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Protein

F-box only protein 5

Gene

FBXO5

Organism
Homo sapiens (Human)
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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri357 – 41963IBR-typeAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • protein kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-113510. E2F mediated regulation of DNA replication.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-68881. Mitotic Metaphase/Anaphase Transition.
R-HSA-69205. G1/S-Specific Transcription.
SIGNORiQ9UKT4.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 5
Alternative name(s):
Early mitotic inhibitor 1
Gene namesi
Name:FBXO5
Synonyms:EMI1, FBX5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:13584. FBXO5.

Subcellular locationi

  • Nucleus
  • Cytoplasm
  • Cytoplasmcytoskeletonspindle

  • 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.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi143 – 1431E → A: Delays degradation. 1 Publication
Mutagenesisi145 – 1451S → E: Degraded in similar manner to wild-type. 3 Publications
Mutagenesisi145 – 1451S → N: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-149. 3 Publications
Mutagenesisi148 – 1481S → A: Degraded in similar manner to wild-type. 1 Publication
Mutagenesisi149 – 1491S → E: Degraded in similar manner to wild-type. 3 Publications
Mutagenesisi149 – 1491S → N: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-145. 3 Publications
Mutagenesisi182 – 1821S → A: Shows impaired interaction with BTRC. 1 Publication
Mutagenesisi210 – 2167KRNPKVD → AAAAAAA: Loss of interaction with EVI5. 1 Publication
Mutagenesisi401 – 4011C → S: Reduced inhibition of APC. 1 Publication

Organism-specific databases

PharmGKBiPA28045.

Polymorphism and mutation databases

BioMutaiFBXO5.
DMDMi24636847.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447F-box only protein 5PRO_0000119881Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941PhosphoserineBy similarity
Modified residuei102 – 1021PhosphoserineCombined sources

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.
Ubiquitinated by the by the SCF(BTRC) complex following phosphorylation by PLK1.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9UKT4.
PaxDbiQ9UKT4.
PeptideAtlasiQ9UKT4.
PRIDEiQ9UKT4.

PTM databases

iPTMnetiQ9UKT4.
PhosphoSiteiQ9UKT4.

Expressioni

Developmental stagei

Accumulates in late G1 phase, levels rise during S phase and drop in early mitosis.1 Publication

Gene expression databases

BgeeiENSG00000112029.
CleanExiHS_FBXO5.
GenevisibleiQ9UKT4. HS.

Organism-specific databases

HPAiCAB008106.
HPA029048.

Interactioni

Subunit structurei

Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By similarity). 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 similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC27P302602EBI-852298,EBI-994813
EVI5O604476EBI-852298,EBI-852291

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117655. 37 interactions.
DIPiDIP-38023N.
IntActiQ9UKT4. 16 interactions.
MINTiMINT-4789777.
STRINGi9606.ENSP00000229758.

Structurei

Secondary structure

1
447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni379 – 3813Combined sources
Beta strandi384 – 3885Combined sources
Turni389 – 3924Combined sources
Beta strandi393 – 3964Combined sources
Beta strandi404 – 4063Combined sources
Turni407 – 4093Combined sources
Beta strandi410 – 4123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M6NNMR-A364-447[»]
4UI9electron microscopy3.60S1-447[»]
U1-27[»]
ProteinModelPortaliQ9UKT4.
SMRiQ9UKT4. Positions 319-436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini250 – 29647F-boxAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 244110Interaction with EVI5Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 F-box domain.Curated
Contains 1 IBR-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri357 – 41963IBR-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IJ4T. Eukaryota.
ENOG4111MJS. LUCA.
GeneTreeiENSGT00530000063692.
HOGENOMiHOG000035122.
HOVERGENiHBG010089.
InParanoidiQ9UKT4.
KOiK10292.
OMAiSTTWKKI.
OrthoDBiEOG091G08DI.
PhylomeDBiQ9UKT4.
TreeFamiTF101170.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UKT4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSRRPCSCAL RPPRCSCSAS PSAVTAAGRP RPSDSCKEES STLSVKMKCD
60 70 80 90 100
FNCNHVHSGL KLVKPDDIGR LVSYTPAYLE GSCKDCIKDY ERLSCIGSPI
110 120 130 140 150
VSPRIVQLET ESKRLHNKEN QHVQQTLNST NEIEALETSR LYEDSGYSSF
160 170 180 190 200
SLQSGLSEHE EGSLLEENFG DSLQSCLLQI QSPDQYPNKN LLPVLHFEKV
210 220 230 240 250
VCSTLKKNAK RNPKVDREML KEIIARGNFR LQNIIGRKMG LECVDILSEL
260 270 280 290 300
FRRGLRHVLA TILAQLSDMD LINVSKVSTT WKKILEDDKG AFQLYSKAIQ
310 320 330 340 350
RVTENNNKFS PHASTREYVM FRTPLASVQK SAAQTSLKKD AQTKLSNQGD
360 370 380 390 400
QKGSTYSRHN EFSEVAKTLK KNESLKACIR CNSPAKYDCY LQRATCKREG
410 420 430 440
CGFDYCTKCL CNYHTTKDCS DGKLLKASCK IGPLPGTKKS KKNLRRL
Length:447
Mass (Da):50,146
Last modified:May 1, 2000 - v1
Checksum:i196FBC2578F92120
GO
Isoform 2 (identifier: Q9UKT4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.

Show »
Length:401
Mass (Da):45,353
Checksum:i8E9E775625E62A4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121N → D in BAG51487 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071Q → E.2 Publications
Corresponds to variant rs2073260 [ dbSNP | Ensembl ].
VAR_024440
Natural varianti164 – 1641L → F.
Corresponds to variant rs7763565 [ dbSNP | Ensembl ].
VAR_049038

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646Missing in isoform 2. 1 PublicationVSP_041362Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129535 mRNA. Translation: AAF04469.1.
AY079515 mRNA. Translation: AAL86610.1.
AK055221 mRNA. Translation: BAG51487.1.
AL080276 Genomic DNA. Translation: CAI18894.1.
AL080276 Genomic DNA. Translation: CAI18895.1.
CH471051 Genomic DNA. Translation: EAW47719.1.
BC018905 mRNA. Translation: AAH18905.1.
CCDSiCCDS47501.1. [Q9UKT4-2]
CCDS5242.1. [Q9UKT4-1]
RefSeqiNP_001135994.1. NM_001142522.1. [Q9UKT4-2]
NP_036309.1. NM_012177.3. [Q9UKT4-1]
UniGeneiHs.520506.

Genome annotation databases

EnsembliENST00000229758; ENSP00000229758; ENSG00000112029. [Q9UKT4-1]
ENST00000367241; ENSP00000356210; ENSG00000112029. [Q9UKT4-2]
GeneIDi26271.
KEGGihsa:26271.
UCSCiuc003qpg.4. human. [Q9UKT4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129535 mRNA. Translation: AAF04469.1.
AY079515 mRNA. Translation: AAL86610.1.
AK055221 mRNA. Translation: BAG51487.1.
AL080276 Genomic DNA. Translation: CAI18894.1.
AL080276 Genomic DNA. Translation: CAI18895.1.
CH471051 Genomic DNA. Translation: EAW47719.1.
BC018905 mRNA. Translation: AAH18905.1.
CCDSiCCDS47501.1. [Q9UKT4-2]
CCDS5242.1. [Q9UKT4-1]
RefSeqiNP_001135994.1. NM_001142522.1. [Q9UKT4-2]
NP_036309.1. NM_012177.3. [Q9UKT4-1]
UniGeneiHs.520506.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M6NNMR-A364-447[»]
4UI9electron microscopy3.60S1-447[»]
U1-27[»]
ProteinModelPortaliQ9UKT4.
SMRiQ9UKT4. Positions 319-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117655. 37 interactions.
DIPiDIP-38023N.
IntActiQ9UKT4. 16 interactions.
MINTiMINT-4789777.
STRINGi9606.ENSP00000229758.

PTM databases

iPTMnetiQ9UKT4.
PhosphoSiteiQ9UKT4.

Polymorphism and mutation databases

BioMutaiFBXO5.
DMDMi24636847.

Proteomic databases

MaxQBiQ9UKT4.
PaxDbiQ9UKT4.
PeptideAtlasiQ9UKT4.
PRIDEiQ9UKT4.

Protocols and materials databases

DNASUi26271.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229758; ENSP00000229758; ENSG00000112029. [Q9UKT4-1]
ENST00000367241; ENSP00000356210; ENSG00000112029. [Q9UKT4-2]
GeneIDi26271.
KEGGihsa:26271.
UCSCiuc003qpg.4. human. [Q9UKT4-1]

Organism-specific databases

CTDi26271.
GeneCardsiFBXO5.
HGNCiHGNC:13584. FBXO5.
HPAiCAB008106.
HPA029048.
MIMi606013. gene.
neXtProtiNX_Q9UKT4.
PharmGKBiPA28045.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJ4T. Eukaryota.
ENOG4111MJS. LUCA.
GeneTreeiENSGT00530000063692.
HOGENOMiHOG000035122.
HOVERGENiHBG010089.
InParanoidiQ9UKT4.
KOiK10292.
OMAiSTTWKKI.
OrthoDBiEOG091G08DI.
PhylomeDBiQ9UKT4.
TreeFamiTF101170.

Enzyme and pathway databases

ReactomeiR-HSA-113510. E2F mediated regulation of DNA replication.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-176408. Regulation of APC/C activators between G1/S and early anaphase.
R-HSA-176417. Phosphorylation of Emi1.
R-HSA-68881. Mitotic Metaphase/Anaphase Transition.
R-HSA-69205. G1/S-Specific Transcription.
SIGNORiQ9UKT4.

Miscellaneous databases

GeneWikiiFBXO5.
GenomeRNAii26271.
PROiQ9UKT4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000112029.
CleanExiHS_FBXO5.
GenevisibleiQ9UKT4. HS.

Family and domain databases

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

Entry informationi

Entry nameiFBX5_HUMAN
AccessioniPrimary (citable) accession number: Q9UKT4
Secondary accession number(s): B3KNX5
, Q5TF47, Q8WV29, Q9UGC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 136 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.