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Protein

Geminin

Gene

Gmnn

Organism
Mus musculus (Mouse)
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.2 Publications
Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control.By similarity

GO - Molecular functioni

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

GO - Biological processi

  • animal organ morphogenesis Source: MGI
  • DNA replication preinitiation complex assembly Source: Ensembl
  • negative regulation of cell cycle Source: UniProtKB
  • negative regulation of DNA-dependent DNA replication Source: Ensembl
  • negative regulation of DNA replication Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of chromatin binding Source: Ensembl
  • protein complex assembly Source: UniProtKB

Keywordsi

Molecular functionDNA replication inhibitor
Biological processCell cycle

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Geminin
Gene namesi
Name:Gmnn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1927344. Gmnn.

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001487301 – 206GemininAdd BLAST206

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27N6-acetyllysineBy similarity1
Modified residuei36PhosphoserineBy similarity1
Modified residuei63PhosphoserineBy similarity1
Modified residuei64PhosphoserineBy similarity1
Modified residuei181Phosphoserine; by CK2By similarity1

Post-translational modificationi

Phosphorylated during mitosis. Phosphorylation at Ser-181 by CK2 results in enhanced binding to Hox proteins and more potent inhibitory effect on Hox transcriptional activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO88513.
PaxDbiO88513.
PRIDEiO88513.

PTM databases

iPTMnetiO88513.
PhosphoSitePlusiO88513.

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

BgeeiENSMUSG00000006715.
CleanExiMM_GMNN.
ExpressionAtlasiO88513. baseline and differential.
GenevisibleiO88513. MM.

Interactioni

Subunit structurei

Homotetramer. 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 (By similarity). 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.By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi208298. 18 interactors.
DIPiDIP-32562N.
IntActiO88513. 13 interactors.
MINTiMINT-1172279.
STRINGi10090.ENSMUSP00000006898.

Structurei

Secondary structure

1206
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni82 – 86Combined sources5
Helixi95 – 136Combined sources42
Helixi139 – 154Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZXXX-ray2.80A/B/D/E79-157[»]
ProteinModelPortaliO88513.
SMRiO88513.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88513.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni79 – 158Necessary and sufficient for interaction with IDAS and CDT1By similarityAdd BLAST80
Regioni167 – 187Homeodomain bindingBy similarityAdd BLAST21

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili91 – 141Add BLAST51

Sequence similaritiesi

Belongs to the geminin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG0B. Eukaryota.
ENOG410XZS9. LUCA.
GeneTreeiENSGT00390000016394.
HOGENOMiHOG000112711.
HOVERGENiHBG002965.
InParanoidiO88513.
KOiK10749.
OMAiVPEHSEN.
OrthoDBiEOG091G19OS.
PhylomeDBiO88513.
TreeFamiTF101171.

Family and domain databases

InterProiView protein in InterPro
IPR029697. Geminin.
IPR022786. Geminin/Multicilin.
PANTHERiPTHR13372:SF7. PTHR13372:SF7. 1 hit.
PfamiView protein in Pfam
PF07412. Geminin. 1 hit.

Sequencei

Sequence statusi: Complete.

O88513-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLSMKQKQE GAQENVKNSP VPRRTLKMIQ PSADGSLVGR ENELPKGLFK
60 70 80 90 100
RKLWDDQLAS QTSSCGPEAN ENKDVGDLTQ EAFDLISKEN PSSQYWKEVA
110 120 130 140 150
EQRRKALYEA LKENEKLHKE IEQKDSEIAR LRKENKDLAE VAEHVQYMAE
160 170 180 190 200
VIERLSNEPL DNFESPDSQE FDSEEEAVEY SELEDSGAGT CAEETVSSST

DARPCT
Length:206
Mass (Da):23,300
Last modified:November 1, 1998 - v1
Checksum:iB87153A5D5BCF5CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068780 mRNA. Translation: AAC24228.1.
BC020061 mRNA. Translation: AAH20061.1.
CCDSiCCDS26378.1.
RefSeqiNP_065592.1. NM_020567.2.
XP_006516786.1. XM_006516723.3.
UniGeneiMm.12239.

Genome annotation databases

EnsembliENSMUST00000006898; ENSMUSP00000006898; ENSMUSG00000006715.
ENSMUST00000110382; ENSMUSP00000106011; ENSMUSG00000006715.
GeneIDi57441.
KEGGimmu:57441.
UCSCiuc007pwg.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiGEMI_MOUSE
AccessioniPrimary (citable) accession number: O88513
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1998
Last modified: August 30, 2017
This is version 133 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families