O75496 · GEMI_HUMAN
- ProteinGeminin
- GeneGMNN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids209 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | transcription repressor complex | |
Molecular Function | chromatin binding | |
Molecular Function | DNA-binding transcription factor binding | |
Molecular Function | histone deacetylase binding | |
Molecular Function | transcription corepressor activity | |
Biological Process | animal organ morphogenesis | |
Biological Process | DNA replication preinitiation complex assembly | |
Biological Process | negative regulation of cell cycle | |
Biological Process | negative regulation of DNA replication | |
Biological Process | negative regulation of DNA-templated DNA replication | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | positive regulation of chromatin binding | |
Biological Process | regulation of DNA replication | |
Biological Process | regulation of DNA-templated DNA replication initiation | |
Biological Process | regulation of mitotic cell cycle |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGeminin
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75496
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Involvement in disease
Meier-Gorlin syndrome 6 (MGORS6)
- Note
- DescriptionA 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 alsoMIM:616835
Natural variants in MGORS6
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_076172 | 17 | K>R | in MGORS6; dbSNP:rs864309488 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_033959 | 15 | in dbSNP:rs34891389 | |||
Sequence: N → H | ||||||
Natural variant | VAR_076172 | 17 | in MGORS6; dbSNP:rs864309488 | |||
Sequence: K → R | ||||||
Natural variant | VAR_024233 | 18 | in dbSNP:rs1923185 | |||
Sequence: N → T | ||||||
Natural variant | VAR_033960 | 48 | in dbSNP:rs2307307 | |||
Sequence: L → F | ||||||
Natural variant | VAR_033961 | 54 | in dbSNP:rs2307306 | |||
Sequence: R → W | ||||||
Natural variant | VAR_053107 | 60 | in dbSNP:rs2307302 | |||
Sequence: S → P | ||||||
Natural variant | VAR_053108 | 203 | in dbSNP:rs2307303 | |||
Sequence: T → M |
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.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000148729 | 1-209 | UniProt | Geminin | |||
Sequence: MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLGGVTQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGEPLDNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI | |||||||
Modified residue | 27 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 34 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 36 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 49 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 63 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 64 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 184 | UniProt | Phosphoserine; by CK2 | ||||
Sequence: S |
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
- PTM
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).
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O75496 | CCDC146 Q8IYE0 | 5 | EBI-371669, EBI-10749669 | |
BINARY | O75496 | CCDC146 Q8IYE0-2 | 4 | EBI-371669, EBI-10247802 | |
BINARY | O75496 | CDKN2A P42771 | 2 | EBI-371669, EBI-375053 | |
BINARY | O75496 | CDT1 Q9H211 | 22 | EBI-371669, EBI-456953 | |
BINARY | O75496 | GLIS2 Q9BZE0 | 3 | EBI-371669, EBI-7251368 | |
BINARY | O75496 | HOXC9 P31274 | 3 | EBI-371669, EBI-1779423 | |
BINARY | O75496 | KANK2 Q63ZY3 | 3 | EBI-371669, EBI-2556193 | |
BINARY | O75496 | LNX1 Q8TBB1 | 3 | EBI-371669, EBI-739832 | |
BINARY | O75496 | MCIDAS D6RGH6 | 9 | EBI-371669, EBI-3954372 | |
BINARY | O75496 | PTPN11 Q06124-2 | 3 | EBI-371669, EBI-17635971 | |
BINARY | O75496 | SAPCD2 Q86UD0 | 3 | EBI-371669, EBI-2561646 | |
BINARY | O75496 | ZNF250 P15622-3 | 3 | EBI-371669, EBI-10177272 | |
BINARY | O75496 | ZNF439 Q8NDP4 | 7 | EBI-371669, EBI-747580 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-79 | Disordered | ||||
Sequence: MNPSMKQKQEEIKENIKNSSVPRRTLKMIQPSASGSLVGRENELSAGLSKRKHRNDHLTSTTSSPGVIVPESSENKNLG | ||||||
Compositional bias | 21-39 | Polar residues | ||||
Sequence: VPRRTLKMIQPSASGSLVG | ||||||
Compositional bias | 59-79 | Polar residues | ||||
Sequence: TSTTSSPGVIVPESSENKNLG | ||||||
Region | 82-161 | Necessary and sufficient for interaction with IDAS and CDT1 | ||||
Sequence: TQESFDLMIKENPSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNGE | ||||||
Coiled coil | 94-144 | |||||
Sequence: PSSQYWKEVAEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEV | ||||||
Region | 164-209 | Disordered | ||||
Sequence: DNFESLDNQEFDSEEETVEDSLVEDSEIGTCAEGTVSSSTDAKPCI | ||||||
Compositional bias | 168-186 | Acidic residues | ||||
Sequence: SLDNQEFDSEEETVEDSLV | ||||||
Region | 170-190 | Homeodomain binding | ||||
Sequence: DNQEFDSEEETVEDSLVEDSE | ||||||
Compositional bias | 194-209 | Polar residues | ||||
Sequence: CAEGTVSSSTDAKPCI |
Sequence similarities
Belongs to the geminin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length209
- Mass (Da)23,565
- Last updated1998-11-01 v1
- Checksum0BABE60F6F5AC252
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 21-39 | Polar residues | ||||
Sequence: VPRRTLKMIQPSASGSLVG | ||||||
Compositional bias | 59-79 | Polar residues | ||||
Sequence: TSTTSSPGVIVPESSENKNLG | ||||||
Compositional bias | 168-186 | Acidic residues | ||||
Sequence: SLDNQEFDSEEETVEDSLV | ||||||
Compositional bias | 194-209 | Polar residues | ||||
Sequence: CAEGTVSSSTDAKPCI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |