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O75496

- GEMI_HUMAN

UniProt

O75496 - GEMI_HUMAN

Protein

Geminin

Gene

GMNN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (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.
    Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control.

    GO - Molecular functioni

    1. histone deacetylase binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. transcription corepressor activity Source: Ensembl

    GO - Biological processi

    1. mitotic cell cycle Source: Reactome
    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: Ensembl
    6. protein complex assembly Source: Ensembl

    Keywords - Molecular functioni

    DNA replication inhibitor

    Keywords - Biological processi

    Cell cycle

    Enzyme and pathway databases

    ReactomeiREACT_1181. Association of licensing factors with the pre-replicative complex.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_207. Removal of licensing factors from origins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Geminin
    Gene namesi
    Name:GMNN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17493. GMNN.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38455.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 209209GemininPRO_0000148729Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271N6-acetyllysine1 Publication
    Modified residuei63 – 631Phosphoserine2 Publications
    Modified residuei64 – 641Phosphoserine2 Publications
    Modified residuei184 – 1841Phosphoserine; by CK22 Publications

    Post-translational modificationi

    Phosphorylated during mitosis. Phosphorylation at Ser-184 by CK2 results in enhanced binding to Hox proteins and more potent inhibitory effect on Hox transcriptional activity.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO75496.
    PaxDbiO75496.
    PRIDEiO75496.

    PTM databases

    PhosphoSiteiO75496.

    Miscellaneous databases

    PMAP-CutDBO75496.

    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

    ArrayExpressiO75496.
    BgeeiO75496.
    CleanExiHS_GMNN.
    GenevestigatoriO75496.

    Organism-specific databases

    HPAiCAB011458.
    CAB047327.
    CAB047328.
    HPA049977.
    HPA054597.

    Interactioni

    Subunit structurei

    Homotetramer. 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. Interacts (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.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDT1Q9H21111EBI-371669,EBI-456953
    MCIDASD6RGH67EBI-371669,EBI-3954372

    Protein-protein interaction databases

    BioGridi119246. 25 interactions.
    DIPiDIP-31088N.
    IntActiO75496. 9 interactions.
    MINTiMINT-1201770.
    STRINGi9606.ENSP00000230056.

    Structurei

    Secondary structure

    1
    209
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi110 – 14233
    Turni177 – 1793

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T6FX-ray1.47A/B109-145[»]
    1UIIX-ray2.00A/B70-152[»]
    2LP0NMR-B171-190[»]
    2WVRX-ray3.30A/B1-209[»]
    4BRYX-ray2.89A83-160[»]
    ProteinModelPortaliO75496.
    SMRiO75496. Positions 92-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75496.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni82 – 16180Necessary and sufficient for interaction with IDAS and CDT1Add
    BLAST
    Regioni170 – 19021Homeodomain bindingAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili94 – 144514 PublicationsAdd
    BLAST

    Sequence similaritiesi

    Belongs to the geminin family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG39688.
    HOGENOMiHOG000112711.
    HOVERGENiHBG002965.
    InParanoidiO75496.
    KOiK10749.
    OMAiVPEHSEN.
    OrthoDBiEOG7RFTJX.
    PhylomeDBiO75496.
    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.

    O75496-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNPSMKQKQE EIKENIKNSS VPRRTLKMIQ PSASGSLVGR ENELSAGLSK    50
    RKHRNDHLTS TTSSPGVIVP ESSENKNLGG VTQESFDLMI KENPSSQYWK 100
    EVAEKRRKAL YEALKENEKL HKEIEQKDNE IARLKKENKE LAEVAEHVQY 150
    MAELIERLNG EPLDNFESLD NQEFDSEEET VEDSLVEDSE IGTCAEGTVS 200
    SSTDAKPCI 209
    Length:209
    Mass (Da):23,565
    Last modified:November 1, 1998 - v1
    Checksum:i0BABE60F6F5AC252
    GO

    Sequence cautioni

    The sequence CAC21511.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151N → H.
    Corresponds to variant rs34891389 [ dbSNP | Ensembl ].
    VAR_033959
    Natural varianti18 – 181N → T.1 Publication
    Corresponds to variant rs1923185 [ dbSNP | Ensembl ].
    VAR_024233
    Natural varianti48 – 481L → F.
    Corresponds to variant rs2307307 [ dbSNP | Ensembl ].
    VAR_033960
    Natural varianti54 – 541R → W.
    Corresponds to variant rs2307306 [ dbSNP | Ensembl ].
    VAR_033961
    Natural varianti60 – 601S → P.
    Corresponds to variant rs2307302 [ dbSNP | Ensembl ].
    VAR_053107
    Natural varianti203 – 2031T → M.
    Corresponds to variant rs2307303 [ dbSNP | Ensembl ].
    VAR_053108

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF067855 mRNA. Translation: AAC39787.1.
    AK021685 mRNA. Translation: BAG51040.1.
    AL133264 Genomic DNA. Translation: CAC21511.1. Different initiation.
    BC005185 mRNA. Translation: AAH05185.1.
    BC005389 mRNA. Translation: AAH05389.1.
    CCDSiCCDS4560.1.
    RefSeqiNP_001238918.1. NM_001251989.1.
    NP_001238919.1. NM_001251990.1.
    NP_001238920.1. NM_001251991.1.
    NP_056979.1. NM_015895.4.
    XP_005249216.1. XM_005249159.1.
    UniGeneiHs.234896.

    Genome annotation databases

    EnsembliENST00000230056; ENSP00000230056; ENSG00000112312.
    ENST00000356509; ENSP00000348902; ENSG00000112312.
    GeneIDi51053.
    KEGGihsa:51053.
    UCSCiuc003nem.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF067855 mRNA. Translation: AAC39787.1 .
    AK021685 mRNA. Translation: BAG51040.1 .
    AL133264 Genomic DNA. Translation: CAC21511.1 . Different initiation.
    BC005185 mRNA. Translation: AAH05185.1 .
    BC005389 mRNA. Translation: AAH05389.1 .
    CCDSi CCDS4560.1.
    RefSeqi NP_001238918.1. NM_001251989.1.
    NP_001238919.1. NM_001251990.1.
    NP_001238920.1. NM_001251991.1.
    NP_056979.1. NM_015895.4.
    XP_005249216.1. XM_005249159.1.
    UniGenei Hs.234896.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T6F X-ray 1.47 A/B 109-145 [» ]
    1UII X-ray 2.00 A/B 70-152 [» ]
    2LP0 NMR - B 171-190 [» ]
    2WVR X-ray 3.30 A/B 1-209 [» ]
    4BRY X-ray 2.89 A 83-160 [» ]
    ProteinModelPortali O75496.
    SMRi O75496. Positions 92-152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119246. 25 interactions.
    DIPi DIP-31088N.
    IntActi O75496. 9 interactions.
    MINTi MINT-1201770.
    STRINGi 9606.ENSP00000230056.

    Chemistry

    ChEMBLi CHEMBL1293278.

    PTM databases

    PhosphoSitei O75496.

    Proteomic databases

    MaxQBi O75496.
    PaxDbi O75496.
    PRIDEi O75496.

    Protocols and materials databases

    DNASUi 51053.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000230056 ; ENSP00000230056 ; ENSG00000112312 .
    ENST00000356509 ; ENSP00000348902 ; ENSG00000112312 .
    GeneIDi 51053.
    KEGGi hsa:51053.
    UCSCi uc003nem.3. human.

