Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 125 (12 Aug 2020)
Sequence version 2 (13 Jun 2006)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

DNA replication licensing factor mcm2

Gene

mcm2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri314 – 340C4-typeSequence analysisAdd BLAST27
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi508 – 515ATPSequence analysis8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase
Biological processCell cycle, DNA replication
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:mcm2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiXenopus laevis (African clawed frog)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri8355 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...
Xenbasei
XB-GENE-999979, mcm2.L

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001940891 – 886DNA replication licensing factor mcm2Add BLAST886

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P55861

PRoteomics IDEntifications database

More...
PRIDEi
P55861

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P55861

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 (Probable).

Component of the replisome complex (By similarity).

By similarityCurated5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
98693, 10 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2943, MCM complex

Protein interaction database and analysis system

More...
IntActi
P55861, 7 interactors

Molecular INTeraction database

More...
MINTi
P55861

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini458 – 665MCMAdd BLAST208

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi640 – 643Arginine finger4

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the MCM family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri314 – 340C4-typeSequence analysisAdd BLAST27

Keywords - Domaini

Zinc-finger

Phylogenomic databases

KEGG Orthology (KO)

More...
KOi
K02540

Identification of Orthologs from Complete Genome Data

More...
OMAi
IFDERYQ

Database of Orthologous Groups

More...
OrthoDBi
266497at2759

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR031327, MCM
IPR008045, MCM2
IPR018525, MCM_CS
IPR001208, MCM_dom
IPR041562, MCM_lid
IPR027925, MCM_N
IPR033762, MCM_OB
IPR012340, NA-bd_OB-fold
IPR027417, P-loop_NTPase

The PANTHER Classification System

More...
PANTHERi
PTHR11630, PTHR11630, 1 hit
PTHR11630:SF44, PTHR11630:SF44, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00493, MCM, 1 hit
PF12619, MCM2_N, 1 hit
PF17855, MCM_lid, 1 hit
PF14551, MCM_N, 1 hit
PF17207, MCM_OB, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01657, MCMFAMILY
PR01658, MCMPROTEIN2

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00350, MCM, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50249, SSF50249, 1 hit
SSF52540, SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00847, MCM_1, 1 hit
PS50051, MCM_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P55861-1 [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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i524C7B3673E2B2DD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti169E → K in AAC60223 (PubMed:9214647).Curated1
Sequence conflicti439G → R in BAA09948 (PubMed:8917078).Curated1
Sequence conflicti563L → F in BAA09948 (PubMed:8917078).Curated1
Sequence conflicti728M → I in BAA09948 (PubMed:8917078).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D63919 mRNA Translation: BAA09948.1
U44047 mRNA Translation: AAC60223.1
BC046274 mRNA Translation: AAH46274.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC5085

NCBI Reference Sequences

More...
RefSeqi
NP_001080759.1, NM_001087290.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
380451

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
xla:380451

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63919 mRNA Translation: BAA09948.1
U44047 mRNA Translation: AAC60223.1
BC046274 mRNA Translation: AAH46274.1
PIRiJC5085
RefSeqiNP_001080759.1, NM_001087290.2

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGRIDi98693, 10 interactors
ComplexPortaliCPX-2943, MCM complex
IntActiP55861, 7 interactors
MINTiP55861

PTM databases

iPTMnetiP55861

Proteomic databases

MaxQBiP55861
PRIDEiP55861

Genome annotation databases

GeneIDi380451
KEGGixla:380451

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
380451
XenbaseiXB-GENE-999979, mcm2.L

Phylogenomic databases

KOiK02540
OMAiIFDERYQ
OrthoDBi266497at2759

Family and domain databases

InterProiView protein in InterPro
IPR031327, MCM
IPR008045, MCM2
IPR018525, MCM_CS
IPR001208, MCM_dom
IPR041562, MCM_lid
IPR027925, MCM_N
IPR033762, MCM_OB
IPR012340, NA-bd_OB-fold
IPR027417, P-loop_NTPase
PANTHERiPTHR11630, PTHR11630, 1 hit
PTHR11630:SF44, PTHR11630:SF44, 1 hit
PfamiView protein in Pfam
PF00493, MCM, 1 hit
PF12619, MCM2_N, 1 hit
PF17855, MCM_lid, 1 hit
PF14551, MCM_N, 1 hit
PF17207, MCM_OB, 1 hit
PRINTSiPR01657, MCMFAMILY
PR01658, MCMPROTEIN2
SMARTiView protein in SMART
SM00350, MCM, 1 hit
SUPFAMiSSF50249, SSF50249, 1 hit
SSF52540, SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00847, MCM_1, 1 hit
PS50051, MCM_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMCM2_XENLA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P55861
Secondary accession number(s): O42588, Q7ZX05
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 13, 2006
Last modified: August 12, 2020
This is version 125 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again