CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017622
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF169 
Protein Synonyms/Alias
 RING finger protein 169 
Gene Name
 RNF169 
Gene Synonyms/Alias
 KIAA1991 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
236RDEPLVLKTNLERCPubiquitination[1]
282SLAFLAGKLNSKVERubiquitination[1, 2, 3]
347APDLTIEKRLPFSSLubiquitination[1]
473SEGIHSSKEKPLVAVubiquitination[1]
475GIHSSKEKPLVAVNTubiquitination[1]
535TCCSSELKGGGSGTSubiquitination[1]
569TCISRAMKITTVNSVubiquitination[1]
590LGGVLKTKQQLKTLNubiquitination[1]
691RRTVSRRKGSVDQYLubiquitination[1, 2, 3, 4, 5]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 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. 
Sequence Annotation
 ZN_FING 68 107 RING-type.
 MOTIF 205 213 UMI motif.
 MOTIF 665 682 MIU motif.
 MOTIF 689 701 LR motif.
 MOD_RES 247 247 Phosphoserine.
 MOD_RES 249 249 Phosphoserine.
 MOD_RES 403 403 Phosphoserine.
 MOD_RES 409 409 Phosphoserine.
 MOD_RES 410 410 Phosphothreonine.
 MOD_RES 485 485 Phosphoserine.
 MOD_RES 554 554 Phosphothreonine.
 MOD_RES 693 693 Phosphoserine.  
Keyword
 Complete proteome; DNA damage; Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 708 AA 
Protein Sequence
MAAAGPSTRA SSAAAAAALS RRGRRGRCDE TAAAKTGAPG PASGPSLLVL SPPLLQPPLP 60
PRPEESGCAG CLEPPGEAAA LPCGHSLCRG CAQRAADAAG PGCPRCRARG PGWARRRARD 120
DGQADSEVLG ECARRSQPER CRPRRDGGAA AAGPRPEQEP RAAPAEPDFI FRAPIKLSKP 180
GELREEYESL RKLREEKLQE EKPSEDQIHK LLPEDTETGK RKMDEQKKRD EPLVLKTNLE 240
RCPARLSDSE NEEPSRGQMT QTHRSAFVSK NNSYSLAFLA GKLNSKVERS QSCSDTAQER 300
AKSRVRAVPG NKAKVTTMTP ASNPIIGVLL STQNNRCVSA PDLTIEKRLP FSSLSSLASL 360
HKPERSVSPE SNDSISEELN HFKPIVCSPC TPPKRLPDGR VLSPLIIKST PRNLNRSLQK 420
QTSYEASPRI LKKWEQIFQE RQIKKTLSKA TLTSLAPEMG EELLGSEGIH SSKEKPLVAV 480
NTRLSGGQVL SEYTGPTSAD LDHFPSVSQT KAEQDSDNKS STEIPLETCC SSELKGGGSG 540
TSLEREQFEG LGSTPDAKLD KTCISRAMKI TTVNSVLPQN SVLGGVLKTK QQLKTLNHFD 600
LTNGVLVESL SEEPLPSLRR GRKRHCKTKH LEQNGSLKKL RQTSGEVGLA PTDPVLREME 660
QKLQQEEEDR QLALQLQRMF DNERRTVSRR KGSVDQYLLR SSNMAGAK 708 
Gene Ontology
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0035861; C:site of double-strand break; IDA:UniProtKB.
 GO:0070530; F:K63-linked polyubiquitin binding; IDA:UniProtKB.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0031491; F:nucleosome binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:2000780; P:negative regulation of double-strand break repair; IDA:UniProtKB.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
 GO:0006974; P:response to DNA damage stimulus; IDA:UniProtKB. 
Interpro
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
  
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS