Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P33992

- MCM5_HUMAN

UniProt

P33992 - MCM5_HUMAN

Protein

DNA replication licensing factor MCM5

Gene

MCM5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 5 (14 Aug 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 By similarity. Interacts with MCMBP.By similarity

    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 binding Source: UniProtKB-KW
    3. DNA helicase activity Source: InterPro
    4. protein binding Source: IntAct

    GO - Biological processi

    1. DNA replication Source: Reactome
    2. DNA replication initiation Source: InterPro
    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 MCM5 (EC:3.6.4.12)
    Alternative name(s):
    CDC46 homolog
    P1-CDC46
    Gene namesi
    Name:MCM5
    Synonyms:CDC46
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:6948. MCM5.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30695.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 734733DNA replication licensing factor MCM5PRO_0000194107Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei392 – 3921N6-acetyllysine1 Publication
    Modified residuei396 – 3961N6-acetyllysine1 Publication
    Modified residuei696 – 6961N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP33992.
    PaxDbiP33992.
    PeptideAtlasiP33992.
    PRIDEiP33992.

    PTM databases

    PhosphoSiteiP33992.

    Miscellaneous databases

    PMAP-CutDBP33992.

    Expressioni

    Gene expression databases

    ArrayExpressiP33992.
    BgeeiP33992.
    CleanExiHS_MCM5.
    GenevestigatoriP33992.

    Organism-specific databases

    HPAiCAB000101.
    HPA000845.
    HPA052880.

    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).2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIST2H4BP628052EBI-359410,EBI-302023
    MCM2P497365EBI-359410,EBI-374819
    MCM3P252054EBI-359410,EBI-355153
    MCM7P339938EBI-359410,EBI-355924
    MCMBPQ9BTE313EBI-359410,EBI-749378

    Protein-protein interaction databases

    BioGridi110342. 52 interactions.
    DIPiDIP-27578N.
    IntActiP33992. 40 interactions.
    MINTiMINT-5004198.
    STRINGi9606.ENSP00000216122.

    Structurei

    3D structure databases

    ProteinModelPortaliP33992.
    SMRiP33992. Positions 35-646.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini331 – 537207MCMAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1241.
    HOGENOMiHOG000224128.
    HOVERGENiHBG104907.
    InParanoidiP33992.
    KOiK02209.
    OMAiIVKDTHD.
    OrthoDBiEOG7SV0TR.
    PhylomeDBiP33992.
    TreeFamiTF105653.

    Family and domain databases

    Gene3Di2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR008048. MCM5.
    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.
    PR01661. MCMPROTEIN5.
    SMARTiSM00350. 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.

    P33992-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGFDDPGIF YSDSFGGDAQ ADEGQARKSQ LQRRFKEFLR QYRVGTDRTG    50
    FTFKYRDELK RHYNLGEYWI EVEMEDLASF DEDLADYLYK QPAEHLQLLE 100
    EAAKEVADEV TRPRPSGEEV LQDIQVMLKS DASPSSIRSL KSDMMSHLVK 150
    IPGIIIAASA VRAKATRISI QCRSCRNTLT NIAMRPGLEG YALPRKCNTD 200
    QAGRPKCPLD PYFIMPDKCK CVDFQTLKLQ ELPDAVPHGE MPRHMQLYCD 250
    RYLCDKVVPG NRVTIMGIYS IKKFGLTTSR GRDRVGVGIR SSYIRVLGIQ 300
    VDTDGSGRSF AGAVSPQEEE EFRRLAALPN VYEVISKSIA PSIFGGTDMK 350
    KAIACLLFGG SRKRLPDGLT RRGDINLLML GDPGTAKSQL LKFVEKCSPI 400
    GVYTSGKGSS AAGLTASVMR DPSSRNFIME GGAMVLADGG VVCIDEFDKM 450
    REDDRVAIHE AMEQQTISIA KAGITTTLNS RCSVLAAANS VFGRWDETKG 500
    EDNIDFMPTI LSRFDMIFIV KDEHNEERDV MLAKHVITLH VSALTQTQAV 550
    EGEIDLAKLK KFIAYCRVKC GPRLSAEAAE KLKNRYIIMR SGARQHERDS 600
    DRRSSIPITV RQLEAIVRIA EALSKMKLQP FATEADVEEA LRLFQVSTLD 650
    AALSGTLSGV EGFTSQEDQE MLSRIEKQLK RRFAIGSQVS EHSIIKDFTK 700
    QKYPEHAIHK VLQLMLRRGE IQHRMQRKVL YRLK 734
    Length:734
    Mass (Da):82,286
    Last modified:August 14, 2001 - v5
    Checksum:iA80280E61749998D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411Q → R in AAH03656. (PubMed:15489334)Curated
    Sequence conflicti434 – 4341M → W(PubMed:8265339)Curated
    Sequence conflicti527 – 5271E → V in BAA12176. 1 PublicationCurated
    Sequence conflicti591 – 5911S → T in BAA12176. 1 PublicationCurated
    Sequence conflicti593 – 60311ARQHERDSDRR → PVSTRGTVTA in BAA12176. 1 PublicationCuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti136 – 1361S → T.1 Publication
    Corresponds to variant rs2307334 [ dbSNP | Ensembl ].
    VAR_014813
    Natural varianti180 – 1801T → S.1 Publication
    Corresponds to variant rs2307340 [ dbSNP | Ensembl ].
    VAR_014814
    Natural varianti258 – 2581V → I.1 Publication
    Corresponds to variant rs2230933 [ dbSNP | Ensembl ].
    VAR_014815

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74795 mRNA. Translation: CAA52802.2.
    D83986 mRNA. Translation: BAA12176.1.
    CR456517 mRNA. Translation: CAG30403.1.
    AY212028 Genomic DNA. Translation: AAO21127.1.
    Z82244 Genomic DNA. No translation available.
    BC000142 mRNA. Translation: AAH00142.1.
    BC003656 mRNA. Translation: AAH03656.1.
    CCDSiCCDS13915.1.
    PIRiI38080.
    RefSeqiNP_006730.2. NM_006739.3.
    UniGeneiHs.517582.

    Genome annotation databases

    EnsembliENST00000216122; ENSP00000216122; ENSG00000100297.
    GeneIDi4174.
    KEGGihsa:4174.
    UCSCiuc003anu.4. human.

    Polymorphism databases

    DMDMi19858646.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74795 mRNA. Translation: CAA52802.2 .
    D83986 mRNA. Translation: BAA12176.1 .
    CR456517 mRNA. Translation: CAG30403.1 .
    AY212028 Genomic DNA. Translation: AAO21127.1 .
    Z82244 Genomic DNA. No translation available.
    BC000142 mRNA. Translation: AAH00142.1 .
    BC003656 mRNA. Translation: AAH03656.1 .
    CCDSi CCDS13915.1.
    PIRi I38080.
    RefSeqi NP_006730.2. NM_006739.3.
    UniGenei Hs.517582.

    3D structure databases

    ProteinModelPortali P33992.
    SMRi P33992. Positions 35-646.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110342. 52 interactions.
    DIPi DIP-27578N.
    IntActi P33992. 40 interactions.
    MINTi MINT-5004198.
    STRINGi 9606.ENSP00000216122.

    PTM databases

    PhosphoSitei P33992.

    Polymorphism databases

    DMDMi 19858646.

    Proteomic databases

    MaxQBi P33992.
    PaxDbi P33992.
    PeptideAtlasi P33992.
    PRIDEi P33992.

    Protocols and materials databases

    DNASUi 4174.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216122 ; ENSP00000216122 ; ENSG00000100297 .
    GeneIDi 4174.
    KEGGi hsa:4174.
    UCSCi uc003anu.4. human.

    Organism-specific databases

    CTDi 4174.
    GeneCardsi GC22P035798.
    HGNCi HGNC:6948. MCM5.
    HPAi CAB000101.
    HPA000845.
    HPA052880.
    MIMi 602696. gene.
    neXtProti NX_P33992.
    PharmGKBi PA30695.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1241.
    HOGENOMi HOG000224128.
    HOVERGENi HBG104907.
    InParanoidi P33992.
    KOi K02209.
    OMAi IVKDTHD.
    OrthoDBi EOG7SV0TR.
    PhylomeDBi P33992.
    TreeFami TF105653.

    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 MCM5. human.
    GeneWikii MCM5.
    GenomeRNAii 4174.
    NextBioi 16442.
    PMAP-CutDB P33992.
    PROi P33992.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P33992.
    Bgeei P33992.
    CleanExi HS_MCM5.
    Genevestigatori P33992.

    Family and domain databases

    Gene3Di 2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR008048. MCM5.
    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.
    PR01661. MCMPROTEIN5.
    SMARTi 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. Hu B.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cervix carcinoma.
    2. Goehring F., Jehnichen P., Hemmer W.H.
      Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Homo sapiens DNA replication licensing factor (huMCM5)."
      Mimura S., Nishimoto S., Kubota Y., Takisawa H., Nojima H.
      Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. NIEHS SNPs program
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-136; SER-180 AND ILE-258.
    6. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 Placenta.
    8. "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 352-590.
      Tissue: Cervix.
    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: INTERACTION WITH MCMBP, IDENTIFICATION IN THE MCM2-7 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    12. "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-392; LYS-396 AND LYS-696, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMCM5_HUMAN
    AccessioniPrimary (citable) accession number: P33992
    Secondary accession number(s): O60785
    , Q14578, Q9BTJ4, Q9BWL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: August 14, 2001
    Last modified: October 1, 2014
    This is version 159 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. The MCM2-7 hexamer is the proposed physiological active complex.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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