Origin recognition complex subunit 1

Names and origin

Protein names

Recommended name:
Origin recognition complex subunit 1
Alternative name(s):
Replication control protein 1

Gene names

Name:	ORC1L
Synonyms:	ORC1, PARC1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	861 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication in an ATP-dependent manner.
Subunit structure	ORC is composed of six subunits. Interacts with CDC6 and MYST2/HBO1. Ref.4 Ref.5
Subcellular location	Nucleus.
Sequence similarities	Belongs to the ORC1 family. Contains 1 BAH domain.

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Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA replication initiation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytosol Inferred from Experiment. Source: Reactome nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Ref.1 Traceable author statement. Source: ProtInc nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
ABL1	P00519	1	EBI-374847,EBI-375543
CDC5L	Q99459	1	EBI-374847,EBI-374880
CDC6	Q99741	1	EBI-374847,EBI-374862
CDT1	Q9H211	1	EBI-374847,EBI-456953
FYN	P06241	1	EBI-374847,EBI-515315
MCM5	P33992	1	EBI-374847,EBI-359410
ORC2L	Q13416	1	EBI-374847,EBI-374957
ORC3L	Q9UBD5	1	EBI-374847,EBI-374916
ORC5L	O43913	1	EBI-374847,EBI-374928
RPS27A	P62988	1	EBI-374847,EBI-413034
SKP2	Q13309	2	EBI-374847,EBI-456291

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 861

861

Origin recognition complex subunit 1

PRO_0000127067

Regions

Domain

45 – 171

127

BAH

Nucleotide binding

534 – 541

8

ATP Potential

Amino acid modifications

Modified residue

196

1

Phosphoserine Ref.7

Modified residue

203

1

Phosphothreonine Ref.7

Modified residue

337

1

Phosphothreonine Ref.7

Modified residue

340

1

Phosphoserine Ref.7

Modified residue

417

1

Phosphoserine Ref.7 Ref.6

Modified residue

419

1

Phosphoserine Ref.6

Modified residue

420

1

Phosphoserine Ref.7 Ref.6

Modified residue

421

1

Phosphoserine Ref.7 Ref.6

Modified residue

427

1

Phosphoserine Ref.7

Modified residue

478

1

Phosphoserine Ref.7

Natural variations

Natural variant

19

1

R → S: dbSNP rs3087473.

VAR_014507

Natural variant

180

1

Q → H: dbSNP rs3087482.

VAR_014508

Natural variant

190

1

V → M: dbSNP rs3087477.

VAR_014509

Natural variant

372

1

A → V: dbSNP rs3087476.

VAR_014510

Natural variant

441

1

R → M: dbSNP rs3087472.

VAR_014511

Natural variant

456

1

K → E: dbSNP rs3087470.

VAR_014512

Natural variant

466

1

T → M: dbSNP rs3087481.

VAR_014513

Natural variant

469

1

C → Y: dbSNP rs3087483.

VAR_014514

Natural variant

816

1

M → T: dbSNP rs34521609.

VAR_050426

Experimental info

Sequence conflict

582

1

Q → H in AAC50325. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q13415-1 [UniParc].

Last modified September 27, 2005. Version 2.
Checksum: 5C594553F7F808E2
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FASTA

861

97,350

        10         20         30         40         50         60 
MAHYPTRLKT RKTYSWVGRP LLDRKLHYQT YREMCVKTEG CSTEIHIQIG QFVLIEGDDD 

        70         80         90        100        110        120 
ENPYVAKLLE LFEDDSDPPP KKRARVQWFV RFCEVPACKR HLLGRKPGAQ EIFWYDYPAC 

       130        140        150        160        170        180 
DSNINAETII GLVRVIPLAP KDVVPTNLKN EKTLFVKLSW NEKKFRPLSS ELFAELNKPQ 

       190        200        210        220        230        240 
ESAAKCQKPV RAKSKSAESP SWTPAEHVAK RIESRHSASK SRQTPTHPLT PRARKRLELG 

       250        260        270        280        290        300 
NLGNPQMSQQ TSCASLDSPG RIKRKVAFSE ITSPSKRSQP DKLQTLSPAL KAPEKTRETG 

       310        320        330        340        350        360 
LSYTEDDKKA SPEHRIILRT RIAASKTIDI REERTLTPIS GGQRSSVVPS VILKPENIKK 

       370        380        390        400        410        420 
RDAKEAKAQN EATSTPHRIR RKSSVLTMNR IRQQLRFLGN SKSDQEEKEI LPAAEISDSS 

       430        440        450        460        470        480 
SDEEEASTPP LPRRAPRTVS RNLRSSLKSS LHTLTKVPKK SLKPRTPRCA APQIRSRSLA 

       490        500        510        520        530        540 
AQEPASVLEE ARLRLHVSAV PESLPCREQE FQDIYNFVES KLLDHTGGCM YISGVPGTGK 

       550        560        570        580        590        600 
TATVHEVIRC LQQAAQANDV PPFQYIEVNG MKLTEPHQVY VQILQKLTGQ KATANHAAEL 

       610        620        630        640        650        660 
LAKQFCTRGS PQETTVLLVD ELDLLWTHKQ DIMYNLFDWP THKEARLVVL AIANTMDLPE 

       670        680        690        700        710        720 
RIMMNRVSSR LGLTRMCFQP YTYSQLQQIL RSRLKHLKAF EDDAIQLVAR KVAALSGDAR 

       730        740        750        760        770        780 
RCLDICRRAT EICEFSQQKP DSPGLVTIAH SMEAVDEMFS SSYITAIKNS SVLEQSFLRA 

       790        800        810        820        830        840 
ILAEFRRSGL EEATFQQIYS QHVALCRMEG LPYPTMSETM AVCSHLGSCR LLLVEPSRND 

       850        860 
LLLRVRLNVS QDDVLYALKD E

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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]	Wolf D.A., McKeon F. Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively eliminated from the nucleus at the onset of S phase." Saha P., Chen J., Thome K.C., Lawlis S.J., Hou Z.H., Hendricks M., Parvin J.D., Dutta A. Mol. Cell. Biol. 18:2758-2767(1998) [PubMed: 9566895] [Abstract] Cited for: INTERACTION WITH CDC6.
[5]	"Histone acetyltransferase HBO1 interacts with the ORC1 subunit of the human initiator protein." Iizuka M., Stillman B. J. Biol. Chem. 274:23027-23034(1999) [PubMed: 10438470] [Abstract] Cited for: INTERACTION WITH MYST2.
[6]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417; SER-419; SER-420 AND SER-421, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"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 SER-196; THR-203; THR-337; SER-340; SER-417; SER-420; SER-421; SER-427 AND SER-478, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	U40152 mRNA. Translation: AAC50325.1. U43416 mRNA. Translation: AAA86260.1. AL513218 Genomic DNA. Translation: CAI12288.1.
IPI	IPI00013215.
PIR	G02329.
RefSeq	NP_004144.2.
UniGene	Hs.17908
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13415. 14 interactions.
PTM databases
PhosphoSite	Q13415.
Proteomic databases
PRIDE	Q13415.
Genome annotation databases
Ensembl	ENSG00000085840. Homo sapiens. [Contig view]
GeneID	4998.
KEGG	hsa:4998.
NMPDR	fig\|9606.3.peg.1166.
UCSC	uc001ctt.1. human.
Organism-specific databases
GeneCards	GC01M052611.
H-InvDB	HIX0000584.
HGNC	HGNC:8487. ORC1L.
MIM	601902. gene.
PharmGKB	PA32808.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q13415.
HOVERGEN	Q13415.
OMA	Q13415. KAFEDDA.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	Q13415.
Bgee	Q13415.
CleanEx	HS_ORC1L.
GermOnline	ENSG00000085840. Homo sapiens.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR003959. ATPase_AAA_core. IPR001025. BAH. IPR015163. Cdc6_C. [Graphical view]
Pfam	PF00004. AAA. 1 hit. PF01426. BAH. 1 hit. PF09079. Cdc6_C. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. SM00439. BAH. 1 hit. [Graphical view]
PROSITE	PS51038. BAH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	19240.
SOURCE	Search...

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Entry information

Entry name

ORC1_HUMAN

Accession

Primary (citable) accession number: Q13415
Secondary accession number(s): Q13471, Q5T0F5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 27, 2005
Last modified:	July 7, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents