Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

F-box only protein 5

Gene

Fbxo5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates progression through early mitosis by inhibiting the anaphase promoting complex/cyclosome (APC). Binds to the APC activators CDC20 and FZR1/CDH1 to prevent APC activation. Can also bind directly to the APC to inhibit substrate-binding.By similarity1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri331 – 393IBR-typeSequence analysisAdd BLAST63

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • microtubule polymerization Source: MGI
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of meiotic nuclear division Source: MGI
  • negative regulation of ubiquitin-protein ligase activity involved in meiotic cell cycle Source: MGI
  • negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: UniProtKB
  • oocyte maturation Source: MGI
  • positive regulation of meiosis I Source: MGI
  • protein ubiquitination Source: UniProtKB-UniPathway
  • regulation of meiotic nuclear division Source: MGI
  • regulation of mitotic cell cycle Source: UniProtKB
  • regulation of mitotic nuclear division Source: GO_Central
  • spindle assembly Source: MGI
  • spindle assembly involved in female meiosis I Source: MGI
  • vesicle organization Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-113510. E2F mediated regulation of DNA replication.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-MMU-176417. Phosphorylation of Emi1.
R-MMU-68881. Mitotic Metaphase/Anaphase Transition.
R-MMU-69205. G1/S-Specific Transcription.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 5
Alternative name(s):
Early mitotic inhibitor 1
Gene namesi
Name:Fbxo5Imported
Synonyms:Emi11 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1914391. Fbxo5.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Cytoplasmcytoskeletonspindle By similarity

  • Note: In interphase, localizes in a punctate manner in the nucleus and cytoplasm with some perinuclear concentration. In mitotic cells, localizes throughout the cell, particularly at the spindle (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

Death at the preimplantation stage. Embryos display normal cell proliferation but mitotic progression is severely defective during embryonic cleavage with multipolar spindles and misaligned chromosomes frequently observed.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002580081 – 421F-box only protein 5Add BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei85PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation by CDK2 and subsequently by PLK1 triggers degradation during early mitosis through ubiquitin-mediated proteolysis by the SCF ubiquitin ligase complex containing the F-box protein BTRC. This degradation is necessary for the activation of APC in late mitosis and subsequent mitotic progression (By similarity).By similarity
Ubiquitinated by the by the SCF(BTRC) complex following phosphorylation by PLK1.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ7TSG3.
MaxQBiQ7TSG3.
PaxDbiQ7TSG3.
PeptideAtlasiQ7TSG3.
PRIDEiQ7TSG3.

PTM databases

iPTMnetiQ7TSG3.
PhosphoSitePlusiQ7TSG3.

Expressioni

Gene expression databases

BgeeiENSMUSG00000019773.
CleanExiMM_FBXO5.
GenevisibleiQ7TSG3. MM.

Interactioni

Subunit structurei

Part of a SCF (SKP1-cullin-F-box) protein ligase complex. Interacts with BTRC, FZR1/CDH1 and the N-terminal substrate-binding domain of CDC20. Also interacts with EVI5 which blocks its phosphorylation by PLK1 and prevents its subsequent binding to BTRC and degradation (By similarity).Sequence analysisBy similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211971. 2 interactors.
STRINGi10090.ENSMUSP00000019907.

Structurei

3D structure databases

ProteinModelPortaliQ7TSG3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini223 – 273F-boxSequence analysisAdd BLAST51

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni114 – 219Interaction with EVI5By similarityAdd BLAST106

Domaini

The C-terminal region is required for inhibition of APC activity.By similarity

Sequence similaritiesi

Contains 1 F-box domain.Sequence analysis
Contains 1 IBR-type zinc finger.Sequence analysis

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri331 – 393IBR-typeSequence analysisAdd BLAST63

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IJ4T. Eukaryota.
ENOG4111MJS. LUCA.
GeneTreeiENSGT00530000063692.
HOGENOMiHOG000035122.
HOVERGENiHBG010089.
InParanoidiQ7TSG3.
KOiK10292.
OMAiSTTWKKI.
OrthoDBiEOG091G08DI.
PhylomeDBiQ7TSG3.
TreeFamiTF101170.

Family and domain databases

InterProiIPR001810. F-box_dom.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7TSG3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRRTCSDLR RPSSCPCRLG ARTTVDGCKE ESPVLSVTMK CFNCNPDLSE
60 70 80 90 100
LEVVKPEDSG IEASYSPVCL EPSCNDCVRN HERLSFIDSP IVGHDNKENQ
110 120 130 140 150
RVQNTLDSSN ETEELEASRL YEDSGYSSFT QSDRDDGILI LENFRNSPQA
160 170 180 190 200
RLLPSQSPDQ HPNKTLLPVL HFERVVCSTL KKNGKRNPKV DREMLKEVIA
210 220 230 240 250
SGNFRLQNII GKKMGLEHLD ILAELSRRGF VHLLANILTK LSGMDLVNLS
260 270 280 290 300
KVSRIWKKIL ENNKGAFQLY SKTMQRVIES SKLSLHATTR GYVVGRAALT
310 320 330 340 350
CVQKSSTWAP PKKDVQIKSS SQRGQRVSTY SRHNEFVEVA KTLKNNESLK
360 370 380 390 400
ACVRCNFPAK YDHYLERAVC KRESCQFEYC TKCLCAYHNN KDCLNGKILK
410 420
ASCKVGPLPG TKKSKKNLQR L
Length:421
Mass (Da):47,508
Last modified:October 1, 2003 - v1
Checksum:iA3624DA41F8DA285
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC053434 mRNA. Translation: AAH53434.1.
CCDSiCCDS56683.1.
RefSeqiNP_080271.2. NM_025995.2.
UniGeneiMm.197520.

Genome annotation databases

EnsembliENSMUST00000019907; ENSMUSP00000019907; ENSMUSG00000019773.
GeneIDi67141.
KEGGimmu:67141.
UCSCiuc007egj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC053434 mRNA. Translation: AAH53434.1.
CCDSiCCDS56683.1.
RefSeqiNP_080271.2. NM_025995.2.
UniGeneiMm.197520.

3D structure databases

ProteinModelPortaliQ7TSG3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211971. 2 interactors.
STRINGi10090.ENSMUSP00000019907.

PTM databases

iPTMnetiQ7TSG3.
PhosphoSitePlusiQ7TSG3.

Proteomic databases

EPDiQ7TSG3.
MaxQBiQ7TSG3.
PaxDbiQ7TSG3.
PeptideAtlasiQ7TSG3.
PRIDEiQ7TSG3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019907; ENSMUSP00000019907; ENSMUSG00000019773.
GeneIDi67141.
KEGGimmu:67141.
UCSCiuc007egj.1. mouse.

Organism-specific databases

CTDi26271.
MGIiMGI:1914391. Fbxo5.

Phylogenomic databases

eggNOGiENOG410IJ4T. Eukaryota.
ENOG4111MJS. LUCA.
GeneTreeiENSGT00530000063692.
HOGENOMiHOG000035122.
HOVERGENiHBG010089.
InParanoidiQ7TSG3.
KOiK10292.
OMAiSTTWKKI.
OrthoDBiEOG091G08DI.
PhylomeDBiQ7TSG3.
TreeFamiTF101170.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-113510. E2F mediated regulation of DNA replication.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-MMU-176417. Phosphorylation of Emi1.
R-MMU-68881. Mitotic Metaphase/Anaphase Transition.
R-MMU-69205. G1/S-Specific Transcription.

Miscellaneous databases

PROiQ7TSG3.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000019773.
CleanExiMM_FBXO5.
GenevisibleiQ7TSG3. MM.

Family and domain databases

InterProiIPR001810. F-box_dom.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFBX5_MOUSE
AccessioniPrimary (citable) accession number: Q7TSG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 1, 2003
Last modified: November 2, 2016
This is version 105 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.