CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001544
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Reticulon-3 
Protein Synonyms/Alias
 Homolog of ASY protein; HAP; Neuroendocrine-specific protein-like 2; NSP-like protein 2; Neuroendocrine-specific protein-like II; NSP-like protein II; NSPLII 
Gene Name
 RTN3 
Gene Synonyms/Alias
 ASYIP; NSPL2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
540KTGEREIKEIPSCERmethylation[1]
998PIVYEKYKTQIDHYVubiquitination[2, 3, 4]
1013GIARDQTKSIVEKIQubiquitination[2, 4, 5]
1018QTKSIVEKIQAKLPGubiquitination[2, 3, 4, 5, 6]
1022IVEKIQAKLPGIAKKubiquitination[2, 3, 4]
Reference
 [1] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional 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. 
Sequence Annotation
 DOMAIN 844 1032 Reticulon.
 REGION 987 1032 Interaction with FADD.
 REGION 1000 1002 Interaction with BACE1.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 243 243 Phosphoserine (By similarity).
 MOD_RES 649 649 Phosphoserine.
 MOD_RES 650 650 Phosphoserine.
 MOD_RES 735 735 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Apoptosis; Complete proteome; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Host-virus interaction; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Stress response; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1032 AA 
Protein Sequence
MAEPSAATQS HSISSSSFGA EPSAPGGGGS PGACPALGTK SCSSSCADSF VSSSSSQPVS 60
LFSTSQEGLS SLCSDEPSSE IMTSSFLSSS EIHNTGLTIL HGEKSHVLGS QPILAKEGKD 120
HLDLLDMKKM EKPQGTSNNV SDSSVSLAAG VHCDRPSIPA SFPEHPAFLS KKIGQVEEQI 180
DKETKNPNGV SSREAKTALD ADDRFTLLTA QKPPTEYSKV EGIYTYSLSP SKVSGDDVIE 240
KDSPESPFEV IIDKAAFDKE FKDSYKESTD DFGSWSVHTD KESSEDISET NDKLFPLRNK 300
EAGRYPMSAL LSRQFSHTNA ALEEVSRCVN DMHNFTNEIL TWDLVPQVKQ QTDKSSDCIT 360
KTTGLDMSEY NSEIPVVNLK TSTHQKTPVC SIDGSTPITK STGDWAEASL QQENAITGKP 420
VPDSLNSTKE FSIKGVQGNM QKQDDTLAEL PGSPPEKCDS LGSGVATVKV VLPDDHLKDE 480
MDWQSSALGE ITEADSSGES DDTVIEDITA DTSFENNKIQ AEKPVSIPSA VVKTGEREIK 540
EIPSCEREEK TSKNFEELVS DSELHQDQPD ILGRSPASEA ACSKVPDTNV SLEDVSEVAP 600
EKPITTENPK LPSTVSPNVF NETEFSLNVT TSAYLESLHG KNVKHIDDSS PEDLIAAFTE 660
TRDKGIVDSE RNAFKAISEK MTDFKTTPPV EVLHENESGG SEIKDIGSKY SEQSKETNGS 720
EPLGVFPTQG TPVASLDLEQ EQLTIKALKE LGERQVEKST SAQRDAELPS EEVLKQTFTF 780
APESWPQRSY DILERNVKNG SDLGISQKPI TIRETTRVDA VSSLSKTELV KKHVLARLLT 840
DFSVHDLIFW RDVKKTGFVF GTTLIMLLSL AAFSVISVVS YLILALLSVT ISFRIYKSVI 900
QAVQKSEEGH PFKAYLDVDI TLSSEAFHNY MNAAMVHINR ALKLIIRLFL VEDLVDSLKL 960
AVFMWLMTYV GAVFNGITLL ILAELLIFSV PIVYEKYKTQ IDHYVGIARD QTKSIVEKIQ 1020
AKLPGIAKKK AE 1032 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:HPA.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0005615; C:extracellular space; TAS:ProtInc.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB.
 GO:0006950; P:response to stress; IEA:UniProtKB-KW.
 GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR003388; Reticulon. 
Pfam
 PF02453; Reticulon 
SMART
  
PROSITE
 PS50845; RETICULON 
PRINTS