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Protein

F-box only protein 5

Gene

FBXO5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Zinc fingeri357 – 419IBR-typeAdd BLAST63

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • protein kinase binding Source: UniProtKB
  • ubiquitin ligase inhibitor activity Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processCell cycle, Cell division, Mitosis, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-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-539107 Activation of E2F1 target genes at G1/S
R-HSA-68881 Mitotic Metaphase/Anaphase Transition
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

EuPathDBiHostDB:ENSG00000112029.9
HGNCiHGNC:13584 FBXO5
MIMi606013 gene
neXtProtiNX_Q9UKT4

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, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi143E → A: Delays degradation. 1 Publication1
Mutagenesisi145S → E: Degraded in similar manner to wild-type. 3 Publications1
Mutagenesisi145S → N: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-149. 3 Publications1
Mutagenesisi148S → A: Degraded in similar manner to wild-type. 1 Publication1
Mutagenesisi149S → E: Degraded in similar manner to wild-type. 3 Publications1
Mutagenesisi149S → N: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-145. 3 Publications1
Mutagenesisi182S → A: Shows impaired interaction with BTRC. 1 Publication1
Mutagenesisi210 – 216KRNPKVD → AAAAAAA: Loss of interaction with EVI5. 1 Publication7
Mutagenesisi401C → S: Reduced inhibition of APC. 1 Publication1

Organism-specific databases

DisGeNETi26271
OpenTargetsiENSG00000112029
PharmGKBiPA28045

Polymorphism and mutation databases

BioMutaiFBXO5
DMDMi24636847

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001198811 – 447F-box only protein 5Add BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei94PhosphoserineBy similarity1
Modified residuei102PhosphoserineCombined 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.
Ubiquitinated by the by the SCF(BTRC) complex following phosphorylation by PLK1.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UKT4
PaxDbiQ9UKT4
PeptideAtlasiQ9UKT4
PRIDEiQ9UKT4

PTM databases

iPTMnetiQ9UKT4
PhosphoSitePlusiQ9UKT4

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

Show more details

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi117655, 38 interactors
DIPiDIP-38023N
ELMiQ9UKT4
IntActiQ9UKT4, 22 interactors
MINTiQ9UKT4
STRINGi9606.ENSP00000229758

Structurei

Secondary structure

1447
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni379 – 381Combined sources3
Beta strandi384 – 388Combined sources5
Turni389 – 392Combined sources4
Beta strandi393 – 396Combined sources4
Beta strandi404 – 406Combined sources3
Turni407 – 409Combined sources3
Beta strandi410 – 412Combined sources3

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini250 – 296F-boxAdd BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni135 – 244Interaction with EVI51 PublicationAdd BLAST110

Domaini

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri357 – 419IBR-typeAdd BLAST63

Keywords - Domaini

Zinc-finger

Phylogenomic databases

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

Family and domain databases

InterProiView protein in InterPro
IPR001810 F-box_dom
PfamiView protein in Pfam
PF00646 F-box, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti212N → D in BAG51487 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_024440107Q → E2 PublicationsCorresponds to variant dbSNP:rs2073260Ensembl.1
Natural variantiVAR_049038164L → F. Corresponds to variant dbSNP:rs7763565Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0413621 – 46Missing in isoform 2. 1 PublicationAdd BLAST46

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 No translation available.
CH471051 Genomic DNA Translation: EAW47719.1
BC018905 mRNA Translation: AAH18905.1
CCDSiCCDS47501.1 [Q9UKT4-2]
CCDS5242.1 [Q9UKT4-1]
RefSeqiNP_001135994.1, NM_001142522.2 [Q9UKT4-2]
NP_036309.1, NM_012177.4 [Q9UKT4-1]
UniGeneiHs.520506
Hs.713801

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

Similar proteinsi

Entry informationi

Entry nameiFBX5_HUMAN
AccessioniPrimary (citable) accession number: Q9UKT4
Secondary accession number(s): B3KNX5
, Q5TF47, Q8WV29, Q9UGC8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: May 1, 2000
Last modified: February 28, 2018
This is version 148 of the entry and version 1 of the sequence. See 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
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Main funding by: National Institutes of Health