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P55861

- MCM2_XENLA

UniProt

P55861 - MCM2_XENLA

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Protein

DNA replication licensing factor mcm2

Gene

mcm2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - 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.3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri314 – 34027C4-typeSequence AnalysisAdd
BLAST
Nucleotide bindingi508 – 5158ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. DNA helicase activity Source: InterPro
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. cell cycle Source: UniProtKB-KW
  3. DNA replication initiation Source: InterPro
  4. DNA unwinding involved in DNA replication Source: UniProtKB
  5. regulation of DNA-dependent DNA replication initiation Source: UniProtKB
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

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:mcm2
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-999979. mcm2.

Subcellular locationi

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

GO - Cellular componenti

  1. chromatin Source: UniProtKB
  2. MCM complex Source: UniProtKB
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 886886DNA replication licensing factor mcm2PRO_0000194089Add
BLAST

Post-translational modificationi

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.2 Publications

Proteomic databases

PRIDEiP55861.

Interactioni

Subunit structurei

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).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
mmcm3P497399EBI-876864,EBI-491720

Protein-protein interaction databases

BioGridi98693. 9 interactions.
IntActiP55861. 7 interactions.
MINTiMINT-6540654.

Structurei

3D structure databases

ProteinModelPortaliP55861.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini458 – 665208MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi640 – 6434Arginine finger

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri314 – 34027C4-typeSequence AnalysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOVERGENiHBG106398.
KOiK02540.

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.

P55861 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADSSESFNI ATSPRAGSRR DALTSSPGRD LPPFEDESEG MFGDGVVPEE
60 70 80 90 100
EEDGEELIGD AMERDYRPIS ELDRYEVEGL DDEEDVEDLT ASQREAAEQS
110 120 130 140 150
MRMRDREMGR ELGRMRRGLL YDSDEEEEDR PARKRRMAER AAEGAPEEDE
160 170 180 190 200
EMIESIENLE DMKGHTVREW VSMAATRLEI YHRFKNFLRT HVDEHGHNVF
210 220 230 240 250
KEKISDMCKE NKESLPVNYE DLAAREHVLA YFLPEAPAEM LKIFDEAAKE
260 270 280 290 300
VVLVMYPKYD RIAREIHVRI SHLPLVEELR SLRQLHLNQL IRTSGVVTCC
310 320 330 340 350
TGVLPQLSMV KYNCNKCNFI LGPFFQSQNQ EVRPGSCPEC QSFGPFEINM
360 370 380 390 400
EETVYQNYQR ITIQESPGKV AAGRLPRSKD AILLADLVDS CKPGDEIELT
410 420 430 440 450
GIYHNNYDGS LNTANGFPVF ATVILANHIT KKDDKVAVGE LTDEDVKAIV
460 470 480 490 500
ALSKDERIGE RIFASIAPSI YGHEDIKRGL ALALFGGEAK NPGGKHKVRG
510 520 530 540 550
DINVLLCGDP GTAKSQFLKY VEKVASRAVF TTGQGASAVG LTAYVQRHPV
560 570 580 590 600
TKEWTLEAGA LVLADRGVCL IDEFDKMNDQ DRTSIHEAME QQSISISKAG
610 620 630 640 650
IVTSLQARCT VIAASNPIGG RYDPSLTFSE NVDLTEPIVS RFDILCVVRD
660 670 680 690 700
TVDPVQDEML ARFVVSSHIK HHPSSKDIAN GDAAEFALPN TFGVEALPQE
710 720 730 740 750
VLKKYIMYAK EKIRPKLNQM DQDKVAKMYS DLRKESMATG SIPITVRHIE
760 770 780 790 800
SMIRMAEAHA RMHLRDYVVE DDVNMAIRVM LESFIDTQKF SVMRSMRKTF
810 820 830 840 850
ARYLAFRRDN NELLLFVLKQ LIAEQVTYQR NRYGAQQDTI EVPEKDLVDK
860 870 880
ARQINIHNLS AFYDSDLFKM NKFTHDVKKK LIIQQF
Length:886
Mass (Da):100,262
Last modified:June 13, 2006 - v2
Checksum:i524C7B3673E2B2DD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691E → K in AAC60223. (PubMed:9214647)Curated
Sequence conflicti439 – 4391G → R in BAA09948. (PubMed:8917078)Curated
Sequence conflicti563 – 5631L → F in BAA09948. (PubMed:8917078)Curated
Sequence conflicti728 – 7281M → I in BAA09948. (PubMed:8917078)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63919 mRNA. Translation: BAA09948.1.
U44047 mRNA. Translation: AAC60223.1.
BC046274 mRNA. Translation: AAH46274.1.
PIRiJC5085.
RefSeqiNP_001080759.1. NM_001087290.1.
UniGeneiXl.382.

Genome annotation databases

GeneIDi380451.
KEGGixla:380451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63919 mRNA. Translation: BAA09948.1 .
U44047 mRNA. Translation: AAC60223.1 .
BC046274 mRNA. Translation: AAH46274.1 .
PIRi JC5085.
RefSeqi NP_001080759.1. NM_001087290.1.
UniGenei Xl.382.

3D structure databases

ProteinModelPortali P55861.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 98693. 9 interactions.
IntActi P55861. 7 interactions.
MINTi MINT-6540654.

Proteomic databases

PRIDEi P55861.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 380451.
KEGGi xla:380451.

Organism-specific databases

CTDi 4171.
Xenbasei XB-GENE-999979. mcm2.

Phylogenomic databases

HOVERGENi HBG106398.
KOi K02540.

Family and domain databases

Gene3Di 2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProi IPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view ]
PRINTSi PR01657. MCMFAMILY.
PR01658. MCMPROTEIN2.
SMARTi SM00350. MCM. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiMCM2_XENLA
AccessioniPrimary (citable) accession number: P55861
Secondary accession number(s): O42588, Q7ZX05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 13, 2006
Last modified: October 29, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3