RNF31_HUMAN - dbPTM
RNF31_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RNF31_HUMAN
UniProt AC Q96EP0
Protein Name E3 ubiquitin-protein ligase RNF31
Gene Name RNF31 {ECO:0000312|HGNC:HGNC:16031}
Organism Homo sapiens (Human).
Sequence Length 1072
Subcellular Localization Cytoplasm .
Protein Description E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. [PubMed: 17006537]
Protein Sequence MPGEEEERAFLVAREELASALRRDSGQAFSLEQLRPLLASSLPLAARYLQLDAARLVRCNAHGEPRNYLNTLSTALNILEKYGRNLLSPQRPRYWRGVKFNNPVFRSTVDAVQGGRDVLRLYGYTEEQPDGLSFPEGQEEPDEHQVATVTLEVLLLRTELSLLLQNTHPRQQALEQLLEDKVEDDMLQLSEFDPLLREIAPGPLTTPSVPGSTPGPCFLCGSAPGTLHCPSCKQALCPACDHLFHGHPSRAHHLRQTLPGVLQGTHLSPSLPASAQPRPQSTSLLALGDSSLSSPNPASAHLPWHCAACAMLNEPWAVLCVACDRPRGCKGLGLGTEGPQGTGGLEPDLARGRWACQSCTFENEAAAVLCSICERPRLAQPPSLVVDSRDAGICLQPLQQGDALLASAQSQVWYCIHCTFCNSSPGWVCVMCNRTSSPIPAQHAPRPYASSLEKGPPKPGPPRRLSAPLPSSCGDPEKQRQDKMREEGLQLVSMIREGEAAGACPEEIFSALQYSGTEVPLQWLRSELPYVLEMVAELAGQQDPGLGAFSCQEARRAWLDRHGNLDEAVEECVRTRRRKVQELQSLGFGPEEGSLQALFQHGGDVSRALTELQRQRLEPFRQRLWDSGPEPTPSWDGPDKQSLVRRLLAVYALPSWGRAELALSLLQETPRNYELGDVVEAVRHSQDRAFLRRLLAQECAVCGWALPHNRMQALTSCECTICPDCFRQHFTIALKEKHITDMVCPACGRPDLTDDTQLLSYFSTLDIQLRESLEPDAYALFHKKLTEGVLMRDPKFLWCAQCSFGFIYEREQLEATCPQCHQTFCVRCKRQWEEQHRGRSCEDFQNWKRMNDPEYQAQGLAMYLQENGIDCPKCKFSYALARGGCMHFHCTQCRHQFCSGCYNAFYAKNKCPEPNCRVKKSLHGHHPRDCLFYLRDWTALRLQKLLQDNNVMFNTEPPAGARAVPGGGCRVIEQKEVPNGLRDEACGKETPAGYAGLCQAHYKEYLVSLINAHSLDPATLYEVEELETATERYLHVRPQPLAGEDPPAYQARLLQKLTEEVPLGQSIPRRRK
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
19PhosphorylationVAREELASALRRDSG
HHHHHHHHHHHCCCC
40.2226434776
81UbiquitinationTALNILEKYGRNLLS
HHHHHHHHHCCCCCC
49.95-
88PhosphorylationKYGRNLLSPQRPRYW
HHCCCCCCCCCCCCC
23.3524719451
99UbiquitinationPRYWRGVKFNNPVFR
CCCCCCCCCCCHHHH
45.2421890473
99UbiquitinationPRYWRGVKFNNPVFR
CCCCCCCCCCCHHHH
45.2427667366
99 (in isoform 1)Ubiquitination-45.2421890473
179UbiquitinationQALEQLLEDKVEDDM
HHHHHHHHHHCHHCH
65.4623000965
179 (in isoform 3)Ubiquitination-65.4621890473
225 (in isoform 2)Ubiquitination-40.4021906983
226 (in isoform 2)Ubiquitination-16.5721906983
257PhosphorylationRAHHLRQTLPGVLQG
HHHHHHHHCCCCCCC
28.6123312004
265PhosphorylationLPGVLQGTHLSPSLP
CCCCCCCCCCCCCCC
13.4923312004
268PhosphorylationVLQGTHLSPSLPASA
CCCCCCCCCCCCCCC
12.5828188228
270PhosphorylationQGTHLSPSLPASAQP
CCCCCCCCCCCCCCC
43.5425849741
274PhosphorylationLSPSLPASAQPRPQS
CCCCCCCCCCCCCCC
26.0423312004
281PhosphorylationSAQPRPQSTSLLALG
CCCCCCCCCCEEEEC
23.7328787133
290PhosphorylationSLLALGDSSLSSPNP
CEEEECCCCCCCCCC
31.2328787133
303UbiquitinationNPASAHLPWHCAACA
CCCCCCCCHHHHHHH
14.6521890473
303 (in isoform 3)Ubiquitination-14.6521890473
307UbiquitinationAHLPWHCAACAMLNE
CCCCHHHHHHHHHCC
7.8421890473
307 (in isoform 3)Ubiquitination-7.8421890473
315PhosphorylationACAMLNEPWAVLCVA
HHHHHCCCEEEEEHH
24.2132142685
327UbiquitinationCVACDRPRGCKGLGL
EHHCCCCCCCCCCCC
65.1327667366
330UbiquitinationCDRPRGCKGLGLGTE
CCCCCCCCCCCCCCC
61.0521890473
330UbiquitinationCDRPRGCKGLGLGTE
CCCCCCCCCCCCCCC
61.0523000965
330 (in isoform 1)Ubiquitination-61.0521890473
358PhosphorylationRGRWACQSCTFENEA
CCCEECCCCCCCHHH
18.2727251275
383PhosphorylationPRLAQPPSLVVDSRD
CCCCCCCCEEEECCC
40.2429255136
388PhosphorylationPPSLVVDSRDAGICL
CCCEEEECCCCCCCC
22.0529255136
428UbiquitinationCNSSPGWVCVMCNRT
CCCCCCEEEEEECCC
1.8722817900
428 (in isoform 3)Ubiquitination-1.8721890473
435PhosphorylationVCVMCNRTSSPIPAQ
EEEEECCCCCCCCCC
21.4023403867
436PhosphorylationCVMCNRTSSPIPAQH
EEEECCCCCCCCCCC
30.7721712546
437PhosphorylationVMCNRTSSPIPAQHA
EEECCCCCCCCCCCC
26.6623401153
448PhosphorylationAQHAPRPYASSLEKG
CCCCCCCCHHHCCCC
22.0123403867
450PhosphorylationHAPRPYASSLEKGPP
CCCCCCHHHCCCCCC
29.6123403867
451PhosphorylationAPRPYASSLEKGPPK
CCCCCHHHCCCCCCC
32.1623403867
454UbiquitinationPYASSLEKGPPKPGP
CCHHHCCCCCCCCCC
80.2621890473
454UbiquitinationPYASSLEKGPPKPGP
CCHHHCCCCCCCCCC
80.2627667366
454 (in isoform 1)Ubiquitination-80.2621890473
458UbiquitinationSLEKGPPKPGPPRRL
HCCCCCCCCCCCCCC
66.7821890473
458UbiquitinationSLEKGPPKPGPPRRL
HCCCCCCCCCCCCCC
66.7827667366
458 (in isoform 1)Ubiquitination-66.7821890473
466PhosphorylationPGPPRRLSAPLPSSC
CCCCCCCCCCCCCCC
26.4828189684
471PhosphorylationRLSAPLPSSCGDPEK
CCCCCCCCCCCCHHH
46.0423927012
472PhosphorylationLSAPLPSSCGDPEKQ
CCCCCCCCCCCHHHH
21.8523927012
478UbiquitinationSSCGDPEKQRQDKMR
CCCCCHHHHHHHHHH
57.0527667366
483UbiquitinationPEKQRQDKMREEGLQ
HHHHHHHHHHHHHHH
31.36-
489UbiquitinationDKMREEGLQLVSMIR
HHHHHHHHHHHHHHH
3.9421890473
489 (in isoform 2)Ubiquitination-3.9421906983
489 (in isoform 3)Ubiquitination-3.9421890473
493PhosphorylationEEGLQLVSMIREGEA
HHHHHHHHHHHCCCC
19.6527251275
579UbiquitinationCVRTRRRKVQELQSL
HHHHHHHHHHHHHHC
46.5921906983
579 (in isoform 1)Ubiquitination-46.5921890473
632PhosphorylationWDSGPEPTPSWDGPD
HHCCCCCCCCCCCCC
28.43-
632UbiquitinationWDSGPEPTPSWDGPD
HHCCCCCCCCCCCCC
28.4322817900
632 (in isoform 3)Ubiquitination-28.4321890473
633UbiquitinationDSGPEPTPSWDGPDK
HCCCCCCCCCCCCCH
44.1022817900
633 (in isoform 3)Ubiquitination-44.1021890473
634PhosphorylationSGPEPTPSWDGPDKQ
CCCCCCCCCCCCCHH
40.0327251275
640UbiquitinationPSWDGPDKQSLVRRL
CCCCCCCHHHHHHHH
44.9421890473
640UbiquitinationPSWDGPDKQSLVRRL
CCCCCCCHHHHHHHH
44.9421963094
640 (in isoform 1)Ubiquitination-44.9421890473
642PhosphorylationWDGPDKQSLVRRLLA
CCCCCHHHHHHHHHH
34.2724719451
651PhosphorylationVRRLLAVYALPSWGR
HHHHHHHHHCCCCCH
9.2327642862
655PhosphorylationLAVYALPSWGRAELA
HHHHHCCCCCHHHHH
42.9128857561
664PhosphorylationGRAELALSLLQETPR
CHHHHHHHHHHHCCC
22.7930108239
669PhosphorylationALSLLQETPRNYELG
HHHHHHHCCCCCCCH
18.0030108239
685PhosphorylationVVEAVRHSQDRAFLR
HHHHHHHHHHHHHHH
24.1828555341
697UbiquitinationFLRRLLAQECAVCGW
HHHHHHHHHHHHHCC
46.3929967540
715PhosphorylationHNRMQALTSCECTIC
CCHHHHHHHCEEEEC
34.0527251275
716PhosphorylationNRMQALTSCECTICP
CHHHHHHHCEEEECH
14.5827251275
735UbiquitinationQHFTIALKEKHITDM
HHEEEEECHHHCCCC
56.55-
759UbiquitinationLTDDTQLLSYFSTLD
CCCCHHHHHHHHHHC
2.5429967540
783UbiquitinationDAYALFHKKLTEGVL
CHHHHHHCCCCCCCC
41.9921906983
783 (in isoform 1)Ubiquitination-41.9921890473
784UbiquitinationAYALFHKKLTEGVLM
HHHHHHCCCCCCCCC
52.6621906983
784 (in isoform 1)Ubiquitination-52.6621890473
793UbiquitinationTEGVLMRDPKFLWCA
CCCCCCCCCCCEEEE
36.4529967540
837UbiquitinationRQWEEQHRGRSCEDF
HHHHHHHCCCCCHHH
41.7529967540
840PhosphorylationEEQHRGRSCEDFQNW
HHHHCCCCCHHHHHH
25.3623312004
848UbiquitinationCEDFQNWKRMNDPEY
CHHHHHHHHCCCHHH
49.6829967540
863PhosphorylationQAQGLAMYLQENGID
HHHHHHHHHHHCCCC
10.3029083192
873UbiquitinationENGIDCPKCKFSYAL
HCCCCCCCCHHHHHH
57.28-
877PhosphorylationDCPKCKFSYALARGG
CCCCCHHHHHHHCCC
8.5924719451
899PhosphorylationQCRHQFCSGCYNAFY
HHHCHHHHHHHHHHH
32.9424247654
902PhosphorylationHQFCSGCYNAFYAKN
CHHHHHHHHHHHCCC
17.0427251275
905UbiquitinationCSGCYNAFYAKNKCP
HHHHHHHHHCCCCCC
5.6222817900
905 (in isoform 3)Ubiquitination-5.6221890473
910UbiquitinationNAFYAKNKCPEPNCR
HHHHCCCCCCCCCCC
50.9229967540
944UbiquitinationWTALRLQKLLQDNNV
HHHHHHHHHHHCCCC
56.6129967540
952SulfoxidationLLQDNNVMFNTEPPA
HHHCCCCEECCCCCC
2.0321406390
988UbiquitinationLRDEACGKETPAGYA
CCCCCCCCCCCCCHH
59.3029967540
1005PhosphorylationCQAHYKEYLVSLINA
HHHHHHHHHHHHHHH
14.3026074081
1008PhosphorylationHYKEYLVSLINAHSL
HHHHHHHHHHHHHCC
22.4226074081
1014PhosphorylationVSLINAHSLDPATLY
HHHHHHHCCCHHHEE
31.8626074081
1019PhosphorylationAHSLDPATLYEVEEL
HHCCCHHHEEEHHHH
34.9526074081
1021PhosphorylationSLDPATLYEVEELET
CCCHHHEEEHHHHHH
17.3626074081
1056UbiquitinationYQARLLQKLTEEVPL
HHHHHHHHHHHCCCC
58.3022817900
1056 (in isoform 1)Ubiquitination-58.3021890473
1066PhosphorylationEEVPLGQSIPRRRK-
HCCCCCCCCCCCCC-
32.5328857561

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

Oops, there are no upstream regulatory protein records of RNF31_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RNF31_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 RNF31_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HOIL1_HUMANRBCK1physical
20005846
DDX58_HUMANDDX58physical
21292167
TRI25_HUMANTRIM25physical
21292167
NR0B1_HUMANNR0B1physical
19237537
NR0B2_HUMANNR0B2physical
19237537
HOIL1_HUMANRBCK1physical
22430200
KPCB_HUMANPRKCBphysical
17069764
HOIL1_HUMANRBCK1physical
17069764
TNAP3_HUMANTNFAIP3physical
23032187
NEMO_HUMANIKBKGphysical
23032187
HOIL1_HUMANRBCK1physical
23032187
UB2D1_HUMANUBE2D1physical
17069764
UB2D3_HUMANUBE2D3physical
21292167
HOIL1_HUMANRBCK1physical
17006537
UBC_HUMANUBCphysical
23727886
OTUL_HUMANOTULINphysical
23708998
HOIL1_HUMANRBCK1physical
23708998
SMAD3_HUMANSMAD3physical
21988832
SOCS3_HUMANSOCS3physical
21988832
NEMO_MOUSEIkbkgphysical
24469399
NEMO_HUMANIKBKGphysical
24469399
UBC_HUMANUBCphysical
24469399
OTUL_HUMANOTULINphysical
24726327
HOIL1_HUMANRBCK1physical
24726327
SHRPN_HUMANSHARPINphysical
24726327
UBC_HUMANUBCphysical
24726327
TERA_HUMANVCPphysical
24726327
NDUA8_HUMANNDUFA8physical
24726327
BIRC2_HUMANBIRC2physical
24726327
TRAF2_HUMANTRAF2physical
24726327
CCD14_HUMANCCDC14physical
24726327
WRIP1_HUMANWRNIP1physical
24726327
AKP8L_HUMANAKAP8Lphysical
24726327
ESR1_HUMANESR1physical
24441041
OTUL_HUMANOTULINphysical
24726323
RNF31_HUMANRNF31physical
24726323
TERA_HUMANVCPphysical
24726323
SHRPN_HUMANSHARPINphysical
21455180
HOIL1_HUMANRBCK1physical
21455180
UBC_HUMANUBCphysical
21455180
KPCA_HUMANPRKCAphysical
25118570
KRA92_HUMANKRTAP9-2physical
25416956
VASN_HUMANVASNphysical
25416956
CCD24_HUMANCCDC24physical
25416956
UB2D3_HUMANUBE2D3physical
21455180
NEMO_HUMANIKBKGphysical
21455180
NEMO_HUMANIKBKGphysical
19675569
SHRPN_RATSharpinphysical
22253853
UBC_HUMANUBCphysical
17006537
UB2D3_HUMANUBE2D3physical
17006537
UB2D1_HUMANUBE2D1physical
17006537
UB2D2_HUMANUBE2D2physical
17006537
UB2L3_HUMANUBE2L3physical
17006537
UBC_HUMANUBCphysical
23986494
UBC_HUMANUBCphysical
25494483
SHRPN_HUMANSHARPINphysical
26600301
TRAF1_HUMANTRAF1physical
25996949
UB2L3_HUMANUBE2L3physical
25996949
UB2D2_HUMANUBE2D2physical
26789245
UBC_HUMANUBCphysical
26789245
HOIL1_HUMANRBCK1physical
26670046
SHRPN_HUMANSHARPINphysical
26670046
OTUL_HUMANOTULINphysical
26670046
CYLD_HUMANCYLDphysical
26670046
RIPK1_HUMANRIPK1physical
26670046
TNR1A_HUMANTNFRSF1Aphysical
26670046
HOIL1_HUMANRBCK1physical
26525107
UBC_HUMANUBCphysical
22791023
HOIL1_HUMANRBCK1physical
22791023
SHRPN_HUMANSHARPINphysical
22791023
PDLI7_HUMANPDLIM7physical
27903798
IRF7_HUMANIRF7physical
27903798
CAR11_HUMANCARD11physical
27777308
BCL10_HUMANBCL10physical
27777308
TRAF1_HUMANTRAF1physical
27893701
OTUL_HUMANOTULINphysical
28189684
SPAT2_HUMANSPATA2physical
28189684
CYLD_HUMANCYLDphysical
28189684
SHRPN_HUMANSHARPINphysical
28514442
HOIL1_HUMANRBCK1physical
28514442
PRI2_HUMANPRIM2physical
28514442
GBP1_HUMANGBP1physical
28514442
PRI1_HUMANPRIM1physical
28514442
ACTBL_HUMANACTBL2physical
28514442
SPAT2_HUMANSPATA2physical
27458237
CYLD_HUMANCYLDphysical
27458237
OTUL_HUMANOTULINphysical
27458237
CYLD_HUMANCYLDphysical
27591049
SPAT2_HUMANSPATA2physical
27591049
UBC_HUMANUBCphysical
28319114
SEPT2_HUMANSEPT2physical
28319114
HDAC6_HUMANHDAC6physical
28319114
VDAC1_HUMANVDAC1physical
28319114
TRAF6_HUMANTRAF6physical
28319114
PRKN_HUMANPARK2physical
27348524

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RNF31_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466, AND MASSSPECTROMETRY.

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