FBXO5

Functionⁱ

Regulator of APC activity during mitotic and meiotic cell cycle (PubMed:17485488, PubMed:17234884, PubMed:17875940, PubMed:23708001, PubMed:23708605, PubMed:16921029). During mitotic cell cycle plays a role as both substrate and inhibitor of APC-FZR1 complex (PubMed:29875408, PubMed:17485488, PubMed:17234884, PubMed:17875940, PubMed:23708001, PubMed:23708605, PubMed:16921029). During G1 phase, plays a role as substrate of APC-FZR1 complex E3 ligase (PubMed:29875408). Then switches as an inhibitor of APC-FZR1 complex during S and G2 leading to cell-cycle commitment (PubMed:29875408). As APC inhibitor, prevents the degradation of APC substrates at multiple levels: by interacting with APC and blocking access of APC substrates to the D-box coreceptor, formed by FZR1 and ANAPC10; by suppressing ubiquitin ligation and chain elongation by APC by preventing the UBE2C and UBE2S activities (PubMed:23708605, PubMed:23708001, PubMed:16921029). Plays a role in genome integrity preservation by coordinating DNA replication with mitosis through APC inhibition in interphase to stabilize CCNA2 and GMNN in order to promote mitosis and prevent rereplication and DNA damage-induced cellular senescence (PubMed:17234884, PubMed:17485488, PubMed:17875940). During oocyte maturation, plays a role in meiosis through inactivation of APC-FZR1 complex. Inhibits APC through RPS6KA2 interaction that increases FBXO5 affiniy for CDC20 leading to the metaphase arrest of the second meiotic division before fertilization (By similarity). Controls entry into the first meiotic division through inactivation of APC-FZR1 complex (By similarity). Promotes migration and osteogenic differentiation of mesenchymal stem cells (PubMed:29850565).By similarity8 Publications

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 key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	374 – 422	ZBR-typePROSITE-ProRule annotationAdd BLAST		49

GO - Molecular functionⁱ

anaphase-promoting complex binding
Source: UniProtKB
Inferred from direct assayⁱ
- 16921029
- 26083744
metal ion binding Source: UniProtKB-KW
protein kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 15148369
ubiquitin ligase inhibitor activity
Source: UniProtKB
Inferred from direct assayⁱ
- 15148369

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

anaphase-promoting complex-dependent catabolic process Source: Reactome
cell division Source: UniProtKB-KW
microtubule polymerization Source: Ensembl
negative regulation of cellular senescence
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 17875940
negative regulation of DNA endoreduplication
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 17875940
negative regulation of meiotic nuclear division
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
negative regulation of mitotic metaphase/anaphase transition
Source: UniProtKB
Inferred from direct assayⁱ
- 11988738
- 16921029
negative regulation of response to DNA damage stimulus
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 17875940
negative regulation of ubiquitin protein ligase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 11988738
- 16921029
negative regulation of ubiquitin-protein transferase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 23708001
oocyte maturation Source: Ensembl
positive regulation of biomineral tissue development
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 29850565
positive regulation of cell proliferation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 17234884
positive regulation of G2/M transition of mitotic cell cycle
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 17485488
positive regulation of mesenchymal stem cell migration
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 29850565
positive regulation of osteoblast differentiation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 29850565
protein ubiquitination Source: UniProtKB-UniPathway
regulation of DNA replication
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 17234884
- 17485488
regulation of mitotic cell cycle Source: UniProtKB
regulation of transcription involved in G1/S transition of mitotic cell cycle Source: Reactome
spindle assembly involved in female meiosis I Source: Ensembl
vesicle organization Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Cell cycle, Cell division, Mitosis, Ubl conjugation pathway
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

Reactomeⁱ	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-539107 Activation of E2F1 target genes at G1/S R-HSA-68881 Mitotic Metaphase/Anaphase Transition
SIGNORⁱ	Q9UKT4
UniPathwayⁱ	UPA00143

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: F-box only protein 5Curated Alternative name(s): Early mitotic inhibitor 11 Publication
Gene namesⁱ	Name:FBXO5Imported Synonyms:EMI11 Publication, FBX5Imported
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 6

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000112029.9
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:13584 FBXO5
MIMⁱ	606013 gene
neXtProtⁱ	NX_Q9UKT4

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	143	E → A: Delays degradation. 1 Publication	1
Mutagenesisⁱ	144	D → A: Does not affect protein stability. 1 Publication	1
Mutagenesisⁱ	145	S → A: Does not affect protein stability; when associated with A-149. 1 Publication	1
Mutagenesisⁱ	145	S → E: Degraded in similar manner to wild-type. 3 Publications	1
Mutagenesisⁱ	145	S → N: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-149. 3 Publications	1
Mutagenesisⁱ	146	G → V: Does not affect protein stability. 1 Publication	1
Mutagenesisⁱ	148	S → A: Degraded in similar manner to wild-type. 1 Publication	1
Mutagenesisⁱ	149	S → A: Does not affect protein stability; when associated with A-145. 1 Publication	1
Mutagenesisⁱ	149	S → E: Degraded in similar manner to wild-type. 3 Publications	1
Mutagenesisⁱ	149	S → N: Not mitotically degraded. Shows impaired interaction with BTRC and reduced phosphate incorporation; when associated with N-145. 3 Publications	1
Mutagenesisⁱ	182	S → A: Shows impaired interaction with BTRC. 1 Publication	1
Mutagenesisⁱ	210 – 216	KRNPKVD → AAAAAAA: Loss of interaction with EVI5. 1 Publication	7
Mutagenesisⁱ	322 – 325	RTPL → ATPA: Does not affect inhibition of UBE2S-catalyzed chain elongation. Efficiently inhibits the degradation of PTTG1 at relatively high concentration. Reduces the competitive ability of FBXO5 to inhibit the association of PTTG1 to APC. Can not compete with the APC substrate for APC binding. Decreases inhibition of CCNB1 ubiquitination by UBE2C. 2 Publications	4
Mutagenesisⁱ	339 – 345	Missing : Impairs CCNB1 ubiquitination by UBE2C; when associated with 356-Y--R-358 del. 1 Publication	7
Mutagenesisⁱ	345	L → A: Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with 346-S--T-355 del. 1 Publication	1
Mutagenesisⁱ	346 – 355	Missing : Inhibits CCNB1 ubiquitination by UBE2C. Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with A-345; A-356 and A-358. 1 Publication	10
Mutagenesisⁱ	356 – 358	Missing : Impairs CCNB1 ubiquitination by UBE2C; when associated with 339-K--L-345 del. 1 Publication	3
Mutagenesisⁱ	356	Y → A: Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with 346-S--T-355 del. 1 Publication	1
Mutagenesisⁱ	358	R → A: Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with 346-S--T-355 del. 1 Publication	1
Mutagenesisⁱ	375	L → A: Decreases UBE2C-mediated ubiquitination. 1 Publication	1
Mutagenesisⁱ	376	K → A: Decreases UBE2C-mediated ubiquitination. 1 Publication	1
Mutagenesisⁱ	393	R → A: Decreases UBE2C-mediated ubiquitination. 1 Publication	1
Mutagenesisⁱ	401	C → S: Reduced inhibition of APC. Does not affect the FBXO5-mediated inhibitory activity against ubiquitin chain assembly. Does not affect the FBXO5-mediated inhibitory activity against ubiquitin chain assembly; when associated with S-401. Does not affect inhibition of UBE2S-catalyzed chain elongation. Reduces the competitive ability of FBXO5 to inhibit the association of securin to APC. Can still compete with the APC substrate for APC binding. Fails to inhibit ubiquitin chain assembly by UBE2C or mono-ubiquitination by UBE2D1. Largely abolishes the inhibitory activity against protein degradation. Fails to inactivate APC-FZR1 complex. Allows FBXO5 degradation in the absence of CDK4 inhibitor. 3 Publications	1
Mutagenesisⁱ	406	C → S: Does not affect the inhibitory activity against chain assembly; when associated with S-401. 1 Publication	1
Mutagenesisⁱ	409	C → A: Decreases UBE2C-mediated ubiquitination. 1 Publication	1
Mutagenesisⁱ	444 – 445	LR → AA: Loses inhibitory activity on UBE2S-catalyzed chain elongation. 1 Publication	2

Organism-specific databases

DisGeNET More...DisGeNETⁱ	26271
Open Targets More...OpenTargetsⁱ	ENSG00000112029
PharmGKBⁱ	PA28045

Polymorphism and mutation databases

BioMutaⁱ	FBXO5
DMDMⁱ	24636847

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000119881	1 – 447	F-box only protein 5Add BLAST		447

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	94	PhosphoserineBy similarity		1
Modified residueⁱ	102	PhosphoserineCombined sources		1

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 (PubMed:12791267, PubMed:15469984). Phosphorylated by RPS6KA2; increases and stabilizes interaction with CDC20 (By similarity).By similarity2 Publications

Ubiquitinated by the SCF(BTRC) complex following phosphorylation by PLK1 (PubMed:15469984). Undergoes both 'Lys-11' and 'Lys-48'-linked polyubiquitination by APC-FZR1 complex leading to degradation by proteasome during G1 phase (PubMed:29875408). Degraded through the SCF(BTRC) complex; degradation occurs during oocyte maturation, between germinal vesicle breakdown (GVBD) and meiosis I, and is required for the meiosis I-meiosis II transition (By similarity).By similarity2 Publications

Keywords - PTMⁱ

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q9UKT4
PaxDbⁱ	Q9UKT4
PeptideAtlas More...PeptideAtlasⁱ	Q9UKT4
PRIDEⁱ	Q9UKT4
ProteomicsDBⁱ	84847 84848 [Q9UKT4-2]

PTM databases

iPTMnetⁱ	Q9UKT4
PhosphoSitePlusⁱ	Q9UKT4

Expressionⁱ

Developmental stageⁱ

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

Inductionⁱ

Up-regulated at 7 days after osteogenic induction (PubMed:29850565). Down-regulated in late G2 phase or mitosis (PubMed:17485488). Down-regulated in G2 phase after DNA damage in a CDKN1A-dependent manner (PubMed:19211842). Down-regulated in G1 phase when APC-FZR1 complex is active and accumulates at the G1-S transition, coincident with the inactivation of APC-FZR1 complex (PubMed:29875408). At the G1-S transition, transcriptionally induced by the E2F transcription factor (PubMed:11988738).5 Publications

Gene expression databases

Bgeeⁱ	ENSG00000112029 Expressed in 170 organ(s), highest expression level in liver
CleanExⁱ	HS_FBXO5
Genevisibleⁱ	Q9UKT4 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB008106 HPA029048

HPAⁱ

CAB008106
HPA029048

Interactionⁱ

Subunit structureⁱ

Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By similarity). Interacts with BTRC; mediates proteolysis by the SCF ubiquitin ligase complex leading to activation of APC in late mitosis and subsequent mitotic progression (PubMed:12791267). Interacts with FZR1/CDH1 and the N-terminal substrate-binding domain of CDC20; prevents APC activation (PubMed:11988738). Also interacts with EVI5 which blocks its phosphorylation by PLK1 and prevents its subsequent binding to BTRC and degradation (PubMed:16439210). Interacts simultaneously with anaphase promoting complex (APC), through at least ANAPC2, CDC23, CDC27, the APC substrate GMNN and the APC activator FZR1 (PubMed:23708001, PubMed:26083744). Interacts with UBE2S; interferes with the activity of UBE2S mainly by disrupting the dynamic electrostatic association between the C-terminal tail of UBE2S and ANAPC2 (PubMed:23708001). Interacts with RPS6KA2; cooperates to induce the metaphase arrest of early blastomeres; increases and stabilizes interaction of FBXO5 with CDC20 (By similarity).By similarity5 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
ANAPC2	Q9UJX6	7	EBI-16059332,EBI-396211
CDC27	P30260	2	EBI-852298,EBI-994813
EVI5	O60447	6	EBI-852298,EBI-852291

GO - Molecular functionⁱ

protein kinase binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 15148369

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	117655, 38 interactors
Database of interacting proteins More...DIPⁱ	DIP-38023N
ELMⁱ	Q9UKT4
IntActⁱ	Q9UKT4, 22 interactors
Molecular INTeraction database More...MINTⁱ	Q9UKT4
STRINGⁱ	9606.ENSP00000229758

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	379 – 381	Combined sources	3
Beta strandⁱ	384 – 388	Combined sources	5
Turnⁱ	389 – 392	Combined sources	4
Beta strandⁱ	393 – 396	Combined sources	4
Beta strandⁱ	404 – 406	Combined sources	3
Turnⁱ	407 – 409	Combined sources	3
Beta strandⁱ	410 – 412	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	Q9UKT4
SMRⁱ	Q9UKT4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	250 – 296	F-boxAdd BLAST		47

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	135 – 244	Interaction with EVI51 PublicationAdd BLAST	110
Regionⁱ	261 – 409	Requires for efficient binding to CDC20By similarityAdd BLAST	149
Regionⁱ	261 – 339	Sufficient for interaction with RPS6KA2; Prevents association of CDC20 with RPS6KA2By similarityAdd BLAST	79
Regionⁱ	305 – 447	Inhibits APC ubiquitin ligase activity1 PublicationAdd BLAST	143
Regionⁱ	322 – 325	Competitively blocks access of APC substrates to the D-box coreceptor formed by FZR1 and ANAPC101 Publication	4
Regionⁱ	378 – 420	Allows a rapid multiple mono-ubiquitination of the APC substrate, but strongly inhibits the slow ubiquitin chain elongation catalyzed by UBCH101 PublicationAdd BLAST	43
Regionⁱ	437 – 447	Sufficient to suppress UBE2S activity; essential for interaction with UBE2S; competitively inhibits the rapide ubiquitin chain elongation by UBE2D1 which blocks UBE2D1 with APC; indispensable for recruitment and position of FBXO5 to the catalytic site of APC; abrogates the inhibition of ubiquitin chain assembly primarily catalyzed by UBE2S; inhibits the ubiquitination by either UBE2C or UBE2D11 PublicationAdd BLAST	11

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	374 – 422	ZBR-typePROSITE-ProRule annotationAdd BLAST		49

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

eggNOGⁱ	ENOG410IJ4T Eukaryota ENOG4111MJS LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063692
HOGENOMⁱ	HOG000035122
HOVERGENⁱ	HBG010089
InParanoidⁱ	Q9UKT4
KEGG Orthology (KO) More...KOⁱ	K10292
OMAⁱ	DYCTRCL
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G08DI
PhylomeDBⁱ	Q9UKT4
TreeFamⁱ	TF101170

Family and domain databases

InterProⁱ	View protein in InterPro IPR001810 F-box_dom
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00646 F-box, 1 hit
PROSITEⁱ	View protein in PROSITE PS51872 ZF_ZBR, 1 hit

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

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

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

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

« Hide

        10         20         30         40         50
MKCDFNCNHV HSGLKLVKPD DIGRLVSYTP AYLEGSCKDC IKDYERLSCI 
        60         70         80         90        100
GSPIVSPRIV QLETESKRLH NKENQHVQQT LNSTNEIEAL ETSRLYEDSG 
       110        120        130        140        150
YSSFSLQSGL SEHEEGSLLE ENFGDSLQSC LLQIQSPDQY PNKNLLPVLH 
       160        170        180        190        200
FEKVVCSTLK KNAKRNPKVD REMLKEIIAR GNFRLQNIIG RKMGLECVDI 
       210        220        230        240        250
LSELFRRGLR HVLATILAQL SDMDLINVSK VSTTWKKILE DDKGAFQLYS 
       260        270        280        290        300
KAIQRVTENN NKFSPHASTR EYVMFRTPLA SVQKSAAQTS LKKDAQTKLS 
       310        320        330        340        350
NQGDQKGSTY SRHNEFSEVA KTLKKNESLK ACIRCNSPAK YDCYLQRATC 
       360        370        380        390        400
KREGCGFDYC TKCLCNYHTT KDCSDGKLLK ASCKIGPLPG TKKSKKNLRR 

L

Show »

Length:401

Mass (Da):45,353

Checksum:ⁱ8E9E775625E62A4F

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	212	N → D in BAG51487 (PubMed:14702039).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_024440	107	Q → E2 PublicationsCorresponds to variant dbSNP:rs2073260Ensembl.		1
Natural variantⁱVAR_049038	164	L → F. Corresponds to variant dbSNP:rs7763565Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_041362	1 – 46	Missing in isoform 2. 1 PublicationAdd BLAST		46

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS47501.1 [Q9UKT4-2] CCDS5242.1 [Q9UKT4-1]
NCBI Reference Sequences More...RefSeqⁱ	NP_001135994.1, NM_001142522.2 [Q9UKT4-2] NP_036309.1, NM_012177.4 [Q9UKT4-1]
UniGeneⁱ	Hs.520506 Hs.713801

Genome annotation databases

Ensemblⁱ	ENST00000229758; ENSP00000229758; ENSG00000112029 [Q9UKT4-1] ENST00000367241; ENSP00000356210; ENSG00000112029 [Q9UKT4-2]
GeneIDⁱ	26271
KEGGⁱ	hsa:26271
UCSC genome browser More...UCSCⁱ	uc003qpg.4 human [Q9UKT4-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q9UKT4	Isoform 2 of F-box only protein 5		HUMAN		401	UniRef90_Q9UKT4
Uncharacterized protein		MACMU		448
Uncharacterized protein		CERAT		448
Uncharacterized protein		MACFA		448
Uncharacterized protein		COLAP		448
+40

Protein	Similar proteins		Species	Score	Length	Source
Q9UKT4	F-box only protein 5		MOUSE		421	UniRef50_Q9UKT4
Isoform 2 of F-box only protein 5		HUMAN		401
Uncharacterized protein		PAPAN		448
Uncharacterized protein		MANLE		448
Uncharacterized protein		RHIRO		448
+209

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 No translation available. CH471051 Genomic DNA Translation: EAW47719.1 BC018905 mRNA Translation: AAH18905.1
CCDSⁱ	CCDS47501.1 [Q9UKT4-2] CCDS5242.1 [Q9UKT4-1]
RefSeqⁱ	NP_001135994.1, NM_001142522.2 [Q9UKT4-2] NP_036309.1, NM_012177.4 [Q9UKT4-1]
UniGeneⁱ	Hs.520506 Hs.713801

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2M6N	NMR	-	A	364-447	[»]
	4UI9	electron microscopy	3.60	S	1-447	[»]
				U	1-27	[»]
ProteinModelPortalⁱ	Q9UKT4
SMRⁱ	Q9UKT4
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	117655, 38 interactors
DIPⁱ	DIP-38023N
ELMⁱ	Q9UKT4
IntActⁱ	Q9UKT4, 22 interactors
MINTⁱ	Q9UKT4
STRINGⁱ	9606.ENSP00000229758

PTM databases

iPTMnetⁱ	Q9UKT4
PhosphoSitePlusⁱ	Q9UKT4

Polymorphism and mutation databases

BioMutaⁱ	FBXO5
DMDMⁱ	24636847

Proteomic databases

EPDⁱ	Q9UKT4
PaxDbⁱ	Q9UKT4
PeptideAtlasⁱ	Q9UKT4
PRIDEⁱ	Q9UKT4
ProteomicsDBⁱ	84847 84848 [Q9UKT4-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	26271
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000229758; ENSP00000229758; ENSG00000112029 [Q9UKT4-1] ENST00000367241; ENSP00000356210; ENSG00000112029 [Q9UKT4-2]
GeneIDⁱ	26271
KEGGⁱ	hsa:26271
UCSCⁱ	uc003qpg.4 human [Q9UKT4-1]

Organism-specific databases

CTDⁱ	26271
DisGeNETⁱ	26271
EuPathDBⁱ	HostDB:ENSG00000112029.9
GeneCardsⁱ	FBXO5
HGNCⁱ	HGNC:13584 FBXO5
HPAⁱ	CAB008106 HPA029048
MIMⁱ	606013 gene
neXtProtⁱ	NX_Q9UKT4
OpenTargetsⁱ	ENSG00000112029
PharmGKBⁱ	PA28045
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410IJ4T Eukaryota ENOG4111MJS LUCA
GeneTreeⁱ	ENSGT00530000063692
HOGENOMⁱ	HOG000035122
HOVERGENⁱ	HBG010089
InParanoidⁱ	Q9UKT4
KOⁱ	K10292
OMAⁱ	DYCTRCL
OrthoDBⁱ	EOG091G08DI
PhylomeDBⁱ	Q9UKT4
TreeFamⁱ	TF101170

Enzyme and pathway databases

UniPathwayⁱ	UPA00143
Reactomeⁱ	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-539107 Activation of E2F1 target genes at G1/S R-HSA-68881 Mitotic Metaphase/Anaphase Transition
SIGNORⁱ	Q9UKT4

Miscellaneous databases

GeneWikiⁱ	FBXO5
GenomeRNAiⁱ	26271
Protein Ontology More...PROⁱ	PR:Q9UKT4
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000112029 Expressed in 170 organ(s), highest expression level in liver
CleanExⁱ	HS_FBXO5
Genevisibleⁱ	Q9UKT4 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR001810 F-box_dom
Pfamⁱ	View protein in Pfam PF00646 F-box, 1 hit
PROSITEⁱ	View protein in PROSITE PS51872 ZF_ZBR, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FBX5_HUMAN
Accessionⁱ	Q9UKT4Primary (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:	November 7, 2018
	This is version 153 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9UKT4 (FBX5_HUMAN)

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F-box only protein 5

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Cytoskeleton

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Cytoskeleton

Cytosol

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Pathwayⁱ: protein ubiquitination

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