Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

E3 ubiquitin-protein ligase RNF8

Gene

RNF8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 evidences are however required to confirm these data.UniRule annotation1 Publication

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.UniRule annotation

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
Zinc fingeri403 – 441RING-typeUniRule annotationAdd BLAST39

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

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
UniPathwayi
UPA00143

Names & Taxonomyi

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
Gene namesi
Name:RNF8UniRule annotation
Synonyms:KIAA0646
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000112130.16
HGNCiHGNC:10071 RNF8
MIMi611685 gene
neXtProtiNX_O76064

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi9025
OpenTargetsiENSG00000112130
PharmGKBiPA34445

Polymorphism and mutation databases

BioMutaiRNF8

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000560481 – 485E3 ubiquitin-protein ligase RNF8Add BLAST485

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei157PhosphoserineCombined sources1

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

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

PTM databases

iPTMnetiO76064
PhosphoSitePlusiO76064

Expressioni

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

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

BgeeiENSG00000112130 Expressed in 217 organ(s), highest expression level in frontal cortex
CleanExiHS_RNF8
ExpressionAtlasiO76064 baseline and differential
GenevisibleiO76064 HS

Organism-specific databases

HPAiHPA050731
HPA064925

Interactioni

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

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114492, 62 interactors
DIPiDIP-31265N
IntActiO76064, 68 interactors
MINTiO76064
STRINGi9606.ENSP00000362578

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliO76064
SMRiO76064
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO76064

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 92FHAUniRule annotationAdd BLAST55

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni68 – 72Required for interaction with PIWIL1UniRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi276 – 345Gln-richAdd BLAST70

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

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

eggNOGiENOG410INBI Eukaryota
ENOG410Z9IW LUCA
GeneTreeiENSGT00400000022349
HOGENOMiHOG000154169
HOVERGENiHBG023954
InParanoidiO76064
KOiK10667
OMAiQEHRALM
OrthoDBiEOG091G0I40
PhylomeDBiO76064
TreeFamiTF330957

Family and domain databases

CDDicd00060 FHA, 1 hit
Gene3Di3.30.40.10, 1 hit
HAMAPiMF_03067 RNF8, 1 hit
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

Sequences (3+)i

Sequence statusi: Complete.

This entry describes 3 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 'canonical' 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
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. No experimental confirmation available.
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.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:448
Mass (Da):50,829
Checksum:iC20C2E1E5A761106
GO

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:
H7C4L7H7C4L7_HUMAN
E3 ubiquitin-protein ligase RNF8
RNF8
208Annotation score:
F8WEW6F8WEW6_HUMAN
E3 ubiquitin-protein ligase RNF8
RNF8
89Annotation score:
F8WDH8F8WDH8_HUMAN
E3 ubiquitin-protein ligase RNF8
RNF8
49Annotation score:

Sequence cautioni

The sequence BAA31621 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.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
Sequence conflicti230V → A in BAD96485 (Ref. 6) Curated1
Sequence conflicti334K → R in BAD96485 (Ref. 6) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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:
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]
UniGeneiHs.485278

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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

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]
UniGeneiHs.485278

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliO76064
SMRiO76064
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114492, 62 interactors
DIPiDIP-31265N
IntActiO76064, 68 interactors
MINTiO76064
STRINGi9606.ENSP00000362578

PTM databases

iPTMnetiO76064
PhosphoSitePlusiO76064

Polymorphism and mutation databases

BioMutaiRNF8

Proteomic databases

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

Protocols and materials databases

DNASUi9025
Structural Biology KnowledgebaseSearch...

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

CTDi9025
DisGeNETi9025
EuPathDBiHostDB:ENSG00000112130.16
GeneCardsiRNF8
HGNCiHGNC:10071 RNF8
HPAiHPA050731
HPA064925
MIMi611685 gene
neXtProtiNX_O76064
OpenTargetsiENSG00000112130
PharmGKBiPA34445
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INBI Eukaryota
ENOG410Z9IW LUCA
GeneTreeiENSGT00400000022349
HOGENOMiHOG000154169
HOVERGENiHBG023954
InParanoidiO76064
KOiK10667
OMAiQEHRALM
OrthoDBiEOG091G0I40
PhylomeDBiO76064
TreeFamiTF330957

Enzyme and pathway databases

UniPathwayi
UPA00143

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

ChiTaRSiRNF8 human
EvolutionaryTraceiO76064
GeneWikiiRNF8
GenomeRNAii9025
PROiPR:O76064
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000112130 Expressed in 217 organ(s), highest expression level in frontal cortex
CleanExiHS_RNF8
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
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
ProtoNetiSearch...

Entry informationi

Entry nameiRNF8_HUMAN
AccessioniPrimary (citable) accession number: O76064
Secondary accession number(s): A6NN24
, A8MYC0, B4DPG0, Q53H16, Q5NKW5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 1, 1998
Last modified: November 7, 2018
This is version 185 of the entry and version 1 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again