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Protein

E3 ubiquitin-protein ligase RNF168

Gene

RNF168

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent histone ubiquitination. Recruited to sites of DNA damage at double-strand breaks (DSBs) by binding to ubiquitinated histone H2A and H2AX and amplifies the RNF8-dependent H2A ubiquitination, promoting the formation of 'Lys-63'-linked ubiquitin conjugates. This leads to concentrate ubiquitinated histones H2A and H2AX at DNA lesions to the threshold required for recruitment of TP53BP1 and BRCA1. Also recruited at DNA interstrand cross-links (ICLs) sites and promotes accumulation of '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. Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. Following DNA damage, promotes the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF8, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites. Not able to initiate 'Lys-63'-linked ubiquitination in vitro; possibly due to partial occlusion of the UBE2N/UBC13-binding region. Catalyzes monoubiquitination of 'Lys-13' and 'Lys-15' of nucleosomal histone H2A (H2AK13Ub and H2AK15Ub, respectively).8 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 5540RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • K63-linked polyubiquitin binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • nucleosome binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • double-strand break repair Source: UniProtKB
  • double-strand break repair via nonhomologous end joining Source: Reactome
  • histone H2A-K13 ubiquitination Source: UniProtKB
  • histone H2A-K15 ubiquitination Source: UniProtKB
  • histone H2A K63-linked ubiquitination Source: UniProtKB
  • histone H2A monoubiquitination Source: UniProtKB
  • interstrand cross-link repair Source: UniProtKB
  • isotype switching Source: UniProtKB
  • negative regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of DNA repair Source: UniProtKB
  • protein K63-linked ubiquitination Source: UniProtKB
  • protein sumoylation Source: Reactome
  • protein ubiquitination Source: UniProtKB
  • response to ionizing radiation Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
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.
SIGNORiQ8IYW5.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF168 (EC:6.3.2.-)
Short name:
hRNF168
Alternative name(s):
RING finger protein 168
Gene namesi
Name:RNF168
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:26661. RNF168.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • protein complex Source: MGI
  • site of double-strand break Source: UniProtKB
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Riddle syndrome (RIDDLES)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized by increased radiosensitivity, immunodeficiency, mild motor control and learning difficulties, facial dysmorphism, and short stature. Defects are probably due to impaired localization of TP53BP1 and BRCA1 at DNA lesions.
See also OMIM:611943

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161C → S: Does not affect ability to bind ubiquitin and localization to DSBs sites, while it abolishes E3 ligase activity; when associated with S-19. 1 Publication
Mutagenesisi18 – 181I → A: Abolishes ability to ubiquitinate KDM4A. 1 Publication
Mutagenesisi19 – 191C → S: Does not affect ability to bind ubiquitin and localization to DSBs sites, while it abolishes E3 ligase activity; when associated with S-16. 1 Publication
Mutagenesisi57 – 571R → D: Does not affect the monomeric structure but abolishes ability to monoubiquitinate H2A in nucleosomes. 1 Publication
Mutagenesisi149 – 1502LL → AA: Impaired ability to bind ubiquitin. 1 Publication
Mutagenesisi179 – 1791A → G: Impairs ability to form foci following ionizing radiation and impaired binding to 'Lys-63'-linked ubiquitin. 3 Publications
Mutagenesisi450 – 4501A → G: Still able to bind 'Lys-63'-linked ubiquitin. 3 Publications
Mutagenesisi476 – 4772LR → AA: Does not affect ubiquitin-binding but impairs recruitment to DSBs. 1 Publication

Organism-specific databases

MalaCardsiRNF168.
MIMi611943. phenotype.
PharmGKBiPA134945219.

Polymorphism and mutation databases

BioMutaiRNF168.
DMDMi74762499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 571571E3 ubiquitin-protein ligase RNF168PRO_0000245596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701PhosphoserineBy similarity
Modified residuei134 – 1341PhosphoserineCombined sources
Modified residuei197 – 1971PhosphoserineBy similarity
Modified residuei362 – 3621PhosphothreonineBy similarity
Modified residuei411 – 4111PhosphoserineCombined sources
Modified residuei414 – 4141PhosphoserineCombined sources
Modified residuei415 – 4151PhosphoserineCombined sources
Modified residuei470 – 4701PhosphoserineCombined sources

Post-translational modificationi

Sumoylated with SUMO1 by PIAS4 in response to double-strand breaks (DSBs).1 Publication
Ubiquitinated.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8IYW5.
MaxQBiQ8IYW5.
PaxDbiQ8IYW5.
PeptideAtlasiQ8IYW5.
PRIDEiQ8IYW5.

PTM databases

iPTMnetiQ8IYW5.
PhosphoSiteiQ8IYW5.

Expressioni

Gene expression databases

BgeeiQ8IYW5.
CleanExiHS_RNF168.
ExpressionAtlasiQ8IYW5. baseline and differential.
GenevisibleiQ8IYW5. HS.

