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Protein

DNA replication licensing factor MCM2

Gene

MCM2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri329 – 35527C4-typeSequence AnalysisAdd
BLAST
Nucleotide bindingi523 – 5308ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: ProtInc
  3. DNA helicase activity Source: InterPro
  4. DNA replication origin binding Source: Ensembl
  5. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cell cycle Source: ProtInc
  2. cellular response to interleukin-4 Source: Ensembl
  3. DNA replication Source: Reactome
  4. DNA replication initiation Source: UniProtKB
  5. DNA strand elongation involved in DNA replication Source: Reactome
  6. DNA unwinding involved in DNA replication Source: Ensembl
  7. G1/S transition of mitotic cell cycle Source: Reactome
  8. mitotic cell cycle Source: Reactome
  9. nucleosome assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1156. Orc1 removal from chromatin.
REACT_207. Removal of licensing factors from origins.
REACT_2148. Switching of origins to a post-replicative state.
REACT_2243. Assembly of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.
REACT_6776. Unwinding of DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor MCM2 (EC:3.6.4.12)
Alternative name(s):
Minichromosome maintenance protein 2 homolog
Nuclear protein BM28
Gene namesi
Name:MCM2
Synonyms:BM28, CCNL1, CDCL1, KIAA0030
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6944. MCM2.

Subcellular locationi

  1. Nucleus 1 Publication

GO - Cellular componenti

  1. chromatin Source: UniProtKB
  2. cytoplasm Source: HPA
  3. MCM complex Source: UniProtKB
  4. microtubule cytoskeleton Source: HPA
  5. nuclear origin of replication recognition complex Source: Ensembl
  6. nucleoplasm Source: HPA
  7. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi27 – 271S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-41 and A-139. 1 Publication
Mutagenesisi41 – 411S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-139. 1 Publication
Mutagenesisi108 – 1081S → A: Reduces phosphorylation by ATR. 1 Publication
Mutagenesisi139 – 1391S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-41. 1 Publication

Organism-specific databases

PharmGKBiPA164742061.

Polymorphism and mutation databases

DMDMi41019490.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 904903DNA replication licensing factor MCM2PRO_0000194087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine5 Publications
Modified residuei12 – 121PhosphoserineBy similarity
Modified residuei13 – 131Phosphoserine3 Publications
Modified residuei26 – 261Phosphoserine2 Publications
Modified residuei27 – 271Phosphoserine6 Publications
Modified residuei39 – 391Phosphothreonine1 Publication
Modified residuei40 – 401Phosphoserine; by CDC72 Publications
Modified residuei41 – 411Phosphoserine5 Publications
Modified residuei53 – 531Phosphoserine; by CDC73 Publications
Modified residuei59 – 591Phosphothreonine1 Publication
Modified residuei108 – 1081Phosphoserine; by ATR5 Publications
Modified residuei137 – 1371Phosphotyrosine1 Publication
Modified residuei139 – 1391Phosphoserine6 Publications
Modified residuei216 – 2161N6-acetyllysine1 Publication
Modified residuei381 – 3811Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on Ser-108 by ATR in proliferating cells. Ser-108 proliferation is increased by genotoxic agents. Ser-40 is mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is only mediated by the CDC7-DBF4 complex. Phosphorylation by the CDC7-DBF4 complex during G1/S phase is required for the initiation of DNA replication.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP49736.
PaxDbiP49736.
PeptideAtlasiP49736.
PRIDEiP49736.

PTM databases

PhosphoSiteiP49736.

Miscellaneous databases

PMAP-CutDBP49736.

Expressioni

Gene expression databases

BgeeiP49736.
CleanExiHS_CCNL1.
HS_MCM2.
ExpressionAtlasiP49736. baseline and differential.
GenevestigatoriP49736.

Organism-specific databases

HPAiCAB000303.
HPA031495.
HPA031496.

Interactioni

Subunit structurei

Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (By simililarity). Interacts with DBF4 (By similarity). Interacts with KAT7. May interact with MCM10.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST2H4BP628053EBI-374819,EBI-302023
MCM3P252055EBI-374819,EBI-355153
MCM5P339925EBI-374819,EBI-359410
MCM6Q1456612EBI-374819,EBI-374900
MCM7P3399321EBI-374819,EBI-355924
MCMBPQ9BTE34EBI-374819,EBI-749378
SNF8Q96H208EBI-374819,EBI-747719

Protein-protein interaction databases

BioGridi110339. 98 interactions.
DIPiDIP-31732N.
IntActiP49736. 47 interactions.
MINTiMINT-5004296.
STRINGi9606.ENSP00000265056.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UUZX-ray2.90C69-138[»]
ProteinModelPortaliP49736.
SMRiP49736. Positions 199-798.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini473 – 679207MCMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 257256Interaction with KAT7By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi655 – 6584Arginine finger

Sequence similaritiesi

Belongs to the MCM family.Curated
Contains 1 MCM domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri329 – 35527C4-typeSequence AnalysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG1241.
GeneTreeiENSGT00740000115337.
HOVERGENiHBG106398.
InParanoidiP49736.
KOiK02540.
OMAiKMHLREY.
OrthoDBiEOG71VSRZ.
PhylomeDBiP49736.
TreeFamiTF300772.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01658. MCMPROTEIN2.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49736-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAESSESFTM ASSPAQRRRG NDPLTSSPGR SSRRTDALTS SPGRDLPPFE
60 70 80 90 100
DESEGLLGTE GPLEEEEDGE ELIGDGMERD YRAIPELDAY EAEGLALDDE
110 120 130 140 150
DVEELTASQR EAAERAMRQR DREAGRGLGR MRRGLLYDSD EEDEERPARK
160 170 180 190 200
RRQVERATED GEEDEEMIES IENLEDLKGH SVREWVSMAG PRLEIHHRFK
210 220 230 240 250
NFLRTHVDSH GHNVFKERIS DMCKENRESL VVNYEDLAAR EHVLAYFLPE
260 270 280 290 300
APAELLQIFD EAALEVVLAM YPKYDRITNH IHVRISHLPL VEELRSLRQL
310 320 330 340 350
HLNQLIRTSG VVTSCTGVLP QLSMVKYNCN KCNFVLGPFC QSQNQEVKPG
360 370 380 390 400
SCPECQSAGP FEVNMEETIY QNYQRIRIQE SPGKVAAGRL PRSKDAILLA
410 420 430 440 450
DLVDSCKPGD EIELTGIYHN NYDGSLNTAN GFPVFATVIL ANHVAKKDNK
460 470 480 490 500
VAVGELTDED VKMITSLSKD QQIGEKIFAS IAPSIYGHED IKRGLALALF
510 520 530 540 550
GGEPKNPGGK HKVRGDINVL LCGDPGTAKS QFLKYIEKVS SRAIFTTGQG
560 570 580 590 600
ASAVGLTAYV QRHPVSREWT LEAGALVLAD RGVCLIDEFD KMNDQDRTSI
610 620 630 640 650
HEAMEQQSIS ISKAGIVTSL QARCTVIAAA NPIGGRYDPS LTFSENVDLT
660 670 680 690 700
EPIISRFDIL CVVRDTVDPV QDEMLARFVV GSHVRHHPSN KEEEGLANGS
710 720 730 740 750
AAEPAMPNTY GVEPLPQEVL KKYIIYAKER VHPKLNQMDQ DKVAKMYSDL
760 770 780 790 800
RKESMATGSI PITVRHIESM IRMAEAHARI HLRDYVIEDD VNMAIRVMLE
810 820 830 840 850
SFIDTQKFSV MRSMRKTFAR YLSFRRDNNE LLLFILKQLV AEQVTYQRNR
860 870 880 890 900
FGAQQDTIEV PEKDLVDKAR QINIHNLSAF YDSELFRMNK FSHDLKRKMI

LQQF
Length:904
Mass (Da):101,896
Last modified:January 16, 2004 - v4
Checksum:i52C6DC61F128B404
GO

Sequence cautioni

The sequence BAA04642.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA12177.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA47749.1 differs from that shown. Reason: Frameshift at positions 115, 124, 127, 129, 154, 158, 773 and 811. Curated
The sequence CAA47749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → S in CAA47749 (PubMed:8175912).Curated
Sequence conflicti109 – 1091Q → R in CAA47749 (PubMed:8175912).Curated
Sequence conflicti388 – 3881G → R in CAA47749 (PubMed:8175912).Curated
Sequence conflicti407 – 4082KP → NA in CAA47749 (PubMed:8175912).Curated
Sequence conflicti407 – 4082KP → NA in BAA12177 (Ref. 5) Curated
Sequence conflicti495 – 4951L → P in CAA47749 (PubMed:8175912).Curated
Sequence conflicti555 – 5562GL → AV in CAA47749 (PubMed:8175912).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681D → E.1 Publication
Corresponds to variant rs3087452 [ dbSNP | Ensembl ].
VAR_021111
Natural varianti135 – 1351L → F.1 Publication
Corresponds to variant rs2307314 [ dbSNP | Ensembl ].
VAR_021112
Natural varianti166 – 1661E → Q.1 Publication
Corresponds to variant rs1048225 [ dbSNP | Ensembl ].
VAR_033298
Natural varianti396 – 3961A → T.1 Publication
Corresponds to variant rs3087450 [ dbSNP | Ensembl ].
VAR_016137
Natural varianti501 – 5011G → R.1 Publication
Corresponds to variant rs13087457 [ dbSNP | Ensembl ].
VAR_033299
Natural varianti667 – 6671V → M.1 Publication
Corresponds to variant rs2307311 [ dbSNP | Ensembl ].
VAR_016138
Natural varianti727 – 7271A → T.2 Publications
Corresponds to variant rs2307313 [ dbSNP | Ensembl ].
VAR_016139

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67334 mRNA. Translation: CAA47749.1. Sequence problems.
D21063 mRNA. Translation: BAA04642.1. Different initiation.
AY675259 Genomic DNA. Translation: AAT70723.1.
BC006165 mRNA. Translation: AAH06165.3.
BC007670 mRNA. Translation: AAH07670.2.
BC007938 mRNA. Translation: AAH07938.2.
BC014272 mRNA. Translation: AAH14272.2.
BC017258 mRNA. Translation: AAH17258.2.
BC017490 mRNA. Translation: AAH17490.2.
BC030131 mRNA. Translation: AAH30131.2.
D83987 mRNA. Translation: BAA12177.1. Different initiation.
BT009734 mRNA. Translation: AAP88736.1.
CCDSiCCDS3043.1.
PIRiS42228.
RefSeqiNP_004517.2. NM_004526.3.
UniGeneiHs.477481.

Genome annotation databases

EnsembliENST00000265056; ENSP00000265056; ENSG00000073111.
GeneIDi4171.
KEGGihsa:4171.
UCSCiuc003ejp.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67334 mRNA. Translation: CAA47749.1. Sequence problems.
D21063 mRNA. Translation: BAA04642.1. Different initiation.
AY675259 Genomic DNA. Translation: AAT70723.1.
BC006165 mRNA. Translation: AAH06165.3.
BC007670 mRNA. Translation: AAH07670.2.
BC007938 mRNA. Translation: AAH07938.2.
BC014272 mRNA. Translation: AAH14272.2.
BC017258 mRNA. Translation: AAH17258.2.
BC017490 mRNA. Translation: AAH17490.2.
BC030131 mRNA. Translation: AAH30131.2.
D83987 mRNA. Translation: BAA12177.1. Different initiation.
BT009734 mRNA. Translation: AAP88736.1.
CCDSiCCDS3043.1.
PIRiS42228.
RefSeqiNP_004517.2. NM_004526.3.
UniGeneiHs.477481.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UUZX-ray2.90C69-138[»]
ProteinModelPortaliP49736.
SMRiP49736. Positions 199-798.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110339. 98 interactions.
DIPiDIP-31732N.
IntActiP49736. 47 interactions.
MINTiMINT-5004296.
STRINGi9606.ENSP00000265056.

PTM databases

PhosphoSiteiP49736.

Polymorphism and mutation databases

DMDMi41019490.

Proteomic databases

MaxQBiP49736.
PaxDbiP49736.
PeptideAtlasiP49736.
PRIDEiP49736.

Protocols and materials databases

DNASUi4171.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265056; ENSP00000265056; ENSG00000073111.
GeneIDi4171.
KEGGihsa:4171.
UCSCiuc003ejp.4. human.

Organism-specific databases

CTDi4171.
GeneCardsiGC03P127317.
HGNCiHGNC:6944. MCM2.
HPAiCAB000303.
HPA031495.
HPA031496.
MIMi116945. gene.
neXtProtiNX_P49736.
PharmGKBiPA164742061.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1241.
GeneTreeiENSGT00740000115337.
HOVERGENiHBG106398.
InParanoidiP49736.
KOiK02540.
OMAiKMHLREY.
OrthoDBiEOG71VSRZ.
PhylomeDBiP49736.
TreeFamiTF300772.

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1156. Orc1 removal from chromatin.
REACT_207. Removal of licensing factors from origins.
REACT_2148. Switching of origins to a post-replicative state.
REACT_2243. Assembly of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.
REACT_6776. Unwinding of DNA.

Miscellaneous databases

ChiTaRSiMCM2. human.
GeneWikiiMCM2.
GenomeRNAii4171.
NextBioi16428.
PMAP-CutDBP49736.
PROiP49736.
SOURCEiSearch...

Gene expression databases

BgeeiP49736.
CleanExiHS_CCNL1.
HS_MCM2.
ExpressionAtlasiP49736. baseline and differential.
GenevestigatoriP49736.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01658. MCMPROTEIN2.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human nuclear protein with sequence homology to a family of early S phase proteins is required for entry into S phase and for cell division."
    Todorov I.T., Pepperkok R., Philipova R.N., Kearsey S.E., Ansorge W., Werner D.
    J. Cell Sci. 107:253-265(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, VARIANT GLN-166.
    Tissue: Colon carcinoma.
  2. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
    Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
    DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  3. NIEHS SNPs program
    Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-68; PHE-135; THR-396; MET-667 AND THR-727.
  4. "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], VARIANTS ARG-501 AND THR-727.
    Tissue: Brain, Lung, Lymph, Muscle, Placenta and Uterus.
  5. "Homo sapiens DNA replication licensing factor (huMCM2)."
    Mimura S., Nishimoto S., Kubota Y., Takisawa H., Nojima H.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-904.
    Tissue: Cervix carcinoma.
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-904.
  7. "The human gene for nuclear protein BM28 (CDCL1), a new member of the early S-phase family of proteins, maps to chromosome band 3q21."
    Mincheva A., Todorov I.T., Werner D., Fink T.M., Lichter P.
    Cytogenet. Cell Genet. 65:276-277(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL LOCATION.
  8. "A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex."
    Ishimi Y.
    J. Biol. Chem. 272:24508-24513(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX.
  9. "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.
  10. "Minichromosome maintenance proteins are direct targets of the ATM and ATR checkpoint kinases."
    Cortez D., Glick G., Elledge S.J.
    Proc. Natl. Acad. Sci. U.S.A. 101:10078-10083(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-108, MUTAGENESIS OF SER-108.
  11. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Essential role of phosphorylation of MCM2 by Cdc7/Dbf4 in the initiation of DNA replication in mammalian cells."
    Tsuji T., Ficarro S.B., Jiang W.
    Mol. Biol. Cell 17:4459-4472(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-27; SER-41; SER-53; SER-108 AND SER-139, MUTAGENESIS OF SER-27; SER-41 AND SER-139, IDENTIFICATION IN THE MCM2-7 COMPLEX, ATPASE ACTIVITY OF THE MCM2-7 COMPLEX.
  13. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
    Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
    Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KAT7.
  14. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  16. "Cdc7 is an active kinase in human cancer cells undergoing replication stress."
    Tenca P., Brotherton D., Montagnoli A., Rainoldi S., Albanese C., Santocanale C.
    J. Biol. Chem. 282:208-215(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-40 AND SER-53.
  17. "Identification and characterization of a novel component of the human minichromosome maintenance complex."
    Sakwe A.M., Nguyen T., Athanasopoulos V., Shire K., Frappier L.
    Mol. Cell. Biol. 27:3044-3055(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  19. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  21. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; THR-39; SER-40; SER-41; SER-53 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-59; SER-108 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  25. "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-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-27; SER-41; SER-108 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-26; SER-27; SER-41; SER-139 AND SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  29. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  31. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-27; TYR-137 AND SER-139, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiMCM2_HUMAN
AccessioniPrimary (citable) accession number: P49736
Secondary accession number(s): Q14577
, Q15023, Q8N2V1, Q969W7, Q96AE1, Q9BRM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 16, 2004
Last modified: April 29, 2015
This is version 167 of the entry and version 4 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

Miscellaneous

Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. Specifically a MCM467 subcomplex is shown to have in vitro helicase activity which is inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed physiological active complex.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.