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Protein

E3 ubiquitin-protein ligase RNF169

Gene

RNF169

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

Functioni

Probable E3 ubiquitin-protein ligase that acts as a negative regulator of double-strand breaks (DSBs) repair following DNA damage. Recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168 and competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby acting as a negative regulator of DSBs repair. E3 ubiquitin-protein ligase activity is not required for regulation of DSBs repair.3 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 fingeri68 – 10740RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • K63-linked polyubiquitin binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • nucleosome binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • negative regulation of double-strand break repair Source: UniProtKB
  • protein ubiquitination Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF169 (EC:6.3.2.-)
Alternative name(s):
RING finger protein 169
Gene namesi
Name:RNF169
Synonyms:KIAA1991
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:26961. RNF169.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi68 – 681C → S: Does not affect recruitment to DSBs nor ability to inhibit DSBs repair. 1 Publication
Mutagenesisi673 – 6731A → G: Abolishes ubiquitin-binding. 1 Publication
Mutagenesisi689 – 6891R → A: Impairs recruitment to DSBs. 1 Publication
Mutagenesisi691 – 6911K → A: Impairs recruitment to DSBs. 1 Publication
Mutagenesisi697 – 6971Y → A: Impairs recruitment to DSBs. 1 Publication
Mutagenesisi699 – 7002LR → AA: Does not affect ubiquitin-binding but abolishes recruitment to DSBs. 1 Publication

Organism-specific databases

PharmGKBiPA142671054.

Polymorphism and mutation databases

BioMutaiRNF169.
DMDMi110287945.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 708708E3 ubiquitin-protein ligase RNF169PRO_0000245598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei247 – 2471PhosphoserineCombined sources
Modified residuei249 – 2491PhosphoserineCombined sources
Modified residuei403 – 4031PhosphoserineCombined sources
Modified residuei409 – 4091PhosphoserineCombined sources
Modified residuei410 – 4101PhosphothreonineCombined sources
Modified residuei485 – 4851PhosphoserineCombined sources
Modified residuei554 – 5541PhosphothreonineCombined sources
Modified residuei693 – 6931PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8NCN4.
MaxQBiQ8NCN4.
PaxDbiQ8NCN4.
PRIDEiQ8NCN4.

PTM databases

iPTMnetiQ8NCN4.
PhosphoSiteiQ8NCN4.

Expressioni

Gene expression databases

BgeeiQ8NCN4.
CleanExiHS_RNF169.
ExpressionAtlasiQ8NCN4. baseline and differential.
GenevisibleiQ8NCN4. HS.

Organism-specific databases

HPAiHPA046138.
HPA058368.

Interactioni

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi129022. 13 interactions.
IntActiQ8NCN4. 33 interactions.
MINTiMINT-8173825.
STRINGi9606.ENSP00000299563.

Structurei

3D structure databases

ProteinModelPortaliQ8NCN4.
SMRiQ8NCN4. Positions 61-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi205 – 2139UMI motif
Motifi665 – 68218MIU motifAdd
BLAST
Motifi689 – 70113LR motifAdd
BLAST

Domaini

The MIU motif (motif interacting with ubiquitin) mediates the interaction with both 'Lys-48'- and 'Lys-63'-linked ubiquitin chains (PubMed:22733822 and PubMed:22492721). The UMI motif also mediates interaction with ubiquitin. 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).1 Publication

Sequence similaritiesi

Belongs to the RNF169 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri68 – 10740RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IGCB. Eukaryota.
ENOG4111GT3. LUCA.
GeneTreeiENSGT00730000111203.
HOGENOMiHOG000154157.
HOVERGENiHBG093905.
InParanoidiQ8NCN4.
OMAiVDQYLLR.
OrthoDBiEOG75B84Z.
PhylomeDBiQ8NCN4.
TreeFamiTF332796.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8NCN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAGPSTRA SSAAAAAALS RRGRRGRCDE TAAAKTGAPG PASGPSLLVL
60 70 80 90 100
SPPLLQPPLP PRPEESGCAG CLEPPGEAAA LPCGHSLCRG CAQRAADAAG
110 120 130 140 150
PGCPRCRARG PGWARRRARD DGQADSEVLG ECARRSQPER CRPRRDGGAA
160 170 180 190 200
AAGPRPEQEP RAAPAEPDFI FRAPIKLSKP GELREEYESL RKLREEKLQE
210 220 230 240 250
EKPSEDQIHK LLPEDTETGK RKMDEQKKRD EPLVLKTNLE RCPARLSDSE
260 270 280 290 300
NEEPSRGQMT QTHRSAFVSK NNSYSLAFLA GKLNSKVERS QSCSDTAQER
310 320 330 340 350
AKSRVRAVPG NKAKVTTMTP ASNPIIGVLL STQNNRCVSA PDLTIEKRLP
360 370 380 390 400
FSSLSSLASL HKPERSVSPE SNDSISEELN HFKPIVCSPC TPPKRLPDGR
410 420 430 440 450
VLSPLIIKST PRNLNRSLQK QTSYEASPRI LKKWEQIFQE RQIKKTLSKA
460 470 480 490 500
TLTSLAPEMG EELLGSEGIH SSKEKPLVAV NTRLSGGQVL SEYTGPTSAD
510 520 530 540 550
LDHFPSVSQT KAEQDSDNKS STEIPLETCC SSELKGGGSG TSLEREQFEG
560 570 580 590 600
LGSTPDAKLD KTCISRAMKI TTVNSVLPQN SVLGGVLKTK QQLKTLNHFD
610 620 630 640 650
LTNGVLVESL SEEPLPSLRR GRKRHCKTKH LEQNGSLKKL RQTSGEVGLA
660 670 680 690 700
PTDPVLREME QKLQQEEEDR QLALQLQRMF DNERRTVSRR KGSVDQYLLR

SSNMAGAK
Length:708
Mass (Da):77,194
Last modified:July 11, 2006 - v2
Checksum:i95988AC8D440B8AD
GO

Sequence cautioni

The sequence BAC02700.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB082522 mRNA. Translation: BAC02700.1. Different initiation.
BX640750 mRNA. Translation: CAE45858.1.
CCDSiCCDS41691.1.
RefSeqiNP_001092108.1. NM_001098638.1.
UniGeneiHs.370145.
Hs.745050.

Genome annotation databases

EnsembliENST00000299563; ENSP00000299563; ENSG00000166439.
GeneIDi254225.
KEGGihsa:254225.
UCSCiuc001ovl.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB082522 mRNA. Translation: BAC02700.1. Different initiation.
BX640750 mRNA. Translation: CAE45858.1.
CCDSiCCDS41691.1.
RefSeqiNP_001092108.1. NM_001098638.1.
UniGeneiHs.370145.
Hs.745050.

3D structure databases

ProteinModelPortaliQ8NCN4.
SMRiQ8NCN4. Positions 61-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129022. 13 interactions.
IntActiQ8NCN4. 33 interactions.
MINTiMINT-8173825.
STRINGi9606.ENSP00000299563.

PTM databases

iPTMnetiQ8NCN4.
PhosphoSiteiQ8NCN4.

Polymorphism and mutation databases

BioMutaiRNF169.
DMDMi110287945.

Proteomic databases

EPDiQ8NCN4.
MaxQBiQ8NCN4.
PaxDbiQ8NCN4.
PRIDEiQ8NCN4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299563; ENSP00000299563; ENSG00000166439.
GeneIDi254225.
KEGGihsa:254225.
UCSCiuc001ovl.4. human.

Organism-specific databases

CTDi254225.
GeneCardsiRNF169.
HGNCiHGNC:26961. RNF169.
HPAiHPA046138.
HPA058368.
neXtProtiNX_Q8NCN4.
PharmGKBiPA142671054.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGCB. Eukaryota.
ENOG4111GT3. LUCA.
GeneTreeiENSGT00730000111203.
HOGENOMiHOG000154157.
HOVERGENiHBG093905.
InParanoidiQ8NCN4.
OMAiVDQYLLR.
OrthoDBiEOG75B84Z.
PhylomeDBiQ8NCN4.
TreeFamiTF332796.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiRNF169. human.
GenomeRNAii254225.
PROiQ8NCN4.

Gene expression databases

BgeeiQ8NCN4.
CleanExiHS_RNF169.
ExpressionAtlasiQ8NCN4. baseline and differential.
GenevisibleiQ8NCN4. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method."
    Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S., Takahashi Y., Kitajima S., Saga Y., Koseki H.
    DNA Res. 9:47-57(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-708.
    Tissue: Uterus.
  3. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-249; THR-554 AND SER-693, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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-403 AND THR-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403; SER-409 AND THR-410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Ring finger protein RNF169 antagonises the ubiquitin-dependent signaling cascade at sites of DNA Damage."
    Chen J., Feng W., Jiang J., Deng Y., Huen M.S.
    J. Biol. Chem. 287:27715-27722(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MIU MOTIF, UBIQUITIN-BINDING, SUBCELLULAR LOCATION.
  9. "Human RNF169 is a negative regulator of the ubiquitin-dependent response to DNA double-strand breaks."
    Poulsen M., Lukas C., Lukas J., Bekker-Jensen S., Mailand N.
    J. Cell Biol. 197:189-199(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MIU MOTIF, UBIQUITIN-BINDING, SUBCELLULAR LOCATION.
  10. "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 CYS-68; ALA-673; ARG-689; LYS-691; TYR-697 AND 699-LEU-ARG-700.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRN169_HUMAN
AccessioniPrimary (citable) accession number: Q8NCN4
Secondary accession number(s): Q6N015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 11, 2006
Last modified: June 8, 2016
This is version 107 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.