CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022260
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase RNF216 
Protein Synonyms/Alias
 RING finger protein 216; Triad domain-containing protein 3; Ubiquitin-conjugating enzyme 7-interacting protein 1; Zinc finger protein inhibiting NF-kappa-B 
Gene Name
 RNF216 
Gene Synonyms/Alias
 TRIAD3; UBCE7IP1; ZIN 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
100GQTEREPKPGPSHNQubiquitination[1]
351LASQDETKLPKIDFFubiquitination[1, 2, 3, 4, 5, 6, 7]
354QDETKLPKIDFFDYSubiquitination[5]
362IDFFDYSKLTPLDQRubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
391VLSSQDIKWALHELKubiquitination[1, 2, 5, 6, 7, 9]
398KWALHELKGHYAITRubiquitination[2, 5]
406GHYAITRKALSDAIKubiquitination[5]
413KALSDAIKKWQELSPubiquitination[5]
414ALSDAIKKWQELSPEubiquitination[5]
425LSPETSGKRKKRKQMacetylation[10]
425LSPETSGKRKKRKQMubiquitination[1, 3, 4, 5, 6]
427PETSGKRKKRKQMNQubiquitination[5]
430SGKRKKRKQMNQYSYubiquitination[5]
448KFEQGDIKIEKRMFFubiquitination[5, 8, 9]
459RMFFLENKRRHCRSYubiquitination[2, 5]
485EQEFYEQKIKEMAEHubiquitination[1, 4, 5, 6]
487EFYEQKIKEMAEHEDubiquitination[5, 7, 8]
508MNEEQYQKDGQLIECubiquitination[2]
538ADAHLFCKECLIRYAubiquitination[5]
554EAVFGSGKLELSCMEubiquitination[5]
584LPQTILYKYYERKAEubiquitination[5, 9]
589LYKYYERKAEEEVAAubiquitination[5]
619ALLDSDVKRFSCPNPubiquitination[2, 3, 4, 5, 7]
635CRKETCRKCQGLWKEubiquitination[5]
641RKCQGLWKEHNGLTCubiquitination[8, 9]
654TCEELAEKDDIKYRTubiquitination[2, 4, 5]
658LAEKDDIKYRTSIEEubiquitination[2, 5, 7]
666YRTSIEEKMTAARIRubiquitination[1, 5]
684KCGTGLIKSEGCNRMubiquitination[5]
765KNGENTFKRIGPPLEubiquitination[1]
773RIGPPLEKPVEKVQRubiquitination[1, 5, 7]
777PLEKPVEKVQRVEALubiquitination[5, 7]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] 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]
 [10] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 Isoform 1 acts as an E3 ubiquitin ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome. Promotes degradation of TRAF3, TLR4 and TLR9. Contributes to the regulation of antiviral responses. Down- regulates activation of NF-kappa-B, IRF3 activation and IFNB production. Isoform 3/ZIN inhibits TNF and IL-1 mediated activation of NF-kappa-B. Promotes TNF and RIP mediated apoptosis. 
Sequence Annotation
 ZN_FING 515 566 RING-type 1.
 ZN_FING 583 648 IBR-type.
 ZN_FING 675 714 RING-type 2.  
Keyword
 Alternative splicing; Apoptosis; Coiled coil; Complete proteome; Cytoplasm; Host-virus interaction; Ligase; Metal-binding; Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 866 AA 
Protein Sequence
MEEGNNNEEV IHLNNFHCHR GQEWINLRDG PITISDSSDE ERIPMLVTPA PQQHEEEDLD 60
DDVILTEDDS EDDYGEFLDL GPPGISEFTK PSGQTEREPK PGPSHNQAAN DIVNPRSEQK 120
VIILEEGSLL YTESDPLETQ NQSSEDSETE LLSNLGESAA LADDQAIEED CWLDHPYFQS 180
LNQQPREITN QVVPQERQPE AELGRLLFQH EFPGPAFPRP EPQQGGISGP SSPQPAHPLG 240
EFEDQQLASD DEEPGPAFPM QESQEPNLEN IWGQEAAEVD QELVELLVKE TEARFPDVAN 300
GFIEEIIHFK NYYDLNVLCN FLLENPDYPK REDRIIINPS SSLLASQDET KLPKIDFFDY 360
SKLTPLDQRC FIQAADLLMA DFKVLSSQDI KWALHELKGH YAITRKALSD AIKKWQELSP 420
ETSGKRKKRK QMNQYSYIDF KFEQGDIKIE KRMFFLENKR RHCRSYDRRA LLPAVQQEQE 480
FYEQKIKEMA EHEDFLLALQ MNEEQYQKDG QLIECRCCYG EFPFEELTQC ADAHLFCKEC 540
LIRYAQEAVF GSGKLELSCM EGSCTCSFPT SELEKVLPQT ILYKYYERKA EEEVAAAYAD 600
ELVRCPSCSF PALLDSDVKR FSCPNPHCRK ETCRKCQGLW KEHNGLTCEE LAEKDDIKYR 660
TSIEEKMTAA RIRKCHKCGT GLIKSEGCNR MSCRCGAQMC YLCRVSINGY DHFCQHPRSP 720
GAPCQECSRC SLWTDPTEDD EKLIEEIQKE AEEEQKRKNG ENTFKRIGPP LEKPVEKVQR 780
VEALPRPVPQ NLPQPQMPPY AFAHPPFPLP PVRPVFNNFP LNMGPIPAPY VPPLPNVRVN 840
YDFGPIHMPL EHNLPMHFGP QPRHRF 866 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:LIFEdb.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
 GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
 GO:0050691; P:regulation of defense response to virus by host; IDA:UniProtKB.
 GO:0032648; P:regulation of interferon-beta production; IDA:UniProtKB.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR002867; Znf_C6HC. 
Pfam
  
SMART
 SM00647; IBR 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS