O75496 · GEMI_HUMAN

Function

function

Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC) (PubMed:14993212, PubMed:20129055, PubMed:24064211, PubMed:9635433).
It is degraded during the mitotic phase of the cell cycle (PubMed:14993212, PubMed:24064211, PubMed:9635433).
Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle (PubMed:14993212, PubMed:24064211, PubMed:9635433).
Inhibits histone acetyltransferase activity of KAT7/HBO1 in a CDT1-dependent manner, inhibiting histone H4 acetylation and DNA replication licensing (PubMed:20129055).
Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control (PubMed:22615398).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componenttranscription repressor complex
Molecular Functionchromatin binding
Molecular FunctionDNA-binding transcription factor binding
Molecular Functionhistone deacetylase binding
Molecular Functiontranscription corepressor activity
Biological Processanimal organ morphogenesis
Biological ProcessDNA replication preinitiation complex assembly
Biological Processnegative regulation of cell cycle
Biological Processnegative regulation of DNA replication
Biological Processnegative regulation of DNA-templated DNA replication
Biological Processnegative regulation of DNA-templated transcription
Biological Processpositive regulation of chromatin binding
Biological Processregulation of DNA replication
Biological Processregulation of DNA-templated DNA replication initiation
Biological Processregulation of mitotic cell cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Geminin

Gene names

    • Name
      GMNN

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O75496
  • Secondary accessions
    • B3KMM8
    • Q9H1Z1

Proteomes

Organism-specific databases

Subcellular Location

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

Keywords

Disease & Variants

Involvement in disease

Meier-Gorlin syndrome 6 (MGORS6)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A form of Meier-Gorlin syndrome, a syndrome characterized by bilateral microtia, aplasia/hypoplasia of the patellae, and severe intrauterine and postnatal growth retardation with short stature and poor weight gain. Additional clinical findings include anomalies of cranial sutures, microcephaly, apparently low-set and simple ears, microstomia, full lips, highly arched or cleft palate, micrognathia, genitourinary tract anomalies, and various skeletal anomalies. While almost all cases have primordial dwarfism with substantial prenatal and postnatal growth retardation, not all cases have microcephaly, and microtia and absent/hypoplastic patella are absent in some. Despite the presence of microcephaly, intellect is usually normal.
  • See also
    MIM:616835
Natural variants in MGORS6
Variant IDPosition(s)ChangeDescription
VAR_07617217K>Rin MGORS6; dbSNP:rs864309488

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_03395915in dbSNP:rs34891389
Natural variantVAR_07617217in MGORS6; dbSNP:rs864309488
Natural variantVAR_02423318in dbSNP:rs1923185
Natural variantVAR_03396048in dbSNP:rs2307307
Natural variantVAR_03396154in dbSNP:rs2307306
Natural variantVAR_05310760in dbSNP:rs2307302
Natural variantVAR_053108203in dbSNP:rs2307303

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 212 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00001487291-209UniProtGeminin
Modified residue27UniProtN6-acetyllysine
Modified residue34UniProtPhosphoserine
Modified residue (large scale data)34PRIDEPhosphoserine
Modified residue36UniProtPhosphoserine
Modified residue (large scale data)45PRIDEPhosphoserine
Modified residue49UniProtPhosphoserine
Modified residue (large scale data)49PRIDEPhosphoserine
Modified residue63UniProtPhosphoserine
Modified residue (large scale data)63PRIDEPhosphoserine
Modified residue64UniProtPhosphoserine
Modified residue (large scale data)64PRIDEPhosphoserine
Modified residue184UniProtPhosphoserine; by CK2

Post-translational modification

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.

Keywords

Proteomic databases

PTM databases

Expression

Developmental stage

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

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homotetramer (PubMed:15260975, PubMed:15313623, PubMed:15378034, PubMed:19906994).
Interacts with CDT1; this inhibits binding of the MCM complex to origins of replication (PubMed:14993212, PubMed:15260975, PubMed:19906994, PubMed:21543332).
The complex with CDT1 exists in two forms, a 'permissive' heterotrimer and an 'inhibitory' heterohexamer (PubMed:14993212, PubMed:15260975, PubMed:19906994).
Interacts (via coiled-coil domain) with IDAS (via coiled-coil domain); this targets GMNN to the nucleus (PubMed:21543332).
The heterodimer formed by GMNN and MCIDAS has much lower affinity for CDT1 than the GMNN homodimer (PubMed:24064211).
Interacts with a subset of Hox proteins, affinity increasing from anterior to posterior types, the strongest interaction being with HOXB1, HOXC9 and HOXD10 (PubMed:22615398).
Interacts with LRWD1 from G1/S to mitosis (PubMed:22645314).

Binary interactions

View interactors in UniProtKB
View CPX-6094 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, coiled coil.

TypeIDPosition(s)Description
Region1-79Disordered
Compositional bias21-39Polar residues
Compositional bias59-79Polar residues
Region82-161Necessary and sufficient for interaction with IDAS and CDT1
Coiled coil94-144
Region164-209Disordered
Compositional bias168-186Acidic residues
Region170-190Homeodomain binding
Compositional bias194-209Polar residues

Sequence similarities

Belongs to the geminin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    209
  • Mass (Da)
    23,565
  • Last updated
    1998-11-01 v1
  • Checksum
    0BABE60F6F5AC252
MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9K0U5C9K0U5_HUMANGMNN65
H7C608H7C608_HUMANGMNN102
E2QRF9E2QRF9_HUMANGMNN179

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias21-39Polar residues
Compositional bias59-79Polar residues
Compositional bias168-186Acidic residues
Compositional bias194-209Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF067855
EMBL· GenBank· DDBJ
AAC39787.1
EMBL· GenBank· DDBJ
mRNA
AK021685
EMBL· GenBank· DDBJ
BAG51040.1
EMBL· GenBank· DDBJ
mRNA
AL133264
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC005185
EMBL· GenBank· DDBJ
AAH05185.1
EMBL· GenBank· DDBJ
mRNA
BC005389
EMBL· GenBank· DDBJ
AAH05389.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp