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P33993

- MCM7_HUMAN

UniProt

P33993 - MCM7_HUMAN

Protein

DNA replication licensing factor MCM7

Gene

MCM7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 4 (15 May 2002)
      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 S-phase checkpoint activation upon UV-induced damage.3 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi381 – 3888ATPSequence Analysis

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell proliferation Source: Ensembl
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. cellular response to epidermal growth factor stimulus Source: Ensembl
    4. DNA replication Source: Reactome
    5. DNA replication initiation Source: InterPro
    6. DNA strand elongation involved in DNA replication Source: Reactome
    7. DNA unwinding involved in DNA replication Source: Ensembl
    8. G1/S transition of mitotic cell cycle Source: Reactome
    9. mitotic cell cycle Source: Reactome
    10. regulation of phosphorylation Source: UniProtKB
    11. response to drug Source: Ensembl

    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 MCM7 (EC:3.6.4.12)
    Alternative name(s):
    CDC47 homolog
    P1.1-MCM3
    Gene namesi
    Name:MCM7
    Synonyms:CDC47, MCM2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:6950. MCM7.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. chromatin Source: ProtInc
    2. cytoplasm Source: HPA
    3. cytosol Source: Ensembl
    4. MCM complex Source: UniProtKB
    5. membrane Source: UniProtKB
    6. nucleoplasm Source: Reactome
    7. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30697.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 719718DNA replication licensing factor MCM7PRO_0000194119Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei121 – 1211Phosphoserine3 Publications
    Modified residuei365 – 3651Phosphoserine1 Publication
    Modified residuei500 – 5001Phosphoserine4 Publications

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP33993.
    PaxDbiP33993.
    PRIDEiP33993.

    PTM databases

    PhosphoSiteiP33993.

    Expressioni

    Gene expression databases

    ArrayExpressiP33993.
    BgeeiP33993.
    CleanExiHS_MCM2.
    HS_MCM7.
    GenevestigatoriP33993.

    Organism-specific databases

    HPAiCAB002163.
    CAB016312.
    HPA003898.

    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 the ATR-ATRIP complex and with RAD17. Interacts with TIPIN. Interacts with MCMBP.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC6Q997412EBI-355924,EBI-374862
    CDKN1BP465272EBI-355924,EBI-519280
    CDKN1CP499182EBI-355924,EBI-519256
    E6P031262EBI-355924,EBI-1177242From a different organism.
    E6P064622EBI-355924,EBI-7069993From a different organism.
    E6P064632EBI-355924,EBI-1186926From a different organism.
    INTS6Q9UL0310EBI-355924,EBI-1381827
    LYNP079484EBI-355924,EBI-79452
    LYNP07948-15EBI-355924,EBI-6895930
    MCM2P4973621EBI-355924,EBI-374819
    MCM4P3399114EBI-355924,EBI-374938
    MCM5P339928EBI-355924,EBI-359410
    MCM6Q145665EBI-355924,EBI-374900
    MCMBPQ9BTE316EBI-355924,EBI-749378
    MYCP011066EBI-355924,EBI-447544
    PLK1P533504EBI-355924,EBI-476768
    SMC1AQ146838EBI-355924,EBI-80690
    UBBP0CG472EBI-355924,EBI-413034

    Protein-protein interaction databases

    BioGridi110344. 107 interactions.
    DIPiDIP-27580N.
    IntActiP33993. 146 interactions.
    MINTiMINT-5005969.
    STRINGi9606.ENSP00000307288.

    Structurei

    3D structure databases

    ProteinModelPortaliP33993.
    SMRiP33993. Positions 8-642.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini332 – 538207MCMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni521 – 56444Interaction with RAD17Add
    BLAST
    Regioni577 – 719143Interaction with ATRIPAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi513 – 5164Arginine finger

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1241.
    HOGENOMiHOG000224125.
    HOVERGENiHBG000741.
    InParanoidiP33993.
    KOiK02210.
    OMAiDINICLM.
    OrthoDBiEOG7N0C42.
    PhylomeDBiP33993.
    TreeFamiTF300400.

    Family and domain databases

    Gene3Di2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR008050. MCM7.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR11630:SF26. PTHR11630:SF26. 1 hit.
    PfamiPF00493. MCM. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view]
    PRINTSiPR01657. MCMFAMILY.
    PR01663. MCMPROTEIN7.
    SMARTiSM00382. AAA. 1 hit.
    SM00350. MCM. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P33993-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALKDYALEK EKVKKFLQEF YQDDELGKKQ FKYGNQLVRL AHREQVALYV    50
    DLDDVAEDDP ELVDSICENA RRYAKLFADA VQELLPQYKE REVVNKDVLD 100
    VYIEHRLMME QRSRDPGMVR SPQNQYPAEL MRRFELYFQG PSSNKPRVIR 150
    EVRADSVGKL VTVRGIVTRV SEVKPKMVVA TYTCDQCGAE TYQPIQSPTF 200
    MPLIMCPSQE CQTNRSGGRL YLQTRGSRFI KFQEMKMQEH SDQVPVGNIP 250
    RSITVLVEGE NTRIAQPGDH VSVTGIFLPI LRTGFRQVVQ GLLSETYLEA 300
    HRIVKMNKSE DDESGAGELT REELRQIAEE DFYEKLAASI APEIYGHEDV 350
    KKALLLLLVG GVDQSPRGMK IRGNINICLM GDPGVAKSQL LSYIDRLAPR 400
    SQYTTGRGSS GVGLTAAVLR DSVSGELTLE GGALVLADQG VCCIDEFDKM 450
    AEADRTAIHE VMEQQTISIA KAGILTTLNA RCSILAAANP AYGRYNPRRS 500
    LEQNIQLPAA LLSRFDLLWL IQDRPDRDND LRLAQHITYV HQHSRQPPSQ 550
    FEPLDMKLMR RYIAMCREKQ PMVPESLADY ITAAYVEMRR EAWASKDATY 600
    TSARTLLAIL RLSTALARLR MVDVVEKEDV NEAIRLMEMS KDSLLGDKGQ 650
    TARTQRPADV IFATVRELVS GGRSVRFSEA EQRCVSRGFT PAQFQAALDE 700
    YEELNVWQVN ASRTRITFV 719
    Length:719
    Mass (Da):81,308
    Last modified:May 15, 2002 - v4
    Checksum:i330A1DEFAEFBFB88
    GO
    Isoform 2 (identifier: P33993-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         329-658: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:389
    Mass (Da):44,649
    Checksum:iCCAA37CB2DA54063
    GO
    Isoform 3 (identifier: P33993-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-176: Missing.

    Show »
    Length:543
    Mass (Da):60,643
    Checksum:i4CAA41B4F392F50C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1031I → L in CAA52803. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti114 – 1141R → Q.
    Corresponds to variant rs2307348 [ dbSNP | Ensembl ].
    VAR_029243
    Natural varianti144 – 1441N → S.1 Publication
    Corresponds to variant rs2070215 [ dbSNP | Ensembl ].
    VAR_013297
    Natural varianti473 – 4731G → S.
    Corresponds to variant rs2307347 [ dbSNP | Ensembl ].
    VAR_014817

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 176176Missing in isoform 3. 1 PublicationVSP_044310Add
    BLAST
    Alternative sequencei329 – 658330Missing in isoform 2. 1 PublicationVSP_003205Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D55716 mRNA. Translation: BAA09534.1.
    AK055379 mRNA. Translation: BAG51508.1.
    AC073842 Genomic DNA. No translation available.
    CH236956 Genomic DNA. Translation: EAL23855.1.
    CH236956 Genomic DNA. Translation: EAL23856.1.
    CH471091 Genomic DNA. Translation: EAW76598.1.
    CH471091 Genomic DNA. Translation: EAW76599.1.
    BC009398 mRNA. Translation: AAH09398.1.
    BC013375 mRNA. Translation: AAH13375.1.
    X74796 mRNA. Translation: CAA52803.1.
    D28480 mRNA. Translation: BAA05839.1.
    CCDSiCCDS5683.1. [P33993-1]
    CCDS5684.1. [P33993-3]
    PIRiS70583.
    RefSeqiNP_001265524.1. NM_001278595.1. [P33993-3]
    NP_005907.3. NM_005916.4. [P33993-1]
    NP_877577.1. NM_182776.2. [P33993-3]
    UniGeneiHs.438720.

    Genome annotation databases

    EnsembliENST00000303887; ENSP00000307288; ENSG00000166508. [P33993-1]
    ENST00000343023; ENSP00000344006; ENSG00000166508. [P33993-2]
    ENST00000354230; ENSP00000346171; ENSG00000166508. [P33993-3]
    GeneIDi4176.
    KEGGihsa:4176.
    UCSCiuc003usv.1. human. [P33993-1]

    Polymorphism databases

    DMDMi20981696.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D55716 mRNA. Translation: BAA09534.1 .
    AK055379 mRNA. Translation: BAG51508.1 .
    AC073842 Genomic DNA. No translation available.
    CH236956 Genomic DNA. Translation: EAL23855.1 .
    CH236956 Genomic DNA. Translation: EAL23856.1 .
    CH471091 Genomic DNA. Translation: EAW76598.1 .
    CH471091 Genomic DNA. Translation: EAW76599.1 .
    BC009398 mRNA. Translation: AAH09398.1 .
    BC013375 mRNA. Translation: AAH13375.1 .
    X74796 mRNA. Translation: CAA52803.1 .
    D28480 mRNA. Translation: BAA05839.1 .
    CCDSi CCDS5683.1. [P33993-1 ]
    CCDS5684.1. [P33993-3 ]
    PIRi S70583.
    RefSeqi NP_001265524.1. NM_001278595.1. [P33993-3 ]
    NP_005907.3. NM_005916.4. [P33993-1 ]
    NP_877577.1. NM_182776.2. [P33993-3 ]
    UniGenei Hs.438720.

    3D structure databases

    ProteinModelPortali P33993.
    SMRi P33993. Positions 8-642.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110344. 107 interactions.
    DIPi DIP-27580N.
    IntActi P33993. 146 interactions.
    MINTi MINT-5005969.
    STRINGi 9606.ENSP00000307288.

    Chemistry

    DrugBanki DB01076. Atorvastatin.

    PTM databases

    PhosphoSitei P33993.

    Polymorphism databases

    DMDMi 20981696.

    Proteomic databases

    MaxQBi P33993.
    PaxDbi P33993.
    PRIDEi P33993.

    Protocols and materials databases

    DNASUi 4176.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303887 ; ENSP00000307288 ; ENSG00000166508 . [P33993-1 ]
    ENST00000343023 ; ENSP00000344006 ; ENSG00000166508 . [P33993-2 ]
    ENST00000354230 ; ENSP00000346171 ; ENSG00000166508 . [P33993-3 ]
    GeneIDi 4176.
    KEGGi hsa:4176.
    UCSCi uc003usv.1. human. [P33993-1 ]

    Organism-specific databases

    CTDi 4176.
    GeneCardsi GC07M099690.
    HGNCi HGNC:6950. MCM7.
    HPAi CAB002163.
    CAB016312.
    HPA003898.
    MIMi 600592. gene.
    neXtProti NX_P33993.
    PharmGKBi PA30697.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1241.
    HOGENOMi HOG000224125.
    HOVERGENi HBG000741.
    InParanoidi P33993.
    KOi K02210.
    OMAi DINICLM.
    OrthoDBi EOG7N0C42.
    PhylomeDBi P33993.
    TreeFami TF300400.

    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 MCM7. human.
    GeneWikii MCM7.
    GenomeRNAii 4176.
    NextBioi 16450.
    PROi P33993.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P33993.
    Bgeei P33993.
    CleanExi HS_MCM2.
    HS_MCM7.
    Genevestigatori P33993.

    Family and domain databases

    Gene3Di 2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR008050. MCM7.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR11630:SF26. PTHR11630:SF26. 1 hit.
    Pfami PF00493. MCM. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01657. MCMFAMILY.
    PR01663. MCMPROTEIN7.
    SMARTi SM00382. AAA. 1 hit.
    SM00350. MCM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 2 hits.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "hCDC47, a human member of the MCM family. Dissociation of the nucleus-bound form during S phase."
      Fujita M., Kiyono T., Hayashi Y., Ishibashi M.
      J. Biol. Chem. 271:4349-4354(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-144.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    3. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Lung.
    7. Bienvenut W.V., von Kriegsheim A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-12; 16-29; 33-39; 76-106; 134-147; 252-282; 472-481; 500-514 AND 605-611, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Chronic myeloid leukemia cell.
    8. Hu B.
      Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 103-719.
    9. "Isolation and mapping of a human gene (MCM2) encoding a product homologous to yeast proteins involved in DNA replication."
      Nakatsuru S., Sudo K., Nakamura Y.
      Cytogenet. Cell Genet. 68:226-230(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 177-719.
      Tissue: Lung.
    10. "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 261-557.
      Tissue: Cervix.
    11. "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.
    12. "Interaction between human MCM7 and Rad17 proteins is required for replication checkpoint signaling."
      Tsao C.-C., Geisen C., Abraham R.T.
      EMBO J. 23:4660-4669(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ATR; ATRIP AND RAD17.
    13. "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: INTERACTION WITH ATRIP, FUNCTION.
    14. "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.
    15. "Tipin and Timeless form a mutually protective complex required for genotoxic stress resistance and checkpoint function."
      Chou D.M., Elledge S.J.
      Proc. Natl. Acad. Sci. U.S.A. 103:18143-18147(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIPIN.
    16. "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.
    17. "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-121 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-500, 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-121; SER-365 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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.
    23. "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].

    Entry informationi

    Entry nameiMCM7_HUMAN
    AccessioniPrimary (citable) accession number: P33993
    Secondary accession number(s): A4D2A1
    , A4D2A2, E9PGN9, Q15076, Q96D34, Q96GL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: May 15, 2002
    Last modified: October 1, 2014
    This is version 158 of the entry and version 4 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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