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Q13416 (ORC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Origin recognition complex subunit 2
Gene names
Name:ORC2
Synonyms:ORC2L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.14 Ref.15

Subunit structure

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. Ref.8 Ref.9 Ref.14 Ref.16

Subcellular location

Nucleus.

Sequence similarities

Belongs to the ORC2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577Origin recognition complex subunit 2
PRO_0000127075

Regions

Repeat1 – 100100Involved in LRWD1-binding

Amino acid modifications

Modified residue1161Phosphothreonine Ref.11 Ref.12
Modified residue1221Phosphoserine Ref.12
Modified residue1381Phosphoserine Ref.12
Modified residue2261Phosphothreonine Ref.12
Modified residue2801Phosphoserine Ref.11

Natural variations

Natural variant1061M → K. Ref.4
Corresponds to variant rs2307361 [ dbSNP | Ensembl ].
VAR_014515
Natural variant5211R → Q. Ref.4
Corresponds to variant rs16835624 [ dbSNP | Ensembl ].
VAR_021276

Experimental info

Sequence conflict1311I → V in AAB33970. Ref.3
Sequence conflict2361T → L in AAB33970. Ref.3
Sequence conflict3921I → M in AAB33970. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q13416 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: DF3F9C2CF147DA5F

FASTA57765,972
        10         20         30         40         50         60 
MSKPELKEDK MLEVHFVGDD DVLNHILDRE GGAKLKKERA QLLVNPKKII KKPEYDLEED 

        70         80         90        100        110        120 
DQEVLKDQNY VEIMGRDVQE SLKNGSATGG GNKVYSFQNR KHSEKMAKLA SELAKTPQKS 

       130        140        150        160        170        180 
VSFSLKNDPE ITINVPQSSK GHSASDKVQP KNNDKSEFLS TAPRSLRKRL IVPRSHSDSE 

       190        200        210        220        230        240 
SEYSASNSED DEGVAQEHEE DTNAVIFSQK IQAQNRVVSA PVGKETPSKR MKRDKTSDLV 

       250        260        270        280        290        300 
EEYFEAHSSS KVLTSDRTLQ KLKRAKLDQQ TLRNLLSKVS PSFSAELKQL NQQYEKLFHK 

       310        320        330        340        350        360 
WMLQLHLGFN IVLYGLGSKR DLLERFRTTM LQDSIHVVIN GFFPGISVKS VLNSITEEVL 

       370        380        390        400        410        420 
DHMGTFRSIL DQLDWIVNKF KEDSSLELFL LIHNLDSQML RGEKSQQIIG QLSSLHNIYL 

       430        440        450        460        470        480 
IASIDHLNAP LMWDHAKQSL FNWLWYETTT YSPYTEETSY ENSLLVKQSG SLPLSSLTHV 

       490        500        510        520        530        540 
LRSLTPNARG IFRLLIKYQL DNQDNPSYIG LSFQDFYQQC REAFLVNSDL TLRAQLTEFR 

       550        560        570 
DHKLIRTKKG TDGVEYLLIP VDNGTLTDFL EKEEEEA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2334.1.
RefSeqNP_006181.1. NM_006190.4.
XP_006712618.1. XM_006712555.1.
UniGeneHs.444870.

3D structure databases

ProteinModelPortalQ13416.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111041. 38 interactions.
DIPDIP-29689N.
IntActQ13416. 25 interactions.
MINTMINT-1201828.
STRING9606.ENSP00000234296.

PTM databases

PhosphoSiteQ13416.

Polymorphism databases

DMDM8488999.

Proteomic databases

MaxQBQ13416.
PaxDbQ13416.
PeptideAtlasQ13416.
PRIDEQ13416.

Protocols and materials databases

DNASU4999.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234296; ENSP00000234296; ENSG00000115942.
GeneID4999.
KEGGhsa:4999.
UCSCuc002uwr.3. human.

Organism-specific databases

CTD4999.
GeneCardsGC02M201774.
HGNCHGNC:8488. ORC2.
HPACAB003693.
HPA034976.
MIM601182. gene.
neXtProtNX_Q13416.
PharmGKBPA32809.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5575.
HOGENOMHOG000045588.
HOVERGENHBG007874.
InParanoidQ13416.
KOK02604.
OMASQMLRGE.
OrthoDBEOG7NPFT1.
PhylomeDBQ13416.
TreeFamTF101092.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressQ13416.
BgeeQ13416.
CleanExHS_ORC2L.
GenevestigatorQ13416.

Family and domain databases

InterProIPR007220. ORC2.
[Graphical view]
PANTHERPTHR14052. PTHR14052. 1 hit.
PfamPF04084. ORC2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiORC2.
ORC2L.
GenomeRNAi4999.
NextBio19244.
PROQ13416.
SOURCESearch...

Entry information

Entry nameORC2_HUMAN
AccessionPrimary (citable) accession number: Q13416
Secondary accession number(s): Q13204, Q53TX5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM