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Protein

Geminin

Gene

GMNN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

  • chromatin binding Source: CAFA
  • histone deacetylase binding Source: UniProtKB
  • repressing transcription factor binding Source: Ensembl
  • transcription corepressor activity Source: Ensembl

GO - Biological processi

  • animal organ morphogenesis Source: Ensembl
  • DNA replication preinitiation complex assembly Source: CAFA
  • G1/S transition of mitotic cell cycle Source: Reactome
  • negative regulation of cell cycle Source: UniProtKB
  • negative regulation of DNA-dependent DNA replication Source: CAFA
  • negative regulation of DNA replication Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of chromatin binding Source: CAFA

Keywordsi

Molecular functionDNA replication inhibitor
Biological processCell cycle

Enzyme and pathway databases

ReactomeiR-HSA-68827 CDT1 association with the CDC6:ORC:origin complex
R-HSA-68962 Activation of the pre-replicative complex

Names & Taxonomyi

Protein namesi
Recommended name:
Geminin
Gene namesi
Name:GMNN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000112312.9
HGNCiHGNC:17493 GMNN
MIMi602842 gene
neXtProtiNX_O75496

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Meier-Gorlin syndrome 6 (MGORS6)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:616835
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07617217K → R in MGORS6. 1 PublicationCorresponds to variant dbSNP:rs864309488EnsemblClinVar.1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi51053
MalaCardsiGMNN
MIMi616835 phenotype
OpenTargetsiENSG00000112312
PharmGKBiPA38455

Chemistry databases

ChEMBLiCHEMBL1293278

Polymorphism and mutation databases

BioMutaiGMNN

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001487291 – 209GemininAdd BLAST209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27N6-acetyllysineCombined sources1
Modified residuei34PhosphoserineCombined sources1
Modified residuei36PhosphoserineCombined sources1
Modified residuei49PhosphoserineCombined sources1
Modified residuei63PhosphoserineCombined sources1
Modified residuei64PhosphoserineCombined sources1
Modified residuei184Phosphoserine; by CK21 Publication1

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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO75496
MaxQBiO75496
PaxDbiO75496
PeptideAtlasiO75496
PRIDEiO75496
ProteomicsDBi50053

PTM databases

iPTMnetiO75496
PhosphoSitePlusiO75496

Miscellaneous databases

PMAP-CutDBiO75496

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

BgeeiENSG00000112312
CleanExiHS_GMNN
ExpressionAtlasiO75496 baseline and differential
GenevisibleiO75496 HS

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

Show more details

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB
  • repressing transcription factor binding Source: Ensembl

Protein-protein interaction databases

BioGridi119246, 71 interactors
CORUMiO75496
DIPiDIP-31088N
IntActiO75496, 27 interactors
MINTiO75496
STRINGi9606.ENSP00000230056

Structurei

Secondary structure

1209
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi110 – 142Combined sources33
Turni177 – 179Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
DisProtiDP00901
ProteinModelPortaliO75496
SMRiO75496
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75496

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni82 – 161Necessary and sufficient for interaction with IDAS and CDT11 PublicationAdd BLAST80
Regioni170 – 190Homeodomain bindingAdd BLAST21

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili94 – 1444 PublicationsAdd BLAST51

Sequence similaritiesi

Belongs to the geminin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG0B Eukaryota
ENOG410XZS9 LUCA
GeneTreeiENSGT00900000141037
HOGENOMiHOG000112711
HOVERGENiHBG002965
InParanoidiO75496
KOiK10749
OMAiVPEHSEN
OrthoDBiEOG091G19OS
PhylomeDBiO75496
TreeFamiTF101171

Family and domain databases

InterProiView protein in InterPro
IPR029697 Geminin
IPR022786 Geminin/Multicilin
PANTHERiPTHR13372:SF4 PTHR13372:SF4, 1 hit
PfamiView protein in Pfam
PF07412 Geminin, 1 hit

Sequencei

Sequence statusi: Complete.

O75496-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPSMKQKQE EIKENIKNSS VPRRTLKMIQ PSASGSLVGR ENELSAGLSK
60 70 80 90 100
RKHRNDHLTS TTSSPGVIVP ESSENKNLGG VTQESFDLMI KENPSSQYWK
110 120 130 140 150
EVAEKRRKAL YEALKENEKL HKEIEQKDNE IARLKKENKE LAEVAEHVQY
160 170 180 190 200
MAELIERLNG EPLDNFESLD NQEFDSEEET VEDSLVEDSE IGTCAEGTVS

SSTDAKPCI
Length:209
Mass (Da):23,565
Last modified:November 1, 1998 - v1
Checksum:i0BABE60F6F5AC252
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03395915N → H. Corresponds to variant dbSNP:rs34891389Ensembl.1
Natural variantiVAR_07617217K → R in MGORS6. 1 PublicationCorresponds to variant dbSNP:rs864309488EnsemblClinVar.1
Natural variantiVAR_02423318N → T1 PublicationCorresponds to variant dbSNP:rs1923185Ensembl.1
Natural variantiVAR_03396048L → F. Corresponds to variant dbSNP:rs2307307Ensembl.1
Natural variantiVAR_03396154R → W. Corresponds to variant dbSNP:rs2307306Ensembl.1
Natural variantiVAR_05310760S → P. Corresponds to variant dbSNP:rs2307302Ensembl.1
Natural variantiVAR_053108203T → M. Corresponds to variant dbSNP:rs2307303Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
ENST00000620958; ENSP00000477506; ENSG00000112312
GeneIDi51053
KEGGihsa:51053
UCSCiuc003nem.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiGEMI_HUMAN
AccessioniPrimary (citable) accession number: O75496
Secondary accession number(s): B3KMM8, Q9H1Z1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1998
Last modified: June 20, 2018
This is version 155 of the entry and version 1 of the sequence. See 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

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