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Entry version 119 (08 May 2019)
Sequence version 3 (28 Nov 2006)
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Protein

Ubiquitin thioesterase otulin

Gene

OTULIN

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

Deubiquitinase that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response (PubMed:26997266, PubMed:23708998, PubMed:23746843, PubMed:23806334, PubMed:23827681, PubMed:27523608, PubMed:27559085, PubMed:24726323, PubMed:24726327, PubMed:28919039). Required during angiogenesis, craniofacial and neuronal development by regulating the canonical Wnt signaling together with the LUBAC complex (PubMed:23708998). Acts as a negative regulator of NF-kappa-B by regulating the activity of the LUBAC complex (PubMed:23746843, PubMed:23806334). OTULIN function is mainly restricted to homeostasis of the LUBAC complex: acts by removing 'Met-1'-linked autoubiquitination of the LUBAC complex, thereby preventing inactivation of the LUBAC complex (PubMed:26670046). Acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis (PubMed:27523608). In myeloid cell, required to prevent unwarranted secretion of cytokines leading to inflammation and autoimmunity by restricting linear polyubiquitin formation (PubMed:27523608). Plays a role in innate immune response by restricting linear polyubiquitin formation on LUBAC complex in response to NOD2 stimulation, probably to limit NOD2-dependent proinflammatory signaling (PubMed:23806334).11 Publications

Caution

The key substrates of OTULIN and where OTULIN acts to limit inflammation have been subject to discussion. According to some reports, OTULIN plays active roles in TNF or NOD2 receptor signaling complexes (RSCs) by directly deubiquitinating proteins in these complexes (PubMed:26997266, PubMed:27523608). A publication also suggested that OTULIN directly mediates deubiquitination of RIPK2 (PubMed:23806334). However, a publication reported that OTULIN function is restricted to homeostasis of the LUBAC complex, because it is not stably associated with TNF or NOD2 receptor signaling complexes (RSCs) (PubMed:26670046). The main function of OTULIN in deubiquitinating the LUBAC complex was confirmed by knockin experiments in mouse.By similarity4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 6.3 sec(-1) with linear diubiquitin as substrate.1 Publication
  1. KM=7.98 µM for linear diubiquitin1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei126Combined sources2 Publications1
    Active sitei129NucleophileCombined sources3 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei314Linear diubiquitinCombined sources2 Publications1
    Active sitei339Combined sources2 Publications1

    <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 functionHydrolase, Protease, Thiol protease
    Biological processAngiogenesis, Immunity, Innate immunity, Ubl conjugation pathway, Wnt signaling pathway

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-5357905 Regulation of TNFR1 signaling
    R-HSA-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes

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

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Ubiquitin thioesterase otulinCurated (EC:3.4.19.124 Publications)
    Alternative name(s):
    Deubiquitinating enzyme otulin1 Publication
    OTU domain-containing deubiquitinase with linear linkage specificity1 Publication
    Ubiquitin thioesterase GumbyBy similarity
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:OTULIN1 PublicationImported
    Synonyms:FAM105BImported
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:25118 OTULIN

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    615712 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q96BN8

    <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

    <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

    Autoinflammation, panniculitis, and dermatosis syndrome (AIPDS)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn autosomal recessive autoinflammatory disorder characterized by neonatal-onset of fever, neutrophilic dermatitis, panniculitis, painful joints, failure to thrive. Patients do not exhibit overt primary immunodeficiency.
    Related information in OMIM
    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_076865244Y → C in AIPDS; slightly impaired ability to mediate deubiquitination of linear polyubiquitin chains; does not affect ability to interact with RNF31. 1 PublicationCorresponds to variant dbSNP:rs886037887EnsemblClinVar.1
    Natural variantiVAR_076866272L → P in AIPDS; decreased stability; impaired ability to mediate deubiquitination of linear polyubiquitin chains; increased NF-kappa-B signaling; does not affect ability to interact with RNF31. 2 PublicationsCorresponds to variant dbSNP:rs886037885EnsemblClinVar.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi54D → A: Reduced interaction with RNF31. 1 Publication1
    Mutagenesisi55M → D: Abolished interaction with RNF31. 1 Publication1
    Mutagenesisi56Y → A or D: Abolished interaction with RNF31. 3 Publications1
    Mutagenesisi56Y → E, F or W: Strongly reduced interaction with RNF31. 2 Publications1
    Mutagenesisi91Y → F: Results in strong reduction of kcat while not affecting KM. 1 Publication1
    Mutagenesisi96W → A: Decreased activity toward linear ubiquitin. 2 Publications1
    Mutagenesisi100 – 102TQK → AAA: Decreased activity toward linear ubiquitin. 1 Publication3
    Mutagenesisi129C → A or S: Abolishes deubiquitinase activity. 5 Publications1
    Mutagenesisi259L → E: Decreased affinity for linear diubiquitin. 1 Publication1
    Mutagenesisi314E → R: Decreased affinity for linear diubiquitin. 1 Publication1
    Mutagenesisi336D → A: Stabilizes H-339 in the active conformation, generating a more reactive enzyme. 1 Publication1
    Mutagenesisi339H → A: Impaired deubiquitinase activity. 1 Publication1
    Mutagenesisi341N → A: Abolishes deubiquitinase activity. 1 Publication1
    Mutagenesisi341N → D: Stabilizes H-339 in the active conformation, generating a more reactive enzyme. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    90268

    MalaCards human disease database

    More...
    MalaCardsi
    OTULIN
    MIMi617099 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000154124

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

    More...
    Orphaneti
    500062 Infantile-onset periodic fever-panniculitis-dermatosis syndrome

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA142671789

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    OTULIN

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    118572305

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

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002616371 – 352Ubiquitin thioesterase otulinAdd BLAST352

    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 residuei56Phosphotyrosine2 Publications1

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

    Ubiquitinated.1 Publication
    Acetylated.1 Publication
    Phosphorylated (PubMed:23746843, PubMed:24726323, PubMed:24726327). Phosphorylation at Tyr-56 prevents interaction with RNF31; dephosphorylation promotes interaction with RNF31 and the LUBAC complex (PubMed:24726323, PubMed:24726327).3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q96BN8

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q96BN8

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q96BN8

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

    More...
    PaxDbi
    Q96BN8

    PeptideAtlas

    More...
    PeptideAtlasi
    Q96BN8

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q96BN8

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    76094

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q96BN8

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

    More...
    PhosphoSitePlusi
    Q96BN8

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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000154124 Expressed in 185 organ(s), highest expression level in testis

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q96BN8 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q96BN8 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA051074

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

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

    Interacts (via the PUB domain) with RNF31 (via the PIM motif); the interaction is direct (PubMed:23708998, PubMed:23746843, PubMed:24726323, PubMed:24726327, PubMed:27523608).

    Interacts with DVL2 (By similarity).

    By similarity5 Publications

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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    124684, 38 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    Q96BN8, 13 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q96BN8

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000284274

    <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

    1352
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...
    SMRi
    Q96BN8

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini118 – 346OTUPROSITE-ProRule annotationAdd BLAST229

    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>Regioni95 – 96Linear diubiquitin bindingCombined sources2 Publications2
    Regioni124 – 126Linear diubiquitin bindingCombined sources2 Publications3
    Regioni255 – 259Linear diubiquitin bindingCombined sources2 Publications5
    Regioni283 – 289Linear diubiquitin bindingCombined sources2 Publications7
    Regioni336 – 338Linear diubiquitin bindingCombined sources2 Publications3

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi52 – 57PIM motif3 Publications6

    <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 specificity for linear polyubiquitin is given by the 'Glu-16' residue in ubiquitin chain.1 Publication
    The PIM (PUB-interaction motif) motif mediates interaction with the PUB domain of RNF31 (PubMed:24726323, PubMed:24726327, PubMed:27458237). Does not interact with other PUB domain-containing proteins. Phosphorylation at Tyr-56 prevents interaction with RNF31 (PubMed:24726323, PubMed:24726327).3 Publications

    <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 peptidase C65 family. Otulin subfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410IE61 Eukaryota
    ENOG4111KB3 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000009802

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000294085

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q96BN8

    KEGG Orthology (KO)

    More...
    KOi
    K18343

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    PRDWPVV

    Database of Orthologous Groups

    More...
    OrthoDBi
    1416236at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q96BN8

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF328709

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR023235 FAM105
    IPR023237 Otulin

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR33662 PTHR33662, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF16218 Peptidase_C101, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR02055 PROTEINF105
    PR02057 PROTEINF105B

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. 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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

    Q96BN8-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MSRGTMPQPE AWPGASCAET PAREAAATAR DGGKAAASGQ PRPEMQCPAE
    60 70 80 90 100
    HEEDMYRAAD EIEKEKELLI HERGASEPRL SVAPEMDIMD YCKKEWRGNT
    110 120 130 140 150
    QKATCMKMGY EEVSQKFTSI RRVRGDNYCA LRATLFQAMS QAVGLPPWLQ
    160 170 180 190 200
    DPELMLLPEK LISKYNWIKQ WKLGLKFDGK NEDLVDKIKE SLTLLRKKWA
    210 220 230 240 250
    GLAEMRTAEA RQIACDELFT NEAEEYSLYE AVKFLMLNRA IELYNDKEKG
    260 270 280 290 300
    KEVPFFSVLL FARDTSNDPG QLLRNHLNQV GHTGGLEQVE MFLLAYAVRH
    310 320 330 340 350
    TIQVYRLSKY NTEEFITVYP TDPPKDWPVV TLIAEDDRHY NIPVRVCEET

    SL
    Length:352
    Mass (Da):40,263
    Last modified:November 28, 2006 - v3
    <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:i65071FF7B427C2FA
    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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    D6RD57D6RD57_HUMAN
    Ubiquitin thioesterase otulin
    OTULIN
    58Annotation 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>
    H0Y9T0H0Y9T0_HUMAN
    Ubiquitin thioesterase otulin
    OTULIN
    84Annotation 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>
    H0Y8S4H0Y8S4_HUMAN
    Ubiquitin thioesterase otulin
    OTULIN
    66Annotation 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>

    <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 AAH07706 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAH15392 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAC03828 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.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 conflicti211R → G in BAC03828 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_053819155M → L. Corresponds to variant dbSNP:rs11953822Ensembl.1
    Natural variantiVAR_029469227S → N. Corresponds to variant dbSNP:rs9312870Ensembl.1
    Natural variantiVAR_076865244Y → C in AIPDS; slightly impaired ability to mediate deubiquitination of linear polyubiquitin chains; does not affect ability to interact with RNF31. 1 PublicationCorresponds to variant dbSNP:rs886037887EnsemblClinVar.1
    Natural variantiVAR_076866272L → P in AIPDS; decreased stability; impaired ability to mediate deubiquitination of linear polyubiquitin chains; increased NF-kappa-B signaling; does not affect ability to interact with RNF31. 2 PublicationsCorresponds to variant dbSNP:rs886037885EnsemblClinVar.1
    Natural variantiVAR_053820311N → S. Corresponds to variant dbSNP:rs9312870Ensembl.1

    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
    AC010491 Genomic DNA No translation available.
    CH471102 Genomic DNA Translation: EAX08038.1
    CH471102 Genomic DNA Translation: EAX08039.1
    BC007706 mRNA Translation: AAH07706.3 Different initiation.
    BC015392 mRNA Translation: AAH15392.2 Different initiation.
    AK092203 mRNA Translation: BAC03828.1 Different initiation.

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS43302.1

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_612357.4, NM_138348.5
    XP_011512453.1, XM_011514151.2
    XP_011512454.1, XM_011514152.2

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000284274; ENSP00000284274; ENSG00000154124

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    90268

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:90268

    UCSC genome browser

    More...
    UCSCi
    uc003jfk.4 human

    Keywords - Coding sequence diversityi

    Polymorphism

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

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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC010491 Genomic DNA No translation available.
    CH471102 Genomic DNA Translation: EAX08038.1
    CH471102 Genomic DNA Translation: EAX08039.1
    BC007706 mRNA Translation: AAH07706.3 Different initiation.
    BC015392 mRNA Translation: AAH15392.2 Different initiation.
    AK092203 mRNA Translation: BAC03828.1 Different initiation.
    CCDSiCCDS43302.1
    RefSeqiNP_612357.4, NM_138348.5
    XP_011512453.1, XM_011514151.2
    XP_011512454.1, XM_011514152.2

    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
    3ZNVX-ray1.30A80-352[»]
    3ZNXX-ray1.35A80-352[»]
    3ZNZX-ray1.90A80-352[»]
    4KSJX-ray1.60A79-352[»]
    4KSKX-ray2.40A/B55-352[»]
    4KSLX-ray2.83A/B/E/G/I/K/M/O/Q/S/U/W79-352[»]
    4OYKX-ray2.00C/D49-67[»]
    4P0BX-ray2.70B/D52-61[»]
    5OE7X-ray2.95A80-350[»]
    6I9CX-ray1.77A80-345[»]
    SMRiQ96BN8
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi124684, 38 interactors
    IntActiQ96BN8, 13 interactors
    MINTiQ96BN8
    STRINGi9606.ENSP00000284274

    PTM databases

    iPTMnetiQ96BN8
    PhosphoSitePlusiQ96BN8

    Polymorphism and mutation databases

    BioMutaiOTULIN
    DMDMi118572305

    Proteomic databases

    EPDiQ96BN8
    jPOSTiQ96BN8
    MaxQBiQ96BN8
    PaxDbiQ96BN8
    PeptideAtlasiQ96BN8
    PRIDEiQ96BN8
    ProteomicsDBi76094

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    90268
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000284274; ENSP00000284274; ENSG00000154124
    GeneIDi90268
    KEGGihsa:90268
    UCSCiuc003jfk.4 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    90268
    DisGeNETi90268

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    OTULIN
    HGNCiHGNC:25118 OTULIN
    HPAiHPA051074
    MalaCardsiOTULIN
    MIMi615712 gene
    617099 phenotype
    neXtProtiNX_Q96BN8
    OpenTargetsiENSG00000154124
    Orphaneti500062 Infantile-onset periodic fever-panniculitis-dermatosis syndrome
    PharmGKBiPA142671789

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiENOG410IE61 Eukaryota
    ENOG4111KB3 LUCA
    GeneTreeiENSGT00390000009802
    HOGENOMiHOG000294085
    InParanoidiQ96BN8
    KOiK18343
    OMAiPRDWPVV
    OrthoDBi1416236at2759
    PhylomeDBiQ96BN8
    TreeFamiTF328709

    Enzyme and pathway databases

    ReactomeiR-HSA-5357905 Regulation of TNFR1 signaling
    R-HSA-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes

    Miscellaneous databases

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

    More...
    ChiTaRSi
    OTULIN human

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

    More...
    GenomeRNAii
    90268

    Protein Ontology

    More...
    PROi
    PR:Q96BN8

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000154124 Expressed in 185 organ(s), highest expression level in testis
    ExpressionAtlasiQ96BN8 baseline and differential
    GenevisibleiQ96BN8 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR023235 FAM105
    IPR023237 Otulin
    PANTHERiPTHR33662 PTHR33662, 1 hit
    PfamiView protein in Pfam
    PF16218 Peptidase_C101, 1 hit
    PRINTSiPR02055 PROTEINF105
    PR02057 PROTEINF105B

    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 nameiOTUL_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: Q96BN8
    Secondary accession number(s): D3DTD3, Q8NAS0, Q96IA3
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: November 28, 2006
    Last modified: May 8, 2019
    This is version 119 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. Peptidase families
      Classification of peptidase families and list of entries
    UniProt is an ELIXIR core data resource
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