P49736 (MCM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	904 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Cell cycle DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	ATP-binding DNA-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 replication Inferred from electronic annotation. Source: Compara G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle Traceable author statement. Source: Reactome cell cycle checkpoint Traceable author statement. Source: Reactome nucleosome assembly Inferred from electronic annotation. Source: Compara
Cellular_component	MCM complex Inferred from direct assay Ref.17. Source: UniProtKB chromatin Inferred from direct assay Ref.12. Source: UniProtKB nuclear origin of replication recognition complex Inferred from electronic annotation. Source: Compara nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP 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: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HIST2H4B	P62805	3	EBI-374819,EBI-302023
MCM3	P25205	4	EBI-374819,EBI-355153
MCM5	P33992	4	EBI-374819,EBI-359410
MCM6	Q14566	6	EBI-374819,EBI-374900
MCM7	P33993	5	EBI-374819,EBI-355924

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.25
	Chain	2 – 904	903	DNA replication licensing factor MCM2		PRO_0000194087
Regions
	Domain	473 – 679	207	MCM
	Zinc finger	329 – 355	27	C4-type Potential
	Nucleotide binding	523 – 530	8	ATP Potential
	Region	2 – 257	256	Interaction with KAT7 By similarity
	Motif	655 – 658	4	Arginine finger
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.25 Ref.27
	Modified residue	12	1	Phosphoserine By similarity
	Modified residue	13	1	Phosphoserine Ref.25 Ref.27
	Modified residue	25	1	Phosphothreonine By similarity
	Modified residue	26	1	Phosphoserine Ref.22 Ref.27
	Modified residue	27	1	Phosphoserine Ref.12 Ref.14 Ref.23 Ref.25 Ref.27
	Modified residue	39	1	Phosphothreonine Ref.22
	Modified residue	40	1	Phosphoserine; by CDC7 Ref.16 Ref.22
	Modified residue	41	1	Phosphoserine Ref.12 Ref.14 Ref.22 Ref.25 Ref.27
	Modified residue	53	1	Phosphoserine; by CDC7 Ref.12 Ref.16 Ref.22
	Modified residue	59	1	Phosphothreonine Ref.23
	Modified residue	108	1	Phosphoserine; by ATR Ref.10 Ref.12 Ref.18 Ref.23 Ref.25
	Modified residue	139	1	Phosphoserine Ref.12 Ref.22 Ref.23 Ref.25 Ref.27
	Modified residue	216	1	N6-acetyllysine Ref.24
	Modified residue	381	1	Phosphoserine Ref.27
Natural variations
	Natural variant	68	1	D → E. Ref.3 Corresponds to variant rs3087452 [ dbSNP | Ensembl ].		VAR_021111
	Natural variant	135	1	L → F. Ref.3 Corresponds to variant rs2307314 [ dbSNP | Ensembl ].		VAR_021112
	Natural variant	166	1	E → Q. Ref.1 Corresponds to variant rs1048225 [ dbSNP | Ensembl ].		VAR_033298
	Natural variant	396	1	A → T. Ref.3 Corresponds to variant rs3087450 [ dbSNP | Ensembl ].		VAR_016137
	Natural variant	501	1	G → R. Ref.4 Corresponds to variant rs13087457 [ dbSNP | Ensembl ].		VAR_033299
	Natural variant	667	1	V → M. Ref.3 Corresponds to variant rs2307311 [ dbSNP | Ensembl ].		VAR_016138
	Natural variant	727	1	A → T. Ref.3 Ref.4 Corresponds to variant rs2307313 [ dbSNP | Ensembl ].		VAR_016139
Experimental info
	Mutagenesis	27	1	S → 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
	Mutagenesis	41	1	S → 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
	Mutagenesis	108	1	S → A: Reduces phosphorylation by ATR. Ref.10
	Mutagenesis	139	1	S → 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 conflict	1	1	M → S in CAA47749. Ref.1
	Sequence conflict	109	1	Q → R in CAA47749. Ref.1
	Sequence conflict	388	1	G → R in CAA47749. Ref.1
	Sequence conflict	407 – 408	2	KP → NA in CAA47749. Ref.1
	Sequence conflict	407 – 408	2	KP → NA in BAA12177. Ref.5
	Sequence conflict	495	1	L → P in CAA47749. Ref.1
	Sequence conflict	555 – 556	2	GL → AV in CAA47749. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P49736 [UniParc]. Last modified January 16, 2004. Version 4. Checksum: 52C6DC61F128B404	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

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] [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, MASS SPECTROMETRY. 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[24]	"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, MASS SPECTROMETRY.
[25]	"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, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma.
[26]	"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].
[27]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.
IPI	IPI00184330.
PIR	S42228.
RefSeq	NP_004517.2. NM_004526.3.
UniGene	Hs.477481.
3D structure databases
ProteinModelPortal	P49736.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31732N.
IntAct	P49736. 32 interactions.
MINT	MINT-5004296.
STRING	9606.ENSP00000265056.
PTM databases
PhosphoSite	P49736.
Polymorphism databases
DMDM	41019490.
Proteomic databases
PaxDb	P49736.
PeptideAtlas	P49736.
PRIDE	P49736.
Protocols and materials databases
DNASU	4171.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265056; ENSP00000265056; ENSG00000073111.
GeneID	4171.
KEGG	hsa:4171.
UCSC	uc003ejp.3. human.
Organism-specific databases
CTD	4171.
GeneCards	GC03P127317.
HGNC	HGNC:6944. MCM2.
HPA	CAB000303.
MIM	116945. gene.
neXtProt	NX_P49736.
PharmGKB	PA164742061.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1241.
HOVERGEN	HBG106398.
InParanoid	P49736.
KO	K02540.
OrthoDB	EOG4FTVZZ.
PhylomeDB	P49736.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	P49736.
Bgee	P49736.
CleanEx	HS_CCNL1. HS_MCM2.
Genevestigator	P49736.
GermOnline	ENSG00000073111. Homo sapiens.
Family and domain databases
Gene3D	2.40.50.140. 2 hits.
InterPro	IPR008045. MCM2. IPR018525. MCM_CS. IPR001208. MCM_DNA-dep_ATPase. IPR012340. NA-bd_OB-fold. [Graphical view]
Pfam	PF00493. MCM. 1 hit. PF12619. MCM2_N. 1 hit. [Graphical view]
PRINTS	PR01657. MCMFAMILY. PR01658. MCMPROTEIN2.
SMART	SM00350. MCM. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit.
PROSITE	PS00847. MCM_1. 1 hit. PS50051. MCM_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	4171.
NextBio	16428.
PMAP-CutDB	P49736.
SOURCE	Search...

Entry information

Entry name

MCM2_HUMAN

Accession

Primary (citable) accession number: P49736
Secondary accession number(s): Q14577 , Q15023, Q8N2V1, Q969W7, Q96AE1, Q9BRM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 16, 2004
Last modified:	May 1, 2013
This is version 145 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.