P25205 (MCM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA replication licensing factor MCM3
EC=3.6.4.12

Alternative name(s):
DNA polymerase alpha holoenzyme-associated protein P1
P1-MCM3
RLF subunit beta
p102

Gene names

Name:

MCM3

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	808 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 DNA replication and cell proliferation.
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). Associated with the replication-specific DNA polymerase alpha. Interacts with MCMBP. Ref.11 Ref.14
Subcellular location	Nucleus.
Post-translational modification	O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. Ref.22
Miscellaneous	Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. The MCM2-7 hexamer is the proposed physiological active complex.
Sequence similarities	Belongs to the MCM family. Contains 1 MCM domain.

Ontologies

Keywords
Biological process	Cell cycle DNA replication
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA duplex unwinding Inferred from electronic annotation. Source: GOC DNA replication initiation Traceable author statement Ref.8. Source: ProtInc DNA strand elongation involved in DNA replication Traceable author statement. Source: Reactome G1/S 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
Cellular_component	MCM complex Inferred from direct assay Ref.14. Source: UniProtKB alpha DNA polymerase:primase complex Traceable author statement Ref.8. Source: ProtInc centrosome Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome perinuclear region of cytoplasm Inferred from direct assay PubMed 20531406. Source: BHF-UCL
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Traceable author statement Ref.8. Source: ProtInc DNA helicase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HIST1H4A	P62805	2	EBI-355153,EBI-302023
MCM2	P49736	4	EBI-355153,EBI-374819
MCM5	P33992	3	EBI-355153,EBI-359410
MCM6	Q14566	2	EBI-355153,EBI-374900
ORC2	Q13416	2	EBI-355153,EBI-374957

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 808	807	DNA replication licensing factor MCM3		PRO_0000194093
Regions
	Domain	295 – 502	208	MCM
	Nucleotide binding	345 – 352	8	ATP Potential
	Motif	477 – 480	4	Arginine finger
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7
	Modified residue	160	1	Phosphoserine Ref.16 Ref.21
	Modified residue	535	1	Phosphoserine; by ATM Ref.9
	Modified residue	668	1	Phosphoserine Ref.16 Ref.19
	Modified residue	672	1	Phosphoserine Ref.12 Ref.16 Ref.18 Ref.19 Ref.21
	Modified residue	674	1	Phosphothreonine Ref.12 Ref.16 Ref.18 Ref.21
	Modified residue	681	1	Phosphoserine Ref.16
	Modified residue	708	1	Phosphotyrosine Ref.18
	Modified residue	711	1	Phosphoserine Ref.16 Ref.18 Ref.19 Ref.21
	Modified residue	713	1	Phosphothreonine Ref.16 Ref.18
	Modified residue	722	1	Phosphothreonine Ref.10 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19
	Modified residue	725	1	Phosphothreonine Ref.18
Natural variations
	Natural variant	105	1	S → G. Corresponds to variant rs2307332 [ dbSNP | Ensembl ].		VAR_014810
	Natural variant	280	1	D → V. Ref.4 Corresponds to variant rs2307329 [ dbSNP | Ensembl ].		VAR_014811
	Natural variant	287	1	F → L. Ref.4 Corresponds to variant rs2307328 [ dbSNP | Ensembl ].		VAR_014812
	Natural variant	590	1	I → L. Ref.4 Corresponds to variant rs17240063 [ dbSNP | Ensembl ].		VAR_020516
	Natural variant	774	1	R → W. Ref.4 Corresponds to variant rs2230239 [ dbSNP | Ensembl ].		VAR_020517
	Natural variant	777	1	E → K. Ref.4 Corresponds to variant rs2230240 [ dbSNP | Ensembl ].		VAR_020427
Experimental info
	Mutagenesis	535	1	S → A: 50% reduction in phosphorylation by ATM or ATR. Ref.9
	Sequence conflict	230 – 231	2	KP → NA in BAA07267. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P25205 [UniParc]. Last modified August 14, 2001. Version 3. Checksum: C967C068B7090558	FASTA	808	90,981
	10 20 30 40 50 60 MAGTVVLDDV ELREAQRDYL DFLDDEEDQG IYQSKVRELI SDNQYRLIVN VNDLRRKNEK 70 80 90 100 110 120 RANRLLNNAF EELVAFQRAL KDFVASIDAT YAKQYEEFYV GLEGSFGSKH VSPRTLTSCF 130 140 150 160 170 180 LSCVVCVEGI VTKCSLVRPK VVRSVHYCPA TKKTIERRYS DLTTLVAFPS SSVYPTKDEE 190 200 210 220 230 240 NNPLETEYGL SVYKDHQTIT IQEMPEKAPA GQLPRSVDVI LDDDLVDKAK PGDRVQVVGT 250 260 270 280 290 300 YRCLPGKKGG YTSGTFRTVL IACNVKQMSK DAQPSFSAED IAKIKKFSKT RSKDIFDQLA 310 320 330 340 350 360 KSLAPSIHGH DYVKKAILCL LLGGVERDLE NGSHIRGDIN ILLIGDPSVA KSQLLRYVLC 370 380 390 400 410 420 TAPRAIPTTG RGSSGVGLTA AVTTDQETGE RRLEAGAMVL ADRGVVCIDE FDKMSDMDRT 430 440 450 460 470 480 AIHEVMEQGR VTIAKAGIHA RLNARCSVLA AANPVYGRYD QYKTPMENIG LQDSLLSRFD 490 500 510 520 530 540 LLFIMLDQMD PEQDREISDH VLRMHRYRAP GEQDGDAMPL GSAVDILATD DPNFSQEDQQ 550 560 570 580 590 600 DTQIYEKHDN LLHGTKKKKE KMVSAAFMKK YIHVAKIIKP VLTQESATYI AEEYSRLRSQ 610 620 630 640 650 660 DSMSSDTART SPVTARTLET LIRLATAHAK ARMSKTVDLQ DAEEAVELVQ YAYFKKVLEK 670 680 690 700 710 720 EKKRKKRSED ESETEDEEEK SQEDQEQKRK RRKTRQPDAK DGDSYDPYDF SDTEEEMPQV 730 740 750 760 770 780 HTPKTADSQE TKESQKVELS ESRLKAFKVA LLDVFREAHA QSIGMNRLTE SINRDSEEPF 790 800 SSVEIQAALS KMQDDNQVMV SEGIIFLI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The P1 family: a new class of nuclear mammalian proteins related to the yeast Mcm replication proteins." Hu B., Burkhart R., Schulte D., Musahl C., Knippers R. Nucleic Acids Res. 21:5289-5293(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cervix.
[2]	Goehring F., Jehnichen P., Hemmer W.H. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Identification of the yeast MCM3-related protein as a component of Xenopus DNA replication licensing factor." Kubota Y., Mimura S., Nishimoto S., Takisawa H., Nojima H. Cell 81:601-609(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cervix.
[4]	NIEHS SNPs program Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-280; LEU-287; LEU-590; TRP-774 AND LYS-777.
[5]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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]. Tissue: Lymph and Pancreas.
[7]	Bienvenut W.V., Glen H., Brunton V.G., Frame M.C. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13; 47-55; 337-351 AND 749-756, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Osteosarcoma.
[8]	"Properties of the nuclear P1 protein, a mammalian homologue of the yeast Mcm3 replication protein." Thoemmes P., Fett R., Schray B., Burkhart R., Barnes M., Kennedy C., Brown N.C., Knippers R. Nucleic Acids Res. 20:1069-1074(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 563-808.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-535, MUTAGENESIS OF SER-535.
[10]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: IDENTIFICATION IN THE MCM2-7 COMPLEX, ATPASE ACTIVITY OF THE MCM2-7 COMPLEX.
[12]	"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-672 AND THR-674, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722, MASS SPECTROMETRY. Tissue: Prostate cancer.
[14]	"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: MASS SPECTROMETRY, IDENTIFICATION IN THE MCM2-7 COMPLEX, INTERACTION WITH MCMBP.
[15]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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-160; SER-668; SER-672; THR-674; SER-681; SER-711; THR-713 AND THR-722, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722, MASS SPECTROMETRY.
[18]	"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-672; THR-674; TYR-708; SER-711; THR-713; THR-722 AND THR-725, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668; SER-672; SER-711 AND THR-722, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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].
[21]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-672; THR-674 AND SER-711, MASS SPECTROMETRY.
[22]	"Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition." Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F., Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S. Biochim. Biophys. Acta 1820:1839-1848(2012) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	X62153 mRNA. Translation: CAA44078.2. D38073 mRNA. Translation: BAA07267.1. AY621074 Genomic DNA. Translation: AAT27321.1. AL034343 Genomic DNA. Translation: CAB75298.1. BC001626 mRNA. Translation: AAH01626.1. BC003509 mRNA. Translation: AAH03509.2.
IPI	IPI00013214.
PIR	S62594.
RefSeq	NP_001257401.1. NM_001270472.1. NP_002379.3. NM_002388.4.
UniGene	Hs.179565.
3D structure databases
ProteinModelPortal	P25205.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-31726N.
IntAct	P25205. 25 interactions.
MINT	MINT-1201900.
STRING	9606.ENSP00000229854.
PTM databases
PhosphoSite	P25205.
Polymorphism databases
DMDM	19857543.
Proteomic databases
PaxDb	P25205.
PeptideAtlas	P25205.
PRIDE	P25205.
Protocols and materials databases
DNASU	4172.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000229854; ENSP00000229854; ENSG00000112118.
GeneID	4172.
KEGG	hsa:4172.
UCSC	uc003pan.1. human.
Organism-specific databases
CTD	4172.
GeneCards	GC06M052128.
HGNC	HGNC:6945. MCM3.
HPA	CAB002162. HPA004789. HPA004790.
MIM	602693. gene.
neXtProt	NX_P25205.
PharmGKB	PA30691.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1241.
HOGENOM	HOG000224126.
HOVERGEN	HBG104962.
InParanoid	P25205.
KO	K02541.
OMA	NPIYGQY.
OrthoDB	EOG4M91QV.
PhylomeDB	P25205.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	P25205.
Bgee	P25205.
CleanEx	HS_MCM3.
Genevestigator	P25205.
GermOnline	ENSG00000112118. Homo sapiens.
Family and domain databases
Gene3D	2.40.50.140. 2 hits.
InterPro	IPR003593. AAA+_ATPase. IPR008046. Mcm3. IPR018525. MCM_CS. IPR001208. MCM_DNA-dep_ATPase. IPR012340. NA-bd_OB-fold. IPR027417. P-loop_NTPase. [Graphical view]
Pfam	PF00493. MCM. 1 hit. [Graphical view]
PRINTS	PR01657. MCMFAMILY. PR01659. MCMPROTEIN3.
SMART	SM00382. AAA. 1 hit. SM00350. MCM. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit. SSF52540. SSF52540. 1 hit.
PROSITE	PS00847. MCM_1. 1 hit. PS50051. MCM_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MCM3. human.
GenomeRNAi	4172.
NextBio	13605303.
PMAP-CutDB	P25205.
SOURCE	Search...

Entry information

Entry name

MCM3_HUMAN

Accession

Primary (citable) accession number: P25205
Secondary accession number(s): Q92660, Q9BTR3, Q9NUE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	August 14, 2001
Last modified:	May 29, 2013
This is version 154 of the entry and version 3 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.