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Protein

Origin recognition complex subunit 1

Gene

ORC1

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 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931Histone H4K20me2By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi534 – 5418ATPSequence Analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: Ensembl
  • DNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1156. Orc1 removal from chromatin.
REACT_1181. Association of licensing factors with the pre-replicative complex.
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_471. E2F mediated regulation of DNA replication.
REACT_567. Assembly of the ORC complex at the origin of replication.
REACT_6769. Activation of ATR in response to replication stress.
REACT_683. G1/S-Specific Transcription.

Names & Taxonomyi

Protein namesi
Recommended name:
Origin recognition complex subunit 1
Alternative name(s):
Replication control protein 1
Gene namesi
Name:ORC1
Synonyms:ORC1L, PARC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:8487. ORC1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • nuclear origin of replication recognition complex Source: UniProtKB
  • nucleolus Source: HPA
  • 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 1 (MGORS1)3 Publications

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:224690
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891F → S in MGORS1. 1 Publication
VAR_065481
Natural varianti105 – 1051R → Q in MGORS1. 3 Publications
VAR_065482
Natural varianti127 – 1271E → G in MGORS1. 1 Publication
VAR_065483
Natural varianti666 – 6661R → W in MGORS1. 1 Publication
Corresponds to variant rs201253919 [ dbSNP | Ensembl ].
VAR_065484
Natural varianti720 – 7201R → Q in MGORS1. 1 Publication
VAR_065485

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

MIMi224690. phenotype.
Orphaneti2554. Ear-patella-short stature syndrome.
PharmGKBiPA32808.

Polymorphism and mutation databases

BioMutaiORC1.
DMDMi76803807.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 861861Origin recognition complex subunit 1PRO_0000127067Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031Phosphothreonine2 Publications
Modified residuei273 – 2731Phosphoserine2 Publications
Modified residuei287 – 2871Phosphoserine1 Publication
Modified residuei326 – 3261N6-acetyllysine1 Publication
Modified residuei337 – 3371Phosphothreonine1 Publication
Modified residuei340 – 3401Phosphoserine1 Publication
Modified residuei417 – 4171Phosphoserine1 Publication
Modified residuei420 – 4201Phosphoserine1 Publication
Modified residuei478 – 4781Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated during mitosis.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13415.
PaxDbiQ13415.
PRIDEiQ13415.

PTM databases

PhosphoSiteiQ13415.

Expressioni

Developmental stagei

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).1 Publication

Gene expression databases

BgeeiQ13415.
CleanExiHS_ORC1L.
GenevisibleiQ13415. HS.

Organism-specific databases

HPAiHPA027450.

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 CDC6 and KAT7/HBO1. Interacts with LRWD1 predominantly during the G1 phase and with less affinity during mitosis, when phosphorylated.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EBNA1P032112EBI-374847,EBI-996522From a different organism.
ORC2Q134166EBI-374847,EBI-374957
ORC3Q9UBD512EBI-374847,EBI-374916
ORC5O439135EBI-374847,EBI-374928
SKP2Q133092EBI-374847,EBI-456291
TERF2Q155542EBI-374847,EBI-706637

Protein-protein interaction databases

BioGridi111040. 25 interactions.
DIPiDIP-29688N.
IntActiQ13415. 19 interactions.
MINTiMINT-1201992.
STRINGi9606.ENSP00000360621.

Structurei

3D structure databases

ProteinModelPortaliQ13415.
SMRiQ13415. Positions 12-168, 500-732.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 171127BAHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni501 – 861361Necessary and sufficient for ORC complex assemblyAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the ORC1 family.Curated
Contains 1 BAH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1474.
GeneTreeiENSGT00530000063498.
HOGENOMiHOG000231132.
HOVERGENiHBG007873.
InParanoidiQ13415.
KOiK02603.
OMAiCTRGSPQ.
OrthoDBiEOG7QG44J.
PhylomeDBiQ13415.
TreeFamiTF313743.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR001025. BAH_dom.
IPR015163. Cdc6_C_dom.
IPR027417. P-loop_NTPase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF01426. BAH. 1 hit.
PF09079. Cdc6_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00439. BAH. 1 hit.
SM01074. Cdc6_C. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51038. BAH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13415-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHYPTRLKT RKTYSWVGRP LLDRKLHYQT YREMCVKTEG CSTEIHIQIG
60 70 80 90 100
QFVLIEGDDD ENPYVAKLLE LFEDDSDPPP KKRARVQWFV RFCEVPACKR
110 120 130 140 150
HLLGRKPGAQ EIFWYDYPAC DSNINAETII GLVRVIPLAP KDVVPTNLKN
160 170 180 190 200
EKTLFVKLSW NEKKFRPLSS ELFAELNKPQ ESAAKCQKPV RAKSKSAESP
210 220 230 240 250
SWTPAEHVAK RIESRHSASK SRQTPTHPLT PRARKRLELG NLGNPQMSQQ
260 270 280 290 300
TSCASLDSPG RIKRKVAFSE ITSPSKRSQP DKLQTLSPAL KAPEKTRETG
310 320 330 340 350
LSYTEDDKKA SPEHRIILRT RIAASKTIDI REERTLTPIS GGQRSSVVPS
360 370 380 390 400
VILKPENIKK RDAKEAKAQN EATSTPHRIR RKSSVLTMNR IRQQLRFLGN
410 420 430 440 450
SKSDQEEKEI LPAAEISDSS SDEEEASTPP LPRRAPRTVS RNLRSSLKSS
460 470 480 490 500
LHTLTKVPKK SLKPRTPRCA APQIRSRSLA AQEPASVLEE ARLRLHVSAV
510 520 530 540 550
PESLPCREQE FQDIYNFVES KLLDHTGGCM YISGVPGTGK TATVHEVIRC
560 570 580 590 600
LQQAAQANDV PPFQYIEVNG MKLTEPHQVY VQILQKLTGQ KATANHAAEL
610 620 630 640 650
LAKQFCTRGS PQETTVLLVD ELDLLWTHKQ DIMYNLFDWP THKEARLVVL
660 670 680 690 700
AIANTMDLPE RIMMNRVSSR LGLTRMCFQP YTYSQLQQIL RSRLKHLKAF
710 720 730 740 750
EDDAIQLVAR KVAALSGDAR RCLDICRRAT EICEFSQQKP DSPGLVTIAH
760 770 780 790 800
SMEAVDEMFS SSYITAIKNS SVLEQSFLRA ILAEFRRSGL EEATFQQIYS
810 820 830 840 850
QHVALCRMEG LPYPTMSETM AVCSHLGSCR LLLVEPSRND LLLRVRLNVS
860
QDDVLYALKD E
Length:861
Mass (Da):97,350
Last modified:September 27, 2005 - v2
Checksum:i5C594553F7F808E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti582 – 5821Q → H in AAC50325 (PubMed:7502077).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191R → S.
Corresponds to variant rs3087473 [ dbSNP | Ensembl ].
VAR_014507
Natural varianti89 – 891F → S in MGORS1. 1 Publication
VAR_065481
Natural varianti105 – 1051R → Q in MGORS1. 3 Publications
VAR_065482
Natural varianti127 – 1271E → G in MGORS1. 1 Publication
VAR_065483
Natural varianti180 – 1801Q → H.
Corresponds to variant rs3087482 [ dbSNP | Ensembl ].
VAR_014508
Natural varianti190 – 1901V → M.
Corresponds to variant rs3087477 [ dbSNP | Ensembl ].
VAR_014509
Natural varianti372 – 3721A → V.
Corresponds to variant rs3087476 [ dbSNP | Ensembl ].
VAR_014510
Natural varianti441 – 4411R → M.
Corresponds to variant rs3087472 [ dbSNP | Ensembl ].
VAR_014511
Natural varianti456 – 4561K → E.
Corresponds to variant rs3087470 [ dbSNP | Ensembl ].
VAR_014512
Natural varianti466 – 4661T → M.
Corresponds to variant rs3087481 [ dbSNP | Ensembl ].
VAR_014513
Natural varianti469 – 4691C → Y.
Corresponds to variant rs3087483 [ dbSNP | Ensembl ].
VAR_014514
Natural varianti666 – 6661R → W in MGORS1. 1 Publication
Corresponds to variant rs201253919 [ dbSNP | Ensembl ].
VAR_065484
Natural varianti720 – 7201R → Q in MGORS1. 1 Publication
VAR_065485
Natural varianti816 – 8161M → T.
Corresponds to variant rs34521609 [ dbSNP | Ensembl ].
VAR_050426

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS566.1.
PIRiG02329.
RefSeqiNP_001177747.1. NM_001190818.1.
NP_001177748.1. NM_001190819.1.
NP_004144.2. NM_004153.3.
UniGeneiHs.17908.

Genome annotation databases

EnsembliENST00000371566; ENSP00000360621; ENSG00000085840.
ENST00000371568; ENSP00000360623; ENSG00000085840.
GeneIDi4998.
KEGGihsa:4998.
UCSCiuc001ctt.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS566.1.
PIRiG02329.
RefSeqiNP_001177747.1. NM_001190818.1.
NP_001177748.1. NM_001190819.1.
NP_004144.2. NM_004153.3.
UniGeneiHs.17908.

3D structure databases

ProteinModelPortaliQ13415.
SMRiQ13415. Positions 12-168, 500-732.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111040. 25 interactions.
DIPiDIP-29688N.
IntActiQ13415. 19 interactions.
MINTiMINT-1201992.
STRINGi9606.ENSP00000360621.

PTM databases

PhosphoSiteiQ13415.

Polymorphism and mutation databases

BioMutaiORC1.
DMDMi76803807.

Proteomic databases

MaxQBiQ13415.
PaxDbiQ13415.
PRIDEiQ13415.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371566; ENSP00000360621; ENSG00000085840.
ENST00000371568; ENSP00000360623; ENSG00000085840.
GeneIDi4998.
KEGGihsa:4998.
UCSCiuc001ctt.3. human.

Organism-specific databases

CTDi4998.
GeneCardsiGC01M052839.
HGNCiHGNC:8487. ORC1.
HPAiHPA027450.
MIMi224690. phenotype.
601902. gene.
neXtProtiNX_Q13415.
Orphaneti2554. Ear-patella-short stature syndrome.
PharmGKBiPA32808.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1474.
GeneTreeiENSGT00530000063498.
HOGENOMiHOG000231132.
HOVERGENiHBG007873.
InParanoidiQ13415.
KOiK02603.
OMAiCTRGSPQ.
OrthoDBiEOG7QG44J.
PhylomeDBiQ13415.
TreeFamiTF313743.

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1156. Orc1 removal from chromatin.
REACT_1181. Association of licensing factors with the pre-replicative complex.
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_471. E2F mediated regulation of DNA replication.
REACT_567. Assembly of the ORC complex at the origin of replication.
REACT_6769. Activation of ATR in response to replication stress.
REACT_683. G1/S-Specific Transcription.

Miscellaneous databases

GeneWikiiORC1.
GenomeRNAii4998.
NextBioi19240.
PROiQ13415.
SOURCEiSearch...

Gene expression databases

BgeeiQ13415.
CleanExiHS_ORC1L.
GenevisibleiQ13415. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR001025. BAH_dom.
IPR015163. Cdc6_C_dom.
IPR027417. P-loop_NTPase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF01426. BAH. 1 hit.
PF09079. Cdc6_C. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00439. BAH. 1 hit.
SM01074. Cdc6_C. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51038. BAH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: VARIANT MGORS1 GLN-105.
  18. Cited for: VARIANTS MGORS1 GLN-105 AND TRP-666.

Entry informationi

Entry nameiORC1_HUMAN
AccessioniPrimary (citable) accession number: Q13415
Secondary accession number(s): D3DQ34, Q13471, Q5T0F5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 27, 2005
Last modified: July 22, 2015
This is version 137 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. 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.