RTN1_HUMAN - dbPTM
RTN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTN1_HUMAN
UniProt AC Q16799
Protein Name Reticulon-1
Gene Name RTN1
Organism Homo sapiens (Human).
Sequence Length 776
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description May be involved in neuroendocrine secretion or in membrane trafficking in neuroendocrine cells..
Protein Sequence MAAPGDPQDELLPLAGPGSQWLRHRGEGENEAVTPKGATPAPQAGEPSPGLGARAREAASREAGSGPARQSPVAMETASTGVAGVSSAMDHTFSTTSKDGEGSCYTSLISDICYPPQEDSTYFTGILQKENGHVTISESPEELGTPGPSLPDVPGIESRGLFSSDSGIEMTPAESTEVNKILADPLDQMKAEAYKYIDITRPEEVKHQEQHHPELEDKDLDFKNKDTDISIKPEGVREPDKPAPVEGKIIKDHLLEESTFAPYIDDLSEEQRRAPQITTPVKITLTEIEPSVETTTQEKTPEKQDICLKPSPDTVPTVTVSEPEDDSPGSITPPSSGTEPSAAESQGKGSISEDELITAIKEAKGLSYETAENPRPVGQLADRPEVKARSGPPTIPSPLDHEASSAESGDSEIELVSEDPMAAEDALPSGYVSFGHVGGPPPSPASPSIQYSILREEREAELDSELIIESCDASSASEESPKREQDSPPMKPSALDAIREETGVRAEERAPSRRGLAEPGSFLDYPSTEPQPGPELPPGDGALEPETPMLPRKPEEDSSSNQSPAATKGPGPLGPGAPPPLLFLNKQKAIDLLYWRDIKQTGIVFGSFLLLLFSLTQFSVVSVVAYLALAALSATISFRIYKSVLQAVQKTDEGHPFKAYLELEITLSQEQIQKYTDCLQFYVNSTLKELRRLFLVQDLVDSLKFAVLMWLLTYVGALFNGLTLLLMAVVSMFTLPVVYVKHQAQIDQYLGLVRTHINAVVAKIQAKIPGAKRHAE
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
15 (in isoform 3)Phosphorylation-21.86-
34PhosphorylationEGENEAVTPKGATPA
CCCCCCCCCCCCCCC
26.7424719451
39PhosphorylationAVTPKGATPAPQAGE
CCCCCCCCCCCCCCC
28.7527486199
48PhosphorylationAPQAGEPSPGLGARA
CCCCCCCCCCCCHHH
27.5730266825
60PhosphorylationARAREAASREAGSGP
HHHHHHHHHHCCCCC
37.3923532336
65PhosphorylationAASREAGSGPARQSP
HHHHHCCCCCCCCCC
48.9623403867
71PhosphorylationGSGPARQSPVAMETA
CCCCCCCCCCCCHHC
18.7821082442
77PhosphorylationQSPVAMETASTGVAG
CCCCCCHHCCCCCCC
16.9028060719
79PhosphorylationPVAMETASTGVAGVS
CCCCHHCCCCCCCHH
32.8728060719
80PhosphorylationVAMETASTGVAGVSS
CCCHHCCCCCCCHHH
32.9628060719
86PhosphorylationSTGVAGVSSAMDHTF
CCCCCCHHHHCCCEE
16.0928060719
87PhosphorylationTGVAGVSSAMDHTFS
CCCCCHHHHCCCEEE
25.8028060719
92PhosphorylationVSSAMDHTFSTTSKD
HHHHCCCEEECCCCC
18.2828060719
94PhosphorylationSAMDHTFSTTSKDGE
HHCCCEEECCCCCCC
31.7528060719
95PhosphorylationAMDHTFSTTSKDGEG
HCCCEEECCCCCCCC
30.7828060719
96PhosphorylationMDHTFSTTSKDGEGS
CCCEEECCCCCCCCC
32.3628060719
97PhosphorylationDHTFSTTSKDGEGSC
CCEEECCCCCCCCCE
28.9228060719
139PhosphorylationGHVTISESPEELGTP
CEEEECCCHHHHCCC
30.7124719451
145PhosphorylationESPEELGTPGPSLPD
CCHHHHCCCCCCCCC
37.3824719451
163PhosphorylationIESRGLFSSDSGIEM
CCCCCCCCCCCCCCC
37.9727251275
164PhosphorylationESRGLFSSDSGIEMT
CCCCCCCCCCCCCCC
28.5827251275
166PhosphorylationRGLFSSDSGIEMTPA
CCCCCCCCCCCCCCC
43.5526657352
196PhosphorylationMKAEAYKYIDITRPE
HHHHHHHHCCCCCHH
7.3727642862
200O-linked_GlycosylationAYKYIDITRPEEVKH
HHHHCCCCCHHHHCC
36.1028657654
278PhosphorylationQRRAPQITTPVKITL
HHHCCCCCCCCEEEE
21.5730266825
279PhosphorylationRRAPQITTPVKITLT
HHCCCCCCCCEEEEE
27.9330266825
284PhosphorylationITTPVKITLTEIEPS
CCCCCEEEEEEEECC
23.1623312004
286PhosphorylationTPVKITLTEIEPSVE
CCCEEEEEEEECCCC
26.6829978859
291PhosphorylationTLTEIEPSVETTTQE
EEEEEECCCCCCCCC
21.5729978859
294PhosphorylationEIEPSVETTTQEKTP
EEECCCCCCCCCCCC
32.7529978859
295PhosphorylationIEPSVETTTQEKTPE
EECCCCCCCCCCCCC
16.9929978859
296PhosphorylationEPSVETTTQEKTPEK
ECCCCCCCCCCCCCC
41.9929978859
300PhosphorylationETTTQEKTPEKQDIC
CCCCCCCCCCCCCCC
35.6129743597
311PhosphorylationQDICLKPSPDTVPTV
CCCCCCCCCCCCCEE
33.5427486199
314PhosphorylationCLKPSPDTVPTVTVS
CCCCCCCCCCEEEEC
31.5927486199
317PhosphorylationPSPDTVPTVTVSEPE
CCCCCCCEEEECCCC
25.1928270605
319PhosphorylationPDTVPTVTVSEPEDD
CCCCCEEEECCCCCC
22.3128270605
321PhosphorylationTVPTVTVSEPEDDSP
CCCEEEECCCCCCCC
37.7628270605
327PhosphorylationVSEPEDDSPGSITPP
ECCCCCCCCCCCCCC
43.4128270605
330PhosphorylationPEDDSPGSITPPSSG
CCCCCCCCCCCCCCC
27.0328270605
332PhosphorylationDDSPGSITPPSSGTE
CCCCCCCCCCCCCCC
30.7428270605
335PhosphorylationPGSITPPSSGTEPSA
CCCCCCCCCCCCCCH
42.4728270605
336PhosphorylationGSITPPSSGTEPSAA
CCCCCCCCCCCCCHH
56.3528270605
338PhosphorylationITPPSSGTEPSAAES
CCCCCCCCCCCHHHH
46.8227251275
341PhosphorylationPSSGTEPSAAESQGK
CCCCCCCCHHHHCCC
33.6027251275
345PhosphorylationTEPSAAESQGKGSIS
CCCCHHHHCCCCCCC
39.2328270605
350PhosphorylationAESQGKGSISEDELI
HHHCCCCCCCHHHHH
26.8230266825
352PhosphorylationSQGKGSISEDELITA
HCCCCCCCHHHHHHH
40.4719664994
358PhosphorylationISEDELITAIKEAKG
CCHHHHHHHHHHHCC
34.6530266825
368PhosphorylationKEAKGLSYETAENPR
HHHCCCCCCCCCCCC
23.4922817900
470PhosphorylationDSELIIESCDASSAS
CCEEHHHHCCCCCCC
13.5928060719
474PhosphorylationIIESCDASSASEESP
HHHHCCCCCCCCCCC
17.1228060719
475PhosphorylationIESCDASSASEESPK
HHHCCCCCCCCCCCC
37.2228060719
477PhosphorylationSCDASSASEESPKRE
HCCCCCCCCCCCCCC
43.7928060719
480PhosphorylationASSASEESPKREQDS
CCCCCCCCCCCCCCC
31.5028060719
487PhosphorylationSPKREQDSPPMKPSA
CCCCCCCCCCCCHHH
30.5130266825
493PhosphorylationDSPPMKPSALDAIRE
