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UniProtKB - Q96EP0 (RNF31_HUMAN)

Entry version 195 (23 Feb 2022)
Sequence version 1 (01 Dec 2001)
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Protein

E3 ubiquitin-protein ligase RNF31

Gene

RNF31

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 component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed:17006537, PubMed:19136968, PubMed:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28481331, PubMed:28189684).

LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (PubMed:17006537, PubMed:19136968, PubMed:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28189684).

Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:21455173, PubMed:28189684).

LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex (PubMed:20005846, PubMed:27458237).

The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (PubMed:28481331, PubMed:34012115).

LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (PubMed:28481331).

Recruited to the surface of bacteria by RNF213, which initiates the bacterial ubiquitin coat (PubMed:34012115).

The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:28481331, PubMed:34012115).

Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (PubMed:23708998).

RNF31 is required for linear ubiquitination of BCL10, thereby promoting TCR-induced NF-kappa-B activation (PubMed:27777308).

Binds polyubiquitin of different linkage types (PubMed:23708998).

13 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 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.4 Publications
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 bindingi699Zinc 1PROSITE-ProRule annotation1
Metal bindingi702Zinc 1PROSITE-ProRule annotation1
Metal bindingi722Zinc 1PROSITE-ProRule annotation1
Metal bindingi725Zinc 1PROSITE-ProRule annotation1
Metal bindingi799Zinc 2PROSITE-ProRule annotation1
Metal bindingi802Zinc 2PROSITE-ProRule annotation1
Metal bindingi817Zinc 2PROSITE-ProRule annotation1
Metal bindingi820Zinc 2PROSITE-ProRule annotation1
Metal bindingi825Zinc 3PROSITE-ProRule annotation1
Metal bindingi828Zinc 3PROSITE-ProRule annotation1
Metal bindingi836Zinc 3; via tele nitrogenPROSITE-ProRule annotation1
Metal bindingi841Zinc 3PROSITE-ProRule annotation1
Metal bindingi871Zinc 4PROSITE-ProRule annotation1
Metal bindingi874Zinc 4PROSITE-ProRule annotation1
<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 sitei885PROSITE-ProRule annotation1
Metal bindingi890Zinc 4PROSITE-ProRule annotation1
Metal bindingi893Zinc 4PROSITE-ProRule annotation1
Metal bindingi898Zinc 5PROSITE-ProRule annotation1
Metal bindingi901Zinc 5PROSITE-ProRule annotation1
Metal bindingi916Zinc 5PROSITE-ProRule annotation1
Metal bindingi925Zinc 5; via tele nitrogenPROSITE-ProRule annotation1

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 fingeri299 – 329RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri350 – 379RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri409 – 438RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri699 – 749RING-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri779 – 841IBR-typePROSITE-ProRule annotationAdd BLAST63
Zinc fingeri871 – 901RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST31

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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		2.3.2.31, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q96EP0

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-5357905, Regulation of TNFR1 signaling
R-HSA-5357956, TNFR1-induced NFkappaB signaling pathway

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		Q96EP0

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 RNF31 (EC:2.3.2.314 Publications)
Alternative name(s):
HOIL-1-interacting protein1 Publication
Short name:
HOIP1 Publication
RING finger protein 31Imported
RING-type E3 ubiquitin transferase RNF31Curated
Zinc in-between-RING-finger ubiquitin-associated domain protein1 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:RNF31Imported
Synonyms:ZIBRA1 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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 14

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:16031, RNF31

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		612487, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q96EP0

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000092098

<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

Keywords - Cellular componenti

Cytoplasm

<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%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>Mutagenesisi82Y → A: Abolished interaction with OTULIN. 1 Publication1
Mutagenesisi82Y → F: Reduced interaction with OTULIN. 1 Publication1
Mutagenesisi85N → A: Reduced interaction with OTULIN. 1 Publication1
Mutagenesisi99K → E: Reduced interaction with OTULIN. 1 Publication1
Mutagenesisi101N → R: Does not affect interaction with OTULIN. 1 Publication1
Mutagenesisi102N → A: Abolished interaction with SPATA2. 1 Publication1
Mutagenesisi102N → D: Abolished interaction with OTULIN. 1 Publication1
Mutagenesisi104V → A: Reduced interaction with OTULIN. 1 Publication1
Mutagenesisi360T → A: Decreased ubiquitin-binding and ability to promote formation of the bacterial ubiquitin coat. 1 Publication1
Mutagenesisi390D → A: Abolishes cleavage by caspase. 1 Publication1
Mutagenesisi699C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-702. 2 Publications1
Mutagenesisi702C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-699. 2 Publications1
Mutagenesisi735K → R: Reduced ubiquitination; when associated with R-783 and R-875. 1 Publication1
Mutagenesisi783K → R: Reduced ubiquitination; when associated with R-735 and R-875. 1 Publication1
Mutagenesisi871C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-874. 2 Publications1
Mutagenesisi874C → S: Abolishes polyubiquitination activity of LUBAC; when associated with S-871. 2 Publications1
Mutagenesisi875K → R: Reduced ubiquitination; when associated with R-735 and R-783. 1 Publication1
Mutagenesisi885C → A: Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-935 and A-983. 1 Publication1
Mutagenesisi935R → A: Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-885 and A-983. 1 Publication1
Mutagenesisi983D → A: Abolished E3 ubiquitin-protein ligase activity and ability to promote formation of the bacterial ubiquitin coat; when associated with A-885 and A-935. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		55072

MalaCards human disease database

More...MalaCardsi		RNF31

Open Targets

More...OpenTargetsi		ENSG00000092098
ENSG00000259529

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		329173, Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA134906471

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q96EP0, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4296109

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RNF31

Domain mapping of disease mutations (DMDM)

More...DMDMi		45477216

<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_00000560691 – 1072E3 ubiquitin-protein ligase RNF31Add BLAST1072

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 residuei383PhosphoserineCombined sources1
Modified residuei466PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki735(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki783(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki875(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

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

Autoubiquitinated (PubMed:24726323). Interaction with OTULIN is required to suppress formation of 'Met-1'-linked polyubiquitin chains and prevent subsequent inactivation of the LUBAC complex (PubMed:24726323).1 Publication
Cleaved by caspase during apoptosis.1 Publication
(Microbial infection) Ubiquitinated by S.flexneri E3 ubiquitin-protein ligases IpaH1.4 and IpaH2.5, leading to its degradation by the proteasome, thereby preventing formation of the bacterial ubiquitin coat and activation of innate immunity.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei390 – 391Cleavage; by caspase1 Publication2

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q96EP0

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q96EP0

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q96EP0

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q96EP0

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

More...PaxDbi		Q96EP0

PeptideAtlas

More...PeptideAtlasi		Q96EP0

PRoteomics IDEntifications database

More...PRIDEi		Q96EP0

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		76429 [Q96EP0-1]
76430 [Q96EP0-2]
76431 [Q96EP0-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q96EP0

MetOSite database of methionine sulfoxide sites

More...MetOSitei		Q96EP0

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

More...PhosphoSitePlusi		Q96EP0

<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

Expressed in both normal and transformed breast epithelial cell lines.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000092098, Expressed in muscle tissue and 119 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q96EP0, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q96EP0, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000092098, 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

Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31 (PubMed:17006537, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:28481331). LUBAC has a MW of approximately 600 kDa suggesting a heteromultimeric assembly of its subunits (PubMed:17006537, PubMed:21455173, PubMed:21455180, PubMed:21455181). Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner (PubMed:20005846).

Interacts (via the PUB domain) with OTULIN (via the PIM motif); the interaction is direct (PubMed:23708998, PubMed:24726323, PubMed:24726327).

Interacts (via the PUB domain) with VCP (via the PIM motif) (PubMed:24726327).

Interacts (via the PUB domain) with SPATA2 (via the PIM motif); interaction is direct and bridges RNF31 and CYLD (PubMed:27458237, PubMed:27545878, PubMed:28189684, PubMed:27591049).

Interacts with CYLD; the interaction is indirect and is mediated via SPATA2 (PubMed:27458237, PubMed:27545878, PubMed:26997266).

Interacts with MUSK (By similarity).

Interacts with CARD11, promoting linear ubiquitination of BCL10 (PubMed:27777308).

By similarity16 Publications

(Microbial infection) Interacts with S.flexneri E3 ubiquitin-protein ligases IpaH1.4 and IpaH2.5, leading to its ubiquitination.

1 Publication

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

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		120389, 383 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1877, LUBAC ubiquitin ligase complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q96EP0

Database of interacting proteins

More...DIPi		DIP-44034N

Protein interaction database and analysis system

More...IntActi		Q96EP0, 69 interactors

Molecular INTeraction database

More...MINTi		Q96EP0

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000315112

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q96EP0

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q96EP0, 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

11072
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q96EP0

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

More...SMRi		Q96EP0

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q96EP0

<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%5Fand%5Fdomains%5Fsection">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>Domaini71 – 142PUBSequence analysisAdd BLAST72
Domaini564 – 615UBAPROSITE-ProRule annotationAdd BLAST52

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>Regioni1 – 485Polyubiquitin-bindingAdd BLAST485
Regioni263 – 290DisorderedSequence analysisAdd BLAST28
Regioni443 – 484DisorderedSequence analysisAdd BLAST42
Regioni563 – 616Interaction with RBCK1Add BLAST54
Regioni695 – 929TRIAD supradomainPROSITE-ProRule annotationAdd BLAST235
Regioni910 – 1072LDD domainAdd BLAST163

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi452 – 466Pro residuesSequence analysisAdd BLAST15

<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

The PUB domain mediates interaction with the PIM motifs of VCP and RNF31, with a strong preference for RNF31.2 Publications
The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin.1 Publication
The UBA domain mediates association with RBCK1/HOIL1 via interaction with its UBL domain.
RING 1 and IBR zinc-fingers catalyze the first step transfer of ubiquitin from the E2 onto RING 2, to transiently form a HECT-like covalent thioester intermediate.1 Publication
The linear ubiquitin chain determining domain (LDD) mediates the final transfer of ubiquitin from RING 2 onto the N-terminus of a target ubiquitin.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.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri299 – 329RanBP2-type 1PROSITE-ProRule annotationAdd BLAST31
Zinc fingeri350 – 379RanBP2-type 2PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri409 – 438RanBP2-type 3PROSITE-ProRule annotationAdd BLAST30
Zinc fingeri699 – 749RING-type 1PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri779 – 841IBR-typePROSITE-ProRule annotationAdd BLAST63
Zinc fingeri871 – 901RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST31

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1812, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00530000064112

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q96EP0

Identification of Orthologs from Complete Genome Data

More...OMAi		AVLCAMC

Database of Orthologous Groups

More...OrthoDBi		1188714at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q96EP0

TreeFam database of animal gene trees

More...TreeFami		TF350529

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.40.10, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00576

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002867, IBR_dom
IPR036339, PUB-like_dom_sf
IPR018997, PUB_domain
IPR026254, RNF31-like
IPR032065, RNF31-UBA
IPR041031, RNF31_C
IPR040641, RNF31_PUB
IPR044066, TRIAD_supradom
IPR015940, UBA
IPR001876, Znf_RanBP2
IPR036443, Znf_RanBP2_sf
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS

The PANTHER Classification System

More...PANTHERi		PTHR16004, PTHR16004, 2 hits

Pfam protein domain database

More...Pfami		View protein in Pfam
PF18091, E3_UbLigase_RBR, 1 hit
PF16678, HOIP-UBA, 1 hit
PF01485, IBR, 1 hit
PF09409, PUB, 1 hit
PF18486, PUB_1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00647, IBR, 2 hits
SM00547, ZnF_RBZ, 3 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF143503, SSF143503, 1 hit
SSF90209, SSF90209, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51873, TRIAD, 1 hit
PS50030, UBA, 1 hit
PS01358, ZF_RANBP2_1, 3 hits
PS50199, ZF_RANBP2_2, 2 hits
PS00518, ZF_RING_1, 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>Sequences (3+)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 describes 3 <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

This entry has 3 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q96EP0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MPGEEEERAF LVAREELASA LRRDSGQAFS LEQLRPLLAS SLPLAARYLQ 
        60         70         80         90        100
LDAARLVRCN AHGEPRNYLN TLSTALNILE KYGRNLLSPQ RPRYWRGVKF 
       110        120        130        140        150
NNPVFRSTVD AVQGGRDVLR LYGYTEEQPD GLSFPEGQEE PDEHQVATVT 
       160        170        180        190        200
LEVLLLRTEL SLLLQNTHPR QQALEQLLED KVEDDMLQLS EFDPLLREIA 
       210        220        230        240        250
PGPLTTPSVP GSTPGPCFLC GSAPGTLHCP SCKQALCPAC DHLFHGHPSR 
       260        270        280        290        300
AHHLRQTLPG VLQGTHLSPS LPASAQPRPQ STSLLALGDS SLSSPNPASA 
       310        320        330        340        350
HLPWHCAACA MLNEPWAVLC VACDRPRGCK GLGLGTEGPQ GTGGLEPDLA 
       360        370        380        390        400
RGRWACQSCT FENEAAAVLC SICERPRLAQ PPSLVVDSRD AGICLQPLQQ 
       410        420        430        440        450
GDALLASAQS QVWYCIHCTF CNSSPGWVCV MCNRTSSPIP AQHAPRPYAS 
       460        470        480        490        500
SLEKGPPKPG PPRRLSAPLP SSCGDPEKQR QDKMREEGLQ LVSMIREGEA 
       510        520        530        540        550
AGACPEEIFS ALQYSGTEVP LQWLRSELPY VLEMVAELAG QQDPGLGAFS 
       560        570        580        590        600
CQEARRAWLD RHGNLDEAVE ECVRTRRRKV QELQSLGFGP EEGSLQALFQ 
       610        620        630        640        650
HGGDVSRALT ELQRQRLEPF RQRLWDSGPE PTPSWDGPDK QSLVRRLLAV 
       660        670        680        690        700
YALPSWGRAE LALSLLQETP RNYELGDVVE AVRHSQDRAF LRRLLAQECA 
       710        720        730        740        750
VCGWALPHNR MQALTSCECT ICPDCFRQHF TIALKEKHIT DMVCPACGRP 
       760        770        780        790        800
DLTDDTQLLS YFSTLDIQLR ESLEPDAYAL FHKKLTEGVL MRDPKFLWCA 
       810        820        830        840        850
QCSFGFIYER EQLEATCPQC HQTFCVRCKR QWEEQHRGRS CEDFQNWKRM 
       860        870        880        890        900
NDPEYQAQGL AMYLQENGID CPKCKFSYAL ARGGCMHFHC TQCRHQFCSG 
       910        920        930        940        950
CYNAFYAKNK CPEPNCRVKK SLHGHHPRDC LFYLRDWTAL RLQKLLQDNN 
       960        970        980        990       1000
VMFNTEPPAG ARAVPGGGCR VIEQKEVPNG LRDEACGKET PAGYAGLCQA 
      1010       1020       1030       1040       1050
HYKEYLVSLI NAHSLDPATL YEVEELETAT ERYLHVRPQP LAGEDPPAYQ 
      1060       1070 
ARLLQKLTEE VPLGQSIPRR RK
Length:1,072
Mass (Da):119,652
Last modified:December 1, 2001 - 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:iCFAD183A14F764BA
GO
Isoform 2 (identifier: Q96EP0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     73-630: Missing.
     833-841: Missing.

Show »
Length:505
Mass (Da):57,633
Checksum:i04245E2E835AD19C
GO
Isoform 3 (identifier: Q96EP0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-151: Missing.
     152-164: EVLLLRTELSLLL → MDLCTRAGEPSLT

Show »
Length:921
Mass (Da):102,496
Checksum:i2149563718B64B0B
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 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YKX0H0YKX0_HUMAN
RBR-type E3 ubiquitin transferase
RNF31
917Annotation 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>
H0YMG4H0YMG4_HUMAN
E3 ubiquitin-protein ligase RNF31
RNF31
623Annotation 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>
H0YNK5H0YNK5_HUMAN
E3 ubiquitin-protein ligase RNF31
RNF31
149Annotation 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>
H0YMN0H0YMN0_HUMAN
E3 ubiquitin-protein ligase RNF31
RNF31
143Annotation 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>
H0YNT1H0YNT1_HUMAN
E3 ubiquitin-protein ligase RNF31
RNF31
140Annotation 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>
H0YM13H0YM13_HUMAN
E3 ubiquitin-protein ligase RNF31
RNF31
170Annotation 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>
H0YKI4H0YKI4_HUMAN
E3 ubiquitin-protein ligase RNF31
RNF31
165Annotation 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>
H0YMG8H0YMG8_HUMAN
E3 ubiquitin-protein ligase RNF31
RNF31
152Annotation 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>
A0A494C1G4A0A494C1G4_HUMAN
E3 ubiquitin-protein ligase RNF31
RNF31
161Annotation 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>
H0YMK6H0YMK6_HUMAN
E3 ubiquitin-protein ligase RNF31
RNF31
32Annotation 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>
There are more potential isoformsShow all

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAB15675 differs from that shown. Intron retention.Curated
The sequence BAB15675 differs from that shown. Reason: Frameshift.Curated
The sequence BAB15675 differs from that shown. Reason: Erroneous termination. Truncated C-terminus.Curated
The sequence BAB70948 differs from that shown. Reason: Erroneous initiation.Curated

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 conflicti529P → S in AAP12522 (PubMed:15093743).Curated1
Sequence conflicti800A → V in BAA91450 (PubMed:14702039).Curated1
Sequence conflicti925H → R in BAB15675 (PubMed:14702039).Curated1
Sequence conflicti1005Y → N in BAB15675 (PubMed:14702039).Curated1
Sequence conflicti1018A → S in BAB15675 (PubMed:14702039).Curated1
Sequence conflicti1021Y → D in BAB15675 (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_0521021061V → I1 PublicationCorresponds to variant dbSNP:rs2277484Ensembl.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_0140061 – 151Missing in isoform 3. 1 PublicationAdd BLAST151
Alternative sequenceiVSP_00964773 – 630Missing in isoform 2. 1 PublicationAdd BLAST558
Alternative sequenceiVSP_014007152 – 164EVLLL…LSLLL → MDLCTRAGEPSLT in isoform 3. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_009648833 – 841Missing in isoform 2. 1 Publication9

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
AY256461 mRNA Translation: AAP12522.1
AB265810 mRNA Translation: BAF35583.1
AK000973 mRNA Translation: BAA91450.1
AK027154 mRNA Translation: BAB15675.1 Frameshift.
AK055542 mRNA Translation: BAB70948.1 Different initiation.
AK291247 mRNA Translation: BAF83936.1
AL136295 Genomic DNA No translation available.
CH471078 Genomic DNA Translation: EAW66098.1
BC009821 mRNA Translation: AAH09821.3
BC012077 mRNA Translation: AAH12077.1
BC017376 mRNA Translation: AAH17376.3
AK074144 mRNA Translation: BAB84970.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS41931.1 [Q96EP0-1]
CCDS81792.1 [Q96EP0-3]

NCBI Reference Sequences

More...RefSeqi		NP_001297261.1, NM_001310332.1 [Q96EP0-3]
NP_060469.4, NM_017999.4 [Q96EP0-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000324103; ENSP00000315112; ENSG00000092098
ENST00000559275; ENSP00000453574; ENSG00000092098 [Q96EP0-3]
ENST00000642631; ENSP00000494011; ENSG00000285152 [Q96EP0-3]
ENST00000647495; ENSP00000496609; ENSG00000285152

Database of genes from NCBI RefSeq genomes

More...GeneIDi		55072

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:55072

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000324103.11; ENSP00000315112.6; NM_017999.5; NP_060469.4

UCSC genome browser

More...UCSCi		uc001wml.2, human [Q96EP0-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AY256461 mRNA Translation: AAP12522.1
AB265810 mRNA Translation: BAF35583.1
AK000973 mRNA Translation: BAA91450.1
AK027154 mRNA Translation: BAB15675.1 Frameshift.
AK055542 mRNA Translation: BAB70948.1 Different initiation.
AK291247 mRNA Translation: BAF83936.1
AL136295 Genomic DNA No translation available.
CH471078 Genomic DNA Translation: EAW66098.1
BC009821 mRNA Translation: AAH09821.3
BC012077 mRNA Translation: AAH12077.1
BC017376 mRNA Translation: AAH17376.3
AK074144 mRNA Translation: BAB84970.1
CCDSiCCDS41931.1 [Q96EP0-1]
CCDS81792.1 [Q96EP0-3]
RefSeqiNP_001297261.1, NM_001310332.1 [Q96EP0-3]
NP_060469.4, NM_017999.4 [Q96EP0-1]

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
2CT7NMR-A779-851[»]
4DBGX-ray2.71B480-636[»]
4JUYX-ray2.40A/B1-180[»]
4LJOX-ray1.56A853-1072[»]
4LJPX-ray2.15A853-1072[»]
4LJQX-ray2.45A/B/C/D853-1072[»]
4OWFX-ray2.00G350-379[»]
4OYJX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M1-184[»]
4OYKX-ray2.00A/B3-179[»]
4P09X-ray1.70A1-179[»]
4P0AX-ray2.30A/C1-179[»]
4P0BX-ray2.70A/C1-179[»]
5EDVX-ray3.48A/B696-1072[»]
5LJNX-ray2.70A/B5-176[»]
5X0WX-ray3.00A/C/E/G480-639[»]
6GZYX-ray2.15A/B853-1072[»]
6KC5X-ray1.54B853-1072[»]
6KC6X-ray2.12A/C/E/G/I/K853-1072[»]
6SC5X-ray2.10A697-1072[»]
6SC6X-ray2.25A697-1072[»]
6SC7X-ray2.56A697-1072[»]
6SC8X-ray2.11A697-1072[»]
6SC9X-ray2.47A697-1072[»]
BMRBiQ96EP0
SMRiQ96EP0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi120389, 383 interactors
ComplexPortaliCPX-1877, LUBAC ubiquitin ligase complex
CORUMiQ96EP0
DIPiDIP-44034N
IntActiQ96EP0, 69 interactors
MINTiQ96EP0
STRINGi9606.ENSP00000315112

Chemistry databases

BindingDBiQ96EP0
ChEMBLiCHEMBL4296109

PTM databases

iPTMnetiQ96EP0
MetOSiteiQ96EP0
PhosphoSitePlusiQ96EP0

Genetic variation databases

BioMutaiRNF31
DMDMi45477216

Proteomic databases

EPDiQ96EP0
jPOSTiQ96EP0
MassIVEiQ96EP0
MaxQBiQ96EP0
PaxDbiQ96EP0
PeptideAtlasiQ96EP0
PRIDEiQ96EP0
ProteomicsDBi76429 [Q96EP0-1]
76430 [Q96EP0-2]
76431 [Q96EP0-3]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		Q96EP0, 10 sequenced antibodies

Antibodypedia a portal for validated antibodies

More...Antibodypediai		22671, 257 antibodies from 36 providers

The DNASU plasmid repository

More...DNASUi		55072

Genome annotation databases

EnsembliENST00000324103; ENSP00000315112; ENSG00000092098
ENST00000559275; ENSP00000453574; ENSG00000092098 [Q96EP0-3]
ENST00000642631; ENSP00000494011; ENSG00000285152 [Q96EP0-3]
ENST00000647495; ENSP00000496609; ENSG00000285152
GeneIDi55072
KEGGihsa:55072
MANE-SelectiENST00000324103.11; ENSP00000315112.6; NM_017999.5; NP_060469.4
UCSCiuc001wml.2, human [Q96EP0-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		55072
DisGeNETi55072

GeneCards: human genes, protein and diseases

More...GeneCardsi		RNF31
HGNCiHGNC:16031, RNF31
HPAiENSG00000092098, Low tissue specificity
MalaCardsiRNF31
MIMi612487, gene
neXtProtiNX_Q96EP0
OpenTargetsiENSG00000092098
ENSG00000259529
Orphaneti329173, Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis
PharmGKBiPA134906471
VEuPathDBiHostDB:ENSG00000092098

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1812, Eukaryota
GeneTreeiENSGT00530000064112
InParanoidiQ96EP0
OMAiAVLCAMC
OrthoDBi1188714at2759
PhylomeDBiQ96EP0
TreeFamiTF350529

Enzyme and pathway databases

UniPathwayiUPA00143
BRENDAi2.3.2.31, 2681
PathwayCommonsiQ96EP0
ReactomeiR-HSA-5357905, Regulation of TNFR1 signaling
R-HSA-5357956, TNFR1-induced NFkappaB signaling pathway
SignaLinkiQ96EP0

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		55072, 76 hits in 1088 CRISPR screens

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

More...ChiTaRSi		RNF31, human
EvolutionaryTraceiQ96EP0

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		RNF31

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

More...GenomeRNAii		55072
PharosiQ96EP0, Tbio

Protein Ontology

More...PROi		PR:Q96EP0
RNActiQ96EP0, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000092098, Expressed in muscle tissue and 119 other tissues
ExpressionAtlasiQ96EP0, baseline and differential
GenevisibleiQ96EP0, HS

Family and domain databases

Gene3Di3.30.40.10, 1 hit
IDEALiIID00576
InterProiView protein in InterPro
IPR002867, IBR_dom
IPR036339, PUB-like_dom_sf
IPR018997, PUB_domain
IPR026254, RNF31-like
IPR032065, RNF31-UBA
IPR041031, RNF31_C
IPR040641, RNF31_PUB
IPR044066, TRIAD_supradom
IPR015940, UBA
IPR001876, Znf_RanBP2
IPR036443, Znf_RanBP2_sf
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS
PANTHERiPTHR16004, PTHR16004, 2 hits
PfamiView protein in Pfam
PF18091, E3_UbLigase_RBR, 1 hit
PF16678, HOIP-UBA, 1 hit
PF01485, IBR, 1 hit
PF09409, PUB, 1 hit
PF18486, PUB_1, 1 hit
SMARTiView protein in SMART
SM00647, IBR, 2 hits
SM00547, ZnF_RBZ, 3 hits
SUPFAMiSSF143503, SSF143503, 1 hit
SSF90209, SSF90209, 1 hit
PROSITEiView protein in PROSITE
PS51873, TRIAD, 1 hit
PS50030, UBA, 1 hit
PS01358, ZF_RANBP2_1, 3 hits
PS50199, ZF_RANBP2_2, 2 hits
PS00518, ZF_RING_1, 1 hit

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 nameiRNF31_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: Q96EP0
Secondary accession number(s): A0A962
, Q86VI2, Q8TEI0, Q96GB4, Q96NF1, Q9H5F1, Q9NWD2
<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: March 15, 2004
Last sequence update: December 1, 2001
Last modified: February 23, 2022
This is version 195 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, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families
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