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P25205

- MCM3_HUMAN

UniProt

P25205 - MCM3_HUMAN

Protein

DNA replication licensing factor MCM3

Gene

MCM3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 3 (14 Aug 2001)
      Previous versions | rss
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    Functioni

    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 activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi345 – 3528ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: ProtInc
    3. DNA helicase activity Source: InterPro
    4. protein binding Source: IntAct

    GO - Biological processi

    1. DNA replication Source: Reactome
    2. DNA replication initiation Source: ProtInc
    3. DNA strand elongation involved in DNA replication Source: Reactome
    4. G1/S transition of mitotic cell cycle Source: Reactome
    5. mitotic cell cycle Source: Reactome

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Cell cycle, DNA replication

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1095. Activation of the pre-replicative complex.
    REACT_1156. Orc1 removal from chromatin.
    REACT_207. Removal of licensing factors from origins.
    REACT_2148. Switching of origins to a post-replicative state.
    REACT_2243. Assembly of the pre-replicative complex.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_6776. Unwinding of DNA.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:MCM3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:6945. MCM3.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha DNA polymerase:primase complex Source: ProtInc
    2. centrosome Source: HPA
    3. intracellular membrane-bounded organelle Source: HPA
    4. MCM complex Source: UniProtKB
    5. membrane Source: UniProtKB
    6. nucleoplasm Source: Reactome
    7. nucleus Source: BHF-UCL
    8. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi535 – 5351S → A: 50% reduction in phosphorylation by ATM or ATR. 1 Publication

    Organism-specific databases

    PharmGKBiPA30691.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 808807DNA replication licensing factor MCM3PRO_0000194093Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei160 – 1601Phosphoserine2 Publications
    Modified residuei293 – 2931N6-acetyllysineBy similarity
    Modified residuei535 – 5351Phosphoserine; by ATM1 Publication
    Modified residuei547 – 5471N6-acetyllysineBy similarity
    Modified residuei668 – 6681Phosphoserine2 Publications
    Modified residuei672 – 6721Phosphoserine5 Publications
    Modified residuei674 – 6741Phosphothreonine4 Publications
    Modified residuei681 – 6811Phosphoserine1 Publication
    Modified residuei708 – 7081Phosphotyrosine1 Publication
    Modified residuei711 – 7111Phosphoserine4 Publications
    Modified residuei713 – 7131Phosphothreonine2 Publications
    Modified residuei722 – 7221Phosphothreonine7 Publications
    Modified residuei725 – 7251Phosphothreonine1 Publication

    Post-translational modificationi

    O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.1 Publication

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP25205.
    PaxDbiP25205.
    PeptideAtlasiP25205.
    PRIDEiP25205.

    PTM databases

    PhosphoSiteiP25205.

    Miscellaneous databases

    PMAP-CutDBP25205.

    Expressioni

    Gene expression databases

    ArrayExpressiP25205.
    BgeeiP25205.
    CleanExiHS_MCM3.
    GenevestigatoriP25205.

    Organism-specific databases

    HPAiCAB002162.
    HPA004789.
    HPA004790.

    Interactioni

    Subunit structurei

    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.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST2H4BP628052EBI-355153,EBI-302023
    MCM2P497365EBI-355153,EBI-374819
    MCM5P339924EBI-355153,EBI-359410
    MCM6Q145662EBI-355153,EBI-374900
    MCMBPQ9BTE311EBI-355153,EBI-749378
    ORC2Q134162EBI-355153,EBI-374957

    Protein-protein interaction databases

    BioGridi110340. 88 interactions.
    DIPiDIP-31726N.
    IntActiP25205. 38 interactions.
    MINTiMINT-1201900.
    STRINGi9606.ENSP00000229854.

    Structurei

    3D structure databases

    ProteinModelPortaliP25205.
    SMRiP25205. Positions 10-650.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini295 – 502208MCMAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi477 – 4804Arginine finger

    Sequence similaritiesi

    Belongs to the MCM family.Curated
    Contains 1 MCM domain.Curated

    Phylogenomic databases

    eggNOGiCOG1241.
    HOGENOMiHOG000224126.
    HOVERGENiHBG104962.
    InParanoidiP25205.
    KOiK02541.
    PhylomeDBiP25205.
    TreeFamiTF106459.

    Family and domain databases

    Gene3Di2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR008046. Mcm3.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00493. MCM. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view]
    PRINTSiPR01657. MCMFAMILY.
    PR01659. MCMPROTEIN3.
    SMARTiSM00382. AAA. 1 hit.
    SM00350. MCM. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEiPS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P25205-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGTVVLDDV ELREAQRDYL DFLDDEEDQG IYQSKVRELI SDNQYRLIVN    50
    VNDLRRKNEK RANRLLNNAF EELVAFQRAL KDFVASIDAT YAKQYEEFYV 100
    GLEGSFGSKH VSPRTLTSCF LSCVVCVEGI VTKCSLVRPK VVRSVHYCPA 150
    TKKTIERRYS DLTTLVAFPS SSVYPTKDEE NNPLETEYGL SVYKDHQTIT 200
    IQEMPEKAPA GQLPRSVDVI LDDDLVDKAK PGDRVQVVGT YRCLPGKKGG 250
    YTSGTFRTVL IACNVKQMSK DAQPSFSAED IAKIKKFSKT RSKDIFDQLA 300
    KSLAPSIHGH DYVKKAILCL LLGGVERDLE NGSHIRGDIN ILLIGDPSVA 350
    KSQLLRYVLC TAPRAIPTTG RGSSGVGLTA AVTTDQETGE RRLEAGAMVL 400
    ADRGVVCIDE FDKMSDMDRT AIHEVMEQGR VTIAKAGIHA RLNARCSVLA 450
    AANPVYGRYD QYKTPMENIG LQDSLLSRFD LLFIMLDQMD PEQDREISDH 500
    VLRMHRYRAP GEQDGDAMPL GSAVDILATD DPNFSQEDQQ DTQIYEKHDN 550
    LLHGTKKKKE KMVSAAFMKK YIHVAKIIKP VLTQESATYI AEEYSRLRSQ 600
    DSMSSDTART SPVTARTLET LIRLATAHAK ARMSKTVDLQ DAEEAVELVQ 650
    YAYFKKVLEK EKKRKKRSED ESETEDEEEK SQEDQEQKRK RRKTRQPDAK 700
    DGDSYDPYDF SDTEEEMPQV HTPKTADSQE TKESQKVELS ESRLKAFKVA 750
    LLDVFREAHA QSIGMNRLTE SINRDSEEPF SSVEIQAALS KMQDDNQVMV 800
    SEGIIFLI 808
    Length:808
    Mass (Da):90,981
    Last modified:August 14, 2001 - v3
    Checksum:iC967C068B7090558
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti230 – 2312KP → NA in BAA07267. (PubMed:7758114)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti105 – 1051S → G.
    Corresponds to variant rs2307332 [ dbSNP | Ensembl ].
    VAR_014810
    Natural varianti280 – 2801D → V.1 Publication
    Corresponds to variant rs2307329 [ dbSNP | Ensembl ].
    VAR_014811
    Natural varianti287 – 2871F → L.1 Publication
    Corresponds to variant rs2307328 [ dbSNP | Ensembl ].
    VAR_014812
    Natural varianti590 – 5901I → L.1 Publication
    Corresponds to variant rs17240063 [ dbSNP | Ensembl ].
    VAR_020516
    Natural varianti774 – 7741R → W.1 Publication
    Corresponds to variant rs2230239 [ dbSNP | Ensembl ].
    VAR_020517
    Natural varianti777 – 7771E → K.1 Publication
    Corresponds to variant rs2230240 [ dbSNP | Ensembl ].
    VAR_020427

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS62594.
    RefSeqiNP_001257401.1. NM_001270472.1.
    NP_002379.3. NM_002388.4.
    UniGeneiHs.179565.

    Genome annotation databases

    EnsembliENST00000229854; ENSP00000229854; ENSG00000112118.
    GeneIDi4172.
    KEGGihsa:4172.

    Polymorphism databases

    DMDMi19857543.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S62594.
    RefSeqi NP_001257401.1. NM_001270472.1.
    NP_002379.3. NM_002388.4.
    UniGenei Hs.179565.

    3D structure databases

    ProteinModelPortali P25205.
    SMRi P25205. Positions 10-650.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110340. 88 interactions.
    DIPi DIP-31726N.
    IntActi P25205. 38 interactions.
    MINTi MINT-1201900.
    STRINGi 9606.ENSP00000229854.

    PTM databases

    PhosphoSitei P25205.

    Polymorphism databases

    DMDMi 19857543.

    Proteomic databases

    MaxQBi P25205.
    PaxDbi P25205.
    PeptideAtlasi P25205.
    PRIDEi P25205.

    Protocols and materials databases

    DNASUi 4172.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229854 ; ENSP00000229854 ; ENSG00000112118 .
    GeneIDi 4172.
    KEGGi hsa:4172.

    Organism-specific databases

    CTDi 4172.
    GeneCardsi GC06M052128.
    HGNCi HGNC:6945. MCM3.
    HPAi CAB002162.
    HPA004789.
    HPA004790.
    MIMi 602693. gene.
    neXtProti NX_P25205.
    PharmGKBi PA30691.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1241.
    HOGENOMi HOG000224126.
    HOVERGENi HBG104962.
    InParanoidi P25205.
    KOi K02541.
    PhylomeDBi P25205.
    TreeFami TF106459.

    Enzyme and pathway databases

    Reactomei REACT_1095. Activation of the pre-replicative complex.
    REACT_1156. Orc1 removal from chromatin.
    REACT_207. Removal of licensing factors from origins.
    REACT_2148. Switching of origins to a post-replicative state.
    REACT_2243. Assembly of the pre-replicative complex.
    REACT_6769. Activation of ATR in response to replication stress.
    REACT_6776. Unwinding of DNA.

    Miscellaneous databases

    ChiTaRSi MCM3. human.
    GeneWikii MCM3.
    GenomeRNAii 4172.
    NextBioi 13605303.
    PMAP-CutDB P25205.
    PROi P25205.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25205.
    Bgeei P25205.
    CleanExi HS_MCM3.
    Genevestigatori P25205.

    Family and domain databases

    Gene3Di 2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR008046. Mcm3.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00493. MCM. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01657. MCMFAMILY.
    PR01659. MCMPROTEIN3.
    SMARTi SM00382. AAA. 1 hit.
    SM00350. MCM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEi PS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      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: IDENTIFICATION IN THE MCM2-7 COMPLEX, INTERACTION WITH MCMBP, IDENTIFICATION BY MASS SPECTROMETRY.
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-668; SER-672; THR-674; SER-681; SER-711; THR-713 AND THR-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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.
    24. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMCM3_HUMAN
    AccessioniPrimary (citable) accession number: P25205
    Secondary accession number(s): Q92660, Q9BTR3, Q9NUE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: August 14, 2001
    Last modified: October 1, 2014
    This is version 169 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    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.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3