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UniProtKB - O76064 (RNF8_HUMAN)

Entry version 201 (02 Dec 2020)
Sequence version 1 (01 Nov 1998)
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Protein

E3 ubiquitin-protein ligase RNF8

Gene

RNF8

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 that plays a key role in DNA damage signaling via 2 distinct roles: by mediating the 'Lys-63'-linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and H2AX, thereby promoting the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF). Also controls the recruitment of UIMC1-BRCC3 (RAP80-BRCC36) and PAXIP1/PTIP to DNA damage sites. Also recruited at DNA interstrand cross-links (ICLs) sites and catalyzes 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Promotes the formation of 'Lys-63'-linked polyubiquitin chains via interactions with the specific ubiquitin-conjugating UBE2N/UBC13 and ubiquitinates non-histone substrates such as PCNA. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation. Also catalyzes the formation of 'Lys-48'-linked polyubiquitin chains via interaction with the ubiquitin-conjugating UBE2L6/UBCH8, leading to degradation of substrate proteins such as CHEK2, JMJD2A/KDM4A and KU80/XRCC5: it is still unclear how the preference toward 'Lys-48'- versus 'Lys-63'-linked ubiquitination is regulated but it could be due to RNF8 ability to interact with specific E2 specific ligases. For instance, interaction with phosphorylated HERC2 promotes the association between RNF8 and UBE2N/UBC13 and favors the specific formation of 'Lys-63'-linked ubiquitin chains. Promotes non-homologous end joining (NHEJ) by promoting the 'Lys-48'-linked ubiquitination and degradation the of KU80/XRCC5. Following DNA damage, mediates the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF168, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites (PubMed:11322894, PubMed:14981089, PubMed:17724460, PubMed:18001824, PubMed:18001825, PubMed:18006705, PubMed:18077395, PubMed:18337245, PubMed:18948756, PubMed:19015238, PubMed:19124460, PubMed:19202061, PubMed:19203578, PubMed:19203579, PubMed:20550933, PubMed:21558560, PubMed:21857671, PubMed:21911360, PubMed:22266820, PubMed:22373579, PubMed:22531782, PubMed:22705371, PubMed:22865450, PubMed:22980979). Following DNA damage, mediates the ubiquitination and degradation of POLD4/p12, a subunit of DNA polymerase delta. In the absence of POLD4, DNA polymerase delta complex exhibits higher proofreading activity (PubMed:23233665). In addition to its function in damage signaling, also plays a role in higher-order chromatin structure by mediating extensive chromatin decondensation. Involved in the activation of ATM by promoting histone H2B ubiquitination, which indirectly triggers histone H4 'Lys-16' acetylation (H4K16ac), establishing a chromatin environment that promotes efficient activation of ATM kinase. Required in the testis, where it plays a role in the replacement of histones during spermatogenesis. At uncapped telomeres, promotes the joining of deprotected chromosome ends by inducing H2A ubiquitination and TP53BP1 recruitment, suggesting that it may enhance cancer development by aggravating telomere-induced genome instability in case of telomeric crisis. Promotes the assembly of RAD51 at DNA DSBs in the absence of BRCA1 and TP53BP1 Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. May be required for proper exit from mitosis after spindle checkpoint activation and may regulate cytokinesis. May play a role in the regulation of RXRA-mediated transcriptional activity. Not involved in RXRA ubiquitination by UBE2E2 (PubMed:11322894, PubMed:14981089, PubMed:17724460, PubMed:18001824, PubMed:18001825, PubMed:18006705, PubMed:18077395, PubMed:18337245, PubMed:18948756, PubMed:19015238, PubMed:19124460, PubMed:19202061, PubMed:19203578, PubMed:19203579, PubMed:20550933, PubMed:21558560, PubMed:21857671, PubMed:21911360, PubMed:22266820, PubMed:22373579, PubMed:22531782, PubMed:22705371, PubMed:22865450, PubMed:22980979).25 Publications

Caution

According to a well-established model, RNF8 initiate H2A 'Lys-63'-linked ubiquitination leading to recruitment of RNF168 to amplify H2A 'Lys-63'-linked ubiquitination (PubMed:19203578 and PubMed:19203579). However, other data suggest that RNF168 is the priming ubiquitin ligase by mediating monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub respectively) (PubMed:22980979). These data suggest that RNF168 might be recruited to DSBs sites in a RNF8-dependent manner by binding to non-histone proteins ubiquitinated via 'Lys-63'-linked and initiates monoubiquitination of H2A, which is then amplified by RNF8 (PubMed:22980979). Additional evidence is however required to confirm these data.UniRule annotation1 Publication

<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.UniRule annotation 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.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <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 fingeri403 – 441RING-typeUniRule annotationAdd BLAST39

<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 functionChromatin regulator, Transferase
Biological processCell cycle, Cell division, DNA damage, DNA repair, Host-virus interaction, Mitosis, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		O76064

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693571, Nonhomologous End-Joining (NHEJ)
R-HSA-5693607, Processing of DNA double-strand break ends
R-HSA-69473, G2/M DNA damage checkpoint

SIGNOR Signaling Network Open Resource

More...SIGNORi		O76064

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 RNF8UniRule annotation (EC:2.3.2.27UniRule annotation)
Short name:
hRNF8
Alternative name(s):
RING finger protein 8UniRule annotation
RING-type E3 ubiquitin transferase RNF8UniRule annotation
<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:RNF8UniRule annotation
Synonyms:KIAA0646
<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 6

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000112130.16

Human Gene Nomenclature Database

More...HGNCi		HGNC:10071, RNF8

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		611685, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O76064

<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

Chromosome, Cytoplasm, Nucleus, Telomere

<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>Mutagenesisi42R → A: Abolishes interaction with ATM-phosphorylated MDC1. Abolishes interaction with human herpesvirus 1 ICP0. Abolishes recruitment to DNA damage sites after UV irradiation, ionizing radiation, or treatment with an alkylating agent. 4 Publications1
Mutagenesisi403C → S: Marked reduction of E2-dependent ubiquitination of histone H2A. Loss of UBE2E2- and UBE2N-binding. Loss of nuclear localization. 4 Publications1
Mutagenesisi405I → A: Impairs interaction with UBE2L6/UBCH8 and ability to mediate 'Lys-48'-linked ubiquitination E3 ligase activity, while it still catalyzes 'Lys-63'-linked ubiquitination and still interacts with UBE2N/UBC13. 3 Publications1
Mutagenesisi406C → S: Abolishes ubiquitin-ligase activity. 1 Publication1
Mutagenesisi443D → R: Does not affect the monomeric structure but abolishes ability to monoubiquitinate H2A in nucleosomes. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		9025

Open Targets

More...OpenTargetsi		ENSG00000112130

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34445

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		O76064, Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RNF8

<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_00000560481 – 485E3 ubiquitin-protein ligase RNF8Add BLAST485

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 residuei157PhosphoserineCombined sources1

<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 through 'Lys-48' and 'Lys-63' of ubiquitin. 'Lys-63' polyubiquitination is mediated by UBE2N. 'Lys-29'-type polyubiquitination is also observed, but it doesn't require its own functional RING-type zinc finger.UniRule annotation1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O76064

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O76064

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		O76064

MaxQB - The MaxQuant DataBase

More...MaxQBi		O76064

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

More...PaxDbi		O76064

PeptideAtlas

More...PeptideAtlasi		O76064

PRoteomics IDEntifications database

More...PRIDEi		O76064

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		50370 [O76064-1]
50371 [O76064-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O76064

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

More...PhosphoSitePlusi		O76064

<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

Ubiquitous. In fetal tissues, highest expression in brain, thymus and liver. In adult tissues, highest levels in brain and testis, lowest levels in peripheral blood cells.2 Publications

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

Low levels at the G1-S boundary increase in intensity during S phase and until the end of the G2 phase. Abruptly decreases in late mitosis (at protein level). Barely detectable in anaphase.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000112130, Expressed in frontal cortex and 230 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		O76064, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O76064, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000112130, 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

Homodimer.

Forms a E2-E3 ubiquitin ligase complex composed of the RNF8 homodimer and a E2 heterodimer of UBE2N and UBE2V2.

Interacts with class III E2s, including UBE2E1, UBE2E2, and UBE2E3 and with UBE2N.

Interacts with RXRA.

Interacts (via FHA domain) with ATM-phosphorylated MDC1.

Interacts (via FHA domain) with 'Thr-4827' phosphorylated HERC2 (via C-terminus).

Interacts with PIWIL1; leading to sequester RNF8 in the cytoplasm (By similarity).

Interacts with WRAP53/TCAB1 (PubMed:25512560).

By similarity12 Publications

(Microbial infection) Interacts (via FHA domain) with phosphorylated human herpesvirus 1 ICP0 protein; leading to RNF8 degradation by the proteasome.

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

O76064
With#Exp.IntAct
AMOTL2 [Q9Y2J4]3EBI-373337,EBI-746752
C2CD6 [Q53TS8]3EBI-373337,EBI-739879
CALCOCO1 [Q9P1Z2]3EBI-373337,EBI-749920
CCDC14 - isoform 3 [Q49A88-3]3EBI-373337,EBI-12105646
CCDC50 [Q8IVM0]3EBI-373337,EBI-723996
CEP44 [Q9C0F1]4EBI-373337,EBI-744115
CEP85 - isoform 3 [Q6P2H3-3]3EBI-373337,EBI-12368239
CLK2 [P49760]5EBI-373337,EBI-750020
CLK3 [P49761]3EBI-373337,EBI-745579
DDIT4L [Q96D03]3EBI-373337,EBI-742054
DNM2 [P50570]3EBI-373337,EBI-346547
DNTTIP2 [Q5QJE6]3EBI-373337,EBI-5666736
EPN2 - isoform 2 [O95208-2]3EBI-373337,EBI-12135243
EPN3 [I6L9I8]3EBI-373337,EBI-12866582
FAM118B [Q9BPY3]3EBI-373337,EBI-726822
FAM9B [Q8IZU0]3EBI-373337,EBI-10175124
FSD2 [A1L4K1]3EBI-373337,EBI-5661036
GPRASP2 [Q96D09]3EBI-373337,EBI-473189
HEL-S-70 [V9HW80]3EBI-373337,EBI-10175326
HOMEZ - isoform 2 [Q8IX15-3]3EBI-373337,EBI-10172004
KANK2 [Q63ZY3]3EBI-373337,EBI-2556193
KIF24 - isoform 2 [Q5T7B8-2]3EBI-373337,EBI-10213781
KRTAP10-8 [P60410]3EBI-373337,EBI-10171774
KRTAP9-2 [Q9BYQ4]3EBI-373337,EBI-1044640
KRTAP9-8 [Q9BYQ0]3EBI-373337,EBI-11958364
LMO4 [P61968]3EBI-373337,EBI-2798728
MAD1L1 [Q9Y6D9]7EBI-373337,EBI-742610
MAPK1 [P28482]3EBI-373337,EBI-959949
MDC1 [Q14676]11EBI-373337,EBI-495644
PCYT1A [P49585]3EBI-373337,EBI-2563309
PGRMC2 [O15173]3EBI-373337,EBI-1050125
PICK1 [Q9NRD5]3EBI-373337,EBI-79165
PNMA2 [Q9UL42]7EBI-373337,EBI-302355
PPCDC [Q96CD2]3EBI-373337,EBI-724333
PSMB1 [P20618]3EBI-373337,EBI-372273
RBFOX2 [O43251]3EBI-373337,EBI-746056
RBFOX2 - isoform 10 [O43251-10]3EBI-373337,EBI-11963050
itself6EBI-373337,EBI-373337
SCN3B [Q9NY72]3EBI-373337,EBI-17247926
SEPTIN3 [Q9UH03]7EBI-373337,EBI-727037
SH3GL3 [Q8IVP1]3EBI-373337,EBI-6503765
STX11 [O75558]6EBI-373337,EBI-714135
TMEM79 [Q9BSE2]10EBI-373337,EBI-8649725
TNIP1 [Q15025]3EBI-373337,EBI-357849
TOMM20L [Q6UXN7]3EBI-373337,EBI-11954062
UBE2D2 [P62837]4EBI-373337,EBI-347677
VRK1 [Q99986]2EBI-373337,EBI-1769146
WASHC3 [Q9Y3C0]3EBI-373337,EBI-712969
WASL [O00401]8EBI-373337,EBI-957615
ZBTB10 - isoform 3 [Q96DT7-3]3EBI-373337,EBI-12017160
ZNF346 [Q9UL40]3EBI-373337,EBI-2462313
ZNF496 [Q96IT1]3EBI-373337,EBI-743906
Isoform 1 [O76064-1]
With#Exp.IntAct
MDC1 [Q14676]2EBI-15964690,EBI-495644

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		114492, 108 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O76064

Database of interacting proteins

More...DIPi		DIP-31265N

Protein interaction database and analysis system

More...IntActi		O76064, 78 interactors

Molecular INTeraction database

More...MINTi		O76064

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000362578

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O76064, 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

1485
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		O76064

Small Angle Scattering Biological Data Bank

More...SASBDBi		O76064

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

More...SMRi		O76064

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		O76064

<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>Domaini38 – 92FHAUniRule annotationAdd BLAST55

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>Regioni68 – 72Required for interaction with PIWIL1UniRule annotation5

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi276 – 345Gln-richAdd BLAST70

<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 FHA domain specifically recognizes and binds ATM-phosphorylated MDC1 and 'Thr-4827' phosphorylated HERC2 (PubMed:18001824). This domain is required for proper recruitment to DNA damage sites after UV irradiation, ionizing radiation, or treatment with an alkylating agent (PubMed:23233665).2 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 RNF8 family.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri403 – 441RING-typeUniRule annotationAdd BLAST39

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3872, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00400000022349

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_023453_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O76064

Identification of Orthologs from Complete Genome Data

More...OMAi		SYCISEW

Database of Orthologous Groups

More...OrthoDBi		1585372at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O76064

TreeFam database of animal gene trees

More...TreeFami		TF330957

Family and domain databases

Conserved Domains Database

More...CDDi		cd00060, FHA, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.40.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_03067, RNF8, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00118

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000253, FHA_dom
IPR017335, RNF8
IPR008984, SMAD_FHA_dom_sf
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00498, FHA, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF037950, E3_ubiquit_lig_RNF8, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00240, FHA, 1 hit
SM00184, RING, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF49879, SSF49879, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50006, FHA_DOMAIN, 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 (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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O76064-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><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
MGEPGFFVTG DRAGGRSWCL RRVGMSAGWL LLEDGCEVTV GRGFGVTYQL 
        60         70         80         90        100
VSKICPLMIS RNHCVLKQNP EGQWTIMDNK SLNGVWLNRA RLEPLRVYSI 
       110        120        130        140        150
HQGDYIQLGV PLENKENAEY EYEVTEEDWE TIYPCLSPKN DQMIEKNKEL 
       160        170        180        190        200
RTKRKFSLDE LAGPGAEGPS NLKSKINKVS CESGQPVKSQ GKGEVASTPS 
       210        220        230        240        250
DNLDPKLTAL EPSKTTGAPI YPGFPKVTEV HHEQKASNSS ASQRSLQMFK 
       260        270        280        290        300
VTMSRILRLK IQMQEKHEAV MNVKKQTQKG NSKKVVQMEQ ELQDLQSQLC 
       310        320        330        340        350
AEQAQQQARV EQLEKTFQEE EQHLQGLEIA QGEKDLKQQL AQALQEHWAL 
       360        370        380        390        400
MEELNRSKKD FEAIIQAKNK ELEQTKEEKE KMQAQKEEVL SHMNDVLENE 
       410        420        430        440        450
LQCIICSEYF IEAVTLNCAH SFCSYCINEW MKRKIECPIC RKDIKSKTYS 
       460        470        480 
LVLDNCINKM VNNLSSEVKE RRIVLIRERK AKRLF
Length:485
Mass (Da):55,518
Last modified:November 1, 1998 - 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:i54650B2FFC9948B1
GO
Isoform 2 (identifier: O76064-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     81-98: SLNGVWLNRARLEPLRVY → SFPSEKAEDFTAAGERFL
     99-485: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.Curated
Show »
Length:98
Mass (Da):10,846
Checksum:i0E5E5F3D13560D56
GO
Isoform 3 (identifier: O76064-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     413-448: AVTLNCAHSFCSYCINEWMKRKIECPICRKDIKSKT → QRDCSEDRALRAFERLPGSASLRWSGGFSLAVTPLL
     449-485: Missing.

Show »
Length:448
Mass (Da):50,829
Checksum:iC20C2E1E5A761106
GO

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

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9J858C9J858_HUMAN
E3 ubiquitin-protein ligase RNF8
RNF8
205Annotation 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>
H7C4L7H7C4L7_HUMAN
E3 ubiquitin-protein ligase RNF8
RNF8
208Annotation 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>
F8WEW6F8WEW6_HUMAN
E3 ubiquitin-protein ligase RNF8
RNF8
89Annotation 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>
F8WDH8F8WDH8_HUMAN
E3 ubiquitin-protein ligase RNF8
RNF8
49Annotation 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 BAA31621 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence BAG60572 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated
The sequence EAX03945 differs from that shown. Reason: Erroneous gene model prediction.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 conflicti230V → A in BAD96485 (Ref. 6) Curated1
Sequence conflicti334K → R in BAD96485 (Ref. 6) 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_052096162A → T. Corresponds to variant dbSNP:rs34338974Ensembl.1
Natural variantiVAR_052097473I → V. Corresponds to variant dbSNP:rs1139944Ensembl.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_03667181 – 98SLNGV…PLRVY → SFPSEKAEDFTAAGERFL in isoform 2. 1 PublicationAdd BLAST18
Alternative sequenceiVSP_03783199 – 485Missing in isoform 2. 1 PublicationAdd BLAST387
Alternative sequenceiVSP_054037413 – 448AVTLN…IKSKT → QRDCSEDRALRAFERLPGSA SLRWSGGFSLAVTPLL in isoform 3. CuratedAdd BLAST36
Alternative sequenceiVSP_054038449 – 485Missing in isoform 3. CuratedAdd BLAST37

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
AB012770 Genomic DNA Translation: BAA33557.1
AF334675 mRNA Translation: AAQ14887.1
AB014546 mRNA Translation: BAA31621.2 Different initiation.
AK298319 mRNA Translation: BAG60572.1 Sequence problems.
BT007446 mRNA Translation: AAP36114.1
AK222765 mRNA Translation: BAD96485.1
AL096712 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03944.1
CH471081 Genomic DNA Translation: EAX03945.1 Sequence problems.
BC007517 mRNA Translation: AAH07517.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS4833.1 [O76064-3]
CCDS4834.1 [O76064-1]

NCBI Reference Sequences

More...RefSeqi		NP_003949.1, NM_003958.3 [O76064-1]
NP_898901.1, NM_183078.2 [O76064-3]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000229866; ENSP00000229866; ENSG00000112130 [O76064-2]
ENST00000373479; ENSP00000362578; ENSG00000112130 [O76064-1]
ENST00000469731; ENSP00000418879; ENSG00000112130 [O76064-3]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		9025

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:9025

UCSC genome browser

More...UCSCi		uc003onq.4, human [O76064-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012770 Genomic DNA Translation: BAA33557.1
AF334675 mRNA Translation: AAQ14887.1
AB014546 mRNA Translation: BAA31621.2 Different initiation.
AK298319 mRNA Translation: BAG60572.1 Sequence problems.
BT007446 mRNA Translation: AAP36114.1
AK222765 mRNA Translation: BAD96485.1
AL096712 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03944.1
CH471081 Genomic DNA Translation: EAX03945.1 Sequence problems.
BC007517 mRNA Translation: AAH07517.1
CCDSiCCDS4833.1 [O76064-3]
CCDS4834.1 [O76064-1]
RefSeqiNP_003949.1, NM_003958.3 [O76064-1]
NP_898901.1, NM_183078.2 [O76064-3]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CSWNMR-A8-139[»]
2PIEX-ray1.35A13-146[»]
4AYCX-ray1.90A/B351-485[»]
4ORHX-ray4.80C/G/H/K/L345-485[»]
4WHVX-ray8.30C/D/I/J345-485[»]
BMRBiO76064
SASBDBiO76064
SMRiO76064
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi114492, 108 interactors
CORUMiO76064
DIPiDIP-31265N
IntActiO76064, 78 interactors
MINTiO76064
STRINGi9606.ENSP00000362578

PTM databases

iPTMnetiO76064
PhosphoSitePlusiO76064

Polymorphism and mutation databases

BioMutaiRNF8

Proteomic databases

EPDiO76064
jPOSTiO76064
MassIVEiO76064
MaxQBiO76064
PaxDbiO76064
PeptideAtlasiO76064
PRIDEiO76064
ProteomicsDBi50370 [O76064-1]
50371 [O76064-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		15585, 323 antibodies

The DNASU plasmid repository

More...DNASUi		9025

Genome annotation databases

EnsembliENST00000229866; ENSP00000229866; ENSG00000112130 [O76064-2]
ENST00000373479; ENSP00000362578; ENSG00000112130 [O76064-1]
ENST00000469731; ENSP00000418879; ENSG00000112130 [O76064-3]
GeneIDi9025
KEGGihsa:9025
UCSCiuc003onq.4, human [O76064-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		9025
DisGeNETi9025
EuPathDBiHostDB:ENSG00000112130.16

GeneCards: human genes, protein and diseases

More...GeneCardsi		RNF8
HGNCiHGNC:10071, RNF8
HPAiENSG00000112130, Low tissue specificity
MIMi611685, gene
neXtProtiNX_O76064
OpenTargetsiENSG00000112130
PharmGKBiPA34445

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3872, Eukaryota
GeneTreeiENSGT00400000022349
HOGENOMiCLU_023453_1_0_1
InParanoidiO76064
OMAiSYCISEW
OrthoDBi1585372at2759
PhylomeDBiO76064
TreeFamiTF330957

Enzyme and pathway databases

UniPathwayiUPA00143
PathwayCommonsiO76064
ReactomeiR-HSA-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693571, Nonhomologous End-Joining (NHEJ)
R-HSA-5693607, Processing of DNA double-strand break ends
R-HSA-69473, G2/M DNA damage checkpoint
SIGNORiO76064

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		9025, 350 hits in 850 CRISPR screens

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

More...ChiTaRSi		RNF8, human
EvolutionaryTraceiO76064

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		RNF8

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

More...GenomeRNAii		9025
PharosiO76064, Tbio

Protein Ontology

More...PROi		PR:O76064
RNActiO76064, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000112130, Expressed in frontal cortex and 230 other tissues
ExpressionAtlasiO76064, baseline and differential
GenevisibleiO76064, HS

Family and domain databases

CDDicd00060, FHA, 1 hit
Gene3Di3.30.40.10, 1 hit
HAMAPiMF_03067, RNF8, 1 hit
IDEALiIID00118
InterProiView protein in InterPro
IPR000253, FHA_dom
IPR017335, RNF8
IPR008984, SMAD_FHA_dom_sf
IPR001841, Znf_RING
IPR013083, Znf_RING/FYVE/PHD
IPR017907, Znf_RING_CS
PfamiView protein in Pfam
PF00498, FHA, 1 hit
PIRSFiPIRSF037950, E3_ubiquit_lig_RNF8, 1 hit
SMARTiView protein in SMART
SM00240, FHA, 1 hit
SM00184, RING, 1 hit
SUPFAMiSSF49879, SSF49879, 1 hit
PROSITEiView protein in PROSITE
PS50006, FHA_DOMAIN, 1 hit
PS00518, ZF_RING_1, 1 hit
PS50089, ZF_RING_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRNF8_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: O76064
Secondary accession number(s): A6NN24
, A8MYC0, B4DPG0, Q53H16, Q5NKW5
<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: June 6, 2002
Last sequence update: November 1, 1998
Last modified: December 2, 2020
This is version 201 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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
  6. SIMILARITY comments
    Index of protein domains and families
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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