CCCCCCHHHHHHHHH
35.6323927012
558PhosphorylationPRKPEEDSSSNQSPA
CCCCCCCCCCCCCCC
38.6628060719
559PhosphorylationRKPEEDSSSNQSPAA
CCCCCCCCCCCCCCH
45.7028060719
560PhosphorylationKPEEDSSSNQSPAAT
CCCCCCCCCCCCCHH
42.7228060719
563PhosphorylationEDSSSNQSPAATKGP
CCCCCCCCCCHHCCC
22.2828060719
567PhosphorylationSNQSPAATKGPGPLG
CCCCCCHHCCCCCCC
38.3428060719
601PhosphorylationYWRDIKQTGIVFGSF
ECCCHHHHCCHHHHH
24.7124043423
607PhosphorylationQTGIVFGSFLLLLFS
HHCCHHHHHHHHHHH
10.9724043423
614PhosphorylationSFLLLLFSLTQFSVV
HHHHHHHHCCHHHHH
30.4024043423
616PhosphorylationLLLLFSLTQFSVVSV
HHHHHHCCHHHHHHH
26.7724043423
619PhosphorylationLFSLTQFSVVSVVAY
HHHCCHHHHHHHHHH
16.2824043423
622PhosphorylationLTQFSVVSVVAYLAL
CCHHHHHHHHHHHHH
14.5524043423
626PhosphorylationSVVSVVAYLALAALS
HHHHHHHHHHHHHHH
4.8624043423
633PhosphorylationYLALAALSATISFRI
HHHHHHHHHHHHHHH
20.7424043423
635PhosphorylationALAALSATISFRIYK
HHHHHHHHHHHHHHH
17.4924043423
637PhosphorylationAALSATISFRIYKSV
HHHHHHHHHHHHHHH
12.2429496963
650UbiquitinationSVLQAVQKTDEGHPF
HHHHHHHHCCCCCCC
51.88-
772AcetylationQAKIPGAKRHAE---
HHHCCCCHHCCC---
51.1119668229

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 RTN1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTN1_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 RTN1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
F16A2_HUMANFAM160A2physical
16189514
PKHF2_HUMANPLEKHF2physical
16189514
B2CL1_HUMANBCL2L1physical
11126360
SEY1_YEASTSEY1physical
19665976
HDAC8_HUMANHDAC8physical
19140693
SDCB1_HUMANSDCBPphysical
25416956
DYRK2_HUMANDYRK2physical
28514442
RTN4_HUMANRTN4physical
28514442
RTN2_HUMANRTN2physical
28514442
PLS1_HUMANPLSCR1physical
28514442
F210B_HUMANFAM210Bphysical
28514442
MET7A_HUMANMETTL7Aphysical
28514442
CD032_HUMANC4orf32physical
28514442
GDN_HUMANSERPINE2physical
28514442
NB5R3_HUMANCYB5R3physical
28514442
TMM43_HUMANTMEM43physical
28514442
TMM70_HUMANTMEM70physical
28514442
SGMR1_HUMANSIGMAR1physical
28514442
CTR3_HUMANSLC7A3physical
28514442
T120B_HUMANTMEM120Bphysical
28514442
TYSY_HUMANTYMSphysical
28514442
PRAF3_HUMANARL6IP5physical
28514442
DERL2_HUMANDERL2physical
28514442
RASN_HUMANNRASphysical
28514442
F213A_HUMANFAM213Aphysical
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 RTN1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352 AND SER-487, ANDMASS SPECTROMETRY.

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