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E3 ubiquitin-protein ligase RNF8 (EC 2.3.2.27) (ActA-interacting protein 37) (AIP37) (LaXp180) (RING finger protein 8) (RING-type E3 ubiquitin transferase RNF8)

 RNF8_MOUSE              Reviewed;         488 AA.
Q8VC56; Q4FJV7; Q9JK13;
06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
10-OCT-2018, entry version 138.
RecName: Full=E3 ubiquitin-protein ligase RNF8 {ECO:0000255|HAMAP-Rule:MF_03067};
EC=2.3.2.27 {ECO:0000255|HAMAP-Rule:MF_03067};
AltName: Full=ActA-interacting protein 37;
Short=AIP37;
AltName: Full=LaXp180;
AltName: Full=RING finger protein 8 {ECO:0000255|HAMAP-Rule:MF_03067};
AltName: Full=RING-type E3 ubiquitin transferase RNF8 {ECO:0000255|HAMAP-Rule:MF_03067};
Name=Rnf8 {ECO:0000255|HAMAP-Rule:MF_03067};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Extraembryonic tissue, Liver, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
Mollenhauer J., Wiemann S., Schick M., Korn B.;
"Cloning of mouse full open reading frames in Gateway(R) system entry
vector (pDONR201).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-283, AND INTERACTION WITH ACTA
(MICROBIAL INFECTION).
STRAIN=CD-1; TISSUE=Embryo;
PubMed=11207567; DOI=10.1046/j.1462-5822.2000.00034.x;
Pfeuffer T., Goebel W., Laubinger J., Bachmann M., Kuhn M.;
"LaXp180, a mammalian ActA-binding protein, identified with the yeast
two-hybrid system co-localizes with intracellular Listeria
monocytogenes.";
Cell. Microbiol. 2:101-114(2000).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20153262; DOI=10.1016/j.devcel.2010.01.010;
Lu L.Y., Wu J., Ye L., Gavrilina G.B., Saunders T.L., Yu X.;
"RNF8-dependent histone modifications regulate nucleosome removal
during spermatogenesis.";
Dev. Cell 18:371-384(2010).
[6]
FUNCTION.
PubMed=20080757; DOI=10.1073/pnas.0913790107;
Ramachandran S., Chahwan R., Nepal R.M., Frieder D., Panier S.,
Roa S., Zaheen A., Durocher D., Scharff M.D., Martin A.;
"The RNF8/RNF168 ubiquitin ligase cascade facilitates class switch
recombination.";
Proc. Natl. Acad. Sci. U.S.A. 107:809-814(2010).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21706008; DOI=10.1038/nsmb.2078;
Wu J., Chen Y., Lu L.Y., Wu Y., Paulsen M.T., Ljungman M.,
Ferguson D.O., Yu X.;
"Chfr and RNF8 synergistically regulate ATM activation.";
Nat. Struct. Mol. Biol. 18:761-768(2011).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21857671; DOI=10.1038/ncb2326;
Peuscher M.H., Jacobs J.J.;
"DNA-damage response and repair activities at uncapped telomeres
depend on RNF8.";
Nat. Cell Biol. 13:1139-1145(2011).
[9]
SUBCELLULAR LOCATION.
PubMed=22101936; DOI=10.1038/nsmb.2172;
Rai R., Li J.M., Zheng H., Lok G.T., Deng Y., Huen M.S., Chen J.,
Jin J., Chang S.;
"The E3 ubiquitin ligase Rnf8 stabilizes Tpp1 to promote telomere end
protection.";
Nat. Struct. Mol. Biol. 18:1400-1407(2011).
[10]
FUNCTION.
PubMed=22266820; DOI=10.1038/nsmb.2211;
Feng L., Chen J.;
"The E3 ligase RNF8 regulates KU80 removal and NHEJ repair.";
Nat. Struct. Mol. Biol. 19:201-206(2012).
[11]
FUNCTION.
PubMed=24953653; DOI=10.1016/j.celrep.2014.05.041;
Cardamone M.D., Tanasa B., Chan M., Cederquist C.T., Andricovich J.,
Rosenfeld M.G., Perissi V.;
"GPS2/KDM4A pioneering activity regulates promoter-specific
recruitment of PPARgamma.";
Cell Rep. 8:163-176(2014).
[12]
SUBCELLULAR LOCATION, INTERACTION WITH PIWIL1, AND MUTAGENESIS OF
68-GLN--GLY-72.
PubMed=28552346; DOI=10.1016/j.cell.2017.04.034;
Gou L.T., Kang J.Y., Dai P., Wang X., Li F., Zhao S., Zhang M.,
Hua M.M., Lu Y., Zhu Y., Li Z., Chen H., Wu L.G., Li D., Fu X.D.,
Li J., Shi H.J., Liu M.F.;
"Ubiquitination-deficient mutations in human Piwi cause male
infertility by impairing histone-to-protamine exchange during
spermiogenesis.";
Cell 169:1090-1104(2017).
-!- FUNCTION: 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 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. 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. 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 (PubMed:20153262,
PubMed:28552346). 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.
{ECO:0000255|HAMAP-Rule:MF_03067, ECO:0000269|PubMed:20080757,
ECO:0000269|PubMed:20153262, ECO:0000269|PubMed:21706008,
ECO:0000269|PubMed:21857671, ECO:0000269|PubMed:22266820,
ECO:0000269|PubMed:24953653, ECO:0000269|PubMed:28552346}.
-!- CATALYTIC ACTIVITY: 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. {ECO:0000255|HAMAP-Rule:MF_03067}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|HAMAP-Rule:MF_03067}.
-!- SUBUNIT: 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-4829' phosphorylated HERC2 (via C-terminus) (By
similarity). Interacts with PIWIL1; leading to sequester RNF8 in
the cytoplasm (PubMed:28552346). Interacts with WRAP53/TCAB1 (By
similarity). {ECO:0000255|HAMAP-Rule:MF_03067,
ECO:0000269|PubMed:28552346}.
-!- SUBUNIT: (Microbial infection) May interact with the
L.monocytogenes protein actA; however, given these errors in the
sequence (AJ242721), the relevance of the interaction with actA
remains to be confirmed. {ECO:0000269|PubMed:11207567}.
-!- INTERACTION:
Q96AP0:ACD (xeno); NbExp=2; IntAct=EBI-15954293, EBI-717666;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03067,
ECO:0000269|PubMed:28552346}. Cytoplasm {ECO:0000255|HAMAP-
Rule:MF_03067, ECO:0000269|PubMed:28552346}. Midbody
{ECO:0000255|HAMAP-Rule:MF_03067}. Chromosome, telomere
{ECO:0000255|HAMAP-Rule:MF_03067, ECO:0000269|PubMed:21857671,
ECO:0000269|PubMed:22101936}. Note=Recruited at uncapped telomeres
(PubMed:21857671, PubMed:22101936). 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 (By similarity). During spermatogenesis, sequestered in
the cytoplasm by PIWIL1: RNF8 is released following ubiquitination
and degradation of PIWIL1 (PubMed:28552346). {ECO:0000255|HAMAP-
Rule:MF_03067, ECO:0000269|PubMed:21857671,
ECO:0000269|PubMed:22101936, ECO:0000269|PubMed:28552346}.
-!- DOMAIN: The FHA domain specifically recognizes and binds ATM-
phosphorylated MDC1 and phosphorylated HERC2 (By similarity). This
domain is also required for proper recruitment to DNA damage sites
after UV irradiation, ionizing radiation, or treatment with an
alkylating agent (By similarity). {ECO:0000250|UniProtKB:O76064,
ECO:0000255|HAMAP-Rule:MF_03067}.
-!- PTM: 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. {ECO:0000255|HAMAP-
Rule:MF_03067}.
-!- DISRUPTION PHENOTYPE: Male mice are infertile, while females do
not show defects. Male mice display defects in histone H2A and H2B
ubiquitination in testis cells. While meiotic sex chromosome
inactivation in the XY body prior to meiosis is not affected,
H4K16ac is decreased, leading to defects in the replacement of
histones by protamines during spermiogenesis. Mice lacking both
Rnf8 and Chfr develop thymic lymphomas and chromosomes are
frequently altered, due to defects in DNA damage response and
defects in damage-induced activation of ATM kinase.
{ECO:0000269|PubMed:20153262, ECO:0000269|PubMed:21706008}.
-!- SIMILARITY: Belongs to the RNF8 family. {ECO:0000255|HAMAP-
Rule:MF_03067}.
-!- CAUTION: The precise role of Rnf8 at telomeres is subject to
debate. 2 publications reported recruitment of Rnf8 at uncapped
telomeres followed by regulation of non-homologous end joining
(NHEJ), however the 2 publications reported different data and
conclusions. According to a report, Rnf8 promotes telomere end
protection and inhibits NHEJ by mediating ubiquitination via 'Lys-
63'-linked ubiquitin and stabilization of Tpp1 at uncapped
telomeres (PubMed:22101936). According to another report, Rnf8
recruitment at uncapped telomeres leads to promote NHEJ and the
joining of deprotected chromosome ends by inducing H2A
ubiquitination and TP53BP1 recruitment, suggesting that Rnf8 may
have a detrimental role in case of telomeric crisis and enhance
cancer development by aggravating telomere-induced genome
instability (PubMed:21857671). {ECO:0000305|PubMed:21857671,
ECO:0000305|PubMed:22101936}.
-!- 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. 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). 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. Additional evidences are however required to
confirm these data. {ECO:0000255|HAMAP-Rule:MF_03067}.
-!- SEQUENCE CAUTION:
Sequence=CAB92239.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAB92239.1; Type=Frameshift; Positions=219, 266, 283; Evidence={ECO:0000305};
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EMBL; AK076180; BAC36236.1; -; mRNA.
EMBL; AK147168; BAE27732.1; -; mRNA.
EMBL; CT010295; CAJ18503.1; -; mRNA.
EMBL; BC021778; AAH21778.1; -; mRNA.
EMBL; AJ242721; CAB92239.1; ALT_FRAME; mRNA.
CCDS; CCDS37538.1; -.
RefSeq; NP_067394.1; NM_021419.2.
UniGene; Mm.305994; -.
ProteinModelPortal; Q8VC56; -.
SMR; Q8VC56; -.
BioGrid; 208404; 6.
DIP; DIP-59448N; -.
IntAct; Q8VC56; 1.
STRING; 10090.ENSMUSP00000024817; -.
iPTMnet; Q8VC56; -.
PhosphoSitePlus; Q8VC56; -.
MaxQB; Q8VC56; -.
PaxDb; Q8VC56; -.
PRIDE; Q8VC56; -.
Ensembl; ENSMUST00000024817; ENSMUSP00000024817; ENSMUSG00000090083.
GeneID; 58230; -.
KEGG; mmu:58230; -.
UCSC; uc008btf.1; mouse.
CTD; 9025; -.
MGI; MGI:1929069; Rnf8.
eggNOG; ENOG410INBI; Eukaryota.
eggNOG; ENOG410Z9IW; LUCA.
GeneTree; ENSGT00400000022349; -.
HOGENOM; HOG000154169; -.
HOVERGEN; HBG023954; -.
InParanoid; Q8VC56; -.
KO; K10667; -.
OrthoDB; EOG091G0I40; -.
TreeFam; TF330957; -.
Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
UniPathway; UPA00143; -.
PRO; PR:Q8VC56; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000090083; Expressed in 295 organ(s), highest expression level in primary oocyte.
CleanEx; MM_RNF8; -.
ExpressionAtlas; Q8VC56; baseline and differential.
Genevisible; Q8VC56; MM.
GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0042393; F:histone binding; IMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IEA:UniProtKB-UniRule.
GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
GO; GO:0043486; P:histone exchange; IMP:UniProtKB.
GO; GO:0070535; P:histone H2A K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:0033522; P:histone H2A ubiquitination; IMP:UniProtKB.
GO; GO:0033523; P:histone H2B ubiquitination; IMP:UniProtKB.
GO; GO:0045190; P:isotype switching; IMP:UniProtKB.
GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
GO; GO:0007286; P:spermatid development; IMP:UniProtKB.
GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IMP:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
CDD; cd00060; FHA; 1.
Gene3D; 3.30.40.10; -; 1.
HAMAP; MF_03067; RNF8; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR017335; RNF8.
InterPro; IPR008984; SMAD_FHA_dom_sf.
InterPro; IPR018957; Znf_C3HC4_RING-type.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00498; FHA; 1.
Pfam; PF00097; zf-C3HC4; 1.
PIRSF; PIRSF037950; E3_ubiquit_lig_RNF8; 1.
SMART; SM00240; FHA; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Chromatin regulator; Chromosome;
Complete proteome; Cytoplasm; DNA damage; DNA repair; Metal-binding;
Mitosis; Nucleus; Phosphoprotein; Reference proteome; Telomere;
Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 488 E3 ubiquitin-protein ligase RNF8.
/FTId=PRO_0000056049.
DOMAIN 38 92 FHA. {ECO:0000255|HAMAP-Rule:MF_03067}.
ZN_FING 406 444 RING-type. {ECO:0000255|HAMAP-
Rule:MF_03067}.
REGION 68 72 Required for interaction with PIWIL1.
{ECO:0000255|HAMAP-Rule:MF_03067,
ECO:0000269|PubMed:28552346}.
COMPBIAS 299 351 Gln-rich.
MOD_RES 157 157 Phosphoserine.
{ECO:0000250|UniProtKB:O76064}.
MUTAGEN 68 72 QNPEG->AAAAA: Abolishes interaction with
PIWIL1. {ECO:0000269|PubMed:28552346}.
SEQUENCE 488 AA; 55517 MW; 428242204EBC44A1 CRC64;
MGEPDPLVSG QLAARRSWCL RRLGMDCEWL QLEAGTEVTI GRGLSVTYQL ISKVCPLMIS
RSHCVLKQNP EGQWTIMDNK SLNGVWLNRE RLAPLQGYCI RKGDHIQLGV PLESRETAEY
EYEVIEEDWE SLAPCLAPKN DQRMEKHKGS RTKRKFSSPG LENLPAEGSS DLRCPLANVA
SKPIEPEKLH GKGDASSQSL GCLCPGLTSL KASERAAGPH ACSALPKVLE LSCPKKQKAC
RPSASQNSLE LFKVTMSRML KLKTQMQEKQ IAVLNVKRQT RKGSSKKIVR MEKELRNLQS
QLYAEQAQQQ ARVEQLEKTF QEEAHYLQGL EKEQGECDLK QQLVQALQEH QALMEELNCS
KKDFEKIIQA KNKELEQTKE EKDKVQAQKE EVLSHMNDLL ENELQCIICS EYFIEAVTLN
CAHSFCSFCI NEWMKRKVEC PICRKDIESR TNSLVLDNCI SKMVDNLSSD VKERRSVLIR
ERRAKRLS


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