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P97310 (MCM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA replication licensing factor MCM2

EC=3.6.4.12
Alternative name(s):
Minichromosome maintenance protein 2 homolog
Nuclear protein BM28
Gene names
Name:Mcm2
Synonyms:Bm28, Cdcl1, Kiaa0030, Mcmd2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length904 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5. Interacts with KAT7 and DBF4. May interact with MCM10 By similarity. Ref.8 Ref.9

Subcellular location

Nucleus Probable.

Post-translational modification

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 By similarity.

Sequence similarities

Belongs to the MCM family.

Contains 1 MCM domain.

Sequence caution

The sequence BAC97849.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell cycle
DNA replication
   Cellular componentNucleus
   DomainZinc-finger
   LigandATP-binding
DNA-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication initiation

Traceable author statement PubMed 10531422. Source: MGI

DNA unwinding involved in DNA replication

Inferred from direct assay PubMed 10531422. Source: MGI

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to interleukin-4

Inferred from direct assay Ref.7. Source: MGI

nucleosome assembly

Inferred from direct assay PubMed 10531422. Source: MGI

   Cellular_componentMCM complex

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin

Inferred from electronic annotation. Source: Ensembl

nuclear origin of replication recognition complex

Inferred from direct assay PubMed 12941272. Source: MGI

nucleus

Inferred from direct assay PubMed 10531422. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA helicase activity

Inferred from electronic annotation. Source: InterPro

DNA replication origin binding

Inferred from direct assay PubMed 12941272. Source: MGI

histone binding

Inferred from direct assay PubMed 10531422. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 904903DNA replication licensing factor MCM2
PRO_0000194088

Regions

Domain473 – 680208MCM
Zinc finger329 – 35527C4-type Potential
Nucleotide binding523 – 5308ATP Potential
Region2 – 257256Interaction with KAT7
Motif655 – 6584Arginine finger

Amino acid modifications

Modified residue21N-acetylalanine Ref.13
Modified residue121Phosphoserine Ref.13
Modified residue211Phosphoserine Ref.11 Ref.12 Ref.13
Modified residue261Phosphoserine By similarity
Modified residue271Phosphoserine Ref.12 Ref.13
Modified residue391Phosphothreonine By similarity
Modified residue401Phosphoserine; by CDC7 By similarity
Modified residue411Phosphoserine By similarity
Modified residue531Phosphoserine; by CDC7 By similarity
Modified residue591Phosphothreonine By similarity
Modified residue1081Phosphoserine By similarity
Modified residue1391Phosphoserine Ref.12 Ref.13
Modified residue1401Phosphoserine Ref.12 Ref.13
Modified residue2161N6-acetyllysine By similarity
Modified residue3811Phosphoserine By similarity

Experimental info

Mutagenesis2371L → P: Impairs interaction with KAT7. Ref.9
Sequence conflict701E → G in AAC16250. Ref.3
Sequence conflict1351L → P in AAC16250. Ref.3
Sequence conflict1851W → R in BAA22148. Ref.1
Sequence conflict2711Y → H in AAC16250. Ref.3
Sequence conflict5061N → D in AAC36510. Ref.7
Sequence conflict5211L → S in AAC36510. Ref.7
Sequence conflict6481D → N in AAC36510. Ref.7
Sequence conflict8221L → I in AAC16250. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P97310 [UniParc].

Last modified April 13, 2004. Version 3.
Checksum: 7B61C13DAD1CAC58

FASTA904102,078
        10         20         30         40         50         60 
MAESSESLSA SSPARQRRRI SDPLTSSPGR SSRRADALTS SPGRDLPPFE DESEGLLGTE 

        70         80         90        100        110        120 
GPMEEEEDGE ELIGDGMERD YRPIPELDVY EAEGLALDDE DVEELTASQR EAAERTMRQR 

       130        140        150        160        170        180 
DREAGRGLGR MRRGLLYDSS EEDEERPARK RRHVERATED GEEDEEMIES IENLEDLKGH 

       190        200        210        220        230        240 
SVREWVSMAG PRLEIHHRFK NFLRTHVDSH GHNVFKERIS DMCKENRESL VVNYEDLAAR 

       250        260        270        280        290        300 
EHVLAYFLPE APAELLQIFD EAALEVVLAM YPKYDRITNH IHVRISHLPL VEELRSLRQL 

       310        320        330        340        350        360 
HLNQLIRTSG VVTSCTGVLP QLSMVKYNCS KCNFVLGPFC QSQNQEVKPG SCPECQSAGP 

       370        380        390        400        410        420 
FEINMEETIY QNYQRIRIQE SPGKVAAGRL PRSKDAILLA DLVDSCKPGD EIELTGIYHN 

       430        440        450        460        470        480 
NYDGSLNTAN GFPVFATIIL ANHVAKKDNK VAVGELTDED VKMITGLSKD QQIGEKIFAS 

       490        500        510        520        530        540 
IAPSIYGHED IKRGLALALF GGEPKNPGGK HKVRGDINVL LCGDPGTAKS QFLKYIEKVS 

       550        560        570        580        590        600 
SRAIFTTGQG ASAVGLTAYV QRHPVSREWT LEAGALVLAD RGVCLIDEFD KMNDQDRTSI 

       610        620        630        640        650        660 
HEAMEQQSIS ISKAGIVTSL QARCTVIAAA NPIGGRYDPS LTFSENVDLT EPIISRFDVL 

       670        680        690        700        710        720 
CVVRDTVDPV QDEMLARFVV GSHVRHHPSN KKDEGLTNGG TLEPAMPNTY GVEPLPQEVL 

       730        740        750        760        770        780 
KKYIIYAKER VRPKLNQMDQ DKVARMYSDL RKESMATGSI PITVRHIESM IRMAEAHARM 

       790        800        810        820        830        840 
HLRDYVMEDD VNMAIRVMME SFIDTQKFSV MRSMRKTFAR YLSFRRDNND LLLFILKQLV 

       850        860        870        880        890        900 
AEQVTYQRNR FGAQQDTIEI PEKDLMDKAR QINIHNLSAF YDSDLFKFNK FSRDLKRKLI 


LQQF 

« Hide

References

« Hide 'large scale' references
[1]"Mouse MCM proteins: complex formation and transportation to the nucleus."
Kimura H., Ohtomo T., Yamaguchi M., Ishii A., Sugimoto K.
Genes Cells 1:977-993(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 217-224; 376-384 AND 477-487.
[2]Kimura H.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Clone 10d/BM28 (CDCL1), an early S-phase protein, is an important growth regulator of melanoma."
Spanjaard R.A., Lee P.J., Sarkar S., Goedegebuure P.S., Eberlein T.J.
Cancer Res. 57:5122-5128(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Melanoma.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryonic tail.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
Tissue: Thymus.
[6]"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].
Strain: C57BL/6.
Tissue: Brain.
[7]"Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
Chu C.C., Paul W.E.
Mol. Immunol. 35:487-502(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 477-668.
Strain: BALB/c.
Tissue: Spleen.
[8]"Identification, characterization and chromosomal localization of the cognate human and murine DBF4 genes."
Lepke M., Puetter V., Staib C., Kneissl M., Berger C., Hoehn K., Nanda I., Schmid M., Grummt F.
Mol. Gen. Genet. 262:220-229(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DBF4.
Strain: C57BL/6J.
Tissue: Egg and Embryo.
[9]"Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1."
Burke T.W., Cook J.G., Asano M., Nevins J.R.
J. Biol. Chem. 276:15397-15408(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KAT7, MUTAGENESIS OF LEU-237.
[10]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[11]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Teratocarcinoma.
[12]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-27; SER-139 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[13]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-21; SER-27; SER-139 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D86725 mRNA. Translation: BAA22148.1.
AF004105 mRNA. Translation: AAC16250.1.
AK129039 mRNA. Translation: BAC97849.1. Different initiation.
AK088156 mRNA. Translation: BAC40178.1.
BC055318 mRNA. Translation: AAH55318.1.
U89403 mRNA. Translation: AAC36510.1.
PIRT10067.
RefSeqNP_032590.2. NM_008564.2.
UniGeneMm.16711.

3D structure databases

ProteinModelPortalP97310.
SMRP97310. Positions 199-798.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201346. 3 interactions.
DIPDIP-33057N.
IntActP97310. 7 interactions.
MINTMINT-4101561.

PTM databases

PhosphoSiteP97310.

Proteomic databases

PaxDbP97310.
PRIDEP97310.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000058011; ENSMUSP00000061923; ENSMUSG00000002870.
GeneID17216.
KEGGmmu:17216.
UCSCuc009cvx.2. mouse.

Organism-specific databases

CTD4171.
MGIMGI:105380. Mcm2.
RougeSearch...

Phylogenomic databases

eggNOGCOG1241.
GeneTreeENSGT00740000115337.
HOVERGENHBG106398.
InParanoidP97310.
KOK02540.
OMARIHSEIH.
OrthoDBEOG71VSRZ.
PhylomeDBP97310.
TreeFamTF300772.

Gene expression databases

ArrayExpressP97310.
BgeeP97310.
GenevestigatorP97310.

Family and domain databases

Gene3D2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProIPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSPR01657. MCMFAMILY.
PR01658. MCMPROTEIN2.
SMARTSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMCM2. mouse.
NextBio291606.
PMAP-CutDBP97310.
PROP97310.
SOURCESearch...

Entry information

Entry nameMCM2_MOUSE
AccessionPrimary (citable) accession number: P97310
Secondary accession number(s): O08971, O89057, Q8C2R0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 13, 2004
Last modified: April 16, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot