Reviewed, UniProtKB/Swiss-Prot P49735 (MCM2_DROME)

Names and origin

Protein names

Recommended name:
    DNA replication licensing factor Mcm2
Alternative name(s):
    Minichromosome maintenance 2 protein
      Short name=DmMCM2

Gene names

Name:	Mcm2
ORF Names:	CG7538

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	887 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts as a factor that allows the DNA to undergo a single round of replication per cell cycle. Required for DNA replication and cell proliferation. Ref.1
Subunit structure	Heterohexamer. The heterodimers of mcm4/mcm6 and mcm3/mcm5 interact with mcm2 and mcm7. Interacts with Mcm10. Ref.5 Ref.6
Subcellular location	Nucleus Probable.
Sequence similarities	Belongs to the MCM family. Contains 1 MCM domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA replication Mitosis Transcription Transcription regulation
Cellular component	Nucleus
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 division Inferred from electronic annotation. Source: UniProtKB-KW chromosome condensation Ref.6 Inferred from mutant phenotype. Source: FlyBase mitosis Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.6 Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
daw	Q9VQG9	1	EBI-138228,EBI-172782
Mcm10	Q9VIE6	2	EBI-138228,EBI-91264
Mcm5	P91676	1	EBI-138228,EBI-466357
Mcm6	Q9V461	2	EBI-138228,EBI-869161

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 887	887	DNA replication licensing factor Mcm2		PRO_0000194090
Regions
	Domain	458 – 665	208	MCM
	Zinc finger	314 – 340	27	C4-type Potential
	Nucleotide binding	508 – 515	8	ATP Potential
Amino acid modifications
	Modified residue	26	1	Phosphothreonine Ref.7
	Modified residue	27	1	Phosphoserine Ref.7
	Modified residue	89	1	Phosphoserine Ref.8
	Modified residue	92	1	Phosphoserine Ref.8
	Modified residue	124	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P49735-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 26A7092109F09CBE	FASTA	887	100,415
	10 20 30 40 50 60 MDNPSSPPPN TPSDAAERRD LRAAMTSPVG DFEPFENEDE ILGDQTVRDE AEEEDGEELF 70 80 90 100 110 120 GDNMENDYRP MPELDHYDPA LLDDEDDFSE MSQGDRFAAE SEMRRRDRAA GIHRDDRDLG 130 140 150 160 170 180 FGQSDDEDDV GPRAKRRAGE KAAVGEVEDT EMVESIENLE DTKGHSTKEW VSMLGPRTEI 190 200 210 220 230 240 ANRFQSFLRT FVDERGAYTY RDRIRRMCEQ NMSSFVVSYT DLANKEHVLA YFLPEAPFQM 250 260 270 280 290 300 LEIFDKVAKD MVLSIFPTYE RVTTEIHVRI SELPLIEELR TFRKLHLNQL VRTLGVVTAT 310 320 330 340 350 360 TGVLPQLSVI KYDCVKCGYV LGPFVQSQNT EIKPGSCPEC QSTGPFSINM EQTLYRNYQK 370 380 390 400 410 420 ITLQESPGRI PAGRIPRSKD VILLADLCDQ CKPGDELEVT GIYTNNYDGS LNTDQGFPVF 430 440 450 460 470 480 ATVIIANHVV VKDSKQVVQS LTDEDIATIQ KLSKDPRIVE RVVASMAPSI YGHDYIKRAL 490 500 510 520 530 540 ALALFGGESK NPGEKHKVRG DINLLICGDP GTAKSQFLKY TEKVAPRAVF TTGQGASAVG 550 560 570 580 590 600 LTAYVRRNPV SREWTLEAGA LVLADQGVCL IDEFDKMNDQ DRTSIHEAME QQSISISKAG 610 620 630 640 650 660 IVTSLQARCT VIAAANPIGG RYDPSMTFSE NVNLSEPILS RFDVLCVVKD EFDPMQDQQL 670 680 690 700 710 720 AKFVVHSHMK HHPSEEEQPE LEEPQLKTVD EIPQDLLRQY IVYAKENIRP KLTNIDEDKI 730 740 750 760 770 780 AKMYAQLRQE SFATGSLPIT VRHIESVIRM SEAHARMHLR ENVMEADVSM AIRMMLESFI 790 800 810 820 830 840 EAQKFSVMKK MRSTFQKYLS FQKDHSELLF FILRQLTLDQ LAYIRCKDGP GATHVEIMER 850 860 870 880 DLIERAKQLD IVNLKPFYES DLFRTNGFSY DPKRRIILQI VVDGNTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cell proliferation and DNA replication defects in a Drosophila MCM2 mutant." Treisman J.E., Follette P.J., O'Farrell P.H., Rubin G.M. Genes Dev. 9:1709-1715(1995) [PubMed: 7622035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Tissue: Eye-antennal disk.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Drosophila minichromosome maintenance 6 is required for chorion gene amplification and genomic replication." Schwed G., May N., Pechersky Y., Calvi B.R. Mol. Biol. Cell 13:607-620(2002) [PubMed: 11854416] [Abstract] Cited for: INTERACTION WITH MCM6.
[6]	"Drosophila MCM10 interacts with members of the prereplication complex and is required for proper chromosome condensation." Christensen T.W., Tye B.K. Mol. Biol. Cell 14:2206-2215(2003) [PubMed: 12808023] [Abstract] Cited for: INTERACTION WITH MCM10.
[7]	"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed: 17372656] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-26; SER-27 AND SER-124, MASS SPECTROMETRY.
[8]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 AND SER-92, MASS SPECTROMETRY. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42762 mRNA. Translation: AAB36617.1. AE014297 Genomic DNA. Translation: AAF54207.1. AY069702 mRNA. Translation: AAL39847.1.
RefSeq	NP_477121.1.
UniGene	Dm.1996
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:22529N.
IntAct	P49735. 7 interactions.
Proteomic databases
PRIDE	P49735.
Genome annotation databases
Ensembl	FBgn0014861. Drosophila melanogaster. [Contig view]
GeneID	40973.
KEGG	dme:Dmel_CG7538.
NMPDR	fig|7227.3.peg.11661.
Organism-specific databases
FlyBase	FBgn0014861. Mcm2.
Phylogenomic databases
HOGENOM	P49735.
OMA	P49735. GVVTRRT.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-010511-MON.
Gene expression databases
ArrayExpress	P49735.
GermOnline	CG7538. Drosophila melanogaster.
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	821540.

Entry information

Entry name

MCM2_DROME

Accession

Primary (citable) accession number: P49735
Secondary accession number(s): Q9VHU2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project