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P33991

- MCM4_HUMAN

UniProt

P33991 - MCM4_HUMAN

Protein

DNA replication licensing factor MCM4

Gene

MCM4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 5 (10 May 2005)
      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.1 Publication

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi510 – 5178ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA helicase activity Source: Ensembl
    3. protein binding Source: IntAct
    4. single-stranded DNA binding Source: Ensembl

    GO - Biological processi

    1. DNA replication Source: UniProtKB
    2. DNA replication initiation Source: InterPro
    3. DNA strand elongation involved in DNA replication Source: Reactome
    4. DNA unwinding involved in DNA replication Source: Ensembl
    5. G1/S transition of mitotic cell cycle Source: Reactome
    6. 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 MCM4 (EC:3.6.4.12)
    Alternative name(s):
    CDC21 homolog
    P1-CDC21
    Gene namesi
    Name:MCM4
    Synonyms:CDC21
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:6947. MCM4.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. MCM complex Source: UniProtKB
    2. membrane Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Natural killer cell and glucocorticoid deficiency with DNA repair defect (NKGCD) [MIM:609981]: An autosomal recessive disorder characterized by severe intra- and extrauterine growth retardation, microcephaly, decreased numbers of natural killer cells, and recurrent viral infections, most often affecting the respiratory tract and leading to respiratory failure. Affected individuals also have adrenal insufficiency requiring corticosteroid replacement therapy and may have an increased susceptibility to cancer.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi609981. phenotype.
    Orphaneti75391. Immunodeficiency with natural-killer cell deficiency and adrenal insufficiency.
    PharmGKBiPA30694.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 863862DNA replication licensing factor MCM4PRO_0000194101Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei26 – 261Phosphoserine1 Publication
    Modified residuei31 – 311Phosphoserine1 Publication
    Modified residuei32 – 321Phosphoserine2 Publications
    Modified residuei34 – 341Phosphoserine1 Publication
    Modified residuei120 – 1201Phosphoserine4 Publications
    Modified residuei131 – 1311Phosphoserine3 Publications
    Modified residuei142 – 1421Phosphoserine1 Publication
    Modified residuei145 – 1451Phosphoserine1 Publication
    Modified residuei220 – 2201N6-acetyllysine1 Publication
    Modified residuei450 – 4501N6-acetyllysine1 Publication
    Modified residuei858 – 8581N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP33991.
    PaxDbiP33991.
    PeptideAtlasiP33991.
    PRIDEiP33991.

    PTM databases

    PhosphoSiteiP33991.

    Miscellaneous databases

    PMAP-CutDBP33991.

    Expressioni

    Gene expression databases

    ArrayExpressiP33991.
    BgeeiP33991.
    CleanExiHS_MCM4.
    GenevestigatoriP33991.

    Organism-specific databases

    HPAiCAB004497.
    HPA004873.
    HPA031052.

    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). Interacts with MCMBP.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MCM7P3399314EBI-374938,EBI-355924
    MCMBPQ9BTE314EBI-374938,EBI-749378
    ORFQ9Q2G43EBI-374938,EBI-6248094From a different organism.
    SSRP1Q089455EBI-374938,EBI-353771
    SUPT16HQ9Y5B93EBI-374938,EBI-1046849

    Protein-protein interaction databases

    BioGridi110341. 61 interactions.
    DIPiDIP-31729N.
    IntActiP33991. 49 interactions.
    MINTiMINT-1202120.
    STRINGi9606.ENSP00000262105.

    Structurei

    3D structure databases

    ProteinModelPortaliP33991.
    SMRiP33991. Positions 159-766.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini458 – 667210MCMAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi642 – 6454Arginine finger

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1241.
    HOGENOMiHOG000224127.
    HOVERGENiHBG102781.
    InParanoidiP33991.
    KOiK02212.
    OMAiMHSSAIP.
    OrthoDBiEOG78D7JF.
    PhylomeDBiP33991.
    TreeFamiTF300463.

    Family and domain databases

    Gene3Di2.20.28.10. 1 hit.
    2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR008047. MCM_4.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    IPR004039. Rubredoxin-type_fold.
    [Graphical view]
    PfamiPF00493. MCM. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view]
    PRINTSiPR01657. MCMFAMILY.
    PR01660. MCMPROTEIN4.
    SMARTiSM00382. AAA. 1 hit.
    SM00350. MCM. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 1 hit.
    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.

    P33991-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSPASTPSR RGSRRGRATP AQTPRSEDAR SSPSQRRRGE DSTSTGELQP    50
    MPTSPGVDLQ SPAAQDVLFS SPPQMHSSAI PLDFDVSSPL TYGTPSSRVE 100
    GTPRSGVRGT PVRQRPDLGS AQKGLQVDLQ SDGAAAEDIV ASEQSLGQKL 150
    VIWGTDVNVA ACKENFQRFL QRFIDPLAKE EENVGIDITE PLYMQRLGEI 200
    NVIGEPFLNV NCEHIKSFDK NLYRQLISYP QEVIPTFDMA VNEIFFDRYP 250
    DSILEHQIQV RPFNALKTKN MRNLNPEDID QLITISGMVI RTSQLIPEMQ 300
    EAFFQCQVCA HTTRVEMDRG RIAEPSVCGR CHTTHSMALI HNRSLFSDKQ 350
    MIKLQESPED MPAGQTPHTV ILFAHNDLVD KVQPGDRVNV TGIYRAVPIR 400
    VNPRVSNVKS VYKTHIDVIH YRKTDAKRLH GLDEEAEQKL FSEKRVELLK 450
    ELSRKPDIYE RLASALAPSI YEHEDIKKGI LLQLFGGTRK DFSHTGRGKF 500
    RAEINILLCG DPGTSKSQLL QYVYNLVPRG QYTSGKGSSA VGLTAYVMKD 550
    PETRQLVLQT GALVLSDNGI CCIDEFDKMN ESTRSVLHEV MEQQTLSIAK 600
    AGIICQLNAR TSVLAAANPI ESQWNPKKTT IENIQLPHTL LSRFDLIFLL 650
    LDPQDEAYDR RLAHHLVALY YQSEEQAEEE LLDMAVLKDY IAYAHSTIMP 700
    RLSEEASQAL IEAYVDMRKI GSSRGMVSAY PRQLESLIRL AEAHAKVRLS 750
    NKVEAIDVEE AKRLHREALK QSATDPRTGI VDISILTTGM SATSRKRKEE 800
    LAEALKKLIL SKGKTPALKY QQLFEDIRGQ SDIAITKDMF EEALRALADD 850
    DFLTVTGKTV RLL 863
    Length:863
    Mass (Da):96,558
    Last modified:May 10, 2005 - v5
    Checksum:i96D9CA2A7D88D015
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti62 – 621P → T in CAA52801. (PubMed:7601140)Curated
    Sequence conflicti206 – 2061P → Q in CAA52801. (PubMed:7601140)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti460 – 4601E → G.1 Publication
    Corresponds to variant rs17287663 [ dbSNP | Ensembl ].
    VAR_020500
    Natural varianti650 – 6501L → M.3 Publications
    Corresponds to variant rs762679 [ dbSNP | Ensembl ].
    VAR_020501

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74794 mRNA. Translation: CAA52801.1.
    AY588245 Genomic DNA. Translation: AAS83108.1.
    BC031061 mRNA. Translation: AAH31061.1.
    U63630 Genomic DNA. Translation: AAC52018.1.
    U90415 Genomic DNA. Translation: AAB51723.3.
    CCDSiCCDS6143.1.
    PIRiS65954.
    RefSeqiNP_005905.2. NM_005914.3.
    NP_877423.1. NM_182746.2.
    UniGeneiHs.460184.

    Genome annotation databases

    EnsembliENST00000262105; ENSP00000262105; ENSG00000104738.
    ENST00000523944; ENSP00000430194; ENSG00000104738.
    GeneIDi4173.
    KEGGihsa:4173.
    UCSCiuc003xqk.2. human.

    Polymorphism databases

    DMDMi68571766.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74794 mRNA. Translation: CAA52801.1 .
    AY588245 Genomic DNA. Translation: AAS83108.1 .
    BC031061 mRNA. Translation: AAH31061.1 .
    U63630 Genomic DNA. Translation: AAC52018.1 .
    U90415 Genomic DNA. Translation: AAB51723.3 .
    CCDSi CCDS6143.1.
    PIRi S65954.
    RefSeqi NP_005905.2. NM_005914.3.
    NP_877423.1. NM_182746.2.
    UniGenei Hs.460184.

    3D structure databases

    ProteinModelPortali P33991.
    SMRi P33991. Positions 159-766.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110341. 61 interactions.
    DIPi DIP-31729N.
    IntActi P33991. 49 interactions.
    MINTi MINT-1202120.
    STRINGi 9606.ENSP00000262105.

    PTM databases

    PhosphoSitei P33991.

    Polymorphism databases

    DMDMi 68571766.

    Proteomic databases

    MaxQBi P33991.
    PaxDbi P33991.
    PeptideAtlasi P33991.
    PRIDEi P33991.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262105 ; ENSP00000262105 ; ENSG00000104738 .
    ENST00000523944 ; ENSP00000430194 ; ENSG00000104738 .
    GeneIDi 4173.
    KEGGi hsa:4173.
    UCSCi uc003xqk.2. human.

    Organism-specific databases

    CTDi 4173.
    GeneCardsi GC08P048873.
    H-InvDB HIX0007492.
    HGNCi HGNC:6947. MCM4.
    HPAi CAB004497.
    HPA004873.
    HPA031052.
    MIMi 602638. gene.
    609981. phenotype.
    neXtProti NX_P33991.
    Orphaneti 75391. Immunodeficiency with natural-killer cell deficiency and adrenal insufficiency.
    PharmGKBi PA30694.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1241.
    HOGENOMi HOG000224127.
    HOVERGENi HBG102781.
    InParanoidi P33991.
    KOi K02212.
    OMAi MHSSAIP.
    OrthoDBi EOG78D7JF.
    PhylomeDBi P33991.
    TreeFami TF300463.

    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 MCM4. human.
    GeneWikii MCM4.
    GenomeRNAii 4173.
    NextBioi 16436.
    PMAP-CutDB P33991.
    PROi P33991.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P33991.
    Bgeei P33991.
    CleanExi HS_MCM4.
    Genevestigatori P33991.

    Family and domain databases

    Gene3Di 2.20.28.10. 1 hit.
    2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR008047. MCM_4.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    IPR004039. Rubredoxin-type_fold.
    [Graphical view ]
    Pfami PF00493. MCM. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01657. MCMFAMILY.
    PR01660. MCMPROTEIN4.
    SMARTi SM00382. AAA. 1 hit.
    SM00350. MCM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human homologue of the yeast replication protein Cdc21. Interactions with other Mcm proteins."
      Musahl C., Schulte D., Burkhart R., Knippers R.
      Eur. J. Biochem. 230:1096-1101(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-650.
    2. NIEHS SNPs program
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-460.
    3. "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], VARIANT MET-650.
      Tissue: Testis.
    4. "The promoters for human DNA-PKcs (PRKDC) and MCM4: divergently transcribed genes located at chromosome 8 band q11."
      Connelly M.A., Zhang H., Kieleczawa J., Anderson C.W.
      Genomics 47:71-83(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-712.
    5. "MCM4 and PRKDC, human genes encoding proteins MCM4 and DNA-PKcs, are close neighbours located on chromosome 8q12-->q13."
      Ladenburger E.M., Fackelmayer F.O., Hameister H., Knippers R.
      Cytogenet. Cell Genet. 77:268-270(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-23.
    6. "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] OF 440-863, VARIANT MET-650.
      Tissue: Cervix.
    7. "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, FUNCTION.
    8. "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 SER-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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.
    10. "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: HELICASE ACTIVITY OF THE MCM2-3 COMPLEX, INTERACTION WITH MCMBP, IDENTIFICATION IN THE MCM2-7 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "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 SER-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-31; SER-32 AND SER-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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-220 AND LYS-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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 SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-120; SER-131; SER-142 AND SER-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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 SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "MCM4 mutation causes adrenal failure, short stature, and natural killer cell deficiency in humans."
      Hughes C.R., Guasti L., Meimaridou E., Chuang C.H., Schimenti J.C., King P.J., Costigan C., Clark A.J., Metherell L.A.
      J. Clin. Invest. 122:814-820(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN NKGCD.
    19. Cited for: INVOLVEMENT IN NKGCD.
    20. "Recessive mutations in MCM4/PRKDC cause a novel syndrome involving a primary immunodeficiency and a disorder of DNA repair."
      Casey J.P., Nobbs M., McGettigan P., Lynch S., Ennis S.
      J. Med. Genet. 49:242-245(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN NKGCD.
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMCM4_HUMAN
    AccessioniPrimary (citable) accession number: P33991
    Secondary accession number(s): Q8NEH1, Q99658
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 152 of the entry and version 5 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. 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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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