RN216_HUMAN - dbPTM
RN216_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN216_HUMAN
UniProt AC Q9NWF9
Protein Name E3 ubiquitin-protein ligase RNF216
Gene Name RNF216
Organism Homo sapiens (Human).
Sequence Length 866
Subcellular Localization Cytoplasm.
Protein 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 inhibits TNF and IL-1 mediated activation of NF-kappa-B. Promotes TNF and RIP mediated apoptosis..
Protein Sequence MEEGNNNEEVIHLNNFHCHRGQEWINLRDGPITISDSSDEERIPMLVTPAPQQHEEEDLDDDVILTEDDSEDDYGEFLDLGPPGISEFTKPSGQTEREPKPGPSHNQAANDIVNPRSEQKVIILEEGSLLYTESDPLETQNQSSEDSETELLSNLGESAALADDQAIEEDCWLDHPYFQSLNQQPREITNQVVPQERQPEAELGRLLFQHEFPGPAFPRPEPQQGGISGPSSPQPAHPLGEFEDQQLASDDEEPGPAFPMQESQEPNLENIWGQEAAEVDQELVELLVKETEARFPDVANGFIEEIIHFKNYYDLNVLCNFLLENPDYPKREDRIIINPSSSLLASQDETKLPKIDFFDYSKLTPLDQRCFIQAADLLMADFKVLSSQDIKWALHELKGHYAITRKALSDAIKKWQELSPETSGKRKKRKQMNQYSYIDFKFEQGDIKIEKRMFFLENKRRHCRSYDRRALLPAVQQEQEFYEQKIKEMAEHEDFLLALQMNEEQYQKDGQLIECRCCYGEFPFEELTQCADAHLFCKECLIRYAQEAVFGSGKLELSCMEGSCTCSFPTSELEKVLPQTILYKYYERKAEEEVAAAYADELVRCPSCSFPALLDSDVKRFSCPNPHCRKETCRKCQGLWKEHNGLTCEELAEKDDIKYRTSIEEKMTAARIRKCHKCGTGLIKSEGCNRMSCRCGAQMCYLCRVSINGYDHFCQHPRSPGAPCQECSRCSLWTDPTEDDEKLIEEIQKEAEEEQKRKNGENTFKRIGPPLEKPVEKVQRVEALPRPVPQNLPQPQMPPYAFAHPPFPLPPVRPVFNNFPLNMGPIPAPYVPPLPNVRVNYDFGPIHMPLEHNLPMHFGPQPRHRF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
13 (in isoform 3)Ubiquitination-3.7321890473
35PhosphorylationRDGPITISDSSDEER
CCCCEEECCCCCCCC		23.8427732954
37PhosphorylationGPITISDSSDEERIP
CCEEECCCCCCCCCC		32.6627732954
38PhosphorylationPITISDSSDEERIPM
CEEECCCCCCCCCCE		54.7727732954
47 (in isoform 3)Ubiquitination-4.9821890473
80 (in isoform 1)Sumoylation-13.93-
89 (in isoform 1)Sumoylation-37.68-
89 (in isoform 1)Methylation-37.68-
100SumoylationGQTEREPKPGPSHNQ
CCCCCCCCCCCCCCC		58.83-
100SumoylationGQTEREPKPGPSHNQ
CCCCCCCCCCCCCCC		58.8328112733
100UbiquitinationGQTEREPKPGPSHNQ
CCCCCCCCCCCCCCC		58.8321906983
100 (in isoform 2)Ubiquitination-58.8321890473
107 (in isoform 3)Ubiquitination-36.1121890473
157 (in isoform 1)Ubiquitination-40.1321890473
228PhosphorylationEPQQGGISGPSSPQP
CCCCCCCCCCCCCCC		48.1826074081
231PhosphorylationQGGISGPSSPQPAHP
CCCCCCCCCCCCCCC		59.1726074081
232PhosphorylationGGISGPSSPQPAHPL
CCCCCCCCCCCCCCC		30.5926074081
249PhosphorylationFEDQQLASDDEEPGP
CCCCCCCCCCCCCCC		54.9424275569
288 (in isoform 3)Ubiquitination-9.1121890473
340PhosphorylationDRIIINPSSSLLASQ
CCEEECCCHHHCCCC		28.24-
342PhosphorylationIIINPSSSLLASQDE
EEECCCHHHCCCCCC		31.5727050516
346PhosphorylationPSSSLLASQDETKLP
CCHHHCCCCCCCCCC		37.8329523821
350PhosphorylationLLASQDETKLPKIDF
HCCCCCCCCCCCCCC		46.2829523821
351SumoylationLASQDETKLPKIDFF
CCCCCCCCCCCCCCC		61.82-
351SumoylationLASQDETKLPKIDFF
CCCCCCCCCCCCCCC		61.8228112733
351UbiquitinationLASQDETKLPKIDFF
CCCCCCCCCCCCCCC		61.8221906983
351 (in isoform 2)Ubiquitination-61.8221890473
354SumoylationQDETKLPKIDFFDYS
CCCCCCCCCCCCCHH		66.40-
354SumoylationQDETKLPKIDFFDYS
CCCCCCCCCCCCCHH		66.4028112733
354UbiquitinationQDETKLPKIDFFDYS
CCCCCCCCCCCCCHH		66.40-
362UbiquitinationIDFFDYSKLTPLDQR
CCCCCHHHCCCHHHH		50.5921906983
362 (in isoform 2)Ubiquitination-50.5921890473
387PhosphorylationADFKVLSSQDIKWAL
HCCEEECHHHHHHHH		27.9317525332
387 (in isoform 3)Ubiquitination-27.9321890473
391UbiquitinationVLSSQDIKWALHELK
EECHHHHHHHHHHHC		34.4021890473
391 (in isoform 2)Ubiquitination-34.4021890473
395 (in isoform 3)Ubiquitination-30.5121890473
398UbiquitinationKWALHELKGHYAITR
HHHHHHHCCCHHHHH		40.43-
401PhosphorylationLHELKGHYAITRKAL
HHHHCCCHHHHHHHH		14.3617525332
406UbiquitinationGHYAITRKALSDAIK
CCHHHHHHHHHHHHH		45.06-
408 (in isoform 1)Ubiquitination-5.5121890473
411 (in isoform 1)Ubiquitination-16.48-
413UbiquitinationKALSDAIKKWQELSP
HHHHHHHHHHHHCCC		50.08-
414UbiquitinationALSDAIKKWQELSPE
HHHHHHHHHHHCCCC		48.25-
419PhosphorylationIKKWQELSPETSGKR
HHHHHHCCCCCCCCH		21.6719664994
419 (in isoform 1)Ubiquitination-21.6721890473
422PhosphorylationWQELSPETSGKRKKR
HHHCCCCCCCCHHHH		46.2823663014
423PhosphorylationQELSPETSGKRKKRK
HHCCCCCCCCHHHHH		40.4323663014
425AcetylationLSPETSGKRKKRKQM
CCCCCCCCHHHHHHC		61.8923236377
425SumoylationLSPETSGKRKKRKQM
CCCCCCCCHHHHHHC		61.8928112733
425UbiquitinationLSPETSGKRKKRKQM
CCCCCCCCHHHHHHC		61.8921906983
425 (in isoform 2)Ubiquitination-61.8921890473
427UbiquitinationPETSGKRKKRKQMNQ
CCCCCCHHHHHHCCC		61.49-
430SumoylationSGKRKKRKQMNQYSY
CCCHHHHHHCCCCCE		63.8828112733
430UbiquitinationSGKRKKRKQMNQYSY
CCCHHHHHHCCCCCE		63.88-
437PhosphorylationKQMNQYSYIDFKFEQ
HHCCCCCEEEEEECC		10.28-
448SumoylationKFEQGDIKIEKRMFF
EECCCCEEEEEEEEH		49.94-
448SumoylationKFEQGDIKIEKRMFF
EECCCCEEEEEEEEH		49.9428112733
448UbiquitinationKFEQGDIKIEKRMFF
EECCCCEEEEEEEEH		49.94-
448 (in isoform 1)Ubiquitination-49.9421890473
455 (in isoform 1)Ubiquitination-6.46-
459SumoylationRMFFLENKRRHCRSY
EEEHHHHHHHHCHHC		41.2428112733
459UbiquitinationRMFFLENKRRHCRSY
EEEHHHHHHHHCHHC		41.24-
463 (in isoform 1)Ubiquitination-2.68-
470 (in isoform 1)Ubiquitination-17.84-
471 (in isoform 1)Ubiquitination-5.81-
476PhosphorylationRALLPAVQQEQEFYE
HHHHHHHHHHHHHHH		43.1019664994
476 (in isoform 1)Phosphorylation-43.1024719451
482 (in isoform 1)Ubiquitination-19.3921890473
484 (in isoform 1)Ubiquitination-41.20-
485SumoylationEQEFYEQKIKEMAEH
HHHHHHHHHHHHHHC		43.75-
485SumoylationEQEFYEQKIKEMAEH
HHHHHHHHHHHHHHC		43.7528112733
485UbiquitinationEQEFYEQKIKEMAEH
HHHHHHHHHHHHHHC		43.7521906983
485 (in isoform 2)Ubiquitination-43.7521890473
487UbiquitinationEFYEQKIKEMAEHED
HHHHHHHHHHHHCHH		48.77-
487 (in isoform 1)Ubiquitination-48.77-
505 (in isoform 1)Ubiquitination-39.52-
508UbiquitinationMNEEQYQKDGQLIEC
CCHHHHHHCCCEEEE		59.91-
516 (in isoform 1)Ubiquitination-10.76-
538UbiquitinationADAHLFCKECLIRYA
HHHHHHHHHHHHHHH		44.09-
542 (in isoform 1)Ubiquitination-4.8421890473
544 (in isoform 1)Ubiquitination-12.97-
554UbiquitinationEAVFGSGKLELSCME
HHHHCCCEEEEEECC		40.25-
563PhosphorylationELSCMEGSCTCSFPT
EEEECCCEEEEECCH		7.9222468782
565PhosphorylationSCMEGSCTCSFPTSE
EECCCEEEEECCHHH		16.9422468782
570PhosphorylationSCTCSFPTSELEKVL
EEEEECCHHHHHHHC		32.5922468782
571PhosphorylationCTCSFPTSELEKVLP
EEEECCHHHHHHHCC		40.1822468782
584UbiquitinationLPQTILYKYYERKAE
CCHHHHHHHHHHHCH		37.6021890473
584 (in isoform 2)Ubiquitination-37.6021890473
589SumoylationLYKYYERKAEEEVAA
HHHHHHHHCHHHHHH		48.48-
589UbiquitinationLYKYYERKAEEEVAA
HHHHHHHHCHHHHHH		48.48-
595 (in isoform 1)Ubiquitination-6.94-
607PhosphorylationDELVRCPSCSFPALL
HHHCCCCCCCCCHHH		26.4728348404
609PhosphorylationLVRCPSCSFPALLDS
HCCCCCCCCCHHHCC		38.3124719451
611 (in isoform 1)Ubiquitination-13.00-
619SumoylationALLDSDVKRFSCPNP
HHHCCCCHHCCCCCH		53.36-
619SumoylationALLDSDVKRFSCPNP
HHHCCCCHHCCCCCH		53.3628112733
619UbiquitinationALLDSDVKRFSCPNP
HHHCCCCHHCCCCCH		53.36-
622PhosphorylationDSDVKRFSCPNPHCR
CCCCHHCCCCCHHHC		32.4728555341
635UbiquitinationCRKETCRKCQGLWKE
HCHHHHHHCCCHHHH		32.81-
641UbiquitinationRKCQGLWKEHNGLTC
HHCCCHHHHHCCCCH		54.89-
641 (in isoform 1)Ubiquitination-54.8921890473
646 (in isoform 1)Ubiquitination-6.34-
654UbiquitinationTCEELAEKDDIKYRT
CHHHHHHCCCCCCCC		55.91-
655 (in isoform 1)Phosphorylation-55.1427642862
658SumoylationLAEKDDIKYRTSIEE
HHHCCCCCCCCCHHH		35.36-
658SumoylationLAEKDDIKYRTSIEE
HHHCCCCCCCCCHHH		35.3628112733
658UbiquitinationLAEKDDIKYRTSIEE
HHHCCCCCCCCCHHH		35.36-
666SumoylationYRTSIEEKMTAARIR
CCCCHHHHHHHHHHH		28.85-
666SumoylationYRTSIEEKMTAARIR
CCCCHHHHHHHHHHH		28.8528112733
666UbiquitinationYRTSIEEKMTAARIR
CCCCHHHHHHHHHHH		28.8521906983
666 (in isoform 1)Phosphorylation-28.8524719451
