CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022261
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
408LASQDETKLPKIDFFubiquitination[1, 2]
411QDETKLPKIDFFDYSubiquitination[1]
419IDFFDYSKLTPLDQRubiquitination[1, 2]
448VLSSQDIKWALHELKubiquitination[1, 2, 3]
455KWALHELKGHYAITRubiquitination[1]
463GHYAITRKALSDAIKubiquitination[1]
470KALSDAIKKWQELSPubiquitination[1]
471ALSDAIKKWQELSPEubiquitination[1]
482LSPETSGKRKKRKQMubiquitination[1, 2]
484PETSGKRKKRKQMNQubiquitination[1]
487SGKRKKRKQMNQYSYubiquitination[1]
505KFEQGDIKIEKRMFFubiquitination[1]
516RMFFLENKRRHCRSYubiquitination[1]
542EQEFYEQKIKEMAEHubiquitination[1, 2]
544EFYEQKIKEMAEHEDubiquitination[1]
595ADAHLFCKECLIRYAubiquitination[1]
611EAVFGSGKLELSCMEubiquitination[1]
641LPQTILYKYYERKAEubiquitination[1, 3]
646LYKYYERKAEEEVAAubiquitination[1]
676ALLDSDVKRFSCPNPubiquitination[1]
692CRKETCRKCQGLWKEubiquitination[1]
711TCEELAEKDDIKYRTubiquitination[1]
715LAEKDDIKYRTSIEEubiquitination[1]
723YRTSIEEKMTAARIRubiquitination[1]
741KCGTGLIKSEGCNRMubiquitination[1]
830RIGPPLEKPVEKVQRubiquitination[1]
834PLEKPVEKVQRVEALubiquitination[1]
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] 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]
 [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] 
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
DDVILTETNK PQRSRPNLIK PAAQWQDLKR LGEERPKKSR AAFESDKSSY FSVCNNPLFD 120
SGAQDDSEDD YGEFLDLGPP GISEFTKPSG QTEREPKPGP SHNQAANDIV NPRSEQKVII 180
LEEGSLLYTE SDPLETQNQS SEDSETELLS NLGESAALAD DQAIEEDCWL DHPYFQSLNQ 240
QPREITNQVV PQERQPEAEL GRLLFQHEFP GPAFPRPEPQ QGGISGPSSP QPAHPLGEFE 300
DQQLASDDEE PGPAFPMQES QEPNLENIWG QEAAEVDQEL VELLVKETEA RFPDVANGFI 360
EEIIHFKNYY DLNVLCNFLL ENPDYPKRED RIIINPSSSL LASQDETKLP KIDFFDYSKL 420
TPLDQRCFIQ AADLLMADFK VLSSQDIKWA LHELKGHYAI TRKALSDAIK KWQELSPETS 480
GKRKKRKQMN QYSYIDFKFE QGDIKIEKRM FFLENKRRHC RSYDRRALLP AVQQEQEFYE 540
QKIKEMAEHE DFLLALQMNE EQYQKDGQLI ECRCCYGEFP FEELTQCADA HLFCKECLIR 600
YAQEAVFGSG KLELSCMEGS CTCSFPTSEL EKVLPQTILY KYYERKAEEE VAAAYADELV 660
RCPSCSFPAL LDSDVKRFSC PNPHCRKETC RKCQGLWKEH NGLTCEELAE KDDIKYRTSI 720
EEKMTAARIR KCHKCGTGLI KSEGCNRMSC RCGAQMCYLC RVSINGYDHF CQHPRSPGAP 780
CQECSRCSLW TDPTEDDEKL IEEIQKEAEE EQKRKNGENT FKRIGPPLEK PVEKVQRVEA 840
LPRPVPQNLP QPQMPPYAFA HPPFPLPPVR PVFNNFPLNM GPIPAPYVPP LPNVRVNYDF 900
GPIHMPLEHN LPMHFGPQPR HRF 923 
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