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Reviewed, UniProtKB/Swiss-Prot P25205 (MCM3_HUMAN)

Last modified June 16, 2009. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DNA replication licensing factor MCM3
Alternative name(s):
    DNA polymerase alpha holoenzyme-associated protein P1
    RLF subunit beta
    P102 protein
    P1-MCM3
Gene names
Name: MCM3
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length808 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 a factor that allows the DNA to undergo a single round of replication per cell cycle. Required for DNA replication and cell proliferation.

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Miscellaneous

Associated with the replication-specific DNA polymerase alpha.

Sequence similarities

Belongs to the MCM family.

Contains 1 MCM domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 808807DNA replication licensing factor MCM3
PRO_0000194093

Regions

Domain295 – 502208MCM
Nucleotide binding345 – 3528ATP Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue1601Phosphoserine Ref.17
Modified residue5351Phosphoserine; by ATM Ref.9
Modified residue6681Phosphoserine Ref.17
Modified residue6721Phosphoserine Ref.11 Ref.12 Ref.15 Ref.17
Modified residue6741Phosphothreonine Ref.11 Ref.12 Ref.15 Ref.17
Modified residue6811Phosphoserine Ref.15 Ref.17
Modified residue7041Phosphoserine Ref.14
Modified residue7111Phosphoserine Ref.11 Ref.14 Ref.16 Ref.17
Modified residue7131Phosphothreonine Ref.10 Ref.11 Ref.13 Ref.14 Ref.17
Modified residue7221Phosphothreonine Ref.10 Ref.11 Ref.13 Ref.16 Ref.17
Modified residue7281Phosphoserine Ref.15
Modified residue7341Phosphoserine Ref.15

Natural variations

Natural variant1051S → G: dbSNP rs2307332.
VAR_014810
Natural variant2801D → V: dbSNP rs2307329. Ref.4
VAR_014811
Natural variant2871F → L: dbSNP rs2307328. Ref.4
VAR_014812
Natural variant5901I → L: dbSNP rs17240063. Ref.4
VAR_020516
Natural variant7741R → W: dbSNP rs2230239. Ref.4
VAR_020517
Natural variant7771E → K: dbSNP rs2230240. Ref.4
VAR_020427

Experimental info

Mutagenesis5351S → A: 50% reduction in phosphorylation by ATM or ATR. Ref.9
Sequence conflict230 – 2312KP → NA in BAA07267. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P25205-1 [UniParc].

Last modified August 14, 2001. Version 3.
Checksum: C967C068B7090558

FASTA80890,981
        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 

« Hide

References

« Hide '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: 8265339] [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: 7758114] [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. expand/collapse author list , 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: 14574404] [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: 15489334] [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: 1549468] [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: 15210935] [Abstract]
Cited for: PHOSPHORYLATION AT SER-535, MUTAGENESIS OF SER-535.
[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 THR-713 AND THR-722, MASS SPECTROMETRY.
Tissue: Epithelium.
[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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; THR-674; SER-711; THR-713 AND THR-722, MASS SPECTROMETRY.
Tissue: Epithelium.
[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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND THR-674, MASS SPECTROMETRY.
Tissue: Epithelium.
[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: 17487921] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-713 AND THR-722, MASS SPECTROMETRY.
[14]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704; SER-711 AND THR-713, MASS SPECTROMETRY.
[15]"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-672; THR-674; SER-681; SER-728 AND SER-734, MASS SPECTROMETRY.
[16]"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-711 AND THR-722, MASS SPECTROMETRY.
[17]"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 SER-160; SER-668; SER-672; THR-674; SER-681; SER-711; THR-713 AND THR-722, MASS SPECTROMETRY.
[18]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.

Web resources

Cross-references

Sequence databases

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.
IPIIPI00013214.
PIRS62594.
RefSeqNP_002379.2.
UniGeneHs.179565

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP25205. 31 interactions.

PTM databases

PhosphoSiteP25205.

Proteomic databases

PeptideAtlasP25205.
PRIDEP25205.

Genome annotation databases

EnsemblENSG00000112118. Homo sapiens. [Contig view]
GeneID4172.
KEGGhsa:4172.

Organism-specific databases

GeneCardsGC06M052236.
H-InvDBHIX0005950.
HGNCHGNC:6945. MCM3.
HPACAB002162.
HPA004789.
HPA004790.
MIM602693. gene.
PharmGKBPA30691.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP25205.
HOVERGENP25205.
OMAP25205. QVMVSEG.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressP25205.
BgeeP25205.
CleanExHS_MCM3.
GermOnlineENSG00000112118. Homo sapiens.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR001208. DNA-dep_ATPase_MCM.
IPR018525. DNA-dep_ATPase_MCM_CS.
IPR008046. MCM_3.
IPR012340. NA-bd_OB-fold.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PfamPF00493. MCM. 1 hit.
[Graphical view]
PRINTSPR01657. MCMFAMILY.
PR01659. MCMPROTEIN3.
ProDomPD001041. MCM. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
PROSITEPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio16432.
PMAP-CutDBP25205.
SOURCESearch...

Entry information

Entry nameMCM3_HUMAN
AccessionPrimary (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: June 16, 2009
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

Human chromosome 6: 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 · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents