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O88513

- GEMI_MOUSE

UniProt

O88513 - GEMI_MOUSE

Protein

Geminin

Gene

Gmnn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC). It is degraded during the mitotic phase of the cell cycle. Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle.2 Publications
    Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control.By similarity

    GO - Molecular functioni

    1. histone deacetylase binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. repressing transcription factor binding Source: UniProtKB
    4. transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. negative regulation of cell cycle Source: UniProtKB
    3. negative regulation of DNA replication Source: UniProtKB
    4. negative regulation of transcription, DNA-templated Source: UniProtKB
    5. organ morphogenesis Source: MGI
    6. protein complex assembly Source: UniProtKB

    Keywords - Molecular functioni

    DNA replication inhibitor

    Keywords - Biological processi

    Cell cycle

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Geminin
    Gene namesi
    Name:Gmnn
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1927344. Gmnn.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Mainly cytoplasmic but can be relocalized to the nucleus.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 206206GemininPRO_0000148730Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271N6-acetyllysineBy similarity
    Modified residuei63 – 631PhosphoserineBy similarity
    Modified residuei64 – 641PhosphoserineBy similarity
    Modified residuei181 – 1811Phosphoserine; by CK2By similarity

    Post-translational modificationi

    Phosphorylated during mitosis. Phosphorylation at Ser-181 by CK2 results in enhanced binding to Hox proteins and more potent inhibitory effect on Hox transcriptional activity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiO88513.
    PRIDEiO88513.

    PTM databases

    PhosphoSiteiO88513.

    Expressioni

    Developmental stagei

    Absent during G1 phase, accumulates during S, G2, and M phases, and disappears at the time of the metaphase-anaphase transition.1 Publication

    Gene expression databases

    ArrayExpressiO88513.
    BgeeiO88513.
    CleanExiMM_GMNN.
    GenevestigatoriO88513.

    Interactioni

    Subunit structurei

    Homotetramer. nteracts (via coiled-coil domain) with IDAS (via coiled-coil domain); this targets GMNN to the nucleus. The heterodimer formed by GMNN and MCIDAS has much lower affinity for CDT1 than the GMNN homodimer. Interacts with a subset of Hox proteins, affinity increasing from anterior to posterior types, the strongest interaction being with HOXB1, HOXC9 and HOXD10. Interacts with LRWD1 from G1/S to mitosis By similarity. Interacts with CDT1; this inhibits binding of the MCM complex to origins of replication. The complex with CDT1 exists in two forms, a "permissive" heterotrimer and an "inhibitory" heterohexamer.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Cdt1Q8R4E93EBI-445922,EBI-457043
    Hoxa11P313112EBI-445922,EBI-445941
    Hoxd10P283592EBI-445922,EBI-445929
    Scmh1Q8K2142EBI-445922,EBI-445955

    Protein-protein interaction databases

    BioGridi208298. 14 interactions.
    DIPiDIP-32562N.
    IntActiO88513. 9 interactions.
    MINTiMINT-1172279.
    STRINGi10090.ENSMUSP00000006898.

    Structurei

    Secondary structure

    1
    206
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi95 – 13642
    Helixi139 – 15416

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZXXX-ray2.80A/B/D/E79-157[»]
    ProteinModelPortaliO88513.
    SMRiO88513. Positions 79-156.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO88513.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni79 – 15880Necessary and sufficient for interaction with IDAS and CDT1By similarityAdd
    BLAST
    Regioni167 – 18721Homeodomain bindingBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili91 – 14151Add
    BLAST

    Sequence similaritiesi

    Belongs to the geminin family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG39688.
    HOGENOMiHOG000112711.
    HOVERGENiHBG002965.
    InParanoidiO88513.
    KOiK10749.
    OMAiVPEHSEN.
    OrthoDBiEOG7RFTJX.
    PhylomeDBiO88513.
    TreeFamiTF101171.

    Family and domain databases

    InterProiIPR029697. Geminin.
    IPR022786. Geminin/Multicilin.
    [Graphical view]
    PANTHERiPTHR13372:SF4. PTHR13372:SF4. 1 hit.
    PfamiPF07412. Geminin. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O88513-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNLSMKQKQE GAQENVKNSP VPRRTLKMIQ PSADGSLVGR ENELPKGLFK    50
    RKLWDDQLAS QTSSCGPEAN ENKDVGDLTQ EAFDLISKEN PSSQYWKEVA 100
    EQRRKALYEA LKENEKLHKE IEQKDSEIAR LRKENKDLAE VAEHVQYMAE 150
    VIERLSNEPL DNFESPDSQE FDSEEEAVEY SELEDSGAGT CAEETVSSST 200
    DARPCT 206
    Length:206
    Mass (Da):23,300
    Last modified:November 1, 1998 - v1
    Checksum:iB87153A5D5BCF5CF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF068780 mRNA. Translation: AAC24228.1.
    BC020061 mRNA. Translation: AAH20061.1.
    CCDSiCCDS26378.1.
    RefSeqiNP_065592.1. NM_020567.2.
    XP_006516785.1. XM_006516722.1.
    XP_006516786.1. XM_006516723.1.
    UniGeneiMm.12239.

    Genome annotation databases

    EnsembliENSMUST00000006898; ENSMUSP00000006898; ENSMUSG00000006715.
    ENSMUST00000110382; ENSMUSP00000106011; ENSMUSG00000006715.
    GeneIDi57441.
    KEGGimmu:57441.
    UCSCiuc007pwg.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF068780 mRNA. Translation: AAC24228.1 .
    BC020061 mRNA. Translation: AAH20061.1 .
    CCDSi CCDS26378.1.
    RefSeqi NP_065592.1. NM_020567.2.
    XP_006516785.1. XM_006516722.1.
    XP_006516786.1. XM_006516723.1.
    UniGenei Mm.12239.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZXX X-ray 2.80 A/B/D/E 79-157 [» ]
    ProteinModelPortali O88513.
    SMRi O88513. Positions 79-156.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208298. 14 interactions.
    DIPi DIP-32562N.
    IntActi O88513. 9 interactions.
    MINTi MINT-1172279.
    STRINGi 10090.ENSMUSP00000006898.

    PTM databases

    PhosphoSitei O88513.

    Proteomic databases

    PaxDbi O88513.
    PRIDEi O88513.

    Protocols and materials databases

    DNASUi 57441.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006898 ; ENSMUSP00000006898 ; ENSMUSG00000006715 .
    ENSMUST00000110382 ; ENSMUSP00000106011 ; ENSMUSG00000006715 .
    GeneIDi 57441.
    KEGGi mmu:57441.
    UCSCi uc007pwg.1. mouse.

    Organism-specific databases

    CTDi 51053.
    MGIi MGI:1927344. Gmnn.

    Phylogenomic databases

    eggNOGi NOG39688.
    HOGENOMi HOG000112711.
    HOVERGENi HBG002965.
    InParanoidi O88513.
    KOi K10749.
    OMAi VPEHSEN.
    OrthoDBi EOG7RFTJX.
    PhylomeDBi O88513.
    TreeFami TF101171.

    Miscellaneous databases

    EvolutionaryTracei O88513.
    NextBioi 313837.
    PROi O88513.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88513.
    Bgeei O88513.
    CleanExi MM_GMNN.
    Genevestigatori O88513.

    Family and domain databases

    InterProi IPR029697. Geminin.
    IPR022786. Geminin/Multicilin.
    [Graphical view ]
    PANTHERi PTHR13372:SF4. PTHR13372:SF4. 1 hit.
    Pfami PF07412. Geminin. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Geminin, an inhibitor of DNA replication, is degraded during mitosis."
      McGarry T.J., Kirschner M.W.
      Cell 93:1043-1053(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
    2. "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].
    3. "Mouse geminin inhibits not only Cdt1-MCM6 interactions but also a novel intrinsic Cdt1 DNA binding activity."
      Yanagi K., Mizuno T., You Z., Hanaoka F.
      J. Biol. Chem. 277:40871-40880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDT1.
    4. "Structural basis for inhibition of the replication licensing factor Cdt1 by geminin."
      Lee C., Hong B., Choi J.M., Kim Y., Watanabe S., Ishimi Y., Enomoto T., Tada S., Kim Y., Cho Y.
      Nature 430:913-917(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 79-157 IN COMPLEX WITH CDT1, DOMAIN COILED COIL, SUBUNIT.

    Entry informationi

    Entry nameiGEMI_MOUSE
    AccessioniPrimary (citable) accession number: O88513
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3