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O43913

- ORC5_HUMAN

UniProt

O43913 - ORC5_HUMAN

Protein

Origin recognition complex subunit 5

Gene

ORC5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi37 – 448ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA replication origin binding Source: ProtInc
    3. nucleotide binding Source: ProtInc
    4. protein binding Source: IntAct

    GO - Biological processi

    1. DNA replication Source: UniProtKB
    2. DNA replication initiation Source: ProtInc
    3. G1/S transition of mitotic cell cycle Source: Reactome
    4. mitotic cell cycle Source: Reactome

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-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_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 5
    Gene namesi
    Name:ORC5
    Synonyms:ORC5L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:8491. ORC5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nuclear origin of replication recognition complex Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. origin recognition complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA32812.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 435435Origin recognition complex subunit 5PRO_0000127092Add
    BLAST

    Proteomic databases

    MaxQBiO43913.
    PaxDbiO43913.
    PeptideAtlasiO43913.
    PRIDEiO43913.

    PTM databases

    PhosphoSiteiO43913.

    Expressioni

    Tissue specificityi

    Abundant in spleen, ovary, prostate, testis, and colon mucosa.1 Publication

    Gene expression databases

    ArrayExpressiO43913.
    BgeeiO43913.
    CleanExiHS_ORC5L.
    GenevestigatoriO43913.

    Organism-specific databases

    HPAiHPA019730.

    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.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ORC1Q134155EBI-374928,EBI-374847
    ORC2Q134167EBI-374928,EBI-374957
    ORC3Q9UBD515EBI-374928,EBI-374916
    ORC4O439292EBI-374928,EBI-374889

    Protein-protein interaction databases

    BioGridi111043. 34 interactions.
    DIPiDIP-29691N.
    IntActiO43913. 23 interactions.
    MINTiMINT-1201309.

    Structurei

    3D structure databases

    ProteinModelPortaliO43913.
    SMRiO43913. Positions 32-59.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ORC5 family.Curated

    Phylogenomic databases

    eggNOGiNOG249220.
    HOGENOMiHOG000252907.
    HOVERGENiHBG007875.
    InParanoidiO43913.
    KOiK02607.
    OMAiVPCRESQ.
    OrthoDBiEOG7DZ8K4.
    PhylomeDBiO43913.
    TreeFamiTF101095.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR020796. ORC5.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR12705. PTHR12705. 1 hit.
    PfamiPF14630. ORC5_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43913-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPHLENVVLC RESQVSILQS LFGERHHFSF PSIFIYGHTA SGKTYVTQTL    50
    LKTLELPHVF VNCVECFTLR LLLEQILNKL NHLSSSEDGC STEITCETFN 100
    DFVRLFKQVT TAENLKDQTV YIVLDKAEYL RDMEANLLPG FLRLQELADR 150
    NVTVLFLSEI VWEKFRPNTG CFEPFVLYFP DYSIGNLQKI LSHDHPPEYS 200
    ADFYAAYINI LLGVFYTVCR DLKELRHLAV LNFPKYCEPV VKGEASERDT 250
    RKLWRNIEPH LKKAMQTVYL REISSSQWEK LQKDDTDPGQ LKGLSAHTHV 300
    ELPYYSKFIL IAAYLASYNP ARTDKRFFLK HHGKIKKTNF LKKHEKTSNH 350
    LLGPKPFPLD RLLAILYSIV DSRVAPTANI FSQITSLVTL QLLTLVGHDD 400
    QLDGPKYKCT VSLDFIRAIA RTVNFDIIKY LYDFL 435
    Length:435
    Mass (Da):50,283
    Last modified:June 1, 1998 - v1
    Checksum:i0FEB0E829C124745
    GO
    Isoform 2 (identifier: O43913-2) [UniParc]FASTAAdd to Basket

    Also known as: ORC5T

    The sequence of this isoform differs from the canonical sequence as follows:
         294-435: LSAHTHVELP...DIIKYLYDFL → IRGSIETVTGDTSSANYQDTKVNTKEHSVRK

    Note: Does not interact with ORC2.

    Show »
    Length:324
    Mass (Da):37,414
    Checksum:i005B2887929C62C8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371G → R.1 Publication
    Corresponds to variant rs1056677 [ dbSNP | Ensembl ].
    VAR_011800
    Natural varianti52 – 521K → N.
    Corresponds to variant rs2307413 [ dbSNP | Ensembl ].
    VAR_014524
    Natural varianti166 – 1661R → C.
    Corresponds to variant rs2307402 [ dbSNP | Ensembl ].
    VAR_014525

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei294 – 435142LSAHT…LYDFL → IRGSIETVTGDTSSANYQDT KVNTKEHSVRK in isoform 2. 1 PublicationVSP_042037Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047599 mRNA. Translation: AAC80283.1.
    U92538 mRNA. Translation: AAC51933.1.
    AF049127 mRNA. Translation: AAC63972.1.
    AF081459 mRNA. Translation: AAC64401.1.
    AC002067 Genomic DNA. No translation available.
    AC007393 Genomic DNA. No translation available.
    CH236947 Genomic DNA. Translation: EAL24409.1.
    CH471070 Genomic DNA. Translation: EAW83341.1.
    BC023652 mRNA. Translation: AAH23652.1.
    CCDSiCCDS47681.1. [O43913-2]
    CCDS5734.1. [O43913-1]
    RefSeqiNP_002544.1. NM_002553.3. [O43913-1]
    NP_859531.1. NM_181747.3. [O43913-2]
    UniGeneiHs.432948.

    Genome annotation databases

    EnsembliENST00000297431; ENSP00000297431; ENSG00000164815. [O43913-1]
    ENST00000447452; ENSP00000395747; ENSG00000164815. [O43913-2]
    GeneIDi5001.
    KEGGihsa:5001.
    UCSCiuc003vcb.3. human. [O43913-1]
    uc003vcc.3. human. [O43913-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047599 mRNA. Translation: AAC80283.1 .
    U92538 mRNA. Translation: AAC51933.1 .
    AF049127 mRNA. Translation: AAC63972.1 .
    AF081459 mRNA. Translation: AAC64401.1 .
    AC002067 Genomic DNA. No translation available.
    AC007393 Genomic DNA. No translation available.
    CH236947 Genomic DNA. Translation: EAL24409.1 .
    CH471070 Genomic DNA. Translation: EAW83341.1 .
    BC023652 mRNA. Translation: AAH23652.1 .
    CCDSi CCDS47681.1. [O43913-2 ]
    CCDS5734.1. [O43913-1 ]
    RefSeqi NP_002544.1. NM_002553.3. [O43913-1 ]
    NP_859531.1. NM_181747.3. [O43913-2 ]
    UniGenei Hs.432948.

    3D structure databases

    ProteinModelPortali O43913.
    SMRi O43913. Positions 32-59.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111043. 34 interactions.
    DIPi DIP-29691N.
    IntActi O43913. 23 interactions.
    MINTi MINT-1201309.

    PTM databases

    PhosphoSitei O43913.

    Proteomic databases

    MaxQBi O43913.
    PaxDbi O43913.
    PeptideAtlasi O43913.
    PRIDEi O43913.

    Protocols and materials databases

    DNASUi 5001.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297431 ; ENSP00000297431 ; ENSG00000164815 . [O43913-1 ]
    ENST00000447452 ; ENSP00000395747 ; ENSG00000164815 . [O43913-2 ]
    GeneIDi 5001.
    KEGGi hsa:5001.
    UCSCi uc003vcb.3. human. [O43913-1 ]
    uc003vcc.3. human. [O43913-2 ]

    Organism-specific databases

    CTDi 5001.
    GeneCardsi GC07M103767.
    HGNCi HGNC:8491. ORC5.
    HPAi HPA019730.
    MIMi 602331. gene.
    neXtProti NX_O43913.
    PharmGKBi PA32812.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249220.
    HOGENOMi HOG000252907.
    HOVERGENi HBG007875.
    InParanoidi O43913.
    KOi K02607.
    OMAi VPCRESQ.
    OrthoDBi EOG7DZ8K4.
    PhylomeDBi O43913.
    TreeFami TF101095.

    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 ORC5.
    ORC5L.
    GenomeRNAii 5001.
    NextBioi 19256.
    PROi O43913.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43913.
    Bgeei O43913.
    CleanExi HS_ORC5L.
    Genevestigatori O43913.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR020796. ORC5.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR12705. PTHR12705. 1 hit.
    Pfami PF14630. ORC5_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The Orc4p and Orc5p subunits of the Xenopus and human origin recognition complex are related to Orc1p and Cdc6p."
      Tugal T., Zou-Yang X.H., Gavin K., Pappin D., Canas B., Kobayashi R., Hunt T., Stillman B.
      J. Biol. Chem. 273:32421-32429(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Isolation of human and fission yeast homologues of the budding yeast origin recognition complex subunit ORC5: human homologue (ORC5L) maps to 7q22."
      Ishiai M., Dean F.B., Okumura K., Abe M., Moon K.-Y., Amin A.A., Kagotani K., Taguchi H., Murakami Y., Hanaoka F., O'Donnell M., Hurwitz J., Eki T.
      Genomics 46:294-298(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "ORC5L, a new member of the human origin recognition complex, is deleted in uterine leiomyomas and malignant myeloid diseases."
      Quintana D.G., Thome K.C., Hou Z.-H., Ligon A.H., Morton C.C., Dutta A.
      J. Biol. Chem. 273:27137-27145(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, VARIANT ARG-37.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [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] (ISOFORM 1).
      Tissue: Uterus.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiORC5_HUMAN
    AccessioniPrimary (citable) accession number: O43913
    Secondary accession number(s): A4D0P8, O60590, O95268
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 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 7
      Human chromosome 7: 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