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Protein

Geminin

Gene

GMNN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • histone deacetylase binding Source: UniProtKB
  • transcription corepressor activity Source: Ensembl

GO - Biological processi

  • animal organ morphogenesis Source: Ensembl
  • cell cycle Source: UniProtKB-KW
  • negative regulation of cell cycle Source: UniProtKB
  • negative regulation of DNA replication Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • protein complex assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

DNA replication inhibitor

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

BioCyciZFISH:ENSG00000112312-MONOMER.
ReactomeiR-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-69298. Association of licensing factors with the pre-replicative complex.
R-HSA-69300. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:17493. GMNN.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

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 rs864309488dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNETi51053.
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.

PTM databases

iPTMnetiO75496.
PhosphoSitePlusiO75496.

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

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

WithEntry#Exp.IntActNotes
CCDC146Q8IYE0-23EBI-371669,EBI-10247802
CDT1Q9H21114EBI-371669,EBI-456953
MCIDASD6RGH67EBI-371669,EBI-3954372
ZNF439Q8NDP45EBI-371669,EBI-747580

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119246. 67 interactors.
DIPiDIP-31088N.
IntActiO75496. 24 interactors.
MINTiMINT-1201770.
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[»]
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.
GeneTreeiENSGT00390000016394.
HOGENOMiHOG000112711.
HOVERGENiHBG002965.
InParanoidiO75496.
KOiK10749.
OMAiVPEHSEN.
OrthoDBiEOG091G19OS.
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

        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 rs34891389dbSNPEnsembl.1
Natural variantiVAR_07617217K → R in MGORS6. 1 PublicationCorresponds to variant rs864309488dbSNPEnsembl.1
Natural variantiVAR_02423318N → T.1 PublicationCorresponds to variant rs1923185dbSNPEnsembl.1
Natural variantiVAR_03396048L → F.Corresponds to variant rs2307307dbSNPEnsembl.1
Natural variantiVAR_03396154R → W.Corresponds to variant rs2307306dbSNPEnsembl.1
Natural variantiVAR_05310760S → P.Corresponds to variant rs2307302dbSNPEnsembl.1
Natural variantiVAR_053108203T → M.Corresponds to variant rs2307303dbSNPEnsembl.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

Cross-referencesi

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.

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[»]
ProteinModelPortaliO75496.
SMRiO75496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119246. 67 interactors.
DIPiDIP-31088N.
IntActiO75496. 24 interactors.
MINTiMINT-1201770.
STRINGi9606.ENSP00000230056.

Chemistry databases

ChEMBLiCHEMBL1293278.

PTM databases

iPTMnetiO75496.
PhosphoSitePlusiO75496.

Polymorphism and mutation databases

BioMutaiGMNN.

Proteomic databases

EPDiO75496.
MaxQBiO75496.
PaxDbiO75496.
PeptideAtlasiO75496.
PRIDEiO75496.

Protocols and materials databases

DNASUi51053.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000230056; ENSP00000230056; ENSG00000112312.
ENST00000356509; ENSP00000348902; ENSG00000112312.
ENST00000620958; ENSP00000477506; ENSG00000112312.
GeneIDi51053.
KEGGihsa:51053.
UCSCiuc003nem.4. human.

Organism-specific databases

CTDi51053.
DisGeNETi51053.
GeneCardsiGMNN.
HGNCiHGNC:17493. GMNN.
HPAiCAB011458.
CAB047327.
CAB047328.
HPA049977.
HPA054597.
MIMi602842. gene.
616835. phenotype.
neXtProtiNX_O75496.
OpenTargetsiENSG00000112312.
PharmGKBiPA38455.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG0B. Eukaryota.
ENOG410XZS9. LUCA.
GeneTreeiENSGT00390000016394.
HOGENOMiHOG000112711.
HOVERGENiHBG002965.
InParanoidiO75496.
KOiK10749.
OMAiVPEHSEN.
OrthoDBiEOG091G19OS.
PhylomeDBiO75496.
TreeFamiTF101171.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000112312-MONOMER.
ReactomeiR-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-69298. Association of licensing factors with the pre-replicative complex.
R-HSA-69300. Removal of licensing factors from origins.

Miscellaneous databases

ChiTaRSiGMNN. human.
EvolutionaryTraceiO75496.
GeneWikiiGeminin.
GenomeRNAii51053.
PMAP-CutDBO75496.
PROiO75496.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000112312.
CleanExiHS_GMNN.
ExpressionAtlasiO75496. baseline and differential.
GenevisibleiO75496. HS.

Family and domain databases

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

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: November 30, 2016
This is version 145 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.