DNA replication licensing factor MCM2

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Reviewed, UniProtKB/Swiss-Prot P49736 (MCM2_HUMAN)

Last modified July 7, 2009. Version 101. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    DNA replication licensing factor MCM2
Alternative name(s):
    Minichromosome maintenance protein 2 homolog
    Nuclear protein BM28

Gene names

Name:	MCM2
Synonyms:	BM28, CCNL1, CDCL1, KIAA0030

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	904 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Acts as a factor that allows the DNA to undergo a single round of replication per cell cycle. Required for the entry in S phase and for cell division. Ref.1
Subunit structure	Interacts with DBF4 By similarity. Interacts with MYST2. May interact with MCM10.
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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Sequence similarities	Belongs to the MCM family. Contains 1 MCM domain.
Sequence caution	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.

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Ontologies

Keywords
Biological process	Cell cycle DNA replication Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	ATP-binding DNA-binding Metal-binding Nucleotide-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA replication initiation Inferred from electronic annotation. Source: InterPro cell cycle Ref.1 Traceable author statement. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin Traceable author statement. Source: ProtInc nucleoplasm Ref.8 Inferred from Experiment. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.8 Inferred from physical interaction. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
CCNB2	O95067	1	EBI-374819,EBI-375024
CDC6	Q99741	1	EBI-374819,EBI-374862
CDK4	P11802	1	EBI-374819,EBI-295644
CDK6	Q00534	1	EBI-374819,EBI-295663
CDKN2A	P42771	1	EBI-374819,EBI-375053
MCM10	Q7L590	1	EBI-374819,EBI-374912
MCM3	P25205	1	EBI-374819,EBI-355153
MCM5	P33992	1	EBI-374819,EBI-359410
MCM7	P33993	1	EBI-374819,EBI-355924
ORC2L	Q13416	1	EBI-374819,EBI-374957
ORC5L	O43913	1	EBI-374819,EBI-374928
ORC6L	Q9Y5N6	1	EBI-374819,EBI-374840
PLK1	P53350	1	EBI-374819,EBI-476768

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 904

904

DNA replication licensing factor MCM2

PRO_0000194087

Regions

Domain

473 – 679

207

MCM

Zinc finger

329 – 355

C4-type Potential

Nucleotide binding

523 – 530

ATP Potential

Region

1 – 257

257

Interaction with MYST2 By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine Ref.12

Modified residue

Phosphothreonine Ref.22

Modified residue

Phosphoserine Ref.11 Ref.22

Modified residue

Phosphoserine Ref.10 Ref.12 Ref.14 Ref.19 Ref.20 Ref.22

Modified residue

Phosphothreonine Ref.12 Ref.22

Modified residue

Phosphoserine; by CDC7 Ref.12 Ref.16 Ref.22

Modified residue

Phosphoserine Ref.10 Ref.12 Ref.14 Ref.22

Modified residue

Phosphoserine; by CDC7 Ref.16 Ref.22

Modified residue

106

Phosphothreonine Ref.10

Modified residue

108

Phosphoserine; by ATR Ref.9 Ref.18 Ref.21

Modified residue

139

Phosphoserine Ref.11 Ref.12 Ref.15 Ref.17 Ref.20 Ref.21 Ref.22

Modified residue

381

Phosphoserine Ref.22

Natural variations

Natural variant

D → E: dbSNP rs3087452. Ref.3

VAR_021111

Natural variant

135

L → F: dbSNP rs2307314. Ref.3

VAR_021112

Natural variant

166

E → Q: dbSNP rs1048225. Ref.1

VAR_033298

Natural variant

396

A → T: dbSNP rs3087450. Ref.3

VAR_016137

Natural variant

501

G → R: dbSNP rs13087457. Ref.4

VAR_033299

Natural variant

667

V → M: dbSNP rs2307311. Ref.3

VAR_016138

Natural variant

727

A → T: dbSNP rs2307313. Ref.3 Ref.4

VAR_016139

Experimental info

Mutagenesis

108

S → A: Reduces phosphorylation by ATR. Ref.9

Sequence conflict

M → S in CAA47749. Ref.1

Sequence conflict

109

Q → R in CAA47749. Ref.1

Sequence conflict

388

G → R in CAA47749. Ref.1

Sequence conflict

407 – 408

KP → NA in CAA47749. Ref.1

Sequence conflict

407 – 408

KP → NA in BAA12177. Ref.5

Sequence conflict

495

L → P in CAA47749. Ref.1

Sequence conflict

555 – 556

GL → AV in CAA47749. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P49736-1 [UniParc].

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

FASTA

904

101,896

        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

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References

	« Hide 'large scale' referencesShow '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: 8175912] [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: 7584026] [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: 15489334] [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: 8258304] [Abstract] Cited for: CHROMOSOMAL LOCATION.
[8]	"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: 11095689] [Abstract] Cited for: INTERACTION WITH MCM10.
[9]	"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: 15210935] [Abstract] Cited for: PHOSPHORYLATION AT SER-108, MUTAGENESIS OF SER-108.
[10]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-41 AND THR-106, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-139, MASS SPECTROMETRY.
[12]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-27; THR-39; SER-40; SER-41 AND SER-139, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 16387653] [Abstract] Cited for: INTERACTION WITH MYST2.
[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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-41, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, MASS SPECTROMETRY.
[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: 17062569] [Abstract] Cited for: PHOSPHORYLATION AT SER-40 AND SER-53.
[17]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, MASS SPECTROMETRY.
[19]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, MASS SPECTROMETRY.
[20]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-139, MASS SPECTROMETRY.
[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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-139, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25; SER-26; SER-27; THR-39; SER-40; SER-41; SER-53; SER-139 AND SER-381, MASS SPECTROMETRY.
[23]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases
	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.
IPI	IPI00184330.
PIR	S42228.
RefSeq	NP_004517.2.
UniGene	Hs.477481
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P49736. 22 interactions.
PTM databases
PhosphoSite	P49736.
Proteomic databases
PeptideAtlas	P49736.
PRIDE	P49736.
Genome annotation databases
Ensembl	ENSG00000073111. Homo sapiens. [Contig view]
GeneID	4171.
KEGG	hsa:4171.
UCSC	uc003ejp.1. human.
Organism-specific databases
GeneCards	GC03P128799.
H-InvDB	HIX0003643.
HGNC	HGNC:6944. MCM2.
HPA	CAB000303.
MIM	116945. gene.
PharmGKB	PA30690.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P49736.
OMA	P49736. GVVTRRT.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	P49736.
Bgee	P49736.
CleanEx	HS_CCNL1. HS_MCM2.
GermOnline	ENSG00000073111. Homo sapiens.
Family and domain databases
InterPro	IPR001208. DNA-dep_ATPase_MCM. IPR018525. DNA-dep_ATPase_MCM_CS. IPR008045. MCM_2. IPR012340. NA-bd_OB-fold. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	PF00493. MCM. 1 hit. [Graphical view]
PRINTS	PR01657. MCMFAMILY. PR01658. MCMPROTEIN2.
ProDom	PD001041. MCM. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00350. MCM. 1 hit. [Graphical view]
PROSITE	PS00847. MCM_1. 1 hit. PS50051. MCM_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	16428.
PMAP-CutDB	P49736.
SOURCE	Search...

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Entry information

Entry name

MCM2_HUMAN

Accession

Primary (citable) accession number: P49736
Secondary accession number(s): Q14577

Q9BRM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 16, 2004
Last modified:	July 7, 2009
This is version 101 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 3

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents