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Q13416

- ORC2_HUMAN

UniProt

Q13416 - ORC2_HUMAN

Protein

Origin recognition complex subunit 2

Gene

ORC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      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 specific 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. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K20me3 and H4K27me3. Stabilizes LRWD1, by protecting it from ubiquitin-mediated proteasomal degradation. Also stabilizes ORC3.2 Publications

    GO - Molecular functioni

    1. DNA replication origin binding Source: ProtInc
    2. protein binding Source: UniProtKB

    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. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Biological processi

    DNA replication

    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_567. Assembly of the ORC complex at the origin of replication.
    REACT_6769. Activation of ATR in response to replication stress.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Origin recognition complex subunit 2
    Gene namesi
    Name:ORC2
    Synonyms:ORC2L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:8488. ORC2.

    Subcellular locationi

    GO - Cellular componenti

    1. condensed chromosome inner kinetochore Source: Ensembl
    2. heterochromatin Source: Ensembl
    3. membrane Source: UniProtKB
    4. nuclear origin of replication recognition complex Source: UniProtKB
    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

    Organism-specific databases

    PharmGKBiPA32809.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 577577Origin recognition complex subunit 2PRO_0000127075Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei116 – 1161Phosphothreonine2 Publications
    Modified residuei122 – 1221Phosphoserine1 Publication
    Modified residuei138 – 1381Phosphoserine1 Publication
    Modified residuei226 – 2261Phosphothreonine1 Publication
    Modified residuei280 – 2801Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13416.
    PaxDbiQ13416.
    PeptideAtlasiQ13416.
    PRIDEiQ13416.

    PTM databases

    PhosphoSiteiQ13416.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13416.
    BgeeiQ13416.
    CleanExiHS_ORC2L.
    GenevestigatoriQ13416.

    Organism-specific databases

    HPAiCAB003693.
    HPA034976.

    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 DBF4 By similarity. Interacts with MCM10. Interacts with LRWD1 throughout the cell cycle; this interaction, wich occurs only with non-ubiquitinated form of LRWD1, prevents LRWD1 ubiquitination and hence stabilizes the protein.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC5LQ994592EBI-374957,EBI-374880
    EBNA1P032116EBI-374957,EBI-996522From a different organism.
    MCM10Q7L5905EBI-374957,EBI-374912
    MCM3P252052EBI-374957,EBI-355153
    ORC1Q134156EBI-374957,EBI-374847
    ORC4O439296EBI-374957,EBI-374889
    ORC5O439137EBI-374957,EBI-374928
    TERF2Q155543EBI-374957,EBI-706637

    Protein-protein interaction databases

    BioGridi111041. 39 interactions.
    DIPiDIP-29689N.
    IntActiQ13416. 25 interactions.
    MINTiMINT-1201828.
    STRINGi9606.ENSP00000234296.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13416.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1 – 100100Involved in LRWD1-bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ORC2 family.Curated

    Phylogenomic databases

    eggNOGiCOG5575.
    HOGENOMiHOG000045588.
    HOVERGENiHBG007874.
    InParanoidiQ13416.
    KOiK02604.
    OMAiSQMLRGE.
    OrthoDBiEOG7NPFT1.
    PhylomeDBiQ13416.
    TreeFamiTF101092.

    Family and domain databases

    InterProiIPR007220. ORC2.
    [Graphical view]
    PANTHERiPTHR14052. PTHR14052. 1 hit.
    PfamiPF04084. ORC2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q13416-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKPELKEDK MLEVHFVGDD DVLNHILDRE GGAKLKKERA QLLVNPKKII    50
    KKPEYDLEED DQEVLKDQNY VEIMGRDVQE SLKNGSATGG GNKVYSFQNR 100
    KHSEKMAKLA SELAKTPQKS VSFSLKNDPE ITINVPQSSK GHSASDKVQP 150
    KNNDKSEFLS TAPRSLRKRL IVPRSHSDSE SEYSASNSED DEGVAQEHEE 200
    DTNAVIFSQK IQAQNRVVSA PVGKETPSKR MKRDKTSDLV EEYFEAHSSS 250
    KVLTSDRTLQ KLKRAKLDQQ TLRNLLSKVS PSFSAELKQL NQQYEKLFHK 300
    WMLQLHLGFN IVLYGLGSKR DLLERFRTTM LQDSIHVVIN GFFPGISVKS 350
    VLNSITEEVL DHMGTFRSIL DQLDWIVNKF KEDSSLELFL LIHNLDSQML 400
    RGEKSQQIIG QLSSLHNIYL IASIDHLNAP LMWDHAKQSL FNWLWYETTT 450
    YSPYTEETSY ENSLLVKQSG SLPLSSLTHV LRSLTPNARG IFRLLIKYQL 500
    DNQDNPSYIG LSFQDFYQQC REAFLVNSDL TLRAQLTEFR DHKLIRTKKG 550
    TDGVEYLLIP VDNGTLTDFL EKEEEEA 577
    Length:577
    Mass (Da):65,972
    Last modified:May 30, 2000 - v2
    Checksum:iDF3F9C2CF147DA5F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti131 – 1311I → V in AAB33970. (PubMed:8808289)Curated
    Sequence conflicti236 – 2361T → L in AAB33970. (PubMed:8808289)Curated
    Sequence conflicti392 – 3921I → M in AAB33970. (PubMed:8808289)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti106 – 1061M → K.1 Publication
    Corresponds to variant rs2307361 [ dbSNP | Ensembl ].
    VAR_014515
    Natural varianti521 – 5211R → Q.1 Publication
    Corresponds to variant rs16835624 [ dbSNP | Ensembl ].
    VAR_021276

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40268 mRNA. Translation: AAC50326.2.
    U27459 mRNA. Translation: AAB33970.1.
    AY652588 Genomic DNA. Translation: AAT46690.1.
    AC005037 Genomic DNA. Translation: AAY14725.1.
    CH471063 Genomic DNA. Translation: EAW70228.1.
    BC014834 mRNA. Translation: AAH14834.1.
    CCDSiCCDS2334.1.
    RefSeqiNP_006181.1. NM_006190.4.
    XP_006712618.1. XM_006712555.1.
    UniGeneiHs.444870.

    Genome annotation databases

    EnsembliENST00000234296; ENSP00000234296; ENSG00000115942.
    GeneIDi4999.
    KEGGihsa:4999.
    UCSCiuc002uwr.3. human.

    Polymorphism databases

    DMDMi8488999.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40268 mRNA. Translation: AAC50326.2 .
    U27459 mRNA. Translation: AAB33970.1 .
    AY652588 Genomic DNA. Translation: AAT46690.1 .
    AC005037 Genomic DNA. Translation: AAY14725.1 .
    CH471063 Genomic DNA. Translation: EAW70228.1 .
    BC014834 mRNA. Translation: AAH14834.1 .
    CCDSi CCDS2334.1.
    RefSeqi NP_006181.1. NM_006190.4.
    XP_006712618.1. XM_006712555.1.
    UniGenei Hs.444870.

    3D structure databases

    ProteinModelPortali Q13416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111041. 39 interactions.
    DIPi DIP-29689N.
    IntActi Q13416. 25 interactions.
    MINTi MINT-1201828.
    STRINGi 9606.ENSP00000234296.

    PTM databases

    PhosphoSitei Q13416.

    Polymorphism databases

    DMDMi 8488999.

    Proteomic databases

    MaxQBi Q13416.
    PaxDbi Q13416.
    PeptideAtlasi Q13416.
    PRIDEi Q13416.

    Protocols and materials databases

    DNASUi 4999.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000234296 ; ENSP00000234296 ; ENSG00000115942 .
    GeneIDi 4999.
    KEGGi hsa:4999.
    UCSCi uc002uwr.3. human.

    Organism-specific databases

    CTDi 4999.
    GeneCardsi GC02M201774.
    HGNCi HGNC:8488. ORC2.
    HPAi CAB003693.
    HPA034976.
    MIMi 601182. gene.
    neXtProti NX_Q13416.
    PharmGKBi PA32809.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5575.
    HOGENOMi HOG000045588.
    HOVERGENi HBG007874.
    InParanoidi Q13416.
    KOi K02604.
    OMAi SQMLRGE.
    OrthoDBi EOG7NPFT1.
    PhylomeDBi Q13416.
    TreeFami TF101092.

    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_567. Assembly of the ORC complex at the origin of replication.
    REACT_6769. Activation of ATR in response to replication stress.

    Miscellaneous databases

    GeneWikii ORC2.
    ORC2L.
    GenomeRNAii 4999.
    NextBioi 19244.
    PROi Q13416.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13416.
    Bgeei Q13416.
    CleanExi HS_ORC2L.
    Genevestigatori Q13416.

    Family and domain databases

    InterProi IPR007220. ORC2.
    [Graphical view ]
    PANTHERi PTHR14052. PTHR14052. 1 hit.
    Pfami PF04084. ORC2. 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. Hidaka M., Stillman B.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 41-42.
    3. "Mouse and human homologues of the yeast origin of replication recognition complex subunit ORC2 and chromosomal localization of the cognate human gene ORC2L."
      Takahara K., Bong M., Brevard R., Eddy R.L., Haley L.L., Sait S.J., Shows T.B., Hoffman G.G., Greenspan D.S.
      Genomics 31:119-122(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. NIEHS SNPs program
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-106 AND GLN-521.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Placenta.
    8. "The human homolog of Saccharomyces cerevisiae Mcm10 interacts with replication factors and dissociates from nuclease-resistant nuclear structures in G(2) phase."
      Izumi M., Yanagi K., Mizuno T., Yokoi M., Kawasaki Y., Moon K.Y., Hurwitz J., Yatagai F., Hanaoka F.
      Nucleic Acids Res. 28:4769-4777(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MCM10.
    9. "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.
    10. "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.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-116 AND SER-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-116; SER-122; SER-138 AND THR-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Orc2 protects ORCA from ubiquitin-mediated degradation."
      Shen Z., Prasanth S.G.
      Cell Cycle 11:3578-3589(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LRWD1.
    15. "Leucine-rich repeat and WD repeat-containing protein 1 is recruited to pericentric heterochromatin by trimethylated lysine 9 of histone H3 and maintains heterochromatin silencing."
      Chan K.M., Zhang Z.
      J. Biol. Chem. 287:15024-15033(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BINDING TO HISTONE H3 AND H4 TRIMETHYLATION MARKS.
    16. "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.

    Entry informationi

    Entry nameiORC2_HUMAN
    AccessioniPrimary (citable) accession number: Q13416
    Secondary accession number(s): Q13204, Q53TX5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 116 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 2
      Human chromosome 2: 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