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O76064

- RNF8_HUMAN

UniProt

O76064 - RNF8_HUMAN

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Protein

E3 ubiquitin-protein ligase RNF8

Gene
RNF8, KIAA0646
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - 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. 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 UBE2E2.24 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri403 – 44139RING-typeAdd
BLAST

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. chromatin binding Source: UniProtKB
  3. histone binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB
  6. ubiquitin protein ligase binding Source: UniProtKB
  7. ubiquitin-protein transferase activity Source: UniProtKB
  8. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. double-strand break repair Source: UniProtKB
  3. double-strand break repair via nonhomologous end joining Source: UniProtKB
  4. histone exchange Source: UniProtKB
  5. histone H2A K63-linked ubiquitination Source: UniProtKB
  6. histone H2A ubiquitination Source: UniProtKB
  7. histone H2B ubiquitination Source: UniProtKB
  8. interstrand cross-link repair Source: UniProtKB
  9. isotype switching Source: UniProtKB
  10. mitotic nuclear division Source: UniProtKB-KW
  11. negative regulation of translational elongation Source: UniProtKB
  12. positive regulation of DNA repair Source: UniProtKB
  13. protein autoubiquitination Source: UniProtKB
  14. protein K48-linked ubiquitination Source: UniProtKB
  15. protein K63-linked ubiquitination Source: UniProtKB
  16. response to ionizing radiation Source: UniProtKB
  17. spermatid development Source: UniProtKB
  18. ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA repair, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF8 (EC:6.3.2.-)
Short name:
hRNF8
Alternative name(s):
RING finger protein 8
Gene namesi
Name:RNF8
Synonyms:KIAA0646
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:10071. RNF8.

Subcellular locationi

Nucleus. Midbody. Chromosometelomere By similarity
Note: Recruited at uncapped telomeres By similarity. Following DNA double-strand breaks, recruited to the sites of damage. During prophase, concomitant with nuclear envelope breakdown, localizes throughout the cell, with a dotted pattern. In telophase, again in the nucleus and also with a discrete dotted pattern in the cytoplasm. In late telophase and during cytokinesis, localizes in the midbody of the tubulin bridge joining the daughter cells. Does not seem to be associated with condensed chromosomes at any time during the cell cycle.8 Publications

GO - Cellular componenti

  1. chromosome, telomeric region Source: UniProtKB
  2. midbody Source: UniProtKB-SubCell
  3. nucleolus Source: HPA
  4. nucleus Source: UniProtKB
  5. site of double-strand break Source: UniProtKB
  6. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi42 – 421R → A: Abolishes interaction with ATM-phosphorylated MDC1. Abolishes interaction with human herpesvirus 1 ICP0. 3 Publications
Mutagenesisi403 – 4031C → S: Marked reduction of E2-dependent ubiquitination of histone H2A. Loss of UBE2E2- and UBE2N-binding. Loss of nuclear localization. 4 Publications
Mutagenesisi405 – 4051I → 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 Publications
Mutagenesisi406 – 4061C → S: Abolishes ubiquitin-ligase activity. 1 Publication
Mutagenesisi443 – 4431D → R: Does not affect the monomeric structure but abolishes ability to monoubiquitinate H2A in nucleosomes. 1 Publication

Organism-specific databases

PharmGKBiPA34445.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485E3 ubiquitin-protein ligase RNF8PRO_0000056048Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei157 – 1571Phosphoserine2 Publications

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.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO76064.
PaxDbiO76064.
PRIDEiO76064.

PTM databases

PhosphoSiteiO76064.

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

ArrayExpressiO76064.
BgeeiO76064.
CleanExiHS_RNF8.
GenevestigatoriO76064.

Organism-specific databases

HPAiHPA050731.

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 (via FHA domain) with phosphorylated human herpesvirus 1 ICP0 protein; leading to RNF8 degradation by the proteasome.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MDC1Q1467611EBI-373337,EBI-495644

Protein-protein interaction databases

BioGridi114492. 43 interactions.
DIPiDIP-31265N.
IntActiO76064. 21 interactions.
MINTiMINT-1459889.
STRINGi9606.ENSP00000362578.

Structurei

Secondary structure

1
485
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 227
Beta strandi29 – 324
Beta strandi38 – 4912
Helixi56 – 583
Beta strandi64 – 685
Beta strandi74 – 785
Beta strandi85 – 873
Beta strandi105 – 1095
Beta strandi119 – 12810
Helixi129 – 1324
Helixi133 – 1353
Helixi351 – 40050
Turni404 – 4063
Beta strandi411 – 4166
Beta strandi421 – 4233
Helixi424 – 4307
Turni431 – 4333
Turni438 – 4403
Beta strandi447 – 4493
Helixi451 – 46111
Helixi466 – 48015

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CSWNMR-A8-139[»]
2PIEX-ray1.35A13-146[»]
4AYCX-ray1.90A/B351-485[»]
4ORHX-ray4.80C/G/H/K/L345-485[»]
ProteinModelPortaliO76064.
SMRiO76064. Positions 13-140, 345-483.

Miscellaneous databases

EvolutionaryTraceiO76064.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 9255FHAAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi276 – 34570Gln-richAdd
BLAST

Domaini

The FHA domain specifically recognizes and binds ATM-phosphorylated MDC1 and 'Thr-4827' phosphorylated HERC2.1 Publication

Sequence similaritiesi

Belongs to the RNF8 family.
Contains 1 FHA domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri403 – 44139RING-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG242257.
HOGENOMiHOG000154169.
HOVERGENiHBG023954.
KOiK10667.
OMAiIHKGDHI.
OrthoDBiEOG75J0N0.
PhylomeDBiO76064.
TreeFamiTF330957.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR017335. E3_Ub_ligase_RNF8.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
PIRSFiPIRSF037950. E3_ubiquit_lig_RNF8. 1 hit.
SMARTiSM00240. FHA. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

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

MGEPGFFVTG DRAGGRSWCL RRVGMSAGWL LLEDGCEVTV GRGFGVTYQL    50
VSKICPLMIS RNHCVLKQNP EGQWTIMDNK SLNGVWLNRA RLEPLRVYSI 100
HQGDYIQLGV PLENKENAEY EYEVTEEDWE TIYPCLSPKN DQMIEKNKEL 150
RTKRKFSLDE LAGPGAEGPS NLKSKINKVS CESGQPVKSQ GKGEVASTPS 200
DNLDPKLTAL EPSKTTGAPI YPGFPKVTEV HHEQKASNSS ASQRSLQMFK 250
VTMSRILRLK IQMQEKHEAV MNVKKQTQKG NSKKVVQMEQ ELQDLQSQLC 300
AEQAQQQARV EQLEKTFQEE EQHLQGLEIA QGEKDLKQQL AQALQEHWAL 350
MEELNRSKKD FEAIIQAKNK ELEQTKEEKE KMQAQKEEVL SHMNDVLENE 400
LQCIICSEYF IEAVTLNCAH SFCSYCINEW MKRKIECPIC RKDIKSKTYS 450
LVLDNCINKM VNNLSSEVKE RRIVLIRERK AKRLF 485
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

Sequence cautioni

The sequence BAA31621.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence EAX03945.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti162 – 1621A → T.
Corresponds to variant rs34338974 [ dbSNP | Ensembl ].
VAR_052096
Natural varianti473 – 4731I → V.
Corresponds to variant rs1139944 [ dbSNP | Ensembl ].
VAR_052097

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei81 – 9818SLNGV…PLRVY → SFPSEKAEDFTAAGERFL in isoform 2. VSP_036671Add
BLAST
Alternative sequencei99 – 485387Missing in isoform 2. VSP_037831Add
BLAST
Alternative sequencei413 – 44836AVTLN…IKSKT → QRDCSEDRALRAFERLPGSA SLRWSGGFSLAVTPLL in isoform 3. VSP_054037Add
BLAST
Alternative sequencei449 – 48537Missing in isoform 3. VSP_054038Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti230 – 2301V → A in BAD96485. 1 Publication
Sequence conflicti334 – 3341K → R in BAD96485. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. Translation: CAB75689.1.
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]
ENST00000394443; ENSP00000377961; ENSG00000112130. [O76064-2]
GeneIDi9025.
KEGGihsa:9025.
UCSCiuc003onq.4. human. [O76064-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. Translation: CAB75689.1 .
CH471081 Genomic DNA. Translation: EAX03944.1 .
CH471081 Genomic DNA. Translation: EAX03945.1 . Sequence problems.
BC007517 mRNA. Translation: AAH07517.1 .
CCDSi CCDS4833.1. [O76064-3 ]
CCDS4834.1. [O76064-1 ]
RefSeqi NP_003949.1. NM_003958.3. [O76064-1 ]
NP_898901.1. NM_183078.2. [O76064-3 ]
UniGenei Hs.485278.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CSW NMR - A 8-139 [» ]
2PIE X-ray 1.35 A 13-146 [» ]
4AYC X-ray 1.90 A/B 351-485 [» ]
4ORH X-ray 4.80 C/G/H/K/L 345-485 [» ]
ProteinModelPortali O76064.
SMRi O76064. Positions 13-140, 345-483.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114492. 43 interactions.
DIPi DIP-31265N.
IntActi O76064. 21 interactions.
MINTi MINT-1459889.
STRINGi 9606.ENSP00000362578.

PTM databases

PhosphoSitei O76064.

Proteomic databases

MaxQBi O76064.
PaxDbi O76064.
PRIDEi O76064.

Protocols and materials databases

DNASUi 9025.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229866 ; ENSP00000229866 ; ENSG00000112130 . [O76064-2 ]
ENST00000373479 ; ENSP00000362578 ; ENSG00000112130 . [O76064-1 ]
ENST00000394443 ; ENSP00000377961 ; ENSG00000112130 . [O76064-2 ]
GeneIDi 9025.
KEGGi hsa:9025.
UCSCi uc003onq.4. human. [O76064-1 ]

Organism-specific databases

CTDi 9025.
GeneCardsi GC06P037321.
HGNCi HGNC:10071. RNF8.
HPAi HPA050731.
MIMi 611685. gene.
neXtProti NX_O76064.
PharmGKBi PA34445.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG242257.
HOGENOMi HOG000154169.
HOVERGENi HBG023954.
KOi K10667.
OMAi IHKGDHI.
OrthoDBi EOG75J0N0.
PhylomeDBi O76064.
TreeFami TF330957.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

EvolutionaryTracei O76064.
GeneWikii RNF8.
GenomeRNAii 9025.
NextBioi 33813.
PROi O76064.
SOURCEi Search...

Gene expression databases

ArrayExpressi O76064.
Bgeei O76064.
CleanExi HS_RNF8.
Genevestigatori O76064.

Family and domain databases

Gene3Di 2.60.200.20. 1 hit.
3.30.40.10. 1 hit.
InterProi IPR017335. E3_Ub_ligase_RNF8.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
Pfami PF00498. FHA. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF037950. E3_ubiquit_lig_RNF8. 1 hit.
SMARTi SM00240. FHA. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
PROSITEi PS50006. FHA_DOMAIN. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, tissue expression, and chromosomal assignment of a novel human gene which encodes a protein with RING finger motif."
    Seki N., Hattori A., Sugano S., Suzuki Y., Nakagawara A., Ohhira M., Muramatsu M., Hori T., Saito T.
    J. Hum. Genet. 43:272-274(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "The RING finger protein RNF8 recruits UBC13 for lysine 63-based self polyubiquitylation."
    Plans V., Scheper J., Soler M., Loukili N., Okano Y., Thomson T.M.
    J. Cell. Biochem. 97:572-582(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH UBE2E2 AND UBE2N, AUTOUBIQUITINATION, MUTAGENESIS OF CYS-403.
    Tissue: Fetal brain.
  3. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Kidney.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hepatoma.
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Muscle.
  10. "N-terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8."
    Ito K., Adachi S., Iwakami R., Yasuda H., Muto Y., Seki N., Okano Y.
    Eur. J. Biochem. 268:2725-2732(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBE2E1; UBE2E2 AND UBE2E3, MUTAGENESIS OF CYS-403.
  11. "The RING finger protein, RNF8, interacts with retinoid X receptor alpha and enhances its transcription-stimulating activity."
    Takano Y., Adachi S., Okuno M., Muto Y., Yoshioka T., Matsushima-Nishiwaki R., Tsurumi H., Ito K., Friedman S.L., Moriwaki H., Kojima S., Okano Y.
    J. Biol. Chem. 279:18926-18934(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RXRA, MUTAGENESIS OF CYS-403.
  12. "RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins."
    Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J., Lukas C., Lukas J.
    Cell 131:887-900(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH MDC1, DOMAIN, MUTAGENESIS OF ARG-42 AND CYS-403.
  13. "Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage."
    Wang B., Elledge S.J.
    Proc. Natl. Acad. Sci. U.S.A. 104:20759-20763(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. Cited for: FUNCTION, INTERACTION WITH MDC1.
  15. "Regulation of mitotic exit by the RNF8 ubiquitin ligase."
    Plans V., Guerra-Rebollo M., Thomson T.M.
    Oncogene 27:1355-1365(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  16. "PCNA is ubiquitinated by RNF8."
    Zhang S., Chea J., Meng X., Zhou Y., Lee E.Y.C., Lee M.Y.W.T.
    Cell Cycle 7:3399-3404(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "RNF8-dependent and RNF8-independent regulation of 53BP1 in response to DNA damage."
    Sakasai R., Tibbetts R.
    J. Biol. Chem. 283:13549-13555(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Noncanonical E2 variant-independent function of UBC13 in promoting checkpoint protein assembly."
    Huen M.S.Y., Huang J., Yuan J., Yamamoto M., Akira S., Ashley C., Xiao W., Chen J.
    Mol. Cell. Biol. 28:6104-6112(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBE2N.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes."
    Bekker-Jensen S., Rendtlew Danielsen J., Fugger K., Gromova I., Nerstedt A., Lukas C., Bartek J., Lukas J., Mailand N.
    Nat. Cell Biol. 12:80-86(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HERC2.
  22. Cited for: FUNCTION.
  23. "RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins."
    Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H., Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J., Lukas J., Lukas C.
    Cell 136:435-446(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "Accumulation of Pax2 transactivation domain interaction protein (PTIP) at sites of DNA breaks via RNF8-dependent pathway is required for cell survival after DNA damage."
    Gong Z., Cho Y.-W., Kim J.-E., Ge K., Chen J.
    J. Biol. Chem. 284:7284-7293(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  25. "Histone ubiquitination associates with BRCA1-dependent DNA damage response."
    Wu J., Huen M.S.Y., Lu L.-Y., Ye L., Dou Y., Ljungman M., Chen J., Yu X.
    Mol. Cell. Biol. 29:849-860(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. "The Rap80-BRCC36 de-ubiquitinating enzyme complex antagonizes RNF8-Ubc13-dependent ubiquitination events at DNA double strand breaks."
    Shao G., Lilli D.R., Patterson-Fortin J., Coleman K.A., Morrissey D.E., Greenberg R.A.
    Proc. Natl. Acad. Sci. U.S.A. 106:3166-3171(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. "ATM-dependent chromatin changes silence transcription in cis to DNA double-strand breaks."
    Shanbhag N.M., Rafalska-Metcalf I.U., Balane-Bolivar C., Janicki S.M., Greenberg R.A.
    Cell 141:970-981(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. "Critical roles of ring finger protein RNF8 in replication stress responses."
    Sy S.M., Jiang J., Dong S.S., Lok G.T., Wu J., Cai H., Yeung E.S., Huang J., Chen J., Deng Y., Huen M.S.
    J. Biol. Chem. 286:22355-22361(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  29. "DNA-damage response and repair activities at uncapped telomeres depend on RNF8."
    Peuscher M.H., Jacobs J.J.
    Nat. Cell Biol. 13:1139-1145(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-42 AND CYS-406.
  30. "RNF8 regulates assembly of RAD51 at DNA double-strand breaks in the absence of BRCA1 and 53BP1."
    Nakada S., Yonamine R.M., Matsuo K.
    Cancer Res. 72:4974-4983(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  31. "RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites."
    Mallette F.A., Mattiroli F., Cui G., Young L.C., Hendzel M.J., Mer G., Sixma T.K., Richard S.
    EMBO J. 31:1865-1878(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF KDM4A, MUTAGENESIS OF ILE-405.
  32. "A new non-catalytic role for ubiquitin ligase RNF8 in unfolding higher-order chromatin structure."
    Luijsterburg M.S., Acs K., Ackermann L., Wiegant W.W., Bekker-Jensen S., Larsen D.H., Khanna K.K., van Attikum H., Mailand N., Dantuma N.P.
    EMBO J. 31:2511-2527(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  33. "Viral E3 ubiquitin ligase-mediated degradation of a cellular E3: viral mimicry of a cellular phosphorylation mark targets the RNF8 FHA domain."
    Chaurushiya M.S., Lilley C.E., Aslanian A., Meisenhelder J., Scott D.C., Landry S., Ticau S., Boutell C., Yates J.R. III, Schulman B.A., Hunter T., Weitzman M.D.
    Mol. Cell 46:79-90(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN HERPESVIRUS 1 ICP0, MUTAGENESIS OF ARG-42.
  34. "A ubiquitin-binding protein, FAAP20, links RNF8-mediated ubiquitination to the Fanconi anemia DNA repair network."
    Yan Z., Guo R., Paramasivam M., Shen W., Ling C., Fox D. III, Wang Y., Oostra A.B., Kuehl J., Lee D.Y., Takata M., Hoatlin M.E., Schindler D., Joenje H., de Winter J.P., Li L., Seidman M.M., Wang W.
    Mol. Cell 47:61-75(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  35. "The E3 ligase RNF8 regulates KU80 removal and NHEJ repair."
    Feng L., Chen J.
    Nat. Struct. Mol. Biol. 19:201-206(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UBE2N.
  36. "Differential regulation of RNF8-mediated Lys48- and Lys63-based poly-ubiquitylation."
    Lok G.T., Sy S.M., Dong S.S., Ching Y.P., Tsao S.W., Thomson T.M., Huen M.S.
    Nucleic Acids Res. 40:196-205(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ILE-405.
  37. "Solution structure of the FHA domain of human ubiquitin ligase protein RNF8."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 8-139.
  38. "RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly."
    Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.
    Cell 131:901-914(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 13-146 IN COMPLEX WITH PHOSPHOPEPTIDE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  39. "RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage signaling."
    Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E., Vermeulen W., Marteijn J.A., Sixma T.K.
    Cell 150:1182-1195(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 351-483 IN COMPLEX WITH ZINC, SUBUNIT, FUNCTION, MUTAGENESIS OF ASP-443.
  40. "Molecular insights into the function of RING Finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation."
    Campbell S.J., Edwards R.A., Leung C.C., Neculai D., Hodge C.D., Dhe-Paganon S., Glover J.N.
    J. Biol. Chem. 287:23900-23910(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS) OF 345-485 IN COMPLEX WITH UBE2N, MUTAGENESIS OF ILE-405.

Entry informationi

Entry nameiRNF8_HUMAN
AccessioniPrimary (citable) accession number: O76064
Secondary accession number(s): A6NN24
, A8MYC0, B4DPG0, Q53H16, Q5NKW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 1, 1998
Last modified: September 3, 2014
This is version 142 of the entry and version 1 of the sequence. [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, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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