Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P55861 (MCM2_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
DNA replication licensing factor mcm2

EC=3.6.4.12
Alternative name(s):
BM28-homolog
Minichromosome maintenance protein 2
Short name=xMCM2
p112
Gene names
Name:mcm2
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length886 AA.
Sequence statusComplete.
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. Ref.2 Ref.4 Ref.7

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Component of the mcm2-7 complex (RLF-M). The complex forms a toroidal hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-mcm7-mcm3-mcm5 (By simililarity). Ref.1 Ref.2 Ref.4 Ref.5 Ref.7

Subcellular location

Nucleus. Note: Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. Ref.2 Ref.4

Post-translational modification

May be in a phosphorylated state in the mitotic mcm complex. Phosphorylated in the interphase mcm complex. Phosphorylated by the cdc7-dbf4 and cdc7-dbf4b complexes. Ref.6 Ref.8

Sequence similarities

Belongs to the MCM family.

Contains 1 MCM domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mmcm3P497399EBI-876864,EBI-491720

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 886886DNA replication licensing factor mcm2
PRO_0000194089

Regions

Domain458 – 665208MCM
Zinc finger314 – 34027C4-type Potential
Nucleotide binding508 – 5158ATP Potential
Motif640 – 6434Arginine finger

Experimental info

Sequence conflict1691E → K in AAC60223. Ref.2
Sequence conflict4391G → R in BAA09948. Ref.1
Sequence conflict5631L → F in BAA09948. Ref.1
Sequence conflict7281M → I in BAA09948. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P55861 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: 524C7B3673E2B2DD

FASTA886100,262
        10         20         30         40         50         60 
MADSSESFNI ATSPRAGSRR DALTSSPGRD LPPFEDESEG MFGDGVVPEE EEDGEELIGD 

        70         80         90        100        110        120 
AMERDYRPIS ELDRYEVEGL DDEEDVEDLT ASQREAAEQS MRMRDREMGR ELGRMRRGLL 

       130        140        150        160        170        180 
YDSDEEEEDR PARKRRMAER AAEGAPEEDE EMIESIENLE DMKGHTVREW VSMAATRLEI 

       190        200        210        220        230        240 
YHRFKNFLRT HVDEHGHNVF KEKISDMCKE NKESLPVNYE DLAAREHVLA YFLPEAPAEM 

       250        260        270        280        290        300 
LKIFDEAAKE VVLVMYPKYD RIAREIHVRI SHLPLVEELR SLRQLHLNQL IRTSGVVTCC 

       310        320        330        340        350        360 
TGVLPQLSMV KYNCNKCNFI LGPFFQSQNQ EVRPGSCPEC QSFGPFEINM EETVYQNYQR 

       370        380        390        400        410        420 
ITIQESPGKV AAGRLPRSKD AILLADLVDS CKPGDEIELT GIYHNNYDGS LNTANGFPVF 

       430        440        450        460        470        480 
ATVILANHIT KKDDKVAVGE LTDEDVKAIV ALSKDERIGE RIFASIAPSI YGHEDIKRGL 

       490        500        510        520        530        540 
ALALFGGEAK NPGGKHKVRG DINVLLCGDP GTAKSQFLKY VEKVASRAVF TTGQGASAVG 

       550        560        570        580        590        600 
LTAYVQRHPV TKEWTLEAGA LVLADRGVCL IDEFDKMNDQ DRTSIHEAME QQSISISKAG 

       610        620        630        640        650        660 
IVTSLQARCT VIAASNPIGG RYDPSLTFSE NVDLTEPIVS RFDILCVVRD TVDPVQDEML 

       670        680        690        700        710        720 
ARFVVSSHIK HHPSSKDIAN GDAAEFALPN TFGVEALPQE VLKKYIMYAK EKIRPKLNQM 

       730        740        750        760        770        780 
DQDKVAKMYS DLRKESMATG SIPITVRHIE SMIRMAEAHA RMHLRDYVVE DDVNMAIRVM 

       790        800        810        820        830        840 
LESFIDTQKF SVMRSMRKTF ARYLAFRRDN NELLLFVLKQ LIAEQVTYQR NRYGAQQDTI 

       850        860        870        880 
EVPEKDLVDK ARQINIHNLS AFYDSDLFKM NKFTHDVKKK LIIQQF 

« Hide

References

« Hide 'large scale' references
[1]"Identification of two Xenopus laevis genes, xMCM2 and xCDC46, with sequence homology to MCM genes involved in DNA replication."
Miyake S., Saito I., Kobayashi H., Yamashita S.
Gene 175:71-75(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A COMPLEX WITH MCM5.
Tissue: Oocyte.
[2]"Licensing of DNA replication by a multi-protein complex of MCM/P1 proteins in Xenopus eggs."
Kubota Y., Mimura S., Nishimoto S., Masuda T., Nojima H., Takisawa H.
EMBO J. 16:3320-3331(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN A COMPLEX WITH MMCM3; MCM4; MCM5; MMCM6 AND MCM7, SUBCELLULAR LOCATION.
Tissue: Oocyte.
[3]NIH - Xenopus Gene Collection (XGC) project
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[4]"The RLF-M component of the replication licensing system forms complexes containing all six MCM/P1 polypeptides."
Thommes P., Kubota Y., Takisawa H., Blow J.J.
EMBO J. 16:3312-3319(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN RLF-M COMPLEX, SUBCELLULAR LOCATION.
[5]"Evidence for different MCM subcomplexes with differential binding to chromatin in Xenopus."
Coue M., Amariglio F., Maiorano D., Bocquet S., Mechali M.
Exp. Cell Res. 245:282-289(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN MCM COMPLEXES.
[6]"Distinct phosphoisoforms of the Xenopus Mcm4 protein regulate the function of the Mcm complex."
Pereverzeva I., Whitmire E., Khan B., Coue M.
Mol. Cell. Biol. 20:3667-3676(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[7]"The ATPase activity of MCM2-7 is dispensable for pre-RC assembly but is required for DNA unwinding."
Ying C.Y., Gautier J.
EMBO J. 24:4334-4344(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE MCM2-7 COMPLEX, IDENTIFICATION IN A COMPLEX WITH MMCM3; MCM4; MCM5; MMCM6 AND MCM7.
[8]"Cdc7-Drf1 is a developmentally regulated protein kinase required for the initiation of vertebrate DNA replication."
Takahashi T.S., Walter J.C.
Genes Dev. 19:2295-2300(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63919 mRNA. Translation: BAA09948.1.
U44047 mRNA. Translation: AAC60223.1.
BC046274 mRNA. Translation: AAH46274.1.
PIRJC5085.
RefSeqNP_001080759.1. NM_001087290.1.
UniGeneXl.382.

3D structure databases

ProteinModelPortalP55861.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid98693. 9 interactions.
IntActP55861. 7 interactions.
MINTMINT-6540654.

Proteomic databases

PRIDEP55861.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID380451.
KEGGxla:380451.

Organism-specific databases

CTD4171.
XenbaseXB-GENE-999979. mcm2.

Phylogenomic databases

HOVERGENHBG106398.
KOK02540.

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...

Entry information

Entry nameMCM2_XENLA
AccessionPrimary (citable) accession number: P55861
Secondary accession number(s): O42588, Q7ZX05
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 13, 2006
Last modified: June 11, 2014
This is version 93 of the entry and version 2 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