666 (in isoform 2)Ubiquitination-28.8521890473
676 (in isoform 1)Ubiquitination-31.32-
684UbiquitinationKCGTGLIKSEGCNRM
CCCCCCCCCCCCCCC		47.71-
692 (in isoform 1)Ubiquitination-8.65-
706PhosphorylationMCYLCRVSINGYDHF
EEEEECEEECCCCCC		7.3225159151
710PhosphorylationCRVSINGYDHFCQHP
ECEEECCCCCCCCCC		11.19-
711 (in isoform 1)Ubiquitination-29.77-
715 (in isoform 1)Ubiquitination-48.99-
719PhosphorylationHFCQHPRSPGAPCQE
CCCCCCCCCCCCCCC		31.9423927012
723 (in isoform 1)Ubiquitination-26.6621890473
741 (in isoform 1)Ubiquitination-63.18-
765SumoylationKNGENTFKRIGPPLE
HHCCCCHHHCCCCCC		40.8628112733
765UbiquitinationKNGENTFKRIGPPLE
HHCCCCHHHCCCCCC		40.8621906983
765 (in isoform 2)Ubiquitination-40.8621890473
773SumoylationRIGPPLEKPVEKVQR
HCCCCCCCCHHHHHH		63.1428112733
773UbiquitinationRIGPPLEKPVEKVQR
HCCCCCCCCHHHHHH		63.142190698
773 (in isoform 2)Ubiquitination-63.1421890473
776 (in isoform 1)Phosphorylation-56.9124719451
777SumoylationPLEKPVEKVQRVEAL
CCCCCHHHHHHHHCC		43.85-
777AcetylationPLEKPVEKVQRVEAL
CCCCCHHHHHHHHCC		43.8525953088
777UbiquitinationPLEKPVEKVQRVEAL
CCCCCHHHHHHHHCC		43.85-
822 (in isoform 1)Ubiquitination-33.3321890473
830 (in isoform 1)Ubiquitination-27.9121890473
834 (in isoform 1)Ubiquitination-3.84-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
-KUbiquitinationE3 ubiquitin ligaseRNF216Q9NWF9
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN216_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RN216_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TLR3_HUMANTLR3physical
15107846
TLR4_HUMANTLR4physical
15107846
TLR5_HUMANTLR5physical
15107846
TLR9_HUMANTLR9physical
15107846
UBE2H_HUMANUBE2Hphysical
15107846
UB2L3_HUMANUBE2L3physical
15107846
UBE2C_HUMANUBE2Cphysical
15107846
UB2L6_HUMANUBE2L6physical
15107846
RN216_HUMANRNF216physical
16169070
RIPK1_HUMANRIPK1physical
11854271
RIPK1_HUMANRIPK1physical
16968706
TIRAP_HUMANTIRAPphysical
16968706
TRAF3_HUMANTRAF3physical
19893624
VIF_HV1B1vifphysical
15367624
VIF_HV1BRvifphysical
15367624
VIF_HV1H2vifphysical
15367624
BECN1_HUMANBECN1physical
25484083
ARC_HUMANARCphysical
24945773
ARC_HUMANARCphysical
27995769
RIPK1_HUMANRIPK1physical
27995769
TRAF3_HUMANTRAF3physical
27026194
UB2D3_HUMANUBE2D3physical
27026194
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
212840Gordon Holmes syndrome (GDHS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RN216_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.

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