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Q99P72

- RTN4_MOUSE

UniProt

Q99P72 - RTN4_MOUSE

Protein

Reticulon-4

Gene

Rtn4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (02 May 2006)
      Previous versions | rss
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    Functioni

    Developmental neurite growth regulatory factor with a role as a negative regulator of axon-axon adhesion and growth, and as a facilitator of neurite branching. Regulates neurite fasciculation, branching and extension in the developing nervous system. Involved in down-regulation of growth, stabilization of wiring and restriction of plasticity in the adult CNS. Regulates the radial migration of cortical neurons via an RTN4R-LINGO1 containing receptor complex. May inhibit BACE1 activity and amyloid precursor protein processing.2 Publications

    GO - Molecular functioni

    1. protein binding Source: MGI

    GO - Biological processi

    1. angiogenesis Source: MGI
    2. axonal fasciculation Source: UniProtKB
    3. cardiac epithelial to mesenchymal transition Source: MGI
    4. cerebral cortex radial glia guided migration Source: UniProtKB
    5. endoplasmic reticulum tubular network organization Source: Ensembl
    6. negative regulation of axon extension Source: UniProtKB
    7. nervous system development Source: MGI
    8. regulation of branching morphogenesis of a nerve Source: UniProtKB
    9. regulation of cell migration Source: Ensembl
    10. regulation of nervous system development Source: UniProtKB

    Keywords - Biological processi

    Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_203657. Axonal growth inhibition (RHOA activation).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Reticulon-4
    Alternative name(s):
    Neurite outgrowth inhibitor
    Short name:
    Nogo protein
    Gene namesi
    Name:Rtn4
    Synonyms:Kiaa0886, Nogo
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1915835. Rtn4.

    Subcellular locationi

    Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
    Note: Anchored to the membrane of the endoplasmic reticulum through 2 putative transmembrane domains.By similarity

    GO - Cellular componenti

    1. cell projection Source: MGI
    2. endoplasmic reticulum Source: MGI
    3. integral component of endoplasmic reticulum membrane Source: UniProtKB
    4. neuronal cell body Source: MGI
    5. nuclear envelope Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Embryos show defects in the development of fore- and hindlimb innervation. Increased fasciculation and decreased branching of nerves innervating fore- and hindlimbs seen. Disturbances of the radial migration pattern of neuronal precursor cells seen in embryonic cortex.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11621162Reticulon-4PRO_0000168166Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei7 – 71PhosphoserineBy similarity
    Modified residuei16 – 161Phosphoserine1 Publication
    Modified residuei105 – 1051Phosphoserine1 Publication
    Modified residuei145 – 1451Phosphoserine2 Publications
    Modified residuei165 – 1651PhosphoserineBy similarity
    Modified residuei344 – 3441Phosphoserine1 Publication
    Modified residuei489 – 4891Phosphoserine1 Publication
    Modified residuei690 – 6901Phosphoserine1 Publication
    Modified residuei1074 – 10741N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ99P72.
    PaxDbiQ99P72.
    PRIDEiQ99P72.

    PTM databases

    PhosphoSiteiQ99P72.

    Expressioni

    Developmental stagei

    Expressed in radial glial cells, migrating postmitotic as well as postmigratory neurons of the embryonic cortex.1 Publication

    Gene expression databases

    ArrayExpressiQ99P72.
    BgeeiQ99P72.
    CleanExiMM_RTN4.
    GenevestigatoriQ99P72.

    Interactioni

    Subunit structurei

    Binds to RTN4R. Interacts with Bcl-xl and Bcl-2. Interacts in trans with CNTNAP1. Interacts with ATL1 By similarity. Interacts with RTN4IP1.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi212938. 6 interactions.
    DIPiDIP-41976N.
    IntActiQ99P72. 3 interactions.
    MINTiMINT-188330.
    STRINGi10090.ENSMUSP00000099907.

    Structurei

    Secondary structure

    1
    1162
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1026 – 10294
    Helixi1031 – 10355
    Turni1037 – 10404
    Helixi1044 – 105310
    Helixi1057 – 10637
    Turni1065 – 10673
    Helixi1068 – 108215
    Helixi1087 – 10893

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KO2NMR-A1025-1090[»]
    ProteinModelPortaliQ99P72.
    SMRiQ99P72. Positions 1025-1090.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99P72.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 988988CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1010 – 107869LumenalSequence AnalysisAdd
    BLAST
    Topological domaini1100 – 116263CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei989 – 100921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1079 – 109921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini975 – 1162188ReticulonPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi31 – 5727Glu-richAdd
    BLAST
    Compositional biasi68 – 16093Pro-richAdd
    BLAST

    Domaini

    Three regions, residues 59-172, 544-725 and the loop 66 amino acids, between the two transmembrane domains, known as Nogo-66 loop, appear to be responsible for the inhibitory effect on neurite outgrowth and the spreading of neurons. This Nogo-66 loop, mediates also the binding of RTN4 to its receptor By similarity.By similarity

    Sequence similaritiesi

    Contains 1 reticulon domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG306139.
    GeneTreeiENSGT00390000009934.
    HOVERGENiHBG023134.
    InParanoidiQ99P72.
    OMAiHTSENKT.
    OrthoDBiEOG7CZK7J.
    PhylomeDBiQ99P72.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99P72-2) [UniParc]FASTAAdd to Basket

    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

    MEDIDQSSLV SSSADSPPRP PPAFKYQFVT EPEDEEDEED EEEEEDDEDL     50
    EELEVLERKP AAGLSAAPVP PAAAPLLDFS SDSVPPAPRG PLPAAPPTAP 100
    ERQPSWERSP AASAPSLPPA AAVLPSKLPE DDEPPARPPA PAGASPLAEP 150
    AAPPSTPAAP KRRGSGSVDE TLFALPAASE PVIPSSAEKI MDLKEQPGNT 200
    VSSGQEDFPS VLFETAASLP SLSPLSTVSF KEHGYLGNLS AVASTEGTIE 250
    ETLNEASREL PERATNPFVN RESAEFSVLE YSEMGSSFNG SPKGESAMLV 300
    ENTKEEVIVR SKDKEDLVCS AALHNPQESP ATLTKVVKED GVMSPEKTMD 350
    IFNEMKMSVV APVREEYADF KPFEQAWEVK DTYEGSRDVL AARANMESKV 400
    DKKCFEDSLE QKGHGKDSES RNENASFPRT PELVKDGSRA YITCDSFSSA 450
    TESTAANIFP VLEDHTSENK TDEKKIEERK AQIITEKTSP KTSNPFLVAI 500
    HDSEADYVTT DNLSKVTEAV VATMPEGLTP DLVQEACESE LNEATGTKIA 550
    YETKVDLVQT SEAIQESIYP TAQLCPSFEE AEATPSPVLP DIVMEAPLNS 600
    LLPSTGASVA QPSASPLEVP SPVSYDGIKL EPENPPPYEE AMSVALKTSD 650
    SKEEIKEPES FNAAAQEAEA PYISIACDLI KETKLSTEPS PEFSNYSEIA 700
    KFEKSVPDHC ELVDDSSPES EPVDLFSDDS IPEVPQTQEE AVMLMKESLT 750
    EVSETVTQHK HKERLSASPQ EVGKPYLESF QPNLHITKDA ASNEIPTLTK 800
    KETISLQMEE FNTAIYSNDD LLSSKEDKMK ESETFSDSSP IEIIDEFPTF 850
    VSAKDDSPKE YTDLEVSNKS EIANVQSGAN SLPCSELPCD LSFKNTYPKD 900
    EAHVSDEFSK SRSSVSKVPL LLPNVSALES QIEMGNIVKP KVLTKEAEEK 950
    LPSDTEKEDR SLTAVLSAEL NKTSVVDLLY WRDIKKTGVV FGASLFLLLS 1000
    LTVFSIVSVT AYIALALLSV TISFRIYKGV IQAIQKSDEG HPFRAYLESE 1050
    VAISEELVQK YSNSALGHVN STIKELRRLF LVDDLVDSLK FAVLMWVFTY 1100
    VGALFNGLTL LILALISLFS IPVIYERHQA QIDHYLGLAN KSVKDAMAKI 1150
    QAKIPGLKRK AE 1162
    Length:1,162
    Mass (Da):126,613
    Last modified:May 2, 2006 - v2
    Checksum:i855697FBEE11781F
    GO
    Isoform 2 (identifier: Q99P72-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-116: Missing.
         117-169: LPPAAAVLPS...PKRRGSGSVD → MAPPLAGGGQ...RSSRLSAARN

    Show »
    Length:1,046
    Mass (Da):114,222
    Checksum:i8CE2E2238ED51222
    GO
    Isoform 3 (identifier: Q99P72-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-963: Missing.
         964-974: AVLSAELNKTS → MDDQKKRWKDK

    Show »
    Length:199
    Mass (Da):22,466
    Checksum:i07BE5D580059ED9C
    GO

    Sequence cautioni

    The sequence AAH32192.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BC056373 differs from that shown. Reason: Erroneous termination at position 721. Translated as Glu.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41I → V in BAD90301. 1 PublicationCurated
    Sequence conflicti16 – 161S → R in BAD90301. 1 PublicationCurated
    Sequence conflicti21 – 211P → L in BAD90301. 1 PublicationCurated
    Sequence conflicti67 – 671A → V in AAM77068. 1 PublicationCurated
    Sequence conflicti413 – 4131G → S in AAM77068. 1 PublicationCurated
    Sequence conflicti413 – 4131G → S in BAD90301. 1 PublicationCurated
    Sequence conflicti429 – 4291R → S in AAM77068. 1 PublicationCurated
    Sequence conflicti429 – 4291R → S in BAD90301. 1 PublicationCurated
    Sequence conflicti448 – 4481S → T in AAM77068. 1 PublicationCurated
    Sequence conflicti448 – 4481S → T in BAD90301. 1 PublicationCurated
    Sequence conflicti487 – 4904KTSP → HASA in AAH32192. (PubMed:15489334)Curated
    Sequence conflicti651 – 6511S → A in AAM77068. 1 PublicationCurated
    Sequence conflicti651 – 6511S → A in AAH32192. (PubMed:15489334)Curated
    Sequence conflicti651 – 6511S → A in BAD90301. 1 PublicationCurated
    Sequence conflicti665 – 6651A → V in BAD90301. 1 PublicationCurated
    Sequence conflicti692 – 6921E → G in AAM77068. 1 PublicationCurated
    Sequence conflicti692 – 6921E → G in BAC75974. 1 PublicationCurated
    Sequence conflicti733 – 7331E → D in BAD90301. 1 PublicationCurated
    Sequence conflicti772 – 7721V → L in BAD90301. 1 PublicationCurated
    Sequence conflicti916 – 9161S → F in BAC75974. 1 PublicationCurated
    Sequence conflicti990 – 9901V → VY in AAM77068. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 963963Missing in isoform 3. 1 PublicationVSP_018088Add
    BLAST
    Alternative sequencei1 – 116116Missing in isoform 2. 1 PublicationVSP_018089Add
    BLAST
    Alternative sequencei117 – 16953LPPAA…SGSVD → MAPPLAGGGQKGGAASEAWV PSLFVGVSGSTCTAAKSLVP IPARSSRLSAARN in isoform 2. 1 PublicationVSP_018090Add
    BLAST
    Alternative sequencei964 – 97411AVLSAELNKTS → MDDQKKRWKDK in isoform 3. 1 PublicationVSP_018091Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY102280 mRNA. Translation: AAM73502.1.
    AY102284 mRNA. Translation: AAM73506.1.
    AY102286 Genomic DNA. Translation: AAM73507.1.
    AY102286 Genomic DNA. Translation: AAM73511.1.
    AF326337 mRNA. Translation: AAK08076.1.
    AY114152 mRNA. Translation: AAM77068.1.
    AK220511 mRNA. Translation: BAD90301.1.
    AL929371 Genomic DNA. Translation: CAI24273.1.
    AL929371 Genomic DNA. Translation: CAI24274.1.
    BC032192 mRNA. Translation: AAH32192.1. Different initiation.
    BC056373 mRNA. No translation available.
    AB073672 mRNA. Translation: BAC75974.1.
    AK003859 mRNA. No translation available.
    CCDSiCCDS24501.1. [Q99P72-2]
    CCDS24502.1. [Q99P72-3]
    CCDS24503.1. [Q99P72-1]
    RefSeqiNP_077188.1. NM_024226.4. [Q99P72-1]
    NP_918940.1. NM_194051.3. [Q99P72-3]
    NP_918943.1. NM_194054.3. [Q99P72-2]
    UniGeneiMm.192580.
    Mm.440639.
    Mm.488364.

    Genome annotation databases

    EnsembliENSMUST00000060992; ENSMUSP00000053754; ENSMUSG00000020458. [Q99P72-1]
    ENSMUST00000102841; ENSMUSP00000099905; ENSMUSG00000020458. [Q99P72-3]
    ENSMUST00000102843; ENSMUSP00000099907; ENSMUSG00000020458. [Q99P72-2]
    GeneIDi68585.
    KEGGimmu:68585.
    UCSCiuc007ihk.2. mouse. [Q99P72-2]
    uc007ihn.2. mouse. [Q99P72-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Nerve regrowth: nipped by a no-go - Issue 69 of April 2006

