    CH471059 Genomic DNA. Translation: EAX06784.1.
    CCDSiCCDS566.1.
    PIRiG02329.
    RefSeqiNP_001177747.1. NM_001190818.1.
    NP_001177748.1. NM_001190819.1.
    NP_004144.2. NM_004153.3.
    UniGeneiHs.17908.

    Genome annotation databases

    EnsembliENST00000371566; ENSP00000360621; ENSG00000085840.
    ENST00000371568; ENSP00000360623; ENSG00000085840.
    GeneIDi4998.
    KEGGihsa:4998.
    UCSCiuc001ctt.3. human.

    Polymorphism databases

    DMDMi76803807.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40152 mRNA. Translation: AAC50325.1 .
    U43416 mRNA. Translation: AAA86260.1 .
    AL513218 Genomic DNA. Translation: CAI12288.1 .
    CH471059 Genomic DNA. Translation: EAX06783.1 .
    CH471059 Genomic DNA. Translation: EAX06784.1 .
    CCDSi CCDS566.1.
    PIRi G02329.
    RefSeqi NP_001177747.1. NM_001190818.1.
    NP_001177748.1. NM_001190819.1.
    NP_004144.2. NM_004153.3.
    UniGenei Hs.17908.

    3D structure databases

    ProteinModelPortali Q13415.
    SMRi Q13415. Positions 12-168, 500-732.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111040. 25 interactions.
    DIPi DIP-29688N.
    IntActi Q13415. 19 interactions.
    MINTi MINT-1201992.

    PTM databases

    PhosphoSitei Q13415.

    Polymorphism databases

    DMDMi 76803807.

    Proteomic databases

    MaxQBi Q13415.
    PaxDbi Q13415.
    PRIDEi Q13415.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371566 ; ENSP00000360621 ; ENSG00000085840 .
    ENST00000371568 ; ENSP00000360623 ; ENSG00000085840 .
    GeneIDi 4998.
    KEGGi hsa:4998.
    UCSCi uc001ctt.3. human.

    Organism-specific databases

    CTDi 4998.
    GeneCardsi GC01M052839.
    HGNCi HGNC:8487. ORC1.
    HPAi HPA027450.
    MIMi 224690. phenotype.
    601902. gene.
    neXtProti NX_Q13415.
    Orphaneti 2554. Ear-patella-short stature syndrome.
    PharmGKBi PA32808.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1474.
    HOGENOMi HOG000231132.
    HOVERGENi HBG007873.
    InParanoidi Q13415.
    KOi K02603.
    OMAi IYSQHVA.
    OrthoDBi EOG7QG44J.
    PhylomeDBi Q13415.
    TreeFami TF313743.

    Enzyme and pathway databases

    Reactomei REACT_1095. Activation of the pre-replicative complex.
    REACT_1156. Orc1 removal from chromatin.
    REACT_1181. Association of licensing factors with the pre-replicative complex.
    REACT_1321. E2F-enabled inhibition of pre-replication complex formation.
    REACT_1707. CDC6 association with the ORC:origin complex.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_207. Removal of licensing factors from origins.
    REACT_2243. Assembly of the pre-replicative complex.
    REACT_471. E2F mediated regulation of DNA replication.
    REACT_567. Assembly of the ORC complex at the origin of replication.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_683. G1/S-Specific Transcription.

    Miscellaneous databases

    GeneWikii ORC1.
    GenomeRNAii 4998.
    NextBioi 19240.
    PROi Q13415.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q13415.
    CleanExi HS_ORC1L.
    Genevestigatori Q13415.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR001025. BAH_dom.
    IPR015163. Cdc6_C_dom.
    IPR027417. P-loop_NTPase.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    PF01426. BAH. 1 hit.
    PF09079. Cdc6_C. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM00439. BAH. 1 hit.
    SM01074. Cdc6_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS51038. BAH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Conserved initiator proteins in eukaryotes."
      Gavin K.A., Hidaka M., Stillman B.D.
      Science 270:1667-1671(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Wolf D.A., McKeon F.
      Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively eliminated from the nucleus at the onset of S phase."
      Saha P., Chen J., Thome K.C., Lawlis S.J., Hou Z.H., Hendricks M., Parvin J.D., Dutta A.
      Mol. Cell. Biol. 18:2758-2767(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC6.
    6. "Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein."
      Iizuka M., Stillman B.
      J. Biol. Chem. 274:23027-23034(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KAT7.
    7. "The ORC1 cycle in human cells: I. cell cycle-regulated oscillation of human ORC1."
      Tatsumi Y., Ohta S., Kimura H., Tsurimoto T., Obuse C.
      J. Biol. Chem. 278:41528-41534(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    8. "The ORC1 cycle in human cells: II. Dynamic changes in the human ORC complex during the cell cycle."
      Ohta S., Tatsumi Y., Fujita M., Tsurimoto T., Obuse C.
      J. Biol. Chem. 278:41535-41540(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE ORC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, ASSEMBLY OF THE ORC COMPLEX.
    9. "ATP-dependent assembly of the human origin recognition complex."
      Siddiqui K., Stillman B.
      J. Biol. Chem. 282:32370-32383(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECONSTITUTION OF THE ORC COMPLEX, DISASSEMBLY OF THE ORC COMPLEX.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203; THR-337; SER-340; SER-417; SER-420 AND SER-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203; SER-273 AND SER-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Dynamic association of ORCA with prereplicative complex components regulates DNA replication initiation."
      Shen Z., Chakraborty A., Jain A., Giri S., Ha T., Prasanth K.V., Prasanth S.G.
      Mol. Cell. Biol. 32:3107-3120(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRWD1, PHOSPHORYLATION DURING MITOSIS.
    16. "Mutations in ORC1, encoding the largest subunit of the origin recognition complex, cause microcephalic primordial dwarfism resembling Meier-Gorlin syndrome."
      Bicknell L.S., Walker S., Klingseisen A., Stiff T., Leitch A., Kerzendorfer C., Martin C.A., Yeyati P., Al Sanna N., Bober M., Johnson D., Wise C., Jackson A.P., O'Driscoll M., Jeggo P.A.
      Nat. Genet. 43:350-355(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MGORS1 SER-89; GLN-105; GLY-127 AND GLN-720.
    17. Cited for: VARIANT MGORS1 GLN-105.
    18. Cited for: VARIANTS MGORS1 GLN-105 AND TRP-666.

    Entry informationi

    Entry nameiORC1_HUMAN
    AccessioniPrimary (citable) accession number: Q13415
    Secondary accession number(s): D3DQ34, Q13471, Q5T0F5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3