Interactioni

Subunit structurei

Monomer. Interacts with UBE2N/UBC13.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UBE2NP610882EBI-914207,EBI-1052908

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • K63-linked polyubiquitin binding Source: UniProtKB
  • nucleosome binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi127922. 42 interactions.
DIPiDIP-37451N.
IntActiQ8IYW5. 19 interactions.
MINTiMINT-1180501.
STRINGi9606.ENSP00000320898.

Structurei

Secondary structure

1
571
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 144Combined sources
Turni17 – 193Combined sources
Beta strandi24 – 285Combined sources
Beta strandi34 – 363Combined sources
Helixi37 – 437Combined sources
Turni44 – 485Combined sources
Turni52 – 543Combined sources
Helixi59 – 679Combined sources
Helixi74 – 8310Combined sources
Helixi85 – 939Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L11X-ray2.12A1-113[»]
4GB0X-ray2.60A1-111[»]
ProteinModelPortaliQ8IYW5.
SMRiQ8IYW5. Positions 3-93.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IYW5.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi110 – 12819LR motif 1Add
BLAST
Motifi143 – 1519UMI motif
Motifi168 – 19124MIU motif 1Add
BLAST
Motifi439 – 46224MIU motif 2Add
BLAST
Motifi466 – 47712LR motif 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi115 – 17763Glu-richAdd
BLAST

Domaini

The MIU motif (motif interacting with ubiquitin) mediates the interaction with both 'Lys-48'- and 'Lys-63'-linked ubiquitin chains (PubMed:19500350). The UMI motif mediates interaction with ubiquitin with a preference for 'Lys-63'-linked ubiquitin (PubMed:21041483). The specificity for different types of ubiquitin is mediated by juxtaposition of ubiquitin-binding motifs (MIU and UMI motifs) with LR motifs (LRMs) (PubMed:22742833).3 Publications

Sequence similaritiesi

Belongs to the RNF168 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri16 – 5540RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4159. Eukaryota.
COG2802. LUCA.
GeneTreeiENSGT00730000111120.
HOGENOMiHOG000154156.
HOVERGENiHBG067220.
InParanoidiQ8IYW5.
OMAiHKQEEQD.
OrthoDBiEOG7XDBG8.
PhylomeDBiQ8IYW5.
TreeFamiTF332796.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8IYW5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPKDAIPS LSECQCGICM EILVEPVTLP CNHTLCKPCF QSTVEKASLC
60 70 80 90 100
CPFCRRRVSS WTRYHTRRNS LVNVELWTII QKHYPRECKL RASGQESEEV
110 120 130 140 150
ADDYQPVRLL SKPGELRREY EEEISKVAAE RRASEEEENK ASEEYIQRLL
160 170 180 190 200
AEEEEEEKRQ AEKRRRAMEE QLKSDEELAR KLSIDINNFC EGSISASPLN
210 220 230 240 250
SRKSDPVTPK SEKKSKNKQR NTGDIQKYLT PKSQFGSASH SEAVQEVRKD
260 270 280 290 300
SVSKDIDSSD RKSPTGQDTE IEDMPTLSPQ ISLGVGEQGA DSSIESPMPW
310 320 330 340 350
LCACGAEWYH EGNVKTRPSN HGKELCVLSH ERPKTRVPYS KETAVMPCGR
360 370 380 390 400
TESGCAPTSG VTQTNGNNTG ETENEESCLL ISKEISKRKN QESSFEAVKD
410 420 430 440 450
PCFSAKRRKV SPESSPDQEE TEINFTQKLI DLEHLLFERH KQEEQDRLLA
460 470 480 490 500
LQLQKEVDKE QMVPNRQKGS PDEYHLRATS SPPDKVLNGQ RKNPKDGNFK
510 520 530 540 550
RQTHTKHPTP ERGSRDKNRQ VSLKMQLKQS VNRRKMPNST RDHCKVSKSA
560 570
HSLQPSISQK SVFQMFQRCT K
Length:571
Mass (Da):65,020
Last modified:March 1, 2003 - v1
Checksum:i51E16DA92BA654C1
GO

Sequence cautioni

The sequence BAC04060.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91P → L in BAB70801 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti387 – 3871K → R.
Corresponds to variant rs35774921 [ dbSNP | Ensembl ].
VAR_034466
Natural varianti401 – 4011P → Q.1 Publication
Corresponds to variant rs3796129 [ dbSNP | Ensembl ].
VAR_026997
Natural varianti413 – 4131E → K.
Corresponds to variant rs6790173 [ dbSNP | Ensembl ].
VAR_052110

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK054732 mRNA. Translation: BAB70801.1.
AK093113 mRNA. Translation: BAC04060.1. Different initiation.
AC092933 Genomic DNA. No translation available.
AC117490 Genomic DNA. No translation available.
BC033791 mRNA. Translation: AAH33791.1.
CCDSiCCDS3317.1.
RefSeqiNP_689830.2. NM_152617.3.
UniGeneiHs.250648.

Genome annotation databases

EnsembliENST00000318037; ENSP00000320898; ENSG00000163961.
GeneIDi165918.
KEGGihsa:165918.
UCSCiuc003fwq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK054732 mRNA. Translation: BAB70801.1.
AK093113 mRNA. Translation: BAC04060.1. Different initiation.
AC092933 Genomic DNA. No translation available.
AC117490 Genomic DNA. No translation available.
BC033791 mRNA. Translation: AAH33791.1.
CCDSiCCDS3317.1.
RefSeqiNP_689830.2. NM_152617.3.
UniGeneiHs.250648.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L11X-ray2.12A1-113[»]
4GB0X-ray2.60A1-111[»]
ProteinModelPortaliQ8IYW5.
SMRiQ8IYW5. Positions 3-93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127922. 42 interactions.
DIPiDIP-37451N.
IntActiQ8IYW5. 19 interactions.
MINTiMINT-1180501.
STRINGi9606.ENSP00000320898.

PTM databases

iPTMnetiQ8IYW5.
PhosphoSiteiQ8IYW5.

Polymorphism and mutation databases

BioMutaiRNF168.
DMDMi74762499.

Proteomic databases

EPDiQ8IYW5.
MaxQBiQ8IYW5.
PaxDbiQ8IYW5.
PeptideAtlasiQ8IYW5.
PRIDEiQ8IYW5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318037; ENSP00000320898; ENSG00000163961.
GeneIDi165918.
KEGGihsa:165918.
UCSCiuc003fwq.4. human.

Organism-specific databases

CTDi165918.
GeneCardsiRNF168.
HGNCiHGNC:26661. RNF168.
MalaCardsiRNF168.
MIMi611943. phenotype.
612688. gene.
neXtProtiNX_Q8IYW5.
PharmGKBiPA134945219.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4159. Eukaryota.
COG2802. LUCA.
GeneTreeiENSGT00730000111120.
HOGENOMiHOG000154156.
HOVERGENiHBG067220.
InParanoidiQ8IYW5.
OMAiHKQEEQD.
OrthoDBiEOG7XDBG8.
PhylomeDBiQ8IYW5.
TreeFamiTF332796.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
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.
SIGNORiQ8IYW5.

Miscellaneous databases

ChiTaRSiRNF168. human.
EvolutionaryTraceiQ8IYW5.
GenomeRNAii165918.
PROiQ8IYW5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IYW5.
CleanExiHS_RNF168.
ExpressionAtlasiQ8IYW5. baseline and differential.
GenevisibleiQ8IYW5. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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], VARIANT GLN-401.
    Tissue: Cerebellum and Testis.
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-414 AND SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "RNF168, a new RING finger, MIU-containing protein that modifies chromatin by ubiquitination of histones H2A and H2AX."
    Pinato S., Scandiuzzi C., Arnaudo N., Citterio E., Gaudino G., Penengo L.
    BMC Mol. Biol. 10:55-55(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITIN-BINDING, MIU MOTIF, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF CYS-16; CYS-19; ALA-179 AND ALA-450.
  6. Cited for: INVOLVEMENT IN RIDDLES, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH UBE2N, MUTAGENESIS OF ALA-179 AND ALA-450.
  7. "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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
  8. "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-411; SER-414 AND SER-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. "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.
  10. "UMI, a novel RNF168 ubiquitin binding domain involved in the DNA damage signaling pathway."
    Pinato S., Gatti M., Scandiuzzi C., Confalonieri S., Penengo L.
    Mol. Cell. Biol. 31:118-126(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITIN-BINDING, UMI MOTIF, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF 149-LEU-LEU-150; ALA-179 AND ALA-450.
  11. "A novel ubiquitin mark at the N-terminal tail of histone H2As targeted by RNF168 ubiquitin ligase."
    Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L.
    Cell Cycle 11:2538-2544(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "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-18.
  13. "DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger."
    Danielsen J.R., Povlsen L.K., Villumsen B.H., Streicher W., Nilsson J., Wikstrom M., Bekker-Jensen S., Mailand N.
    J. Cell Biol. 197:179-187(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION.
  14. "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.
  15. "Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks."
    Panier S., Ichijima Y., Fradet-Turcotte A., Leung C.C., Kaustov L., Arrowsmith C.H., Durocher D.
    Mol. Cell 47:383-395(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITIN-BINDING, LR MOTIF, SUBCELLULAR LOCATION, MUTAGENESIS OF 476-LEU-ARG-477.
  16. "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: FUNCTION, MUTAGENESIS OF ARG-57.
  17. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-411 AND SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  18. "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 (2.12 ANGSTROMS) OF 1-113, SUBUNIT.

Entry informationi

Entry nameiRN168_HUMAN
AccessioniPrimary (citable) accession number: Q8IYW5
Secondary accession number(s): Q8NA67, Q96NS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 129 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

Caution

According to a well-established model, RNF168 cannot initiate H2A 'Lys-63'-linked ubiquitination and is recruited following RNF8-dependent histone ubiquitination to amplify H2A 'Lys-63'-linked ubiquitination (PubMed:19500350, 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.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.