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Entry version 149 (25 May 2022)
Sequence version 1 (21 Dec 2004)
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Protein

Roquin-1

Gene

RC3H1

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

Post-transcriptional repressor of mRNAs containing a conserved stem loop motif, called constitutive decay element (CDE), which is often located in the 3'-UTR, as in HMGXB3, ICOS, IER3, NFKBID, NFKBIZ, PPP1R10, TNF, TNFRSF4 and in many more mRNAs (PubMed:25026078, PubMed:31636267).

Cleaves translationally inactive mRNAs harboring a stem-loop (SL), often located in their 3'-UTRs, during the early phase of inflammation in a helicase UPF1-independent manner (By similarity).

Binds to CDE and promotes mRNA deadenylation and degradation. This process does not involve miRNAs (By similarity).

In follicular helper T (Tfh) cells, represses of ICOS and TNFRSF4 expression, thus preventing spontaneous Tfh cell differentiation, germinal center B-cell differentiation in the absence of immunization and autoimmunity (By similarity).

In resting or LPS-stimulated macrophages, controls inflammation by suppressing TNF expression (By similarity).

Also recognizes CDE in its own mRNA and in that of paralogous RC3H2, possibly leading to feedback loop regulation (By similarity).

Recognizes and binds mRNAs containing a hexaloop stem-loop motif, called alternative decay element (ADE) (By similarity).

Together with ZC3H12A, destabilizes TNFRSF4/OX40 mRNA by binding to the conserved stem loop structure in its 3'UTR (By similarity).

Able to interact with double-stranded RNA (dsRNA) (PubMed:25504471, PubMed:25026078).

miRNA-binding protein that regulates microRNA homeostasis. Enhances DICER-mediated processing of pre-MIR146a but reduces mature MIR146a levels through an increase of 3' end uridylation. Both inhibits ICOS mRNA expression and they may act together to exert the suppression (PubMed:25697406, PubMed:31636267).

Acts as a ubiquitin E3 ligase. Pairs with E2 enzymes UBE2A, UBE2B, UBE2D2, UBE2F, UBE2G1, UBE2G2 and UBE2L3 and produces polyubiquitin chains (PubMed:26489670).

Shows the strongest activity when paired with UBE2N:UBE2V1 or UBE2N:UBE2V2 E2 complexes and generate both short and long polyubiquitin chains (PubMed:26489670).

By similarity5 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

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.1 Publication EC:2.3.2.27

<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.1 Publication
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 bindingi14Zinc 1By similarity1
Metal bindingi17Zinc 1By similarity1
Metal bindingi33Zinc 2By similarity1
Metal bindingi35Zinc 2; via pros nitrogenBy similarity1
Metal bindingi38Zinc 1By similarity1
Metal bindingi50Zinc 2By similarity1
Metal bindingi53Zinc 2By similarity1

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 fingeri14 – 54RING-type; degeneratePROSITE-ProRule annotationAdd BLAST41
Zinc fingeri413 – 441C3H1-typePROSITE-ProRule annotationAdd BLAST29

<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 functionRNA-binding, Transferase
LigandMetal-binding, Zinc

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
Q5TC82

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

More...
SignaLinki
Q5TC82

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:
Roquin-1Curated (EC:2.3.2.271 Publication)
Short name:
RoquinCurated
Alternative name(s):
RING finger and C3H zinc finger protein 1
RING finger and CCCH-type zinc finger domain-containing protein 1
RING finger protein 198
<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:RC3H1Imported
Synonyms:KIAA2025, RNF198
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:29434, RC3H1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
609424, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q5TC82

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000135870

<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

<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

Immune dysregulation and systemic hyperinflammation syndrome (IMDYSHI)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by systemic hyperinflammation in the absence of an infectious agent or autoimmune trigger. Features include lymphadenopathy, hepatosplenomegaly, recurrent fever, and laboratory evidence of immune dysregulation with abnormal immune cell populations and increased serum levels of inflammatory cytokines.
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_084832688 – 1133Missing in IMDYSHI; decreased protein abundance; loss of localization to P-bodies; decreased interaction with CCR4-NOT deadenylase complex; loss of function in regulation of deadenylation-dependent decapping of nuclear-transcribed mRNA; failed to regulate the production of inflammatory cytokines. 1 PublicationAdd BLAST446

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>Mutagenesisi135 – 136RK → EE: No effect on CDE RNA-binding but abolishes dsRNA binding; when associated with E-164 or A-322-323-A. 1 Publication2
Mutagenesisi164R → E: No effect on CDE RNA-binding but abolishes dsRNA binding; when associated with 135-E-E-136. 1 Publication1
Mutagenesisi219 – 220RK → AA: Strongly decreases binding to RNA containing CDE stem-loop motifs. Abolishes binding to RNA containing CDE stem-loop motifs and dsRNA; when associated with 259-A-A-260. 1 Publication2
Mutagenesisi239 – 240KT → EA: Abolishes CDE RNA-binding but no effect on dsRNA binding. 1 Publication2
Mutagenesisi247 – 251QLLYR → ALLAE: Abolishes CDE RNA-binding but no effect on dsRNA binding. 1 Publication5
Mutagenesisi259 – 260KR → AA: Strongly decreases binding to RNA containing CDE stem-loop motifs. Abolishes binding to RNA containing CDE stem-loop motifs and dsRNA; when associated with 219-A-A-220. 1 Publication2
Mutagenesisi318 – 319QS → AA: Slightly reduces stem-loop RNA and dsRNA binding. 1 Publication2
Mutagenesisi322 – 323DK → AA: No effect on CDE RNA-binding but abolishes dsRNA binding; when associated with 135-E-E-136. 1 Publication2

Keywords - Diseasei

Disease variant

Organism-specific databases

DisGeNET

More...
DisGeNETi
149041

MalaCards human disease database

More...
MalaCardsi
RC3H1
MIMi618998, phenotype

Open Targets

More...
OpenTargetsi
ENSG00000135870

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA142671090

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q5TC82, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
RC3H1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
73621450

<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_00000559651 – 1133Roquin-1Add BLAST1133

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 residuei462PhosphoserineCombined sources1
Modified residuei531PhosphoserineBy similarity1
Modified residuei535PhosphoserineCombined sources1
Modified residuei863PhosphoserineCombined sources1
Modified residuei1110PhosphoserineBy similarity1

<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

Proteolytically cleaved after Arg-510 and Arg-579 by MALT1 in activated CD4+ T cells; cleavage at Arg-510 and Arg-579 is critical for promoting RC3H1 degradation in response to T-cell receptor (TCR) stimulation, and hence is necessary for prolonging the stability of a set of mRNAs controlling Th17 cell differentiation.By similarity

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>Sitei510Cleavage; by MALT1By similarity1
Sitei579Cleavage; by MALT1By similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q5TC82

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q5TC82

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q5TC82

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q5TC82

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

More...
PaxDbi
Q5TC82

PeptideAtlas

More...
PeptideAtlasi
Q5TC82

PRoteomics IDEntifications database

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PRIDEi
Q5TC82

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
64943 [Q5TC82-1]
64944 [Q5TC82-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q5TC82

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

More...
PhosphoSitePlusi
Q5TC82

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

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

Widely expressed. Expressed at higher level in cerebellum, spleen, ovary and liver.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000135870, Expressed in gastrocnemius and 220 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q5TC82, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000135870, 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

Able to homodimerize (PubMed:25504471, PubMed:25026078, PubMed:25697406).

Interacts with DDX6 and EDC4 (By similarity).

Interacts with CCR4-NOT deadenylase complex (PubMed:31636267).

Interacts with RC3H1; the interaction is RNA independent (PubMed:25697406).

By similarity4 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
127186, 665 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q5TC82

Protein interaction database and analysis system

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IntActi
Q5TC82, 7 interactors

Molecular INTeraction database

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MINTi
Q5TC82

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000356669

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q5TC82, 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

11133
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
Q5TC82

Biological Magnetic Resonance Data Bank

More...
BMRBi
Q5TC82

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

More...
SMRi
Q5TC82

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

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>Regioni89 – 173HEPN-N1 PublicationAdd BLAST85
Regioni174 – 326ROQ2 PublicationsAdd BLAST153
Regioni327 – 396HEPN-C1 PublicationAdd BLAST70
Regioni505 – 543DisorderedSequence analysisAdd BLAST39
Regioni1000 – 1019DisorderedSequence analysisAdd BLAST20
Regioni1058 – 1078DisorderedSequence analysisAdd BLAST21
Regioni1094 – 1133DisorderedSequence analysisAdd BLAST40

<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 RING-type zinc finger is required for proper localization to stress granules, but not to P-bodies.By similarity
The ROQ region is required for CDE RNA-binding (PubMed:25504471, PubMed:25026078). Has 2 separate RNA-binding sites, one for CDE RNA and the other for dsRNA, both sites are important for mRNA decay (PubMed:25026078). ADE RNA-binding involves an extended binding surface on the ROQ region with a number of additional residues compared with the CDE RNA (By similarity). It may also be involved in localization to stress granules (By similarity).By similarity2 Publications
HEPN (higher eukaryotes and prokaryotes nucleotide-binding) are observed in both N- and C-terminal sides of ROQ domain with 3D structure even if they are poredcted on the basis of sequence.1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri14 – 54RING-type; degeneratePROSITE-ProRule annotationAdd BLAST41
Zinc fingeri413 – 441C3H1-typePROSITE-ProRule annotationAdd BLAST29

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3161, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157143

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_004948_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q5TC82

Identification of Orthologs from Complete Genome Data

More...
OMAi
YGTHSGW

Database of Orthologous Groups

More...
OrthoDBi
1009668at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q5TC82

TreeFam database of animal gene trees

More...
TreeFami
TF317698

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR032671, RC3H1
IPR041523, ROQ_II
IPR027370, Znf-RING_LisH
IPR000571, Znf_CCCH
IPR036855, Znf_CCCH_sf
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS

The PANTHER Classification System

More...
PANTHERi
PTHR13139:SF6, PTHR13139:SF6, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18386, ROQ_II, 1 hit
PF13445, zf-RING_UBOX, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00184, RING, 1 hit
SM00356, ZnF_C3H1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF90229, SSF90229, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50103, ZF_C3H1, 1 hit
PS00518, ZF_RING_1, 1 hit
PS50089, ZF_RING_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)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 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q5TC82-1) [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
MPVQAPQWTD FLSCPICTQT FDETIRKPIS LGCGHTVCKM CLNKLHRKAC
60 70 80 90 100
PFDQTTINTD IELLPVNSAL LQLVGAQVPE QQPITLCSGV EDTKHYEEAK
110 120 130 140 150
KCVEELALYL KPLSSARGVG LNSTTQSVLS RPMQRKLVTL VHCQLVEEEG
160 170 180 190 200
RIRAMRAARS LGERTVTELI LQHQNPQQLS SNLWAAVRAR GCQFLGPAMQ
210 220 230 240 250
EEALKLVLLA LEDGSALSRK VLVLFVVQRL EPRFPQASKT SIGHVVQLLY
260 270 280 290 300
RASCFKVTKR DEDSSLMQLK EEFRTYEALR REHDSQIVQI AMEAGLRIAP
310 320 330 340 350
DQWSSLLYGD QSHKSHMQSI IDKLQTPASF AQSVQELTIA LQRTGDPANL
360 370 380 390 400
NRLRPHLELL ANIDPSPDAP PPTWEQLENG LVAVRTVVHG LVDYIQNHSK
410 420 430 440 450
KGADQQQPPQ HSKYKTYMCR DMKQRGGCPR GASCTFAHSQ EELEKFRKMN
460 470 480 490 500
KRLVPRRPLS ASLGQLNEVG LPSAAILPDE GAVDLPSRKP PALPNGIVST
510 520 530 540 550
GNTVTQLIPR GTDPSYDSSL KPGKIDHLSS SAPGSPPDLL ESVPKSISAL
560 570 580 590 600
PVNPHSIPPR GPADLPPMPV TKPLQMVPRG SQLYPAQQTD VYYQDPRGAA
610 620 630 640 650
PPFEPAPYQQ GMYYTPPPQC VSRFVRPPPS APEPAPPYLD HYPPYLQERV
660 670 680 690 700
VNSQYGTQPQ QYPPIYPSHY DGRRVYPAPS YTREEIFRES PIPIEIPPAA
710 720 730 740 750
VPSYVPESRE RYQQIESYYP VAPHPTQIRP SYLREPPYSR LPPPPQPHPS
760 770 780 790 800
LDELHRRRKE IMAQLEERKV ISPPPFAPSP TLPPTFHPEE FLDEDLKVAG
810 820 830 840 850
KYKGNDYSQY SPWSCDTIGS YIGTKDAKPK DVVAAGSVEM MNVESKGMRD
860 870 880 890 900
QRLDLQRRAA ETSDDDLIPF GDRPTVSRFG AISRTSKTIY QGAGPMQAMA
910 920 930 940 950
PQGAPTKSIN ISDYSPYGTH GGWGASPYSP HQNIPSQGHF SERERISMSE
960 970 980 990 1000
VASHGKPLPS AEREQLRLEL QQLNHQISQQ TQLRGLEAVS NRLVLQREAN
1010 1020 1030 1040 1050
TLAGQSQPPP PPPPKWPGMI SSEQLSLELH QVEREIGKRT RELSMENQCS
1060 1070 1080 1090 1100
LDMKSKLNTS KQAENGQPEP QNKVPAEDLT LTFSDVPNGS ALTQENISLL
1110 1120 1130
SNKTSSLNLS EDPEGGGDNN DSQRSGVTPS SAP
Length:1,133
Mass (Da):125,736
Last modified:December 21, 2004 - 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:iE307838DF80A7099
GO
Isoform 2 (identifier: Q5TC82-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     988-996: Missing.
     1084-1084: S → SS

Show »
Length:1,125
Mass (Da):124,842
Checksum:iEFBE5179071DFA94
GO

<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 BAC04186 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.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 conflicti986L → P in BAC04186 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_084832688 – 1133Missing in IMDYSHI; decreased protein abundance; loss of localization to P-bodies; decreased interaction with CCR4-NOT deadenylase complex; loss of function in regulation of deadenylation-dependent decapping of nuclear-transcribed mRNA; failed to regulate the production of inflammatory cytokines. 1 PublicationAdd BLAST446

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_015015988 – 996Missing in isoform 2. 1 Publication9
Alternative sequenceiVSP_0150161084S → SS in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AK093501 mRNA Translation: BAC04186.1 Different initiation.
AK122948 mRNA Translation: BAG53813.1
AL121983 Genomic DNA No translation available.
AL136170 Genomic DNA No translation available.
AB095945 mRNA Translation: BAC23121.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS30940.1 [Q5TC82-1]
CCDS72987.1 [Q5TC82-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001287779.1, NM_001300850.1
NP_001287780.1, NM_001300851.1 [Q5TC82-2]
NP_001287781.1, NM_001300852.1
NP_742068.1, NM_172071.3 [Q5TC82-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000258349.8; ENSP00000258349.4; ENSG00000135870.12
ENST00000367694.2; ENSP00000356667.2; ENSG00000135870.12 [Q5TC82-2]
ENST00000367696.7; ENSP00000356669.2; ENSG00000135870.12

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
149041

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:149041

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

More...
MANE-Selecti
ENST00000367696.7; ENSP00000356669.2; NM_172071.4; NP_742068.1

UCSC genome browser

More...
UCSCi
uc001gju.5, human [Q5TC82-1]

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
AK093501 mRNA Translation: BAC04186.1 Different initiation.
AK122948 mRNA Translation: BAG53813.1
AL121983 Genomic DNA No translation available.
AL136170 Genomic DNA No translation available.
AB095945 mRNA Translation: BAC23121.1
CCDSiCCDS30940.1 [Q5TC82-1]
CCDS72987.1 [Q5TC82-2]
RefSeqiNP_001287779.1, NM_001300850.1
NP_001287780.1, NM_001300851.1 [Q5TC82-2]
NP_001287781.1, NM_001300852.1
NP_742068.1, NM_172071.3 [Q5TC82-1]

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
3X1OX-ray2.20A/B145-344[»]
4QIKX-ray1.90A/B88-407[»]
4QILX-ray2.90A/B88-407[»]
4ULWX-ray1.91A/B177-328[»]
4YWQX-ray1.70A/B159-328[»]
AlphaFoldDBiQ5TC82
BMRBiQ5TC82
SMRiQ5TC82
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi127186, 665 interactors
CORUMiQ5TC82
IntActiQ5TC82, 7 interactors
MINTiQ5TC82
STRINGi9606.ENSP00000356669

PTM databases

iPTMnetiQ5TC82
PhosphoSitePlusiQ5TC82

Genetic variation databases

BioMutaiRC3H1
DMDMi73621450

Proteomic databases

EPDiQ5TC82
jPOSTiQ5TC82
MassIVEiQ5TC82
MaxQBiQ5TC82
PaxDbiQ5TC82
PeptideAtlasiQ5TC82
PRIDEiQ5TC82
ProteomicsDBi64943 [Q5TC82-1]
64944 [Q5TC82-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
34400, 140 antibodies from 22 providers

The DNASU plasmid repository

More...
DNASUi
149041

Genome annotation databases

EnsembliENST00000258349.8; ENSP00000258349.4; ENSG00000135870.12
ENST00000367694.2; ENSP00000356667.2; ENSG00000135870.12 [Q5TC82-2]
ENST00000367696.7; ENSP00000356669.2; ENSG00000135870.12
GeneIDi149041
KEGGihsa:149041
MANE-SelectiENST00000367696.7; ENSP00000356669.2; NM_172071.4; NP_742068.1
UCSCiuc001gju.5, human [Q5TC82-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
149041
DisGeNETi149041

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RC3H1
HGNCiHGNC:29434, RC3H1
HPAiENSG00000135870, Low tissue specificity
MalaCardsiRC3H1
MIMi609424, gene
618998, phenotype
neXtProtiNX_Q5TC82
OpenTargetsiENSG00000135870
PharmGKBiPA142671090
VEuPathDBiHostDB:ENSG00000135870

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3161, Eukaryota
GeneTreeiENSGT00940000157143
HOGENOMiCLU_004948_0_0_1
InParanoidiQ5TC82
OMAiYGTHSGW
OrthoDBi1009668at2759
PhylomeDBiQ5TC82
TreeFamiTF317698

Enzyme and pathway databases

UniPathwayiUPA00143
PathwayCommonsiQ5TC82
SignaLinkiQ5TC82

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
149041, 36 hits in 1120 CRISPR screens

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

More...
ChiTaRSi
RC3H1, human

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

More...
GenomeRNAii
149041
PharosiQ5TC82, Tbio

Protein Ontology

More...
PROi
PR:Q5TC82
RNActiQ5TC82, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000135870, Expressed in gastrocnemius and 220 other tissues
GenevisibleiQ5TC82, HS

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR032671, RC3H1
IPR041523, ROQ_II
IPR027370, Znf-RING_LisH
IPR000571, Znf_CCCH
IPR036855, Znf_CCCH_sf
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS
PANTHERiPTHR13139:SF6, PTHR13139:SF6, 1 hit
PfamiView protein in Pfam
PF18386, ROQ_II, 1 hit
PF13445, zf-RING_UBOX, 1 hit
SMARTiView protein in SMART
SM00184, RING, 1 hit
SM00356, ZnF_C3H1, 1 hit
SUPFAMiSSF90229, SSF90229, 1 hit
PROSITEiView protein in PROSITE
PS50103, ZF_C3H1, 1 hit
PS00518, ZF_RING_1, 1 hit
PS50089, ZF_RING_2, 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 nameiRC3H1_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: Q5TC82
Secondary accession number(s): B3KVK1
, Q5W180, Q5W181, Q8IVE6, Q8N9V1
<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: August 16, 2005
Last sequence update: December 21, 2004
Last modified: May 25, 2022
This is version 149 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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