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Q13415 (ORC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Origin recognition complex subunit 1
Alternative name(s):
Replication control protein 1
Gene names
Name:ORC1
Synonyms:ORC1L, PARC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length861 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 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.

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 CDC6 and KAT7/HBO1. Interacts with LRWD1 predominantly during the G1 phase and with less affinity during mitosis, when phosphorylated. Ref.5 Ref.6 Ref.8 Ref.15

Subcellular location

Nucleus.

Developmental stage

Expression is cell-cycle regulated, it starts to accumulate in mid-G1 phase, reaches a peak at the G1/S boundary, and decreases to a basal level in S phase (at protein level). Ref.7

Domain

The BAH domain mediates binding to dimethylated histone H4 'Lys-20' (H4K20me2), which is enriched at replication origins By similarity.

Post-translational modification

Phosphorylated during mitosis. Ref.15

Involvement in disease

Meier-Gorlin syndrome 1 (MGORS1) [MIM:224690]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.17 Ref.18

Sequence similarities

Belongs to the ORC1 family.

Contains 1 BAH domain.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Dwarfism
   LigandATP-binding
DNA-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Traceable author statement. Source: Reactome

DNA replication initiation

Traceable author statement Ref.1. Source: ProtInc

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

regulation of transcription involved in G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nuclear origin of replication recognition complex

Inferred from direct assay PubMed 20932478PubMed 21029866. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

origin recognition complex

Inferred from direct assay Ref.9. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Traceable author statement Ref.1. Source: ProtInc

chromatin binding

Inferred from electronic annotation. Source: InterPro

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 11931757PubMed 15232106PubMed 16799465Ref.9PubMed 18946490. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 861861Origin recognition complex subunit 1
PRO_0000127067

Regions

Domain45 – 171127BAH
Nucleotide binding534 – 5418ATP Potential
Region501 – 861361Necessary and sufficient for ORC complex assembly

Sites

Binding site931Histone H4K20me2 By similarity

Amino acid modifications

Modified residue2031Phosphothreonine Ref.10 Ref.13
Modified residue2731Phosphoserine Ref.13 Ref.14
Modified residue2871Phosphoserine Ref.13
Modified residue3261N6-acetyllysine Ref.12
Modified residue3371Phosphothreonine Ref.10
Modified residue3401Phosphoserine Ref.10
Modified residue4171Phosphoserine Ref.10
Modified residue4201Phosphoserine Ref.10
Modified residue4781Phosphoserine Ref.10

Natural variations

Natural variant191R → S.
Corresponds to variant rs3087473 [ dbSNP | Ensembl ].
VAR_014507
Natural variant891F → S in MGORS1. Ref.16
VAR_065481
Natural variant1051R → Q in MGORS1. Ref.16 Ref.17 Ref.18
VAR_065482
Natural variant1271E → G in MGORS1. Ref.16
VAR_065483
Natural variant1801Q → H.
Corresponds to variant rs3087482 [ dbSNP | Ensembl ].
VAR_014508
Natural variant1901V → M.
Corresponds to variant rs3087477 [ dbSNP | Ensembl ].
VAR_014509
Natural variant3721A → V.
Corresponds to variant rs3087476 [ dbSNP | Ensembl ].
VAR_014510
Natural variant4411R → M.
Corresponds to variant rs3087472 [ dbSNP | Ensembl ].
VAR_014511
Natural variant4561K → E.
Corresponds to variant rs3087470 [ dbSNP | Ensembl ].
VAR_014512
Natural variant4661T → M.
Corresponds to variant rs3087481 [ dbSNP | Ensembl ].
VAR_014513
Natural variant4691C → Y.
Corresponds to variant rs3087483 [ dbSNP | Ensembl ].
VAR_014514
Natural variant6661R → W in MGORS1. Ref.18
Corresponds to variant rs201253919 [ dbSNP | Ensembl ].
VAR_065484
Natural variant7201R → Q in MGORS1. Ref.16
VAR_065485
Natural variant8161M → T.
Corresponds to variant rs34521609 [ dbSNP | Ensembl ].
VAR_050426

Experimental info

Sequence conflict5821Q → H in AAC50325. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q13415 [UniParc].

