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

P49736 (MCM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·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, CCNL1, CDCL1, KIAA0030
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.1

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 (By simililarity). Interacts with DBF4 By similarity. Interacts with KAT7. May interact with MCM10. Ref.8 Ref.9 Ref.12 Ref.13 Ref.17

Subcellular location

Nucleus Ref.1.

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. Ref.10 Ref.12 Ref.16

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.

Sequence similarities

Belongs to the MCM family.

Contains 1 MCM domain.

Sequence caution

The sequence BAA04642.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA12177.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA47749.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAA47749.1 differs from that shown. Reason: Frameshift at positions 115, 124, 127, 129, 154, 158, 773 and 811.

Ontologies

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

Traceable author statement. Source: Reactome

DNA replication initiation

Inferred from mutant phenotype Ref.12. Source: UniProtKB

DNA strand elongation involved in DNA replication

Traceable author statement. Source: Reactome

DNA unwinding involved in DNA replication

Inferred from electronic annotation. Source: Ensembl

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

cell cycle

Traceable author statement Ref.1. Source: ProtInc

cellular response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

nucleosome assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentMCM complex

Inferred from direct assay Ref.17. Source: UniProtKB

chromatin

Inferred from direct assay Ref.12. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

nuclear origin of replication recognition complex

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Traceable author statement Ref.1. Source: ProtInc

DNA helicase activity

Inferred from electronic annotation. Source: InterPro

DNA replication origin binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.9Ref.13. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.23
Chain2 – 904903DNA replication licensing factor MCM2
PRO_0000194087

Regions

Domain473 – 679207MCM
Zinc finger329 – 35527C4-type Potential
Nucleotide binding523 – 5308ATP Potential
Region2 – 257256Interaction with KAT7 By similarity
Motif655 – 6584Arginine finger

Amino acid modifications

Modified residue21N-acetylalanine Ref.23 Ref.26 Ref.28 Ref.29 Ref.30
Modified residue121Phosphoserine By similarity
Modified residue131Phosphoserine Ref.26 Ref.28
Modified residue261Phosphoserine Ref.22 Ref.28
Modified residue271Phosphoserine Ref.12 Ref.14 Ref.24 Ref.26 Ref.28
Modified residue391Phosphothreonine Ref.22
Modified residue401Phosphoserine; by CDC7 Ref.16 Ref.22
Modified residue411Phosphoserine Ref.12 Ref.14 Ref.22 Ref.26 Ref.28
Modified residue531Phosphoserine; by CDC7 Ref.12 Ref.16 Ref.22
Modified residue591Phosphothreonine Ref.24
Modified residue1081Phosphoserine; by ATR Ref.10 Ref.12 Ref.18 Ref.24 Ref.26
Modified residue1391Phosphoserine Ref.12 Ref.22 Ref.24 Ref.26 Ref.28
Modified residue2161N6-acetyllysine Ref.25
Modified residue3811Phosphoserine Ref.28

Natural variations

Natural variant681D → E. Ref.3
Corresponds to variant rs3087452 [ dbSNP | Ensembl ].
VAR_021111
Natural variant1351L → F. Ref.3
Corresponds to variant rs2307314 [ dbSNP | Ensembl ].
VAR_021112
Natural variant1661E → Q. Ref.1
Corresponds to variant rs1048225 [ dbSNP | Ensembl ].
VAR_033298
Natural variant3961A → T. Ref.3
Corresponds to variant rs3087450 [ dbSNP | Ensembl ].
VAR_016137
Natural variant5011G → R. Ref.4
Corresponds to variant rs13087457 [ dbSNP | Ensembl ].
VAR_033299
Natural variant6671V → M. Ref.3
Corresponds to variant rs2307311 [ dbSNP | Ensembl ].
VAR_016138
Natural variant7271A → T. Ref.3 Ref.4
Corresponds to variant rs2307313 [ dbSNP | Ensembl ].
VAR_016139

Experimental info

Mutagenesis271S → 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. Ref.12
Mutagenesis411S → 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. Ref.12
Mutagenesis1081S → A: Reduces phosphorylation by ATR. Ref.10
Mutagenesis1391S → 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. Ref.12
Sequence conflict11M → S in CAA47749. Ref.1
Sequence conflict1091Q → R in CAA47749. Ref.1
Sequence conflict3881G → R in CAA47749. Ref.1
Sequence conflict407 – 4082KP → NA in CAA47749. Ref.1
Sequence conflict407 – 4082KP → NA in BAA12177. Ref.5
Sequence conflict4951L → P in CAA47749. Ref.1
Sequence conflict555 – 5562GL → AV in CAA47749. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49736 [UniParc].

Last modified January 16, 2004. Version 4.
Checksum: 52C6DC61F128B404

FASTA904101,896
        10         20         30         40         50         60 
MAESSESFTM ASSPAQRRRG NDPLTSSPGR SSRRTDALTS SPGRDLPPFE DESEGLLGTE 

        70         80         90        100        110        120 
GPLEEEEDGE ELIGDGMERD YRAIPELDAY EAEGLALDDE DVEELTASQR EAAERAMRQR 

       130        140        150        160        170        180 
DREAGRGLGR MRRGLLYDSD EEDEERPARK RRQVERATED 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 QLSMVKYNCN KCNFVLGPFC QSQNQEVKPG SCPECQSAGP 

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

       430        440        450        460        470        480 
NYDGSLNTAN GFPVFATVIL ANHVAKKDNK VAVGELTDED VKMITSLSKD 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 EPIISRFDIL 

       670        680        690        700        710        720 
CVVRDTVDPV QDEMLARFVV GSHVRHHPSN KEEEGLANGS AAEPAMPNTY GVEPLPQEVL 

       730        740        750        760        770        780 
KKYIIYAKER VHPKLNQMDQ DKVAKMYSDL RKESMATGSI PITVRHIESM IRMAEAHARI 

       790        800        810        820        830        840 
HLRDYVIEDD VNMAIRVMLE SFIDTQKFSV MRSMRKTFAR YLSFRRDNNE LLLFILKQLV 

       850        860        870        880        890        900 
AEQVTYQRNR FGAQQDTIEV PEKDLVDKAR QINIHNLSAF YDSELFRMNK FSHDLKRKMI 


LQQF 

« Hide

References

« Hide 'large scale' references
[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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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].
Tissue: Cervix carcinoma.
[27]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
[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].
[30]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3043.1.
PIRS42228.
RefSeqNP_004517.2. NM_004526.3.
UniGeneHs.477481.

3D structure databases

ProteinModelPortalP49736.
SMRP49736. Positions 199-798.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110339. 83 interactions.
DIPDIP-31732N.
IntActP49736. 45 interactions.
MINTMINT-5004296.
STRING9606.ENSP00000265056.

PTM databases

PhosphoSiteP49736.

Polymorphism databases

DMDM41019490.

Proteomic databases

MaxQBP49736.
PaxDbP49736.
PeptideAtlasP49736.
PRIDEP49736.

Protocols and materials databases

DNASU4171.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265056; ENSP00000265056; ENSG00000073111.
GeneID4171.
KEGGhsa:4171.
UCSCuc003ejp.4. human.

Organism-specific databases

CTD4171.
GeneCardsGC03P127317.
HGNCHGNC:6944. MCM2.
HPACAB000303.
HPA031495.
HPA031496.
MIM116945. gene.
neXtProtNX_P49736.
PharmGKBPA164742061.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1241.
HOVERGENHBG106398.
InParanoidP49736.
KOK02540.
OMANMEETVY.
OrthoDBEOG71VSRZ.
PhylomeDBP49736.
TreeFamTF300772.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressP49736.
BgeeP49736.
CleanExHS_CCNL1.
HS_MCM2.
GenevestigatorP49736.

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

GeneWikiMCM2.
GenomeRNAi4171.
NextBio16428.
PMAP-CutDBP49736.
PROP49736.
SOURCESearch...

Entry information

Entry nameMCM2_HUMAN
AccessionPrimary (citable) accession number: P49736
Secondary accession number(s): Q14577 expand/collapse secondary AC list , Q15023, Q8N2V1, Q969W7, Q96AE1, Q9BRM7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 16, 2004
Last modified: July 9, 2014
This is version 159 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM