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Q9Y5N6

- ORC6_HUMAN

UniProt

Q9Y5N6 - ORC6_HUMAN

Protein

Origin recognition complex subunit 6

Gene

ORC6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      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. Does not bind histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. DNA-dependent DNA replication Source: Ensembl
    2. DNA replication Source: Reactome
    3. G1/S transition of mitotic cell cycle Source: Reactome
    4. mitotic cell cycle Source: Reactome

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1095. Activation of the pre-replicative complex.
    REACT_1156. Orc1 removal from chromatin.
    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 6
    Gene namesi
    Name:ORC6
    Synonyms:ORC6L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:17151. ORC6.

    Subcellular locationi

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nuclear origin of replication recognition complex Source: InterPro
    3. nucleoplasm Source: Reactome
    4. origin recognition complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Meier-Gorlin syndrome 3 (MGORS3) [MIM:613803]: 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti232 – 2321Y → S in MGORS3. 1 Publication
    VAR_065487

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi129 – 1291Q → A: Abolished DNA binding. 1 Publication
    Mutagenesisi137 – 1371R → A: Abolished DNA binding. 1 Publication
    Mutagenesisi168 – 1681K → A: Abolished DNA binding. 1 Publication

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi613803. phenotype.
    Orphaneti2554. Ear-patella-short stature syndrome.
    PharmGKBiPA32813.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 252252Origin recognition complex subunit 6PRO_0000127097Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei195 – 1951Phosphothreonine2 Publications
    Modified residuei229 – 2291Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y5N6.
    PaxDbiQ9Y5N6.
    PRIDEiQ9Y5N6.

    PTM databases

    PhosphoSiteiQ9Y5N6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y5N6.
    BgeeiQ9Y5N6.
    CleanExiHS_ORC6L.
    GenevestigatoriQ9Y5N6.

    Organism-specific databases

    HPAiCAB016330.

    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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ORC3Q9UBD54EBI-374840,EBI-374916

    Protein-protein interaction databases

    BioGridi117129. 22 interactions.
    DIPiDIP-29692N.
    IntActiQ9Y5N6. 8 interactions.
    MINTiMINT-1202310.
    STRINGi9606.ENSP00000219097.

    Structurei

    Secondary structure

    1
    252
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi98 – 1058
    Helixi108 – 1103
    Helixi111 – 12212
    Helixi127 – 1326
    Helixi138 – 15114
    Helixi158 – 1636
    Helixi169 – 18315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3M03X-ray2.50A/B/C94-187[»]
    ProteinModelPortaliQ9Y5N6.
    SMRiQ9Y5N6. Positions 94-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ORC6 family.Curated

    Phylogenomic databases

    eggNOGiNOG285438.
    HOGENOMiHOG000065679.
    HOVERGENiHBG007876.
    InParanoidiQ9Y5N6.
    KOiK02608.
    OMAiVEIPHKP.
    PhylomeDBiQ9Y5N6.
    TreeFamiTF101096.

    Family and domain databases

    InterProiIPR008721. ORC6.
    IPR020529. ORC6_met/pln.
    [Graphical view]
    PfamiPF05460. ORC6. 1 hit.
    [Graphical view]
    ProDomiPD315657. Origin_recog_cplx_su6-like. 1 hit.
    [Graphical view] [Entries sharing at least one domain]

    Sequencei

    Sequence statusi: Complete.

    Q9Y5N6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSELIGRLA PRLGLAEPDM LRKAEEYLRL SRVKCVGLSA RTTETSSAVM    50
    CLDLAASWMK CPLDRAYLIK LSGLNKETYQ SCLKSFECLL GLNSNIGIRD 100
    LAVQFSCIEA VNMASKILKS YESSLPQTQQ VDLDLSRPLF TSAALLSACK 150
    ILKLKVDKNK MVATSGVKKA IFDRLCKQLE KIGQQVDREP GDVATPPRKR 200
    KKIVVEAPAK EMEKVEEMPH KPQKDEDLTQ DYEEWKRKIL ENAASAQKAT 250
    AE 252
    Length:252
    Mass (Da):28,107
    Last modified:November 1, 1999 - v1
    Checksum:i78840387605F45FE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321R → W.
    Corresponds to variant rs3218744 [ dbSNP | Ensembl ].
    VAR_029283
    Natural varianti138 – 1381P → Q.
    Corresponds to variant rs3218745 [ dbSNP | Ensembl ].
    VAR_029284
    Natural varianti232 – 2321Y → S in MGORS3. 1 Publication
    VAR_065487

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF139658 mRNA. Translation: AAD32666.1.
    AK024019 mRNA. Translation: BAG51251.1.
    CH471092 Genomic DNA. Translation: EAW82685.1.
    BC039032 mRNA. Translation: AAH39032.1.
    BC063565 mRNA. Translation: AAH63565.1.
    CCDSiCCDS10722.1.
    RefSeqiNP_055136.1. NM_014321.3.
    UniGeneiHs.49760.

    Genome annotation databases

    EnsembliENST00000219097; ENSP00000219097; ENSG00000091651.
    GeneIDi23594.
    KEGGihsa:23594.
    UCSCiuc002eeg.1. human.

    Polymorphism databases

    DMDMi8928274.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF139658 mRNA. Translation: AAD32666.1 .
    AK024019 mRNA. Translation: BAG51251.1 .
    CH471092 Genomic DNA. Translation: EAW82685.1 .
    BC039032 mRNA. Translation: AAH39032.1 .
    BC063565 mRNA. Translation: AAH63565.1 .
    CCDSi CCDS10722.1.
    RefSeqi NP_055136.1. NM_014321.3.
    UniGenei Hs.49760.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3M03 X-ray 2.50 A/B/C 94-187 [» ]
    ProteinModelPortali Q9Y5N6.
    SMRi Q9Y5N6. Positions 94-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117129. 22 interactions.
    DIPi DIP-29692N.
    IntActi Q9Y5N6. 8 interactions.
    MINTi MINT-1202310.
    STRINGi 9606.ENSP00000219097.

    PTM databases

    PhosphoSitei Q9Y5N6.

    Polymorphism databases

    DMDMi 8928274.

    Proteomic databases

    MaxQBi Q9Y5N6.
    PaxDbi Q9Y5N6.
    PRIDEi Q9Y5N6.

    Protocols and materials databases

    DNASUi 23594.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219097 ; ENSP00000219097 ; ENSG00000091651 .
    GeneIDi 23594.
    KEGGi hsa:23594.
    UCSCi uc002eeg.1. human.

    Organism-specific databases

    CTDi 23594.
    GeneCardsi GC16P046724.
    HGNCi HGNC:17151. ORC6.
    HPAi CAB016330.
    MIMi 607213. gene.
    613803. phenotype.
    neXtProti NX_Q9Y5N6.
    Orphaneti 2554. Ear-patella-short stature syndrome.
    PharmGKBi PA32813.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG285438.
    HOGENOMi HOG000065679.
    HOVERGENi HBG007876.
    InParanoidi Q9Y5N6.
    KOi K02608.
    OMAi VEIPHKP.
    PhylomeDBi Q9Y5N6.
    TreeFami TF101096.

    Enzyme and pathway databases

    Reactomei REACT_1095. Activation of the pre-replicative complex.
    REACT_1156. Orc1 removal from chromatin.
    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

    ChiTaRSi ORC6. human.
    GeneWikii ORC6.
    ORC6L.
    GenomeRNAii 23594.
    NextBioi 46248.
    PROi Q9Y5N6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y5N6.
    Bgeei Q9Y5N6.
    CleanExi HS_ORC6L.
    Genevestigatori Q9Y5N6.

    Family and domain databases

    InterProi IPR008721. ORC6.
    IPR020529. ORC6_met/pln.
    [Graphical view ]
    Pfami PF05460. ORC6. 1 hit.
    [Graphical view ]
    ProDomi PD315657. Origin_recog_cplx_su6-like. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of a homolog for Saccharomyces cerevisiae ORC6 from Homo sapiens."
      Dean F.B., O'Donnell M.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Cervix and Testis.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "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.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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-195, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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: LACK OF BINDING TO HISTONE H3 AND H4 TRIMETHYLATION MARKS, FUNCTION.
    11. "Structural analysis of human Orc6 protein reveals a homology with transcription factor TFIIB."
      Liu S., Balasov M., Wang H., Wu L., Chesnokov I.N., Liu Y.
      Proc. Natl. Acad. Sci. U.S.A. 108:7373-7378(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 94-187, MUTAGENESIS OF GLN-129; ARG-137 AND LYS-168, DNA-BINDING.
    12. Cited for: VARIANT MGORS3 SER-232.

    Entry informationi

    Entry nameiORC6_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5N6
    Secondary accession number(s): B3KN89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 118 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3