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Q99P72

- RTN4_MOUSE

UniProt

Q99P72 - RTN4_MOUSE

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Protein

Reticulon-4

Gene

Rtn4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. poly(A) RNA binding Source: Ensembl

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
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  4. integral component of endoplasmic reticulum membrane Source: UniProtKB
  5. neuronal cell body Source: MGI
  6. nuclear envelope Source: UniProtKB
Complete GO annotation...

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

BgeeiQ99P72.
CleanExiMM_RTN4.
ExpressionAtlasiQ99P72. baseline and differential.
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) [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

        10         20         30         40         50
MEDIDQSSLV SSSADSPPRP PPAFKYQFVT EPEDEEDEED EEEEEDDEDL
60 70 80 90 100
EELEVLERKP AAGLSAAPVP PAAAPLLDFS SDSVPPAPRG PLPAAPPTAP
110 120 130 140 150
ERQPSWERSP AASAPSLPPA AAVLPSKLPE DDEPPARPPA PAGASPLAEP
160 170 180 190 200
AAPPSTPAAP KRRGSGSVDE TLFALPAASE PVIPSSAEKI MDLKEQPGNT
210 220 230 240 250
VSSGQEDFPS VLFETAASLP SLSPLSTVSF KEHGYLGNLS AVASTEGTIE
260 270 280 290 300
ETLNEASREL PERATNPFVN RESAEFSVLE YSEMGSSFNG SPKGESAMLV
310 320 330 340 350
ENTKEEVIVR SKDKEDLVCS AALHNPQESP ATLTKVVKED GVMSPEKTMD
360 370 380 390 400
IFNEMKMSVV APVREEYADF KPFEQAWEVK DTYEGSRDVL AARANMESKV
410 420 430 440 450
DKKCFEDSLE QKGHGKDSES RNENASFPRT PELVKDGSRA YITCDSFSSA
460 470 480 490 500
TESTAANIFP VLEDHTSENK TDEKKIEERK AQIITEKTSP KTSNPFLVAI
510 520 530 540 550
HDSEADYVTT DNLSKVTEAV VATMPEGLTP DLVQEACESE LNEATGTKIA
560 570 580 590 600
YETKVDLVQT SEAIQESIYP TAQLCPSFEE AEATPSPVLP DIVMEAPLNS
610 620 630 640 650
LLPSTGASVA QPSASPLEVP SPVSYDGIKL EPENPPPYEE AMSVALKTSD
660 670 680 690 700
SKEEIKEPES FNAAAQEAEA PYISIACDLI KETKLSTEPS PEFSNYSEIA
710 720 730 740 750
KFEKSVPDHC ELVDDSSPES EPVDLFSDDS IPEVPQTQEE AVMLMKESLT
760 770 780 790 800
EVSETVTQHK HKERLSASPQ EVGKPYLESF QPNLHITKDA ASNEIPTLTK
810 820 830 840 850
KETISLQMEE FNTAIYSNDD LLSSKEDKMK ESETFSDSSP IEIIDEFPTF
860 870 880 890 900
VSAKDDSPKE YTDLEVSNKS EIANVQSGAN SLPCSELPCD LSFKNTYPKD
910 920 930 940 950
EAHVSDEFSK SRSSVSKVPL LLPNVSALES QIEMGNIVKP KVLTKEAEEK
960 970 980 990 1000
LPSDTEKEDR SLTAVLSAEL NKTSVVDLLY WRDIKKTGVV FGASLFLLLS
1010 1020 1030 1040 1050
LTVFSIVSVT AYIALALLSV TISFRIYKGV IQAIQKSDEG HPFRAYLESE
1060 1070 1080 1090 1100
VAISEELVQK YSNSALGHVN STIKELRRLF LVDDLVDSLK FAVLMWVFTY
1110 1120 1130 1140 1150
VGALFNGLTL LILALISLFS IPVIYERHQA QIDHYLGLAN KSVKDAMAKI
1160
QAKIPGLKRK AE
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

Bgeei Q99P72.
CleanExi MM_RTN4.
ExpressionAtlasi Q99P72. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 125 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