RTN3_HUMAN - dbPTM
RTN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTN3_HUMAN
UniProt AC O95197
Protein Name Reticulon-3
Gene Name RTN3
Organism Homo sapiens (Human).
Sequence Length 1032
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Golgi apparatus membrane
Multi-pass membrane protein .
Protein Description May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. In case of enteroviruses infection, RTN3 may be involved in the viral replication or pathogenesis. Induces the formation of endoplasmic reticulum tubules. [PubMed: 25612671]
Protein Sequence MAEPSAATQSHSISSSSFGAEPSAPGGGGSPGACPALGTKSCSSSCADSFVSSSSSQPVSLFSTSQEGLSSLCSDEPSSEIMTSSFLSSSEIHNTGLTILHGEKSHVLGSQPILAKEGKDHLDLLDMKKMEKPQGTSNNVSDSSVSLAAGVHCDRPSIPASFPEHPAFLSKKIGQVEEQIDKETKNPNGVSSREAKTALDADDRFTLLTAQKPPTEYSKVEGIYTYSLSPSKVSGDDVIEKDSPESPFEVIIDKAAFDKEFKDSYKESTDDFGSWSVHTDKESSEDISETNDKLFPLRNKEAGRYPMSALLSRQFSHTNAALEEVSRCVNDMHNFTNEILTWDLVPQVKQQTDKSSDCITKTTGLDMSEYNSEIPVVNLKTSTHQKTPVCSIDGSTPITKSTGDWAEASLQQENAITGKPVPDSLNSTKEFSIKGVQGNMQKQDDTLAELPGSPPEKCDSLGSGVATVKVVLPDDHLKDEMDWQSSALGEITEADSSGESDDTVIEDITADTSFENNKIQAEKPVSIPSAVVKTGEREIKEIPSCEREEKTSKNFEELVSDSELHQDQPDILGRSPASEAACSKVPDTNVSLEDVSEVAPEKPITTENPKLPSTVSPNVFNETEFSLNVTTSAYLESLHGKNVKHIDDSSPEDLIAAFTETRDKGIVDSERNAFKAISEKMTDFKTTPPVEVLHENESGGSEIKDIGSKYSEQSKETNGSEPLGVFPTQGTPVASLDLEQEQLTIKALKELGERQVEKSTSAQRDAELPSEEVLKQTFTFAPESWPQRSYDILERNVKNGSDLGISQKPITIRETTRVDAVSSLSKTELVKKHVLARLLTDFSVHDLIFWRDVKKTGFVFGTTLIMLLSLAAFSVISVVSYLILALLSVTISFRIYKSVIQAVQKSEEGHPFKAYLDVDITLSSEAFHNYMNAAMVHINRALKLIIRLFLVEDLVDSLKLAVFMWLMTYVGAVFNGITLLILAELLIFSVPIVYEKYKTQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE
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
2Acetylation------MAEPSAATQ
------CCCCCCCCC		49.0320068231
5Phosphorylation---MAEPSAATQSHS
---CCCCCCCCCCCC		23.2628464451
5 (in isoform 3)Phosphorylation-23.2621406692
8PhosphorylationMAEPSAATQSHSISS
CCCCCCCCCCCCCCC		30.2625159151
8 (in isoform 2)Phosphorylation-30.26-
8 (in isoform 3)Phosphorylation-30.2621406692
8 (in isoform 4)Phosphorylation-30.26-
8 (in isoform 5)Phosphorylation-30.26-
10PhosphorylationEPSAATQSHSISSSS
CCCCCCCCCCCCCCC		18.1725159151
12PhosphorylationSAATQSHSISSSSFG
CCCCCCCCCCCCCCC		29.4325159151
14PhosphorylationATQSHSISSSSFGAE
CCCCCCCCCCCCCCC		27.4729255136
15PhosphorylationTQSHSISSSSFGAEP
CCCCCCCCCCCCCCC		28.4729255136
16PhosphorylationQSHSISSSSFGAEPS
CCCCCCCCCCCCCCC		23.9329255136
17PhosphorylationSHSISSSSFGAEPSA
CCCCCCCCCCCCCCC		29.6429255136
23PhosphorylationSSFGAEPSAPGGGGS
