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Protein

Origin recognition complex subunit 6

Gene

ORC6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:17151. ORC6.

Subcellular locationi

GO - Cellular componenti

  • membrane Source: UniProtKB
  • nuclear origin of replication recognition complex Source: InterPro
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
  • origin recognition complex Source: UniProtKB
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Meier-Gorlin syndrome 3 (MGORS3)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:613803
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.

Polymorphism and mutation databases

BioMutaiORC6.
DMDMi8928274.

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

BgeeiQ9Y5N6.
CleanExiHS_ORC6L.
ExpressionAtlasiQ9Y5N6. baseline and differential.
GenevisibleiQ9Y5N6. HS.

Organism-specific databases

HPAiCAB016330.
HPA062047.

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
LHX4Q969G23EBI-374840,EBI-2865388
ORC3Q9UBD54EBI-374840,EBI-374916
SPAG5Q96R063EBI-374840,EBI-413317

Protein-protein interaction databases

BioGridi117129. 33 interactions.
DIPiDIP-29692N.
IntActiQ9Y5N6. 10 interactions.
MINTiMINT-1202310.
STRINGi9606.ENSP00000219097.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000007370.
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

        10         20         30         40         50
MGSELIGRLA PRLGLAEPDM LRKAEEYLRL SRVKCVGLSA RTTETSSAVM
60 70 80 90 100
CLDLAASWMK CPLDRAYLIK LSGLNKETYQ SCLKSFECLL GLNSNIGIRD
110 120 130 140 150
LAVQFSCIEA VNMASKILKS YESSLPQTQQ VDLDLSRPLF TSAALLSACK
160 170 180 190 200
ILKLKVDKNK MVATSGVKKA IFDRLCKQLE KIGQQVDREP GDVATPPRKR
210 220 230 240 250
KKIVVEAPAK EMEKVEEMPH KPQKDEDLTQ DYEEWKRKIL ENAASAQKAT

AE
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi117129. 33 interactions.
DIPiDIP-29692N.
IntActiQ9Y5N6. 10 interactions.
MINTiMINT-1202310.
STRINGi9606.ENSP00000219097.

PTM databases

PhosphoSiteiQ9Y5N6.

Polymorphism and mutation databases

BioMutaiORC6.
DMDMi8928274.

Proteomic databases

MaxQBiQ9Y5N6.
PaxDbiQ9Y5N6.
PRIDEiQ9Y5N6.

Protocols and materials databases

DNASUi23594.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23594.
GeneCardsiGC16P046724.
HGNCiHGNC:17151. ORC6.
HPAiCAB016330.
HPA062047.
MIMi607213. gene.
613803. phenotype.
neXtProtiNX_Q9Y5N6.
Orphaneti2554. Ear-patella-short stature syndrome.
PharmGKBiPA32813.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG285438.
GeneTreeiENSGT00390000007370.
HOGENOMiHOG000065679.
HOVERGENiHBG007876.
InParanoidiQ9Y5N6.
KOiK02608.
OMAiVEIPHKP.
PhylomeDBiQ9Y5N6.
TreeFamiTF101096.

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.

Miscellaneous databases

ChiTaRSiORC6. human.
GeneWikiiORC6.
ORC6L.
GenomeRNAii23594.
NextBioi46248.
PROiQ9Y5N6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5N6.
CleanExiHS_ORC6L.
ExpressionAtlasiQ9Y5N6. baseline and differential.
GenevisibleiQ9Y5N6. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 125 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.