RN19A_HUMAN - dbPTM
RN19A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RN19A_HUMAN
UniProt AC Q9NV58
Protein Name E3 ubiquitin-protein ligase RNF19A
Gene Name RNF19A
Organism Homo sapiens (Human).
Sequence Length 838
Subcellular Localization Membrane
Multi-pass membrane protein . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Present in the hyaline inclusion bodies specifically found in motor neurons from amyotrophic lateral sclerosis patients. Present in the Lewy
Protein Description E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection..
Protein Sequence MQEQEIGFISKYNEGLCVNTDPVSILTSILDMSLHRQMGSDRDLQSSASSVSLPSVKKAPKKRRISIGSLFRRKKDNKRKSRELNGGVDGIASIESIHSEMCTDKNSIFSTNTSSDNGLTSISKQIGDFIECPLCLLRHSKDRFPDIMTCHHRSCVDCLRQYLRIEISESRVNISCPECTERFNPHDIRLILSDDVLMEKYEEFMLRRWLVADPDCRWCPAPDCGYAVIAFGCASCPKLTCGREGCGTEFCYHCKQIWHPNQTCDAARQERAQSLRLRTIRSSSISYSQESGAAADDIKPCPRCAAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEISDLHYLSPSGCTFWGKKPWSRKKKILWQLGTLVGAPVGIALIAGIAIPAMIIGIPVYVGRKIHNRYEGKDVSKHKRNLAIAGGVTLSVIVSPVVAAVTVGIGVPIMLAYVYGVVPISLCRSGGCGVSAGNGKGVRIEFDDENDINVGGTNTAVDTTSVAEARHNPSIGEGSVGGLTGSLSASGSHMDRIGAIRDNLSETASTMALAGASITGSLSGSAMVNCFNRLEVQADVQKERYSLSGESGTVSLGTVSDNASTKAMAGSILNSYIPLDKEGNSMEVQVDIESKPSKFRHNSGSSSVDDGSATRSHAGGSSSGLPEGKSSATKWSKEATAGKKSKSGKLRKKGNMKINETREDMDAQLLEQQSTNSSEFEAPSLSDSMPSVADSHSSHFSEFSCSDLESMKTSCSHGSSDYHTRFATVNILPEVENDRLENSPHQCSISVVTQTASCSEVSQLNHIAEEHGNNGIKPNVDLYFGDALKETNNNHSHQTMELKVAIQTEI
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
40PhosphorylationSLHRQMGSDRDLQSS
HHHHHHCCCHHHHHH		24.9128857561
42UbiquitinationHRQMGSDRDLQSSAS
HHHHCCCHHHHHHCC		48.5121890473
43UbiquitinationRQMGSDRDLQSSASS
HHHCCCHHHHHHCCC		54.7921890473
46PhosphorylationGSDRDLQSSASSVSL
CCCHHHHHHCCCCCC		34.8623532336
47PhosphorylationSDRDLQSSASSVSLP
CCHHHHHHCCCCCCH		21.1424719451
49PhosphorylationRDLQSSASSVSLPSV
HHHHHHCCCCCCHHH		32.97-
55PhosphorylationASSVSLPSVKKAPKK
CCCCCCHHHCCCCCC		52.44-
57UbiquitinationSVSLPSVKKAPKKRR
CCCCHHHCCCCCCCC		47.7833845483
66PhosphorylationAPKKRRISIGSLFRR
CCCCCCCCHHHHHHC		21.0523927012
69PhosphorylationKRRISIGSLFRRKKD
CCCCCHHHHHHCCCC		23.7523927012
96PhosphorylationDGIASIESIHSEMCT
CCCEEHHHHHHHHCC		24.7524850871
110PhosphorylationTDKNSIFSTNTSSDN
CCCCCCEECCCCCCC		21.0525627689
111PhosphorylationDKNSIFSTNTSSDNG
CCCCCEECCCCCCCC		31.5925627689
113PhosphorylationNSIFSTNTSSDNGLT
CCCEECCCCCCCCCC		29.6925627689
274PhosphorylationARQERAQSLRLRTIR
HHHHHHHHHCHHHHH		17.9324719451
282PhosphorylationLRLRTIRSSSISYSQ
HCHHHHHHHCCCCCC		25.2923663014
283PhosphorylationRLRTIRSSSISYSQE
CHHHHHHHCCCCCCC		23.1123663014
284PhosphorylationLRTIRSSSISYSQES
HHHHHHHCCCCCCCC		19.4617525332
286PhosphorylationTIRSSSISYSQESGA
HHHHHCCCCCCCCCC		22.2229978859
287PhosphorylationIRSSSISYSQESGAA
HHHHCCCCCCCCCCC		16.8323312004
288PhosphorylationRSSSISYSQESGAAA
HHHCCCCCCCCCCCC		22.2317525332
291PhosphorylationSISYSQESGAAADDI
CCCCCCCCCCCCCCC		26.5426055452
321 (in isoform 3)Ubiquitination-1.7621890473
352UbiquitinationSGCTFWGKKPWSRKK
CCCCCCCCCCCCCHH		46.3822817900
352 (in isoform 2)Ubiquitination-46.3821890473
352 (in isoform 1)Ubiquitination-46.3821890473
353UbiquitinationGCTFWGKKPWSRKKK
CCCCCCCCCCCCHHH		48.0221890473
405UbiquitinationIHNRYEGKDVSKHKR
HHHCCCCCCCCHHCH		42.9133845483
468UbiquitinationGVSAGNGKGVRIEFD
CEECCCCCCEEEEEC		59.23-
502PhosphorylationAEARHNPSIGEGSVG
HHHHCCCCCCCCCCC		48.8427080861
507PhosphorylationNPSIGEGSVGGLTGS
CCCCCCCCCCHHHCE		17.1827080861
512PhosphorylationEGSVGGLTGSLSASG
CCCCCHHHCEEECCC		28.1830108239
514PhosphorylationSVGGLTGSLSASGSH
CCCHHHCEEECCCCC		17.5730108239
516PhosphorylationGGLTGSLSASGSHMD
CHHHCEEECCCCCHH		23.3030108239
518PhosphorylationLTGSLSASGSHMDRI
HHCEEECCCCCHHHH		37.1425849741
520PhosphorylationGSLSASGSHMDRIGA
CEEECCCCCHHHHHH		17.0930108239
537PhosphorylationDNLSETASTMALAGA
HCHHHHHHHHHHHCC		26.5730576142
549PhosphorylationAGASITGSLSGSAMV
HCCEEECCCCCCHHH		15.6530576142
570UbiquitinationEVQADVQKERYSLSG
EEEEEEHHCEEECCC		43.9633845483
574PhosphorylationDVQKERYSLSGESGT
EEHHCEEECCCCCEE		23.4527251275
576PhosphorylationQKERYSLSGESGTVS
HHCEEECCCCCEEEE		34.2827251275
599PhosphorylationSTKAMAGSILNSYIP
CCHHHHHHHHHCCCC		17.8625850435
603PhosphorylationMAGSILNSYIPLDKE
HHHHHHHCCCCCCCC		22.4625002506
604PhosphorylationAGSILNSYIPLDKEG
HHHHHHCCCCCCCCC		12.8925884760
631PhosphorylationPSKFRHNSGSSSVDD
CCCCCCCCCCCCCCC		33.6529255136
633PhosphorylationKFRHNSGSSSVDDGS
CCCCCCCCCCCCCCC		21.1830576142
634PhosphorylationFRHNSGSSSVDDGSA
CCCCCCCCCCCCCCC		37.6030576142
635PhosphorylationRHNSGSSSVDDGSAT
CCCCCCCCCCCCCCC		31.1230576142
640PhosphorylationSSSVDDGSATRSHAG
CCCCCCCCCCCCCCC		33.2029514088
642PhosphorylationSVDDGSATRSHAGGS
CCCCCCCCCCCCCCC		34.1123090842
649PhosphorylationTRSHAGGSSSGLPEG
CCCCCCCCCCCCCCC		22.0329449344
650PhosphorylationRSHAGGSSSGLPEGK
CCCCCCCCCCCCCCC		31.5329449344
651PhosphorylationSHAGGSSSGLPEGKS
CCCCCCCCCCCCCCC		46.1524114839
657UbiquitinationSSGLPEGKSSATKWS
CCCCCCCCCCCCHHH		39.3129967540
714PhosphorylationEFEAPSLSDSMPSVA
CCCCCCCCCCCCCHH		31.7921601212
750PhosphorylationCSHGSSDYHTRFATV
CCCCCCCHHHEEEEE		13.6725884760
811PhosphorylationIKPNVDLYFGDALKE
CCCCCEEEECHHHHH		10.89-
827PhosphorylationNNNHSHQTMELKVAI
CCCCCCCEEEEEEEE		13.7427251275
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 RN19A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RN19A_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 RN19A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UB2L3_HUMANUBE2L3physical
11237715
UB2L6_HUMANUBE2L6physical
11237715
SODC_HUMANSOD1physical
17666395
SNCAP_HUMANSNCAIPphysical
12750386
SODC_HUMANSOD1physical
12145308
TERA_HUMANVCPphysical
15456787
SODC_HUMANSOD1physical
17157513
UB2L3_HUMANUBE2L3physical
12145308
UB2L3_HUMANUBE2L3physical
12750386
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 RN19A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND SER-288, ANDMASS SPECTROMETRY.

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