CCCCCCCCCCCCCCC		38.3029255136
23 (in isoform 2)Phosphorylation-38.3024719451
23 (in isoform 3)Phosphorylation-38.3021406692
23 (in isoform 4)Phosphorylation-38.30-
23 (in isoform 5)Phosphorylation-38.30-
30PhosphorylationSAPGGGGSPGACPAL
CCCCCCCCCCCCCCC		24.3629255136
30 (in isoform 2)Phosphorylation-24.3624719451
30 (in isoform 3)Phosphorylation-24.3621406692
30 (in isoform 4)Phosphorylation-24.36-
30 (in isoform 5)Phosphorylation-24.36-
39PhosphorylationGACPALGTKSCSSSC
CCCCCCCCCCCCCCC		22.1921955146
39 (in isoform 2)Phosphorylation-22.1920068231
39 (in isoform 3)Phosphorylation-22.19-
39 (in isoform 4)Phosphorylation-22.19-
39 (in isoform 5)Phosphorylation-22.19-
91 (in isoform 2)Phosphorylation-50.6524719451
110PhosphorylationEKSHVLGSQPILAKE
CCCCCCCCCCEEHHC		28.7324719451
145 (in isoform 6)Phosphorylation-6.6922985185
202 (in isoform 3)Ubiquitination-47.4821906983
210 (in isoform 2)Phosphorylation-18.50-
217 (in isoform 3)Ubiquitination-19.1021906983
218 (in isoform 5)Phosphorylation-24.80-
221 (in isoform 4)Ubiquitination-43.5421906983
222 (in isoform 3)Ubiquitination-22.6121906983
224PhosphorylationYSKVEGIYTYSLSPS
CCCEEEEEEEECCHH		15.5228796482
225PhosphorylationSKVEGIYTYSLSPSK
CCEEEEEEEECCHHH		12.5228796482
226PhosphorylationKVEGIYTYSLSPSKV
CEEEEEEEECCHHHC		7.2225022875
226 (in isoform 3)Ubiquitination-7.2221906983
227PhosphorylationVEGIYTYSLSPSKVS
EEEEEEEECCHHHCC		17.9930266825
227 (in isoform 2)Phosphorylation-17.99-
229PhosphorylationGIYTYSLSPSKVSGD
EEEEEECCHHHCCCC		22.6122167270
231PhosphorylationYTYSLSPSKVSGDDV
EEEECCHHHCCCCCC		42.1730266825
234PhosphorylationSLSPSKVSGDDVIEK
ECCHHHCCCCCCCCC		40.0027362937
236 (in isoform 4)Ubiquitination-39.2321906983
241 (in isoform 4)Ubiquitination-53.0021906983
243PhosphorylationDDVIEKDSPESPFEV
CCCCCCCCCCCCCEE		41.4530266825
245 (in isoform 4)Ubiquitination-75.0121906983
246PhosphorylationIEKDSPESPFEVIID
CCCCCCCCCCEEEEE		37.9730266825
268PhosphorylationFKDSYKESTDDFGSW
HHHHHHCCCCCCCCC		32.74-
283PhosphorylationSVHTDKESSEDISET
EEECCCCCCCCHHHC		44.78-
297 (in isoform 2)Phosphorylation-8.0524719451
316PhosphorylationALLSRQFSHTNAALE
HHHHHHCCCHHHHHH		22.5122617229
318PhosphorylationLSRQFSHTNAALEEV
HHHHCCCHHHHHHHH		25.9221955146
326PhosphorylationNAALEEVSRCVNDMH
HHHHHHHHHHHHHHH		24.20-
386UbiquitinationLKTSTHQKTPVCSID
ECCCCCCCCCCEEEC		47.38-
387PhosphorylationKTSTHQKTPVCSIDG
CCCCCCCCCCEEECC		17.8725159151
391O-linked_GlycosylationHQKTPVCSIDGSTPI
CCCCCCEEECCCCCC		24.7728657654
395PhosphorylationPVCSIDGSTPITKST
CCEEECCCCCCCCCC		27.5425159151
396O-linked_GlycosylationVCSIDGSTPITKSTG
CEEECCCCCCCCCCC		25.0028657654
396PhosphorylationVCSIDGSTPITKSTG
CEEECCCCCCCCCCC		25.0025159151
399O-linked_GlycosylationIDGSTPITKSTGDWA
ECCCCCCCCCCCCHH		21.8328657654
413 (in isoform 2)Phosphorylation-35.3524719451
419UbiquitinationQENAITGKPVPDSLN
CCCCCCCCCCCCCCC		33.90-
432PhosphorylationLNSTKEFSIKGVQGN
CCCCCCEEEECCCCC		25.2024719451
434AcetylationSTKEFSIKGVQGNMQ
CCCCEEEECCCCCCC		52.4019820029
446PhosphorylationNMQKQDDTLAELPGS
CCCCCCCCHHHCCCC		35.8429396449
453PhosphorylationTLAELPGSPPEKCDS
CHHHCCCCCCHHHCC		35.0330266825
467PhosphorylationSLGSGVATVKVVLPD
CCCCCEEEEEEECCC		20.6021712546
526O-linked_GlycosylationIQAEKPVSIPSAVVK
EEECCCCCCCCEEEE		36.9928657654
540"N6,N6-dimethyllysine"KTGEREIKEIPSCER
ECCCCHHHCCCCCCC		44.85-
540MethylationKTGEREIKEIPSCER
ECCCCHHHCCCCCCC		44.8523644510
541 (in isoform 2)Phosphorylation-66.83-
560PhosphorylationKNFEELVSDSELHQD
CCHHHHHCCHHHHCC		48.3030266825
562PhosphorylationFEELVSDSELHQDQP
HHHHHCCHHHHCCCC		34.2530266825
575PhosphorylationQPDILGRSPASEAAC
CCCHHCCCHHHHHHH		24.0325159151
578PhosphorylationILGRSPASEAACSKV
HHCCCHHHHHHHHCC		31.0228270605
583PhosphorylationPASEAACSKVPDTNV
HHHHHHHHCCCCCCC		31.7728270605
588PhosphorylationACSKVPDTNVSLEDV
HHHCCCCCCCCHHHH		31.3030266825
591PhosphorylationKVPDTNVSLEDVSEV
CCCCCCCCHHHHHHH		28.2830266825
596PhosphorylationNVSLEDVSEVAPEKP
CCCHHHHHHHCCCCC		38.3827251275
613PhosphorylationTENPKLPSTVSPNVF
CCCCCCCCCCCCCCC		52.45-
614PhosphorylationENPKLPSTVSPNVFN
CCCCCCCCCCCCCCC		24.06-
616PhosphorylationPKLPSTVSPNVFNET
CCCCCCCCCCCCCCC		15.73-
630 (in isoform 2)Phosphorylation-17.60-
631 (in isoform 2)Phosphorylation-13.6924719451
637PhosphorylationTTSAYLESLHGKNVK
CHHHHHHHHCCCCCC		24.0724719451
649PhosphorylationNVKHIDDSSPEDLIA
CCCCCCCCCHHHHHH		44.0021712546
650PhosphorylationVKHIDDSSPEDLIAA
CCCCCCCCHHHHHHH		39.0225159151
678PhosphorylationRNAFKAISEKMTDFK
HHHHHHHHHHHCCCC		35.7022210691
686PhosphorylationEKMTDFKTTPPVEVL
HHHCCCCCCCCEEEE		44.5222210691
687PhosphorylationKMTDFKTTPPVEVLH
HHCCCCCCCCEEEEE		26.6221815630
698PhosphorylationEVLHENESGGSEIKD
EEEECCCCCCCCCCH		61.1021815630
701PhosphorylationHENESGGSEIKDIGS
ECCCCCCCCCCHHHH		39.4121815630
708PhosphorylationSEIKDIGSKYSEQSK
CCCCHHHHHCCHHHC		28.84-
735PhosphorylationTQGTPVASLDLEQEQ
CCCCCCCCCCCCHHH		23.73-
754MethylationALKELGERQVEKSTS
HHHHHHHHHHHHCCH		44.0154558937
789PhosphorylationPESWPQRSYDILERN
CCCCCCHHHHHHHHH		23.1628796482
790PhosphorylationESWPQRSYDILERNV
CCCCCHHHHHHHHHC		14.8028796482
811PhosphorylationGISQKPITIRETTRV
CCCCCCEEEEECCCC		23.62-
890PhosphorylationILALLSVTISFRIYK
HHHHHHHHHHHHHHH		13.9223927012
892PhosphorylationALLSVTISFRIYKSV
HHHHHHHHHHHHHHH		10.1029496963
969PhosphorylationVFMWLMTYVGAVFNG
HHHHHHHHHHHHHCH		5.28-
979 (in isoform 2)Ubiquitination-2.3721906983
994 (in isoform 2)Ubiquitination-13.8621906983
997PhosphorylationVPIVYEKYKTQIDHY
CHHHHHHHHHHHHHH		13.8223312004
9982-HydroxyisobutyrylationPIVYEKYKTQIDHYV
HHHHHHHHHHHHHHH		45.05-
998UbiquitinationPIVYEKYKTQIDHYV
HHHHHHHHHHHHHHH		45.0521906983
998 (in isoform 1)Ubiquitination-45.0521906983
999PhosphorylationIVYEKYKTQIDHYVG
HHHHHHHHHHHHHHE		27.8923312004
999 (in isoform 2)Ubiquitination-27.8921906983
1003 (in isoform 2)Ubiquitination-22.3221906983
1004PhosphorylationYKTQIDHYVGIARDQ
HHHHHHHHHEECHHH		9.1628152594
10132-HydroxyisobutyrylationGIARDQTKSIVEKIQ
EECHHHHHHHHHHHH		32.33-
1013AcetylationGIARDQTKSIVEKIQ
EECHHHHHHHHHHHH		32.3325825284
1013UbiquitinationGIARDQTKSIVEKIQ
EECHHHHHHHHHHHH		32.3321906983
1013 (in isoform 1)Ubiquitination-32.3321906983
1014PhosphorylationIARDQTKSIVEKIQA
ECHHHHHHHHHHHHH		34.9429457462
10182-HydroxyisobutyrylationQTKSIVEKIQAKLPG
HHHHHHHHHHHHCCC		29.26-
1018AcetylationQTKSIVEKIQAKLPG
HHHHHHHHHHHHCCC		29.2626822725
1018UbiquitinationQTKSIVEKIQAKLPG
HHHHHHHHHHHHCCC		29.2621906983
1018 (in isoform 1)Ubiquitination-29.2621906983
1022UbiquitinationIVEKIQAKLPGIAKK
HHHHHHHHCCCHHHC		38.552190698
1022 (in isoform 1)Ubiquitination-38.5521906983
10282-HydroxyisobutyrylationAKLPGIAKKKAE---
HHCCCHHHCCCC---		53.54-
1028MalonylationAKLPGIAKKKAE---
HHCCCHHHCCCC---		53.5426320211
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 RTN3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTN3_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 RTN3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
F16A2_HUMANFAM160A2physical
16189514
RTN4_HUMANRTN4physical
16189514
PKHF2_HUMANPLEKHF2physical
16189514
RTN3_HUMANRTN3physical
16189514
RTN3_HUMANRTN3physical
25416956
CDIPT_HUMANCDIPTphysical
25416956
P2R3C_HUMANPPP2R3Cphysical
25416956
ZN391_HUMANZNF391physical
25416956
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 RTN3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-30 AND SER-229, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-30 AND SER-229, AND MASS SPECTROMETRY.
"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-649 AND SER-650, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASSSPECTROMETRY.

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