RN146_HUMAN - dbPTM
RN146_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN146_HUMAN
UniProt AC Q9NTX7
Protein Name E3 ubiquitin-protein ligase RNF146
Gene Name RNF146
Organism Homo sapiens (Human).
Sequence Length 359
Subcellular Localization Cytoplasm, cytosol. Nucleus. Translocates to the nucleus after DNA damage, such as laser-induced DNA breaks, and concentrates at DNA breaks. This translocation requires PARP1 activation and PAR-binding.
Protein Description E3 ubiquitin-protein ligase that specifically binds poly-ADP-ribosylated (PARsylated) proteins and mediates their ubiquitination and subsequent degradation. May regulate many important biological processes, such as cell survival and DNA damage response. Acts as an activator of the Wnt signaling pathway by mediating the ubiquitination of PARsylated AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex. Acts in cooperation with tankyrase proteins (TNKS and TNKS2), which mediate PARsylation of target proteins AXIN1, AXIN2, BLZF1, CASC3, TNKS and TNKS2. Recognizes and binds tankyrase-dependent PARsylated proteins via its WWE domain and mediates their ubiquitination, leading to their degradation. Different ubiquitin linkage types have been observed: TNKS2 undergoes ubiquitination at 'Lys-48' and 'Lys-63', while AXIN1 is only ubiquitinated at 'Lys-48'. May regulate TNKS and TNKS2 subcellular location, preventing aggregation at a centrosomal location. Neuroprotective protein. Protects the brain against N-methyl-D-aspartate (NMDA) receptor-mediated glutamate excitotoxicity and ischemia, by interfering with PAR-induced cell death, called parthanatos. Prevents nuclear translocation of AIFM1 in a PAR-binding dependent manner. Does not affect PARP1 activation (By similarity). Protects against cell death induced by DNA damaging agents, such as N-methyl-N-nitro-N-nitrosoguanidine (MNNG) and rescues cells from G1 arrest. Promotes cell survival after gamma-irradiation. Facilitates DNA repair..
Protein Sequence MMAGCGEIDHSINMLPTNRKANESCSNTAPSLTVPECAICLQTCVHPVSLPCKHVFCYLCVKGASWLGKRCALCRQEIPEDFLDKPTLLSPEELKAASRGNGEYAWYYEGRNGWWQYDERTSRELEDAFSKGKKNTEMLIAGFLYVADLENMVQYRRNEHGRRRKIKRDIIDIPKKGVAGLRLDCDANTVNLARESSADGADSVSAQSGASVQPLVSSVRPLTSVDGQLTSPATPSPDASTSLEDSFAHLQLSGDNTAERSHRGEGEEDHESPSSGRVPAPDTSIEETESDASSDSEDVSAVVAQHSLTQQRLLVSNANQTVPDRSDRSGTDRSVAGGGTVSVSVRSRRPDGQCTVTEV
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
84UbiquitinationEIPEDFLDKPTLLSP
CCCHHHCCCCCCCCH		55.6829967540
85UbiquitinationIPEDFLDKPTLLSPE
CCHHHCCCCCCCCHH		41.8921906983
87PhosphorylationEDFLDKPTLLSPEEL
HHHCCCCCCCCHHHH		46.1822199227
90PhosphorylationLDKPTLLSPEELKAA
CCCCCCCCHHHHHHH		33.1222199227
94UbiquitinationTLLSPEELKAASRGN
CCCCHHHHHHHHCCC		4.3329967540
95UbiquitinationLLSPEELKAASRGNG
CCCHHHHHHHHCCCC		45.2321906983
130UbiquitinationRELEDAFSKGKKNTE
HHHHHHHHCCCCCHH		42.0732142685
131UbiquitinationELEDAFSKGKKNTEM
HHHHHHHCCCCCHHH		69.1921906983
176UbiquitinationDIIDIPKKGVAGLRL
CEECCCCCCCCEEEE		53.9521906983
1762-HydroxyisobutyrylationDIIDIPKKGVAGLRL
CEECCCCCCCCEEEE		53.95-
272PhosphorylationEGEEDHESPSSGRVP
CCCCCCCCCCCCCCC		27.0229255136
274PhosphorylationEEDHESPSSGRVPAP
CCCCCCCCCCCCCCC		55.4929255136
275PhosphorylationEDHESPSSGRVPAPD
CCCCCCCCCCCCCCC		33.7229255136
283PhosphorylationGRVPAPDTSIEETES
CCCCCCCCCCHHCCC		30.4627251275
284PhosphorylationRVPAPDTSIEETESD
CCCCCCCCCHHCCCC		35.0727251275
288PhosphorylationPDTSIEETESDASSD
CCCCCHHCCCCCCCC		28.1827251275
290PhosphorylationTSIEETESDASSDSE
CCCHHCCCCCCCCCH		45.9929802988
293PhosphorylationEETESDASSDSEDVS
HHCCCCCCCCCHHHH		39.4030177828
294PhosphorylationETESDASSDSEDVSA
HCCCCCCCCCHHHHH		47.0429802988
296PhosphorylationESDASSDSEDVSAVV
CCCCCCCCHHHHHHH		37.3327251275
300PhosphorylationSSDSEDVSAVVAQHS
CCCCHHHHHHHHHHC		27.8927251275
307PhosphorylationSAVVAQHSLTQQRLL
HHHHHHHCHHHCCEE		22.4930177828
309PhosphorylationVVAQHSLTQQRLLVS
HHHHHCHHHCCEECC		26.1830177828
340PhosphorylationRSVAGGGTVSVSVRS
CCCCCCCEEEEEEEC		16.9422210691
347PhosphorylationTVSVSVRSRRPDGQC
EEEEEEECCCCCCCE		30.4122210691
357O-linked_GlycosylationPDGQCTVTEV-----
CCCCEEEEEC-----		16.9328657654
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 RN146_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
6Kubiquitylation

21478859
11Kubiquitylation

21478859
33Kubiquitylation

21478859
48Kubiquitylation

21478859
48Kubiquitylation

21478859
85Kubiquitylation

21825151
95Kubiquitylation

21825151
131Kubiquitylation

21825151
176Kubiquitylation

21825151
176Kubiquitylation

21825151
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 RN146_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PROF2_HUMANPFN2physical
16169070
RN146_HUMANRNF146physical
21825151
PARP1_HUMANPARP1physical
21825151
HLTF_HUMANHLTFphysical
21825151
HNRPU_HUMANHNRNPUphysical
21825151
NUCL_HUMANNCLphysical
21825151
XRCC6_HUMANXRCC6physical
21825151
XRCC5_HUMANXRCC5physical
21825151
XRCC1_HUMANXRCC1physical
21825151
PARP2_HUMANPARP2physical
21825151
GRP78_HUMANHSPA5physical
21825151
GRP75_HUMANHSPA9physical
21825151
IPO5_HUMANIPO5physical
21825151
IPO7_HUMANIPO7physical
21825151
ATPA_HUMANATP5A1physical
21825151
TBB5_HUMANTUBBphysical
21825151
H12_HUMANHIST1H1Cphysical
21825151
UB2D3_HUMANUBE2D3physical
21825151
UB2D3_HUMANUBE2D3physical
25327252
TNKS1_HUMANTNKSphysical
25327252
RN146_HUMANRNF146physical
25327252
UB2D1_HUMANUBE2D1physical
25327252
UB2D2_HUMANUBE2D2physical
25327252
KASH5_HUMANCCDC155physical
25416956
XPC_HUMANXPCphysical
26186194
SP16H_HUMANSUPT16Hphysical
26186194
DNLI3_HUMANLIG3physical
26186194
PARP2_HUMANPARP2physical
26186194
PARP1_HUMANPARP1physical
26186194
CHD1L_HUMANCHD1Lphysical
26186194
SSRP1_HUMANSSRP1physical
26186194
H2A2B_HUMANHIST2H2ABphysical
26186194
HLTF_HUMANHLTFphysical
26186194
CETN2_HUMANCETN2physical
26186194
PTEN_HUMANPTENphysical
25547115
CHD1L_HUMANCHD1Lphysical
28514442
PARP2_HUMANPARP2physical
28514442
XPC_HUMANXPCphysical
28514442
DNLI3_HUMANLIG3physical
28514442
SP16H_HUMANSUPT16Hphysical
28514442
SSRP1_HUMANSSRP1physical
28514442
PARP1_HUMANPARP1physical
28514442
CETN2_HUMANCETN2physical
28514442
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 RN146_HUMAN

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