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O95197

- RTN3_HUMAN

UniProt

O95197 - RTN3_HUMAN

Protein

Reticulon-3

Gene

RTN3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (20 Mar 2007)
      Previous versions | rss
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    Functioni

    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.4 Publications

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. endoplasmic reticulum tubular network organization Source: UniProtKB
    3. response to stress Source: UniProtKB-KW
    4. vesicle-mediated transport Source: UniProtKB-KW
    5. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Apoptosis, ER-Golgi transport, Host-virus interaction, Stress response, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Reticulon-3
    Alternative name(s):
    Homolog of ASY protein
    Short name:
    HAP
    Neuroendocrine-specific protein-like 2
    Short name:
    NSP-like protein 2
    Neuroendocrine-specific protein-like II
    Short name:
    NSP-like protein II
    Short name:
    NSPLII
    Gene namesi
    Name:RTN3
    Synonyms:ASYIP, NSPL2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:10469. RTN3.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: HPA
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. extracellular space Source: ProtInc
    4. extracellular vesicular exosome Source: UniProt
    5. Golgi membrane Source: UniProtKB-SubCell
    6. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34882.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 10321031Reticulon-3PRO_0000168163Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei649 – 6491Phosphoserine1 Publication
    Modified residuei650 – 6501Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95197.
    PaxDbiO95197.
    PRIDEiO95197.

    PTM databases

    PhosphoSiteiO95197.

    Expressioni

    Tissue specificityi

    Isoform 3 is widely expressed, with highest levels in brain, where it is enriched in neuronal cell bodies from gray matter (at protein level). Three times more abundant in macula than in peripheral retina. Isoform 1 is expressed at high levels in brain and at low levels in skeletal muscle. Isoform 2 is only found in melanoma.5 Publications

    Inductioni

    By endoplasmic reticulum stress (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiO95197.
    BgeeiO95197.
    GenevestigatoriO95197.

    Organism-specific databases

    HPAiHPA015649.
    HPA015650.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with ATL1 By similarity. Interacts with RTN4. Isoform 3 interacts with BACE1, BACE2, BCL2 and FADD. Interacts with Coxsackievirus A16, enterovirus 71 and poliovirus P2C proteins. Interacts with ATL2.By similarity8 Publications

    Protein-protein interaction databases

    BioGridi115598. 15 interactions.
    IntActiO95197. 12 interactions.
    MINTiMINT-5000642.

    Structurei

    3D structure databases

    ProteinModelPortaliO95197.
    SMRiO95197. Positions 894-959.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 863862CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini888 – 94760CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini969 – 9724CytoplasmicSequence Analysis
    Topological domaini994 – 103239CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei864 – 88724HelicalSequence AnalysisAdd
    BLAST
    Intramembranei948 – 96821HelicalSequence AnalysisAdd
    BLAST
    Intramembranei973 – 99321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini844 – 1032189ReticulonPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni987 – 103246Interaction with FADDAdd
    BLAST
    Regioni1000 – 10023Interaction with BACE1

    Sequence similaritiesi

    Contains 1 reticulon domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG303514.
    HOVERGENiHBG093922.
    InParanoidiO95197.
    OMAiRIYKSVV.
    OrthoDBiEOG7CZK7J.
    PhylomeDBiO95197.
    TreeFamiTF105431.

    Family and domain databases

    InterProiIPR003388. Reticulon.
    [Graphical view]
    PANTHERiPTHR10994. PTHR10994. 1 hit.
    PfamiPF02453. Reticulon. 1 hit.
    [Graphical view]
    PROSITEiPS50845. RETICULON. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95197-1) [UniParc]FASTAAdd to Basket

    Also known as: A1, A4b

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAEPSAATQS HSISSSSFGA EPSAPGGGGS PGACPALGTK SCSSSCADSF     50
    VSSSSSQPVS LFSTSQEGLS SLCSDEPSSE IMTSSFLSSS EIHNTGLTIL 100
    HGEKSHVLGS QPILAKEGKD HLDLLDMKKM EKPQGTSNNV SDSSVSLAAG 150
    VHCDRPSIPA SFPEHPAFLS KKIGQVEEQI DKETKNPNGV SSREAKTALD 200
    ADDRFTLLTA QKPPTEYSKV EGIYTYSLSP SKVSGDDVIE KDSPESPFEV 250
    IIDKAAFDKE FKDSYKESTD DFGSWSVHTD KESSEDISET NDKLFPLRNK 300
    EAGRYPMSAL LSRQFSHTNA ALEEVSRCVN DMHNFTNEIL TWDLVPQVKQ 350
    QTDKSSDCIT KTTGLDMSEY NSEIPVVNLK TSTHQKTPVC SIDGSTPITK 400
    STGDWAEASL QQENAITGKP VPDSLNSTKE FSIKGVQGNM QKQDDTLAEL 450
    PGSPPEKCDS LGSGVATVKV VLPDDHLKDE MDWQSSALGE ITEADSSGES 500
    DDTVIEDITA DTSFENNKIQ AEKPVSIPSA VVKTGEREIK EIPSCEREEK 550
    TSKNFEELVS DSELHQDQPD ILGRSPASEA ACSKVPDTNV SLEDVSEVAP 600
    EKPITTENPK LPSTVSPNVF NETEFSLNVT TSAYLESLHG KNVKHIDDSS 650
    PEDLIAAFTE TRDKGIVDSE RNAFKAISEK MTDFKTTPPV EVLHENESGG 700
    SEIKDIGSKY SEQSKETNGS EPLGVFPTQG TPVASLDLEQ EQLTIKALKE 750
    LGERQVEKST SAQRDAELPS EEVLKQTFTF APESWPQRSY DILERNVKNG 800
    SDLGISQKPI TIRETTRVDA VSSLSKTELV KKHVLARLLT DFSVHDLIFW 850
    RDVKKTGFVF GTTLIMLLSL AAFSVISVVS YLILALLSVT ISFRIYKSVI 900
    QAVQKSEEGH PFKAYLDVDI TLSSEAFHNY MNAAMVHINR ALKLIIRLFL 950
    VEDLVDSLKL AVFMWLMTYV GAVFNGITLL ILAELLIFSV PIVYEKYKTQ 1000
    IDHYVGIARD QTKSIVEKIQ AKLPGIAKKK AE 1032
    Length:1,032
    Mass (Da):112,611
    Last modified:March 20, 2007 - v2
    Checksum:i26B372B82BFC6361
    GO
    Isoform 2 (identifier: O95197-2) [UniParc]FASTAAdd to Basket

    Also known as: A2, A3b

    The sequence of this isoform differs from the canonical sequence as follows:
         48-66: Missing.

    Show »
    Length:1,013
    Mass (Da):110,652
    Checksum:i26EBCFC7BF6351FC
    GO
    Isoform 3 (identifier: O95197-3) [UniParc]FASTAAdd to Basket

    Also known as: B1, A1

    The sequence of this isoform differs from the canonical sequence as follows:
         48-66: Missing.
         67-843: Missing.

    Show »
    Length:236
    Mass (Da):25,609
    Checksum:iDDC6A4544ABCDFB7
    GO
    Isoform 4 (identifier: O95197-4) [UniParc]FASTAAdd to Basket

    Also known as: B2, A2

    The sequence of this isoform differs from the canonical sequence as follows:
         67-843: Missing.

    Show »
    Length:255
    Mass (Da):27,568
    Checksum:iA1EB93C4659AD832
    GO
    Isoform 5 (identifier: O95197-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         48-66: Missing.
         67-843: Missing.
         999-1032: TQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE → DPSKTPWNRQKKGRISTWKPEMQQLLKHHLIVITSLLVL

    Note: No experimental confirmation available.

    Show »
    Length:241
    Mass (Da):26,452
    Checksum:i12919C71F2208160
    GO
    Isoform 6 (identifier: O95197-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         48-843: Missing.
         914-1032: AYLDVDITLS...LPGIAKKKAE → PRLITMLASP...PQYQAQKLMD

    Show »
    Length:214
    Mass (Da):23,489
    Checksum:iD066FBEA9D48E49C
    GO
    Isoform 7 (identifier: O95197-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         48-159: Missing.

    Note: Gene prediction based on EST data.

    Show »
    Length:920
    Mass (Da):100,824
    Checksum:i5C36B72E4243492C
    GO

    Sequence cautioni

    The sequence BAD93008.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti871 – 8711A → V in BAD93008. (PubMed:15946766)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61A → E.1 Publication
    Corresponds to variant rs11551944 [ dbSNP | Ensembl ].
    VAR_031164
    Natural varianti501 – 5011D → H.
    Corresponds to variant rs7936660 [ dbSNP | Ensembl ].
    VAR_057713

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei48 – 843796Missing in isoform 6. 1 PublicationVSP_045319Add
    BLAST
    Alternative sequencei48 – 159112Missing in isoform 7. CuratedVSP_047008Add
    BLAST
    Alternative sequencei48 – 6619Missing in isoform 2, isoform 3 and isoform 5. 7 PublicationsVSP_023759Add
    BLAST
    Alternative sequencei67 – 843777Missing in isoform 3, isoform 4 and isoform 5. 7 PublicationsVSP_023760Add
    BLAST
    Alternative sequencei914 – 1032119AYLDV…KKKAE → PRLITMLASPEIRPSQLLKR SKQNSLESPKKRQNKYMETR NATVTKTPFNSYNVVTCTMK ENTQCQLEPAFQAFFLIWCF LPSFPFNPQYQAQKLMD in isoform 6. 1 PublicationVSP_045320Add
    BLAST
    Alternative sequencei999 – 103234TQIDH…KKKAE → DPSKTPWNRQKKGRISTWKP EMQQLLKHHLIVITSLLVL in isoform 5. CuratedVSP_023761Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF059524 mRNA. Translation: AAC99319.1.
    AF059529
    , AF059525, AF059526, AF059527, AF059528 Genomic DNA. Translation: AAD20951.1.
    AF119297 mRNA. Translation: AAD26810.1.
    AY427821 mRNA. Translation: AAR02474.1.
    AY750848 mRNA. Translation: AAU81930.1.
    AP000753 Genomic DNA. No translation available.
    AP006289 Genomic DNA. No translation available.
    AK297529 mRNA. Translation: BAH12606.1.
    AB209771 mRNA. Translation: BAD93008.1. Different initiation.
    AK075412 mRNA. Translation: BAG52134.1.
    AK222898 mRNA. Translation: BAD96618.1.
    AK295361 mRNA. Translation: BAH12044.1.
    CH471076 Genomic DNA. Translation: EAW74170.1.
    BC000634 mRNA. Translation: AAH00634.1.
    BC010556 mRNA. Translation: AAH10556.1.
    BC011394 mRNA. Translation: AAH11394.1.
    BC022993 mRNA. Translation: AAH22993.1.
    BC100822 mRNA. Translation: AAI00823.1.
    BC100823 mRNA. Translation: AAI00824.1.
    BC105981 mRNA. Translation: AAI05982.1.
    BC105982 mRNA. Translation: AAI05983.1.
    BC118628 mRNA. Translation: AAI18629.1.
    BC118550 mRNA. Translation: AAI18551.1.
    BK001685 mRNA. Translation: DAA01931.1.
    BK001681 mRNA. Translation: DAA01941.1.
    BK001684 mRNA. Translation: DAA01943.1.
    CCDSiCCDS41664.1. [O95197-4]
    CCDS58141.1. [O95197-1]
    CCDS58142.1. [O95197-7]
    CCDS58143.1. [O95197-6]
    CCDS8048.1. [O95197-5]
    CCDS8049.1. [O95197-3]
    CCDS8050.1. [O95197-2]
    RefSeqiNP_001252518.1. NM_001265589.1. [O95197-1]
    NP_001252519.1. NM_001265590.1. [O95197-7]
    NP_001252520.1. NM_001265591.1. [O95197-6]
    NP_006045.1. NM_006054.3. [O95197-3]
    NP_958831.1. NM_201428.2. [O95197-2]
    NP_958832.1. NM_201429.2. [O95197-4]
    NP_958833.1. NM_201430.2. [O95197-5]
    UniGeneiHs.743229.

    Genome annotation databases

    EnsembliENST00000339997; ENSP00000344106; ENSG00000133318. [O95197-2]
    ENST00000341307; ENSP00000340903; ENSG00000133318. [O95197-5]
    ENST00000354497; ENSP00000346492; ENSG00000133318. [O95197-6]
    ENST00000356000; ENSP00000348279; ENSG00000133318. [O95197-4]
    ENST00000377819; ENSP00000367050; ENSG00000133318. [O95197-1]
    ENST00000537981; ENSP00000440874; ENSG00000133318. [O95197-3]
    ENST00000540798; ENSP00000442733; ENSG00000133318. [O95197-7]
    GeneIDi10313.
    KEGGihsa:10313.
    UCSCiuc001nxm.3. human. [O95197-4]
    uc001nxn.3. human. [O95197-2]
    uc001nxo.3. human. [O95197-3]
    uc001nxp.3. human. [O95197-5]
    uc001nxq.3. human. [O95197-1]
    uc010rmu.2. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF059524 mRNA. Translation: AAC99319.1 .
    AF059529
    , AF059525 , AF059526 , AF059527 , AF059528 Genomic DNA. Translation: AAD20951.1 .
    AF119297 mRNA. Translation: AAD26810.1 .
    AY427821 mRNA. Translation: AAR02474.1 .
    AY750848 mRNA. Translation: AAU81930.1 .
    AP000753 Genomic DNA. No translation available.
    AP006289 Genomic DNA. No translation available.
    AK297529 mRNA. Translation: BAH12606.1 .
    AB209771 mRNA. Translation: BAD93008.1 . Different initiation.
    AK075412 mRNA. Translation: BAG52134.1 .
    AK222898 mRNA. Translation: BAD96618.1 .
    AK295361 mRNA. Translation: BAH12044.1 .
    CH471076 Genomic DNA. Translation: EAW74170.1 .
    BC000634 mRNA. Translation: AAH00634.1 .
    BC010556 mRNA. Translation: AAH10556.1 .
    BC011394 mRNA. Translation: AAH11394.1 .
    BC022993 mRNA. Translation: AAH22993.1 .
    BC100822 mRNA. Translation: AAI00823.1 .
    BC100823 mRNA. Translation: AAI00824.1 .
    BC105981 mRNA. Translation: AAI05982.1 .
    BC105982 mRNA. Translation: AAI05983.1 .
    BC118628 mRNA. Translation: AAI18629.1 .
    BC118550 mRNA. Translation: AAI18551.1 .
    BK001685 mRNA. Translation: DAA01931.1 .
    BK001681 mRNA. Translation: DAA01941.1 .
    BK001684 mRNA. Translation: DAA01943.1 .
    CCDSi CCDS41664.1. [O95197-4 ]
    CCDS58141.1. [O95197-1 ]
    CCDS58142.1. [O95197-7 ]
    CCDS58143.1. [O95197-6 ]
    CCDS8048.1. [O95197-5 ]
    CCDS8049.1. [O95197-3 ]
    CCDS8050.1. [O95197-2 ]
    RefSeqi NP_001252518.1. NM_001265589.1. [O95197-1 ]
    NP_001252519.1. NM_001265590.1. [O95197-7 ]
    NP_001252520.1. NM_001265591.1. [O95197-6 ]
    NP_006045.1. NM_006054.3. [O95197-3 ]
    NP_958831.1. NM_201428.2. [O95197-2 ]
    NP_958832.1. NM_201429.2. [O95197-4 ]
    NP_958833.1. NM_201430.2. [O95197-5 ]
    UniGenei Hs.743229.

    3D structure databases

    ProteinModelPortali O95197.
    SMRi O95197. Positions 894-959.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115598. 15 interactions.
    IntActi O95197. 12 interactions.
    MINTi MINT-5000642.

    PTM databases

    PhosphoSitei O95197.

    Proteomic databases

    MaxQBi O95197.
    PaxDbi O95197.
    PRIDEi O95197.

    Protocols and materials databases

    DNASUi 10313.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339997 ; ENSP00000344106 ; ENSG00000133318 . [O95197-2 ]
    ENST00000341307 ; ENSP00000340903 ; ENSG00000133318 . [O95197-5 ]
    ENST00000354497 ; ENSP00000346492 ; ENSG00000133318 . [O95197-6 ]
    ENST00000356000 ; ENSP00000348279 ; ENSG00000133318 . [O95197-4 ]
    ENST00000377819 ; ENSP00000367050 ; ENSG00000133318 . [O95197-1 ]
    ENST00000537981 ; ENSP00000440874 ; ENSG00000133318 . [O95197-3 ]
    ENST00000540798 ; ENSP00000442733 ; ENSG00000133318 . [O95197-7 ]
    GeneIDi 10313.
    KEGGi hsa:10313.
    UCSCi uc001nxm.3. human. [O95197-4 ]
    uc001nxn.3. human. [O95197-2 ]
    uc001nxo.3. human. [O95197-3 ]
    uc001nxp.3. human. [O95197-5 ]
    uc001nxq.3. human. [O95197-1 ]
    uc010rmu.2. human.

    Organism-specific databases

    CTDi 10313.
    GeneCardsi GC11P063448.
    H-InvDB HIX0021346.
    HGNCi HGNC:10469. RTN3.
    HPAi HPA015649.
    HPA015650.
    MIMi 604249. gene.
    neXtProti NX_O95197.
    PharmGKBi PA34882.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG303514.
    HOVERGENi HBG093922.
    InParanoidi O95197.
    OMAi RIYKSVV.
    OrthoDBi EOG7CZK7J.
    PhylomeDBi O95197.
    TreeFami TF105431.

    Miscellaneous databases

    ChiTaRSi RTN3. human.
    GeneWikii RTN3.
    GenomeRNAii 10313.
    NextBioi 39085.
    PROi O95197.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95197.
    Bgeei O95197.
    Genevestigatori O95197.

    Family and domain databases

    InterProi IPR003388. Reticulon.
    [Graphical view ]
    PANTHERi PTHR10994. PTHR10994. 1 hit.
    Pfami PF02453. Reticulon. 1 hit.
    [Graphical view ]
    PROSITEi PS50845. RETICULON. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a novel member of the reticulon gene family (RTN3): gene structure and chromosomal localization to 11q13."
      Moreira E.F., Jaworski C.J., Rodriguez I.R.
      Genomics 58:73-81(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
      Tissue: Retina.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), HOMODIMERIZATION, INTERACTION WITH RTN4, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    3. "Overexpression of human reticulon 3 (hRTN3) in astrocytoma."
      Huang X., Yang H., Zhou Y., Liu J., Yin B., Peng X., Qiang B., Yuan J.
      Clin. Neuropathol. 23:1-7(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
    4. "Identification of a new RTN3 transcript, RTN3-A1, and its distribution in adult mouse brain."
      Cai Y., Saiyin H., Lin Q., Zhang P., Tang L., Pan X., Yu L.
      Brain Res. Mol. Brain Res. 138:236-243(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, VARIANT GLU-6.
      Tissue: Brain.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
      Tissue: Brain and Corpus callosum.
    6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Kidney.
    7. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain, Eye and Lymph.
    11. "A reticular rhapsody: phylogenic evolution and nomenclature of the RTN/Nogo gene family."
      Oertle T., Klinger M., Stuermer C.A.O., Schwab M.E.
      FASEB J. 17:1238-1247(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION (ISOFORMS 3; 4 AND 5).
    12. "Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation."
      He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.
      Nat. Med. 10:959-965(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BACE1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
    13. "Reticulon 3 is involved in membrane trafficking between the endoplasmic reticulum and Golgi."
      Wakana Y., Koyama S., Nakajima K., Hatsuzawa K., Nagahama M., Tani K., Hauri H.-P., Melancon P., Tagaya M.
      Biochem. Biophys. Res. Commun. 334:1198-1205(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION, SUBCELLULAR LOCATION, FUNCTION.
    14. Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4).
    15. "Adaptor FADD is recruited by RTN3/HAP in ER-bound signaling complexes."
      Xiang R., Liu Y., Zhu L., Dong W., Qi Y.
      Apoptosis 11:1923-1932(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FADD, SUBCELLULAR LOCATION, FUNCTION.
    16. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid beta-protein."
      Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.
      Eur. J. Neurosci. 24:1237-1244(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BACE1 AND BACE2.
    18. "Mapping of interaction domains mediating binding between BACE1 and RTN/Nogo proteins."
      He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.
      J. Mol. Biol. 363:625-634(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMODIMERIZATION, INTERACTION WITH BACE1 AND RTN4, SUBCELLULAR LOCATION.
    19. "Reticulon 3 mediates Bcl-2 accumulation in mitochondria in response to endoplasmic reticulum stress."
      Wan Q., Kuang E., Dong W., Zhou S., Xu H., Qi Y., Liu Y.
      Apoptosis 12:319-328(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ER STRESS, INTERACTION WITH BCL2, SUBCELLULAR LOCATION, FUNCTION.
    20. "Reticulon 3 binds the 2C protein of enterovirus 71 and is required for viral replication."
      Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H., Lin K.-H., Lai H.-C., Tang P., Horng J.-T.
      J. Biol. Chem. 282:5888-5898(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COXSACKIEVIRUS A16 P2C; POLIOVIRUS P2C AND ENTEROVIRUS 71 P2C, SUBCELLULAR LOCATION.
    21. "The membrane topology of RTN3 and its effect on binding of RTN3 to BACE1."
      He W., Shi Q., Hu X., Yan R.
      J. Biol. Chem. 282:29144-29151(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649 AND SER-650, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    24. "A class of dynamin-like GTPases involved in the generation of the tubular ER network."
      Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A., Rapoport T.A., Blackstone C.
      Cell 138:549-561(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATL2.
    25. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRTN3_HUMAN
    AccessioniPrimary (citable) accession number: O95197
    Secondary accession number(s): B3KQS2
    , B7Z308, B7Z4M0, F5H774, Q147U9, Q496K2, Q53GN3, Q59EP0, Q5UEP2, Q6T930, Q7RTM7, Q7RTM8, Q7RTN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3