Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 156 (13 Feb 2019)
Sequence version 1 (01 May 2000)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

F-box only protein 5

Gene

FBXO5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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

<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

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
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri374 – 422ZBR-typePROSITE-ProRule annotationAdd BLAST49

<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

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
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

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q9UKT4

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00143

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
F-box only protein 5Curated
Alternative name(s):
Early mitotic inhibitor 11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FBXO5Imported
Synonyms:EMI11 Publication, FBX5Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000112029.9

Human Gene Nomenclature Database

More...
HGNCi
HGNC:13584 FBXO5

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
606013 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9UKT4

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi143E → A: Delays degradation. 1 Publication1
Mutagenesisi144D → A: Does not affect protein stability. 1 Publication1
Mutagenesisi145S → A: Does not affect protein stability; when associated with A-149. 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
Mutagenesisi146G → V: Does not affect protein stability. 1 Publication1
Mutagenesisi148S → A: Degraded in similar manner to wild-type. 1 Publication1
Mutagenesisi149S → A: Does not affect protein stability; when associated with A-145. 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
Mutagenesisi322 – 325RTPL → 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 Publications4
Mutagenesisi339 – 345Missing : Impairs CCNB1 ubiquitination by UBE2C; when associated with 356-Y--R-358 del. 1 Publication7
Mutagenesisi345L → A: Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with 346-S--T-355 del. 1 Publication1
Mutagenesisi346 – 355Missing : Inhibits CCNB1 ubiquitination by UBE2C. Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with A-345; A-356 and A-358. 1 Publication10
Mutagenesisi356 – 358Missing : Impairs CCNB1 ubiquitination by UBE2C; when associated with 339-K--L-345 del. 1 Publication3
Mutagenesisi356Y → A: Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with 346-S--T-355 del. 1 Publication1
Mutagenesisi358R → A: Substantially impairs inhibition of CCNB1 ubiquitination by UBE2C; when associated with 346-S--T-355 del. 1 Publication1
Mutagenesisi375L → A: Decreases UBE2C-mediated ubiquitination. 1 Publication1
Mutagenesisi376K → A: Decreases UBE2C-mediated ubiquitination. 1 Publication1
Mutagenesisi393R → A: Decreases UBE2C-mediated ubiquitination. 1 Publication1
Mutagenesisi401C → 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 Publications1
Mutagenesisi406C → S: Does not affect the inhibitory activity against chain assembly; when associated with S-401. 1 Publication1
Mutagenesisi409C → A: Decreases UBE2C-mediated ubiquitination. 1 Publication1
Mutagenesisi444 – 445LR → AA: Loses inhibitory activity on UBE2S-catalyzed chain elongation. 1 Publication2

Organism-specific databases

DisGeNET

More...
DisGeNETi
26271

Open Targets

More...
OpenTargetsi
ENSG00000112029

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA28045

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
FBXO5

Domain mapping of disease mutations (DMDM)

More...
DMDMi
24636847

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001198811 – 447F-box only protein 5Add BLAST447

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei94PhosphoserineBy similarity1
Modified residuei102PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...
EPDi
Q9UKT4

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q9UKT4

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9UKT4

PeptideAtlas

More...
PeptideAtlasi
Q9UKT4

PRoteomics IDEntifications database

More...
PRIDEi
Q9UKT4

ProteomicsDB human proteome resource

More...
ProteomicsDBi
84847
84848 [Q9UKT4-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9UKT4

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9UKT4

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000112029 Expressed in 170 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9UKT4 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB008106
HPA029048

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
117655, 41 interactors

Database of interacting proteins

More...
DIPi
DIP-38023N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q9UKT4

Protein interaction database and analysis system

More...
IntActi
Q9UKT4, 22 interactors

Molecular INTeraction database

More...
MINTi
Q9UKT4

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000229758

<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

1447
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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 entryMethodResolution (Å)ChainPositionsPDBsum
2M6NNMR-A364-447[»]
4UI9electron microscopy3.60S1-447[»]
U1-27[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q9UKT4

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9UKT4

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini250 – 296F-boxAdd BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni135 – 244Interaction with EVI51 PublicationAdd BLAST110
Regioni261 – 409Requires for efficient binding to CDC20By similarityAdd BLAST149
Regioni261 – 339Sufficient for interaction with RPS6KA2; Prevents association of CDC20 with RPS6KA2By similarityAdd BLAST79
Regioni305 – 447Inhibits APC ubiquitin ligase activity1 PublicationAdd BLAST143
Regioni322 – 325Competitively blocks access of APC substrates to the D-box coreceptor formed by FZR1 and ANAPC101 Publication4
Regioni378 – 420Allows a rapid multiple mono-ubiquitination of the APC substrate, but strongly inhibits the slow ubiquitin chain elongation catalyzed by UBCH101 PublicationAdd BLAST43
Regioni437 – 447Sufficient 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 BLAST11

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri374 – 422ZBR-typePROSITE-ProRule annotationAdd BLAST49

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IJ4T Eukaryota
ENOG4111MJS LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00530000063692

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000035122

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG010089

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9UKT4

KEGG Orthology (KO)

More...
KOi
K10292

Identification of Orthologs from Complete Genome Data

More...
OMAi
DYCTRCL

Database of Orthologous Groups

More...
OrthoDBi
521317at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9UKT4

TreeFam database of animal gene trees

More...
TreeFami
TF101170

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001810 F-box_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00646 F-box, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51872 ZF_ZBR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti212N → D in BAG51487 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0413621 – 46Missing in isoform 2. 1 PublicationAdd BLAST46

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.520506
Hs.713801

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000229758; ENSP00000229758; ENSG00000112029 [Q9UKT4-1]
ENST00000367241; ENSP00000356210; ENSG00000112029 [Q9UKT4-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
26271

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:26271

UCSC genome browser

More...
UCSCi
uc003qpg.4 human [Q9UKT4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

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

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...

Protein-protein interaction databases

BioGridi117655, 41 interactors
DIPiDIP-38023N
ELMiQ9UKT4
IntActiQ9UKT4, 22 interactors
MINTiQ9UKT4
STRINGi9606.ENSP00000229758

PTM databases

iPTMnetiQ9UKT4
PhosphoSitePlusiQ9UKT4

Polymorphism and mutation databases

BioMutaiFBXO5
DMDMi24636847

Proteomic databases

EPDiQ9UKT4
jPOSTiQ9UKT4
PaxDbiQ9UKT4
PeptideAtlasiQ9UKT4
PRIDEiQ9UKT4
ProteomicsDBi84847
84848 [Q9UKT4-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
26271
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

Comparative Toxicogenomics Database

More...
CTDi
26271
DisGeNETi26271
EuPathDBiHostDB:ENSG00000112029.9

GeneCards: human genes, protein and diseases

More...
GeneCardsi
FBXO5
HGNCiHGNC:13584 FBXO5
HPAiCAB008106
HPA029048
MIMi606013 gene
neXtProtiNX_Q9UKT4
OpenTargetsiENSG00000112029
PharmGKBiPA28045

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IJ4T Eukaryota
ENOG4111MJS LUCA
GeneTreeiENSGT00530000063692
HOGENOMiHOG000035122
HOVERGENiHBG010089
InParanoidiQ9UKT4
KOiK10292
OMAiDYCTRCL
OrthoDBi521317at2759
PhylomeDBiQ9UKT4
TreeFamiTF101170

Enzyme and pathway databases

UniPathwayi
UPA00143

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

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
FBXO5

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
26271

Protein Ontology

More...
PROi
PR:Q9UKT4

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000112029 Expressed in 170 organ(s), highest expression level in liver
GenevisibleiQ9UKT4 HS

Family and domain databases

InterProiView protein in InterPro
IPR001810 F-box_dom
PfamiView protein in Pfam
PF00646 F-box, 1 hit
PROSITEiView protein in PROSITE
PS51872 ZF_ZBR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFBX5_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9UKT4
Secondary accession number(s): B3KNX5
, Q5TF47, Q8WV29, Q9UGC8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: May 1, 2000
Last modified: February 13, 2019
This is version 156 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again