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Entry version 183 (22 Apr 2020)
Sequence version 2 (10 May 2002)
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Protein

E3 ubiquitin-protein ligase ARIH1

Gene

ARIH1

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

E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:15236971, PubMed:21532592, PubMed:24076655, PubMed:27565346, PubMed:23707686). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets (PubMed:27565346). The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2 (PubMed:27565346). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes (PubMed:24076655, PubMed:27565346). Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear (PubMed:25624349). According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest (PubMed:25624349). According to another report EIF4E2 ubiquitination leads to its subsequent degradation (PubMed:14623119). Acts as the ligase involved in ISGylation of EIF4E2 (PubMed:17289916). In vitro, controls the degradation of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex member SUN2 and may therefore have a role in the formation and localization of the LINC complex, and as a consequence, nuclear subcellular localization and nuclear morphology (PubMed:29689197).9 Publications

Caution

The RING-type 2 zinc finger was initially reported to only bind 1 zinc ion instead of 2 compared to classical RING-types (PubMed:15236971). But it was later shown that it is not the case and binds 2 zinc ions (PubMed:24058416, PubMed:23707686).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Autoinhibited by the ariadne domain, which masks the second RING-type zinc finger that contains the active site and inhibits the E3 activity (PubMed:23707686). Inhibition is relieved upon binding to neddylated cullin-RING ubiquitin ligase complexes, which activate the E3 ligase activity of ARIH1 (PubMed:24076655, PubMed:27565346).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi186Zinc 1PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi189Zinc 1PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi203Zinc 2PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi205Zinc 2; via pros nitrogenPROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi208Zinc 1PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi211Zinc 1PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi231Zinc 2PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi236Zinc 2PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi276Zinc 3PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi281Zinc 3PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi297Zinc 3PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi299Zinc 3PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi304Zinc 4PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi307Zinc 4PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi312Zinc 4; via tele nitrogenPROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi317Zinc 4PROSITE-ProRule annotationCombined sources1 Publication1
Metal bindingi344Zinc 5PROSITE-ProRule annotationCombined sources3 Publications1
Metal bindingi347Zinc 5PROSITE-ProRule annotationCombined sources3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei357PROSITE-ProRule annotation2 Publications1
Metal bindingi362Zinc 5PROSITE-ProRule annotationCombined sources3 Publications1
Metal bindingi367Zinc 5PROSITE-ProRule annotationCombined sources3 Publications1
Metal bindingi372Zinc 6PROSITE-ProRule annotationCombined sources2 Publications1
Metal bindingi375Zinc 6PROSITE-ProRule annotationCombined sources2 Publications1
Metal bindingi382Zinc 6; via tele nitrogenPROSITE-ProRule annotationCombined sources2 Publications1
Metal bindingi389Zinc 6PROSITE-ProRule annotationCombined sources2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 fingeri186 – 236RING-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri256 – 317IBR-typePROSITE-ProRule annotationAdd BLAST62
Zinc fingeri344 – 375RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST32

<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

<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

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.2.B10 2681
6.3.2.19 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1169408 ISG15 antiviral mechanism

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%5Fand%5Ftaxonomy%5Fsection">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:
E3 ubiquitin-protein ligase ARIH1 (EC:2.3.2.313 Publications)
Alternative name(s):
H7-AP21 Publication
HHARI1 Publication
Monocyte protein 61 Publication
Short name:
MOP-61 Publication
Protein ariadne-1 homolog1 Publication
Short name:
ARI-11 Publication
UbcH7-binding protein1 Publication
UbcM4-interacting protein
Ubiquitin-conjugating enzyme E2-binding protein 11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:ARIH1Imported
Synonyms:ARI, MOP61 Publication, UBCH7BP1 Publication
ORF Names:HUSSY-271 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 15

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:689 ARIH1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
605624 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9Y4X5

<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, 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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Defects in ARIH1 have been found in several individuals with thoracic aortic aneurysms and cerebrovascular disease.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi123V → A: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication1
Mutagenesisi150F → A: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication1
Mutagenesisi156 – 158KLF → AAA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication3
Mutagenesisi187 – 188QI → HV: No loss of interaction with UBE2L3. 1 Publication2
Mutagenesisi188I → A: Loss of interaction with UBE2L3. Decreased E3 ligase activity. Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 3 Publications1
Mutagenesisi205H → A: Impaired interaction with UBE2L3 without affecting interaction with neddylated cullin-RING complexes. 1 Publication1
Mutagenesisi208C → A or H: Loss of interaction with UBE2L3. 1 Publication1
Mutagenesisi257 – 258KY → AAA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication2
Mutagenesisi258Y → A: No loss of interaction with UBE2L3. 1 Publication1
Mutagenesisi265 – 267SFV → AAA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication3
Mutagenesisi340 – 341NT → AA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication2
Mutagenesisi342 – 343KE → AA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication2
Mutagenesisi347C → A: Impairs zinc-binding and folding. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi351 – 352IE → AA: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication2
Mutagenesisi351I → A: Disrupts the hydrophobic network. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi357C → A or S: Does not affect zinc binding and folding. Abolishes ability to transfer ubiquitin and E3 ubiquitin-protein ligase activity. 4 Publications1
Mutagenesisi358N → A: Defects in ligation. 1 Publication1
Mutagenesisi359H → A: Defects in ligation. Does not affect zinc binding, folding. Does not impair E3 ubiquitin-protein ligase activity. 2 Publications1
Mutagenesisi367C → A: Impairs zinc-binding and folding. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi371F → A: Disrupts the hydrophobic network. Abolishes E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi372C → A: Impairs E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi373W → A: Abolishes E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi378 – 379PW → AA: Defects in ligation. 1 Publication2
Mutagenesisi379W → A: Does not affect E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi383 – 385GSA → AAD: Defects in ligation. 1 Publication3
Mutagenesisi386W → A: Does not affect E3 ubiquitin-protein ligase activity. Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 2 Publications1
Mutagenesisi416F → A: Slightly relieves autoinhibition of the E3 ligase activity by the ariadne domain. 1 Publication1
Mutagenesisi417Y → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi420 – 423RYMN → AYMA: Slightly relieves autoinhibition of the E3 ligase activity by the ariadne domain. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with A-503. 2 Publications4
Mutagenesisi427S → A: Slightly relieves autoinhibition of the E3 ligase activity by the ariadne domain. 1 Publication1
Mutagenesisi430 – 431FE → AA: Relieves autoinhibition of the E3 ligase activity by the ariadne domain; when associated with A-503. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with A-503. 3 Publications2
Mutagenesisi476Y → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi492E → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi493N → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi495Q → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi499E → A: Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity. 1 Publication1
Mutagenesisi503E → A: Relieves autoinhibition of the E3 ligase activity by the ariadne domain; when associated with 430-A-A-431. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with 430-A-A-431. Hyperactive 'open' mutant that displays enhanced E3 ubiquitin-protein ligase activity; when associated with 420-A--A-423. 3 Publications1
Mutagenesisi531Y → A: Strongly decreased ability to initiate ubiquitination of cullin-RING complexes. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
25820

Open Targets

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OpenTargetsi
ENSG00000166233

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24982

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q9Y4X5 Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ARIH1

Domain mapping of disease mutations (DMDM)

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DMDMi
20532376

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000557521 – 557E3 ubiquitin-protein ligase ARIH1Add BLAST557

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 residuei142N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9Y4X5

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9Y4X5

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9Y4X5

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9Y4X5

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

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PaxDbi
Q9Y4X5

PeptideAtlas

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PeptideAtlasi
Q9Y4X5

PRoteomics IDEntifications database

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PRIDEi
Q9Y4X5

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
86264

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9Y4X5

MetOSite database of methionine sulfoxide sites

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MetOSitei
Q9Y4X5

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

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PhosphoSitePlusi
Q9Y4X5

<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 a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed.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 following DNA damage (PubMed:25624349).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000166233 Expressed in testis and 235 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9Y4X5 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9Y4X5 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000166233 Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts (via the first RING-type zinc finger) with UBE2L3 (PubMed:11278816, PubMed:21532592, PubMed:24076655, PubMed:23707686). Associates with cullin-RING ubiquitin ligase (CRL) complexes containing CUL1, CUL2 and CUL3 (PubMed:24076655, PubMed:27565346).

Interacts with neddylated CUL1 (PubMed:24076655, PubMed:27565346).

Interacts with neddylated CUL2 (PubMed:24076655, PubMed:27565346).

Interacts with neddylated CUL3 (PubMed:24076655, PubMed:27565346).

Interacts with neddylated CUL4A (PubMed:24076655).

5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
117348, 210 interactors

Database of interacting proteins

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DIPi
DIP-53626N

Protein interaction database and analysis system

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IntActi
Q9Y4X5, 78 interactors

Molecular INTeraction database

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MINTi
Q9Y4X5

STRING: functional protein association networks

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STRINGi
9606.ENSP00000369217

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q9Y4X5 protein

<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

1557
Legend: HelixTurnBeta strandPDB Structure known for this area
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3D structure databases

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

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SMRi
Q9Y4X5

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q9Y4X5

<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

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>Regioni105 – 153UBA-like1 PublicationAdd BLAST49
Regioni182 – 393TRIAD supradomainPROSITE-ProRule annotationAdd BLAST212
Regioni408 – 557Ariadne domain1 PublicationAdd BLAST150

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING-type zinc finger, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved active site Cys residue in the second RING-type zinc finger (PubMed:21532592, PubMed:23707686). The active site probably forms a thioester intermediate with ubiquitin taken from the active-site cysteine of the E2 before ultimately transferring it to a Lys residue on the substrate (PubMed:21532592, PubMed:23707686).2 Publications
The Ariadne domain inhibits activity by masking the second RING-type zinc finger that contains the active site (PubMed:23707686).1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RBR family. Ariadne subfamily.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri186 – 236RING-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri256 – 317IBR-typePROSITE-ProRule annotationAdd BLAST62
Zinc fingeri344 – 375RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST32

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1815 Eukaryota
ENOG410XP9Y LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155744

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_009823_4_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9Y4X5

KEGG Orthology (KO)

More...
KOi
K11968

Identification of Orthologs from Complete Genome Data

More...
OMAi
CKCGHVF

Database of Orthologous Groups

More...
OrthoDBi
469819at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9Y4X5

TreeFam database of animal gene trees

More...
TreeFami
TF300805

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR031127 E3_UB_ligase_RBR
IPR002867 IBR_dom
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD

The PANTHER Classification System

More...
PANTHERi
PTHR11685 PTHR11685, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01485 IBR, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00647 IBR, 2 hits
SM00184 RING, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51873 TRIAD, 1 hit
PS50089 ZF_RING_2, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

Q9Y4X5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDSDEGYNYE FDEDEECSEE DSGAEEEEDE DDDEPDDDTL DLGEVELVEP
60 70 80 90 100
GLGVGGERDG LLCGETGGGG GSALGPGGGG GGGGGGGGGG PGHEQEEDYR
110 120 130 140 150
YEVLTAEQIL QHMVECIREV NEVIQNPATI TRILLSHFNW DKEKLMERYF
160 170 180 190 200
DGNLEKLFAE CHVINPSKKS RTRQMNTRSS AQDMPCQICY LNYPNSYFTG
210 220 230 240 250
LECGHKFCMQ CWSEYLTTKI MEEGMGQTIS CPAHGCDILV DDNTVMRLIT
260 270 280 290 300
DSKVKLKYQH LITNSFVECN RLLKWCPAPD CHHVVKVQYP DAKPVRCKCG
310 320 330 340 350
RQFCFNCGEN WHDPVKCKWL KKWIKKCDDD SETSNWIAAN TKECPKCHVT
360 370 380 390 400
IEKDGGCNHM VCRNQNCKAE FCWVCLGPWE PHGSAWYNCN RYNEDDAKAA
410 420 430 440 450
RDAQERSRAA LQRYLFYCNR YMNHMQSLRF EHKLYAQVKQ KMEEMQQHNM
460 470 480 490 500
SWIEVQFLKK AVDVLCQCRA TLMYTYVFAF YLKKNNQSII FENNQADLEN
510 520 530 540 550
ATEVLSGYLE RDISQDSLQD IKQKVQDKYR YCESRRRVLL QHVHEGYEKD

LWEYIED
Length:557
Mass (Da):64,118
Last modified:May 10, 2002 - v2
<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:iDFFF8965DAB41DC8
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BNB9H3BNB9_HUMAN
RBR-type E3 ubiquitin transferase
ARIH1
204Annotation score:

Annotation score:2 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>
H3BSK4H3BSK4_HUMAN
E3 ubiquitin-protein ligase ARIH1
ARIH1
167Annotation score:

Annotation score:1 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>
A0A087WT96A0A087WT96_HUMAN
E3 ubiquitin-protein ligase ARIH1
ARIH1
114Annotation score:

Annotation score:1 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>
H3BUS0H3BUS0_HUMAN
E3 ubiquitin-protein ligase ARIH1
ARIH1
47Annotation score:

Annotation score:1 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 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 conflicti122E → D in AAD28088 (Ref. 3) Curated1
Sequence conflicti227Q → H in CAB45870 (PubMed:10521492).Curated1
Sequence conflicti237D → N in CAA10274 (PubMed:10880484).Curated1
Sequence conflicti303F → S in CAA08817 (PubMed:11124703).Curated1
Sequence conflicti309 – 316ENWHDPVK → AIGMILFQ in CAA08817 (PubMed:11124703).Curated8
Sequence conflicti322K → T in CAA08817 (PubMed:11124703).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_08264615E → Q Probable disease-associated mutation found in patient with an acute aortic dissection and ascending aortic aneurysm. 1 Publication1
Natural variantiVAR_08264744E → G Probable disease-associated mutation found in patient with basilar tip artery aneurysm and distal left internal carotid artery aneurysm. 1 Publication1
Natural variantiVAR_082648171 – 557Missing Probable disease-associated mutation found in patient with fusiform aneurysm of the aortic root and ascending aorta. 1 PublicationAdd BLAST387

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
AJ243190 mRNA Translation: CAB45870.1
AF072832 mRNA Translation: AAD28088.1
AK312715 mRNA Translation: BAG35590.1
AC079322 Genomic DNA No translation available.
AC100827 Genomic DNA No translation available.
CH471082 Genomic DNA Translation: EAW77907.1
BC051877 mRNA Translation: AAH51877.1
AJ130976 mRNA Translation: CAA10274.1
AJ009771 mRNA Translation: CAA08817.1
AB014774 mRNA Translation: BAB19786.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10244.1

NCBI Reference Sequences

More...
RefSeqi
NP_005735.2, NM_005744.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000379887; ENSP00000369217; ENSG00000166233

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25820

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:25820

UCSC genome browser

More...
UCSCi
uc002aut.5 human

<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
AJ243190 mRNA Translation: CAB45870.1
AF072832 mRNA Translation: AAD28088.1
AK312715 mRNA Translation: BAG35590.1
AC079322 Genomic DNA No translation available.
AC100827 Genomic DNA No translation available.
CH471082 Genomic DNA Translation: EAW77907.1
BC051877 mRNA Translation: AAH51877.1
AJ130976 mRNA Translation: CAA10274.1
AJ009771 mRNA Translation: CAA08817.1
AB014774 mRNA Translation: BAB19786.1
CCDSiCCDS10244.1
RefSeqiNP_005735.2, NM_005744.3

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
1WD2NMR-A336-394[»]
2M9YNMR-A325-396[»]
4KBLX-ray3.30A/B1-557[»]
4KC9X-ray3.60A1-557[»]
5TTEX-ray3.50B1-557[»]
5UDHX-ray3.24A/B90-557[»]
SMRiQ9Y4X5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi117348, 210 interactors
DIPiDIP-53626N
IntActiQ9Y4X5, 78 interactors
MINTiQ9Y4X5
STRINGi9606.ENSP00000369217

PTM databases

iPTMnetiQ9Y4X5
MetOSiteiQ9Y4X5
PhosphoSitePlusiQ9Y4X5

Polymorphism and mutation databases

BioMutaiARIH1
DMDMi20532376

Proteomic databases

EPDiQ9Y4X5
jPOSTiQ9Y4X5
MassIVEiQ9Y4X5
MaxQBiQ9Y4X5
PaxDbiQ9Y4X5
PeptideAtlasiQ9Y4X5
PRIDEiQ9Y4X5
ProteomicsDBi86264

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
1143 102 antibodies

Genome annotation databases

EnsembliENST00000379887; ENSP00000369217; ENSG00000166233
GeneIDi25820
KEGGihsa:25820
UCSCiuc002aut.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
25820
DisGeNETi25820

GeneCards: human genes, protein and diseases

More...
GeneCardsi
ARIH1
HGNCiHGNC:689 ARIH1
HPAiENSG00000166233 Low tissue specificity
MIMi605624 gene
neXtProtiNX_Q9Y4X5
OpenTargetsiENSG00000166233
PharmGKBiPA24982

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1815 Eukaryota
ENOG410XP9Y LUCA
GeneTreeiENSGT00940000155744
HOGENOMiCLU_009823_4_2_1
InParanoidiQ9Y4X5
KOiK11968
OMAiCKCGHVF
OrthoDBi469819at2759
PhylomeDBiQ9Y4X5
TreeFamiTF300805

Enzyme and pathway databases

UniPathwayiUPA00143
BRENDAi2.3.2.B10 2681
6.3.2.19 2681
ReactomeiR-HSA-1169408 ISG15 antiviral mechanism

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
ARIH1 human
EvolutionaryTraceiQ9Y4X5

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
ARIH1

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

More...
GenomeRNAii
25820
PharosiQ9Y4X5 Tbio

Protein Ontology

More...
PROi
PR:Q9Y4X5
RNActiQ9Y4X5 protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000166233 Expressed in testis and 235 other tissues
ExpressionAtlasiQ9Y4X5 baseline and differential
GenevisibleiQ9Y4X5 HS

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR031127 E3_UB_ligase_RBR
IPR002867 IBR_dom
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
PANTHERiPTHR11685 PTHR11685, 1 hit
PfamiView protein in Pfam
PF01485 IBR, 2 hits
SMARTiView protein in SMART
SM00647 IBR, 2 hits
SM00184 RING, 2 hits
PROSITEiView protein in PROSITE
PS51873 TRIAD, 1 hit
PS50089 ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiARI1_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: Q9Y4X5
Secondary accession number(s): B2R6U3
, O76026, Q9H3T6, Q9UEN0, Q9UP39
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 10, 2002
Last modified: April 22, 2020
This is version 183 of the entry and version 2 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
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