Q13416 (ORC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Origin recognition complex subunit 2

Gene names

Name:	ORC2
Synonyms:	ORC2L

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
Subunit structure	ORC is composed of six subunits. In human, ORC is cell cycle-dependent regulated: 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. Ref.8
Subcellular location	Nucleus.
Sequence similarities	Belongs to the ORC2 family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA-dependent DNA replication initiation Traceable author statement. Source: ProtInc G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome cell cycle checkpoint Traceable author statement. Source: Reactome negative regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	nuclear origin of replication recognition complex Inferred from direct assay. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular function	DNA replication origin binding Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MCM10	Q7L590	5	EBI-374957,EBI-374912
MCM3	P25205	2	EBI-374957,EBI-355153
ORC1	Q13415	3	EBI-374957,EBI-374847

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 577	577	Origin recognition complex subunit 2		PRO_0000127075
Amino acid modifications
	Modified residue	116	1	Phosphothreonine Ref.11
	Modified residue	226	1	Phosphothreonine Ref.12
	Modified residue	280	1	Phosphoserine Ref.11
Natural variations
	Natural variant	106	1	M → K. Ref.4 Corresponds to variant rs2307361 [ dbSNP | Ensembl ].		VAR_014515
	Natural variant	521	1	R → Q. Ref.4 Corresponds to variant rs16835624 [ dbSNP | Ensembl ].		VAR_021276
Experimental info
	Sequence conflict	131	1	I → V in AAB33970. Ref.3
	Sequence conflict	236	1	T → L in AAB33970. Ref.3
	Sequence conflict	392	1	I → M in AAB33970. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q13416 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: DF3F9C2CF147DA5F	FASTA	577	65,972
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conserved initiator proteins in eukaryotes." Gavin K.A., Hidaka M., Stillman B.D. Science 270:1667-1671(1995) [PubMed: 7502077] [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: 8808289] [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: 15815621] [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. , 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: 15489334] [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: 11095689] [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: 12909626] [Abstract] Cited for: IDENTIFICATION IN THE ORC COMPLEX, 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: 17716973] [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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-116 AND SER-280, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.
IPI	IPI00013216.
RefSeq	NP_006181.1. NM_006190.4.
UniGene	Hs.444870.
3D structure databases
ProteinModelPortal	Q13416.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29689N.
IntAct	Q13416. 15 interactions.
MINT	MINT-1201828.
STRING	Q13416.
PTM databases
PhosphoSite	Q13416.
Polymorphism databases
DMDM	8488999.
Proteomic databases
PeptideAtlas	Q13416.
PRIDE	Q13416.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000234296; ENSP00000234296; ENSG00000115942.
GeneID	4999.
KEGG	hsa:4999.
UCSC	uc002uwr.1. human.
Organism-specific databases
CTD	4999.
GeneCards	GC02M201774.
HGNC	HGNC:8488. ORC2.
HPA	CAB003693.
MIM	601182. gene.
neXtProt	NX_Q13416.
PharmGKB	PA32809.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05587.
GeneTree	ENSGT00390000015228.
HOGENOM	HBG713936.
HOVERGEN	HBG007874.
InParanoid	Q13416.
OMA	GGNKVYS.
OrthoDB	EOG43FGWM.
PhylomeDB	Q13416.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	Q13416.
Bgee	Q13416.
CleanEx	HS_ORC2L.
Genevestigator	Q13416.
GermOnline	ENSG00000115942. Homo sapiens.
Family and domain databases
InterPro	IPR007220. ORC2. [Graphical view]
KO	K02604.
PANTHER	PTHR14052. ORC2. 1 hit.
Pfam	PF04084. ORC2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	19244.
SOURCE	Search...

Entry information

Entry name

ORC2_HUMAN

Accession

Primary (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:	December 14, 2011
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.