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O88513

- GEMI_MOUSE

UniProt

O88513 - GEMI_MOUSE

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Protein
Geminin
Gene
Gmnn
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.2 Publications

GO - Molecular functioni

  1. histone deacetylase binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. repressing transcription factor binding Source: UniProtKB
  4. transcription corepressor activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. negative regulation of DNA replication Source: UniProtKB
  3. negative regulation of cell cycle Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. organ morphogenesis Source: MGI
  6. protein complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

DNA replication inhibitor

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Geminin
Gene namesi
Name:Gmnn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:1927344. Gmnn.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 206206Geminin
PRO_0000148730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271N6-acetyllysine By similarity
Modified residuei63 – 631Phosphoserine By similarity
Modified residuei64 – 641Phosphoserine By similarity
Modified residuei181 – 1811Phosphoserine; by CK2 By similarity

Post-translational modificationi

Phosphorylated during mitosis By similarity. 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

PaxDbiO88513.
PRIDEiO88513.

PTM databases

PhosphoSiteiO88513.

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

ArrayExpressiO88513.
BgeeiO88513.
CleanExiMM_GMNN.
GenevestigatoriO88513.

Interactioni

Subunit structurei

Homotetramer. nteracts (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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cdt1Q8R4E93EBI-445922,EBI-457043
Hoxa11P313112EBI-445922,EBI-445941
Hoxd10P283592EBI-445922,EBI-445929
Scmh1Q8K2142EBI-445922,EBI-445955

Protein-protein interaction databases

BioGridi208298. 14 interactions.
DIPiDIP-32562N.
IntActiO88513. 9 interactions.
MINTiMINT-1172279.
STRINGi10090.ENSMUSP00000006898.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi95 – 13642
Helixi139 – 15416

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZXXX-ray2.80A/B/D/E79-157[»]
ProteinModelPortaliO88513.
SMRiO88513. Positions 79-156.

Miscellaneous databases

EvolutionaryTraceiO88513.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 15880Necessary and sufficient for interaction with IDAS and CDT1 By similarity
Add
BLAST
Regioni167 – 18721Homeodomain binding By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili91 – 141511 Publication
Add
BLAST

Sequence similaritiesi

Belongs to the geminin family.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG39688.
HOGENOMiHOG000112711.
HOVERGENiHBG002965.
InParanoidiO88513.
KOiK10749.
OMAiVPEHSEN.
OrthoDBiEOG7RFTJX.
PhylomeDBiO88513.
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.

O88513-1 [UniParc]FASTAAdd to Basket

« Hide

MNLSMKQKQE GAQENVKNSP VPRRTLKMIQ PSADGSLVGR ENELPKGLFK    50
RKLWDDQLAS QTSSCGPEAN ENKDVGDLTQ EAFDLISKEN PSSQYWKEVA 100
EQRRKALYEA LKENEKLHKE IEQKDSEIAR LRKENKDLAE VAEHVQYMAE 150
VIERLSNEPL DNFESPDSQE FDSEEEAVEY SELEDSGAGT CAEETVSSST 200
DARPCT 206
Length:206
Mass (Da):23,300
Last modified:November 1, 1998 - v1
Checksum:iB87153A5D5BCF5CF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF068780 mRNA. Translation: AAC24228.1.
BC020061 mRNA. Translation: AAH20061.1.
CCDSiCCDS26378.1.
RefSeqiNP_065592.1. NM_020567.2.
XP_006516785.1. XM_006516722.1.
XP_006516786.1. XM_006516723.1.
UniGeneiMm.12239.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF068780 mRNA. Translation: AAC24228.1 .
BC020061 mRNA. Translation: AAH20061.1 .
CCDSi CCDS26378.1.
RefSeqi NP_065592.1. NM_020567.2.
XP_006516785.1. XM_006516722.1.
XP_006516786.1. XM_006516723.1.
UniGenei Mm.12239.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZXX X-ray 2.80 A/B/D/E 79-157 [» ]
ProteinModelPortali O88513.
SMRi O88513. Positions 79-156.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208298. 14 interactions.
DIPi DIP-32562N.
IntActi O88513. 9 interactions.
MINTi MINT-1172279.
STRINGi 10090.ENSMUSP00000006898.

PTM databases

PhosphoSitei O88513.

Proteomic databases

PaxDbi O88513.
PRIDEi O88513.

Protocols and materials databases

DNASUi 57441.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000006898 ; ENSMUSP00000006898 ; ENSMUSG00000006715 .
ENSMUST00000110382 ; ENSMUSP00000106011 ; ENSMUSG00000006715 .
GeneIDi 57441.
KEGGi mmu:57441.
UCSCi uc007pwg.1. mouse.

Organism-specific databases

CTDi 51053.
MGIi MGI:1927344. Gmnn.

Phylogenomic databases

eggNOGi NOG39688.
HOGENOMi HOG000112711.
HOVERGENi HBG002965.
InParanoidi O88513.
KOi K10749.
OMAi VPEHSEN.
OrthoDBi EOG7RFTJX.
PhylomeDBi O88513.
TreeFami TF101171.

Miscellaneous databases

EvolutionaryTracei O88513.
NextBioi 313837.
PROi O88513.
SOURCEi Search...

Gene expression databases

ArrayExpressi O88513.
Bgeei O88513.
CleanExi MM_GMNN.
Genevestigatori O88513.

Family and domain databases

InterProi IPR029697. Geminin.
IPR022786. Geminin/Multicilin.
[Graphical view ]
PANTHERi PTHR13372:SF4. PTHR13372:SF4. 1 hit.
Pfami PF07412. Geminin. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Geminin, an inhibitor of DNA replication, is degraded during mitosis."
    McGarry T.J., Kirschner M.W.
    Cell 93:1043-1053(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Mouse geminin inhibits not only Cdt1-MCM6 interactions but also a novel intrinsic Cdt1 DNA binding activity."
    Yanagi K., Mizuno T., You Z., Hanaoka F.
    J. Biol. Chem. 277:40871-40880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDT1.
  4. "Structural basis for inhibition of the replication licensing factor Cdt1 by geminin."
    Lee C., Hong B., Choi J.M., Kim Y., Watanabe S., Ishimi Y., Enomoto T., Tada S., Kim Y., Cho Y.
    Nature 430:913-917(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 79-157 IN COMPLEX WITH CDT1, DOMAIN COILED COIL, SUBUNIT.

Entry informationi

Entry nameiGEMI_MOUSE
AccessioniPrimary (citable) accession number: O88513
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1998
Last modified: September 3, 2014
This is version 109 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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