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

FASTA86197,350
        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 

« 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]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. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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].
[5]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC6.
[6]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KAT7.
[7]"The ORC1 cycle in human cells: I. cell cycle-regulated oscillation of human ORC1."
Tatsumi Y., Ohta S., Kimura H., Tsurimoto T., Obuse C.
J. Biol. Chem. 278:41528-41534(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[8]"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.
[9]"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.
[10]"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-203; THR-337; SER-340; SER-417; SER-420 AND SER-478, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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-203; SER-273 AND SER-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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, PHOSPHORYLATION DURING MITOSIS.
[16]"Mutations in ORC1, encoding the largest subunit of the origin recognition complex, cause microcephalic primordial dwarfism resembling Meier-Gorlin syndrome."
Bicknell L.S., Walker S., Klingseisen A., Stiff T., Leitch A., Kerzendorfer C., Martin C.A., Yeyati P., Al Sanna N., Bober M., Johnson D., Wise C., Jackson A.P., O'Driscoll M., Jeggo P.A.
Nat. Genet. 43:350-355(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MGORS1 SER-89; GLN-105; GLY-127 AND GLN-720.
[17]"Mutations in the pre-replication complex cause Meier-Gorlin syndrome."
Bicknell L.S., Bongers E.M., Leitch A., Brown S., Schoots J., Harley M.E., Aftimos S., Al-Aama J.Y., Bober M., Brown P.A., van Bokhoven H., Dean J., Edrees A.Y., Feingold M., Fryer A., Hoefsloot L.H., Kau N., Knoers N.V. expand/collapse author list , Mackenzie J., Opitz J.M., Sarda P., Ross A., Temple I.K., Toutain A., Wise C.A., Wright M., Jackson A.P.
Nat. Genet. 43:356-359(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MGORS1 GLN-105.
[18]"Mutations in origin recognition complex gene ORC4 cause Meier-Gorlin syndrome."
Guernsey D.L., Matsuoka M., Jiang H., Evans S., Macgillivray C., Nightingale M., Perry S., Ferguson M., LeBlanc M., Paquette J., Patry L., Rideout A.L., Thomas A., Orr A., McMaster C.R., Michaud J.L., Deal C., Langlois S. expand/collapse author list , Superneau D.W., Parkash S., Ludman M., Skidmore D.L., Samuels M.E.
Nat. Genet. 43:360-364(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MGORS1 GLN-105 AND TRP-666.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40152 mRNA. Translation: AAC50325.1.
U43416 mRNA. Translation: AAA86260.1.
AL513218 Genomic DNA. Translation: CAI12288.1.
CH471059 Genomic DNA. Translation: EAX06783.1.
CH471059 Genomic DNA. Translation: EAX06784.1.
CCDSCCDS566.1.
PIRG02329.
RefSeqNP_001177747.1. NM_001190818.1.
NP_001177748.1. NM_001190819.1.
NP_004144.2. NM_004153.3.
UniGeneHs.17908.

3D structure databases

ProteinModelPortalQ13415.
SMRQ13415. Positions 12-168, 500-732.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111040. 25 interactions.
DIPDIP-29688N.
IntActQ13415. 19 interactions.
MINTMINT-1201992.

PTM databases

PhosphoSiteQ13415.

Polymorphism databases

DMDM76803807.

Proteomic databases

MaxQBQ13415.
PaxDbQ13415.
PRIDEQ13415.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371566; ENSP00000360621; ENSG00000085840.
ENST00000371568; ENSP00000360623; ENSG00000085840.
GeneID4998.
KEGGhsa:4998.
UCSCuc001ctt.3. human.

Organism-specific databases

CTD4998.
GeneCardsGC01M052839.
HGNCHGNC:8487. ORC1.
HPAHPA027450.
MIM224690. phenotype.
601902. gene.
neXtProtNX_Q13415.
Orphanet2554. Ear-patella-short stature syndrome.
PharmGKBPA32808.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1474.
HOGENOMHOG000231132.
HOVERGENHBG007873.
InParanoidQ13415.
KOK02603.
OMAIYSQHVA.
OrthoDBEOG7QG44J.
PhylomeDBQ13415.
TreeFamTF313743.

Enzyme and pathway databases

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

Gene expression databases

BgeeQ13415.
CleanExHS_ORC1L.
GenevestigatorQ13415.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR001025. BAH_dom.
IPR015163. Cdc6_C_dom.
IPR027417. P-loop_NTPase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF01426. BAH. 1 hit.
PF09079. Cdc6_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00439. BAH. 1 hit.
SM01074. Cdc6_C. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS51038. BAH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiORC1.
GenomeRNAi4998.
NextBio19240.
PROQ13415.
SOURCESearch...

Entry information

Entry nameORC1_HUMAN
AccessionPrimary (citable) accession number: Q13415
Secondary accession number(s): D3DQ34, Q13471, Q5T0F5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 27, 2005
Last modified: July 9, 2014
This is version 128 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 1

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