    Organism-specific databases

    CTDi 51053.
    GeneCardsi GC06P024779.
    HGNCi HGNC:17493. GMNN.
    HPAi CAB011458.
    CAB047327.
    CAB047328.
    HPA049977.
    HPA054597.
    MIMi 602842. gene.
    neXtProti NX_O75496.
    PharmGKBi PA38455.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39688.
    HOGENOMi HOG000112711.
    HOVERGENi HBG002965.
    InParanoidi O75496.
    KOi K10749.
    OMAi VPEHSEN.
    OrthoDBi EOG7RFTJX.
    PhylomeDBi O75496.
    TreeFami TF101171.

    Enzyme and pathway databases

    Reactomei REACT_1181. Association of licensing factors with the pre-replicative complex.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_207. Removal of licensing factors from origins.

    Miscellaneous databases

    EvolutionaryTracei O75496.
    GeneWikii Geminin.
    GenomeRNAii 51053.
    NextBioi 53616.
    PMAP-CutDB O75496.
    PROi O75496.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75496.
    Bgeei O75496.
    CleanExi HS_GMNN.
    Genevestigatori O75496.

    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. "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], VARIANT THR-18.
      Tissue: Embryo.
    3. "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].
    4. "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: Lung and Urinary bladder.
    5. "Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates its function without affecting geminin binding."
      Sugimoto N., Tatsumi Y., Tsurumi T., Matsukage A., Kiyono T., Nishitani H., Fujita M.
      J. Biol. Chem. 279:19691-19697(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDT1.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Idas, a novel phylogenetically conserved geminin-related protein, binds to geminin and is required for cell cycle progression."
      Pefani D.E., Dimaki M., Spella M., Karantzelis N., Mitsiki E., Kyrousi C., Symeonidou I.E., Perrakis A., Taraviras S., Lygerou Z.
      J. Biol. Chem. 286:23234-23246(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IDAS AND CDT1.
    10. "Dynamic association of ORCA with prereplicative complex components regulates DNA replication initiation."
      Shen Z., Chakraborty A., Jain A., Giri S., Ha T., Prasanth K.V., Prasanth S.G.
      Mol. Cell. Biol. 32:3107-3120(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRWD1 AND CDT1, PHOSPHORYLATION DURING MITOSIS.
    11. "Crystal structure of the coiled-coil dimerization motif of geminin: structural and functional insights on DNA replication regulation."
      Thepaut M., Maiorano D., Guichou J.-F., Auge M.-T., Dumas C., Mechali M., Padilla A.
      J. Mol. Biol. 342:275-287(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 110-145, SUBUNIT, COILED-COIL DOMAIN.
    12. "A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition."
      Saxena S., Yuan P., Dhar S.K., Senga T., Takeda D., Robinson H., Kornbluth S., Swaminathan K., Dutta A.
      Mol. Cell 15:245-258(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 70-152, SUBUNIT, INTERACTION WITH CDT1, COILED-COIL DOMAIN.
    13. Cited for: ELECTRON MICROSCOPY (17.5 ANGSTROMS), SUBUNIT, COILED-COIL DOMAIN.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), SUBUNIT.
    15. "Structural basis for homeodomain recognition by the cell-cycle regulator Geminin."
      Zhou B., Liu C., Xu Z., Zhu G.
      Proc. Natl. Acad. Sci. U.S.A. 109:8931-8936(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 171-190 IN COMPLEX WITH HOXC9, FUNCTION, PHOSPHORYLATION AT SER-184.
    16. "The Geminin and Idas coiled coils preferentially form a heterodimer that inhibits Geminin function in DNA replication licensing."
      Caillat C., Pefani E.D., Gillespie P.J., Taraviras S., Blow J.J., Lygerou Z., Perrakis A.
      J. Biol. Chem. 288:31624-31634(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 83-160 IN COMPLEX WITH MCIDAS, SUBUNIT, FUNCTION, COILED-COIL DOMAIN.

    Entry informationi

    Entry nameiGEMI_HUMAN
    AccessioniPrimary (citable) accession number: O75496
    Secondary accession number(s): B3KMM8, Q9H1Z1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 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

    Keywords - Technical termi

    3D-structure, Complete proteome, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3