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY102280 mRNA. Translation: AAM73502.1 .
    AY102284 mRNA. Translation: AAM73506.1 .
    AY102286 Genomic DNA. Translation: AAM73507.1 .
    AY102286 Genomic DNA. Translation: AAM73511.1 .
    AF326337 mRNA. Translation: AAK08076.1 .
    AY114152 mRNA. Translation: AAM77068.1 .
    AK220511 mRNA. Translation: BAD90301.1 .
    AL929371 Genomic DNA. Translation: CAI24273.1 .
    AL929371 Genomic DNA. Translation: CAI24274.1 .
    BC032192 mRNA. Translation: AAH32192.1 . Different initiation.
    BC056373 mRNA. No translation available.
    AB073672 mRNA. Translation: BAC75974.1 .
    AK003859 mRNA. No translation available.
    CCDSi CCDS24501.1. [Q99P72-2 ]
    CCDS24502.1. [Q99P72-3 ]
    CCDS24503.1. [Q99P72-1 ]
    RefSeqi NP_077188.1. NM_024226.4. [Q99P72-1 ]
    NP_918940.1. NM_194051.3. [Q99P72-3 ]
    NP_918943.1. NM_194054.3. [Q99P72-2 ]
    UniGenei Mm.192580.
    Mm.440639.
    Mm.488364.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KO2 NMR - A 1025-1090 [» ]
    ProteinModelPortali Q99P72.
    SMRi Q99P72. Positions 1025-1090.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212938. 6 interactions.
    DIPi DIP-41976N.
    IntActi Q99P72. 3 interactions.
    MINTi MINT-188330.
    STRINGi 10090.ENSMUSP00000099907.

    PTM databases

    PhosphoSitei Q99P72.

    Proteomic databases

    MaxQBi Q99P72.
    PaxDbi Q99P72.
    PRIDEi Q99P72.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000060992 ; ENSMUSP00000053754 ; ENSMUSG00000020458 . [Q99P72-1 ]
    ENSMUST00000102841 ; ENSMUSP00000099905 ; ENSMUSG00000020458 . [Q99P72-3 ]
    ENSMUST00000102843 ; ENSMUSP00000099907 ; ENSMUSG00000020458 . [Q99P72-2 ]
    GeneIDi 68585.
    KEGGi mmu:68585.
    UCSCi uc007ihk.2. mouse. [Q99P72-2 ]
    uc007ihn.2. mouse. [Q99P72-3 ]

    Organism-specific databases

    CTDi 57142.
    MGIi MGI:1915835. Rtn4.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG306139.
    GeneTreei ENSGT00390000009934.
    HOVERGENi HBG023134.
    InParanoidi Q99P72.
    OMAi HTSENKT.
    OrthoDBi EOG7CZK7J.
    PhylomeDBi Q99P72.
    TreeFami TF105431.

    Enzyme and pathway databases

    Reactomei REACT_203657. Axonal growth inhibition (RHOA activation).

    Miscellaneous databases

    ChiTaRSi RTN4. mouse.
    EvolutionaryTracei Q99P72.
    NextBioi 327502.
    PROi Q99P72.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99P72.
    Bgeei Q99P72.
    CleanExi MM_RTN4.
    Genevestigatori Q99P72.

    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. "Genomic structure and functional characterisation of the promoters of human and mouse nogo/rtn4."
      Oertle T., Huber C., van der Putten H., Schwab M.E.
      J. Mol. Biol. 325:299-323(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
      Strain: 129/Sv.
    2. "Mouse vp20/RTN4C cDNA."
      Coulson A.C., Craggs P.D., Morris N.J.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Adipocyte.
    3. "Cloning and expression of the mouse Nogo-A protein."
      Jin W., Long M., Li R., Ju G.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
    4. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
      Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "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 1).
      Strain: C57BL/6.
      Tissue: Brain and Mammary gland.
    7. "The partial sequence of mouse nogo-A cDNA clone#4109."
      Tozaki H., Hirata T.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 585-1162.
    8. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 975-982; 1061-1074 AND 1079-1090, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    9. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1133-1162.
      Strain: C57BL/6J.
      Tissue: Embryo.
    10. "Identification and characterization of a novel Nogo-interacting mitochondrial protein (NIMP)."
      Hu W.-H., Hausmann O.N., Yan M.-S., Walters W.M., Wong P.K.Y., Bethea J.R.
      J. Neurochem. 81:36-45(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RTN4IP1.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    12. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    13. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
      Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
      Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-344 AND SER-489, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    17. "Nogo-a regulates neural precursor migration in the embryonic mouse cortex."
      Mathis C., Schroeter A., Thallmair M., Schwab M.E.
      Cereb. Cortex 20:2380-2390(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
    18. "Neuronal Nogo-A regulates neurite fasciculation, branching and extension in the developing nervous system."
      Petrinovic M.M., Duncan C.S., Bourikas D., Weinman O., Montani L., Schroeter A., Maerki D., Sommer L., Stoeckli E.T., Schwab M.E.
      Development 137:2539-2550(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiRTN4_MOUSE
    AccessioniPrimary (citable) accession number: Q99P72
    Secondary accession number(s): Q5DTK9
    , Q7TNB7, Q80W95, Q8BGK7, Q8BGM9, Q8K290, Q8K3G8, Q9CTE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: May 2, 2006
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3