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Q9NQC3 (RTN4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Reticulon-4
Alternative name(s):
Foocen
Neurite outgrowth inhibitor
Short name=Nogo protein
Neuroendocrine-specific protein
Short name=NSP
Neuroendocrine-specific protein C homolog
RTN-x
Reticulon-5
Gene names
Name:RTN4
Synonyms:KIAA0886, NOGO
ORF Names:My043, SP1507
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1192 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. Isoform 2 reduces the anti-apoptotic activity of Bcl-xl and Bcl-2. This is likely consecutive to their change in subcellular location, from the mitochondria to the endoplasmic reticulum, after binding and sequestration. Isoform 2 and isoform 3 inhibit BACE1 activity and amyloid precursor protein processing. Ref.18 Ref.19 Ref.24

Subunit structure

Binds to RTN4R. Interacts with Bcl-xl and Bcl-2. Isoform 2 binds to NGBR and RTN3. Isoform 2 and isoform 3 interact with BACE1 and BACE2. Interacts with RTN4IP1. Interacts with ATL1. Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.30

Subcellular location

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

Tissue specificity

Isoform 1 is specifically expressed in brain and testis and weakly in heart and skeletal muscle. Isoform 2 is widely expressed except for the liver. Isoform 3 is expressed in brain, skeletal muscle and adipocytes. Isoform 4 is testis-specific.

Domain

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.

Sequence similarities

Contains 1 reticulon domain.

Sequence caution

The sequence AAD39920.1 differs from that shown. Reason: Frameshift at positions 1149 and 1156.

The sequence AAG43160.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAG43160.1 differs from that shown. Reason: Frameshift at positions 684 and 700.

The sequence BAA74909.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processNeurogenesis
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Non-traceable author statement Ref.3. Source: UniProtKB

axonal fasciculation

Inferred from sequence or structural similarity. Source: UniProtKB

cardiac epithelial to mesenchymal transition

Inferred from electronic annotation. Source: Ensembl

cerebral cortex radial glia guided migration

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum tubular network organization

Inferred from mutant phenotype PubMed 18779370. Source: UniProtKB

negative regulation of axon extension

Inferred from direct assay Ref.18. Source: UniProtKB

negative regulation of axonogenesis

Traceable author statement. Source: Reactome

negative regulation of cell growth

Inferred from mutant phenotype PubMed 20463223. Source: DFLAT

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

regulation of apoptotic process

Non-traceable author statement Ref.3. Source: UniProtKB

regulation of axonogenesis

Traceable author statement. Source: Reactome

regulation of branching morphogenesis of a nerve

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell migration

Inferred from direct assay PubMed 15034570. Source: MGI

   Cellular_componentcell projection

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Non-traceable author statement Ref.3. Source: UniProtKB

integral component of endoplasmic reticulum membrane

Inferred from direct assay Ref.18. Source: UniProtKB

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nuclear envelope

Inferred from direct assay Ref.3. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.30. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NQC3-1)

Also known as: RTN 4A; Nogo-A; RTN-xL;

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.
Isoform 2 (identifier: Q9NQC3-2)

Also known as: RTN 4B; ASY; Nogo-B; RTN-xS; Foocen-M;

The sequence of this isoform differs from the canonical sequence as follows:
     186-1004: Missing.
Isoform 3 (identifier: Q9NQC3-3)

Also known as: RTN 4C; Nogo-C; Foocen-S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-993: Missing.
     994-1004: AIFSAELSKTS → MDGQKKNWKDK
Isoform 4 (identifier: Q9NQC3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     58-289: Missing.
Isoform 5 (identifier: Q9NQC3-5)

Also known as: RTN4-B2;

The sequence of this isoform differs from the canonical sequence as follows:
     205-1004: Missing.
Isoform 6 (identifier: Q9NQC3-6)

Also known as: Rtn-T;

The sequence of this isoform differs from the canonical sequence as follows:
     1-206: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11921192Reticulon-4
PRO_0000168165

Regions

Topological domain1 – 10181018Cytoplasmic Potential
Transmembrane1019 – 103921Helical; Potential
Topological domain1040 – 113394Lumenal Potential
Transmembrane1134 – 115421Helical; Potential
Topological domain1155 – 119238Cytoplasmic Potential
Domain1005 – 1192188Reticulon
Compositional bias30 – 4718Poly-Glu
Compositional bias143 – 1486Poly-Pro

Amino acid modifications

Modified residue11N-acetylmethionine Ref.16 Ref.29 Ref.31 Ref.34 Ref.36 Ref.38
Modified residue71Phosphoserine Ref.23 Ref.34
Modified residue151Phosphoserine Ref.16 Ref.34 Ref.36
Modified residue1071Phosphoserine Ref.23 Ref.36
Modified residue1521Phosphoserine By similarity
Modified residue1811Phosphoserine Ref.28
Modified residue1821Phosphoserine Ref.28
Modified residue3611Phosphoserine By similarity
Modified residue5111Phosphoserine By similarity
Modified residue11041N6-acetyllysine Ref.33

Natural variations

Alternative sequence1 – 993993Missing in isoform 3.
VSP_005652
Alternative sequence1 – 206206Missing in isoform 6.
VSP_037112
Alternative sequence58 – 289232Missing in isoform 4.
VSP_005654
Alternative sequence186 – 1004819Missing in isoform 2.
VSP_005655
Alternative sequence205 – 1004800Missing in isoform 5.
VSP_037113
Alternative sequence994 – 100411AIFSAELSKTS → MDGQKKNWKDK in isoform 3.
VSP_005653
Natural variant3571D → V.
Corresponds to variant rs11677099 [ dbSNP | Ensembl ].
VAR_053633
Natural variant4291L → V in a colorectal cancer sample; somatic mutation. Ref.39
VAR_035904
Natural variant8991E → Q.
Corresponds to variant rs6757519 [ dbSNP | Ensembl ].
VAR_053634
Natural variant9201S → C.
Corresponds to variant rs6757705 [ dbSNP | Ensembl ].
VAR_053635

Experimental info

Sequence conflict1071S → C in BAA83712. Ref.6
Sequence conflict1351E → Q in BAA83712. Ref.6
Sequence conflict4581S → P in CAB99248. Ref.2
Sequence conflict5641N → S in AAK20831. Ref.4

Secondary structure

......... 1192
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RTN 4A) (Nogo-A) (RTN-xL) [UniParc].

Last modified November 16, 2001. Version 2.
Checksum: CDE239BBF31589CA

FASTA1,192129,931
        10         20         30         40         50         60 
MEDLDQSPLV SSSDSPPRPQ PAFKYQFVRE PEDEEEEEEE EEEDEDEDLE ELEVLERKPA 

        70         80         90        100        110        120 
AGLSAAPVPT APAAGAPLMD FGNDFVPPAP RGPLPAAPPV APERQPSWDP SPVSSTVPAP 

       130        140        150        160        170        180 
SPLSAAAVSP SKLPEDDEPP ARPPPPPPAS VSPQAEPVWT PPAPAPAAPP STPAAPKRRG 

       190        200        210        220        230        240 
SSGSVDETLF ALPAASEPVI RSSAENMDLK EQPGNTISAG QEDFPSVLLE TAASLPSLSP 

       250        260        270        280        290        300 
LSAASFKEHE YLGNLSTVLP TEGTLQENVS EASKEVSEKA KTLLIDRDLT EFSELEYSEM 

       310        320        330        340        350        360 
GSSFSVSPKA ESAVIVANPR EEIIVKNKDE EEKLVSNNIL HNQQELPTAL TKLVKEDEVV 

       370        380        390        400        410        420 
SSEKAKDSFN EKRVAVEAPM REEYADFKPF ERVWEVKDSK EDSDMLAAGG KIESNLESKV 

       430        440        450        460        470        480 
DKKCFADSLE QTNHEKDSES SNDDTSFPST PEGIKDRSGA YITCAPFNPA ATESIATNIF 

       490        500        510        520        530        540 
PLLGDPTSEN KTDEKKIEEK KAQIVTEKNT STKTSNPFLV AAQDSETDYV TTDNLTKVTE 

       550        560        570        580        590        600 
EVVANMPEGL TPDLVQEACE SELNEVTGTK IAYETKMDLV QTSEVMQESL YPAAQLCPSF 

       610        620        630        640        650        660 
EESEATPSPV LPDIVMEAPL NSAVPSAGAS VIQPSSSPLE ASSVNYESIK HEPENPPPYE 

       670        680        690        700        710        720 
EAMSVSLKKV SGIKEEIKEP ENINAALQET EAPYISIACD LIKETKLSAE PAPDFSDYSE 

       730        740        750        760        770        780 
MAKVEQPVPD HSELVEDSSP DSEPVDLFSD DSIPDVPQKQ DETVMLVKES LTETSFESMI 

       790        800        810        820        830        840 
EYENKEKLSA LPPEGGKPYL ESFKLSLDNT KDTLLPDEVS TLSKKEKIPL QMEELSTAVY 

       850        860        870        880        890        900 
SNDDLFISKE AQIRETETFS DSSPIEIIDE FPTLISSKTD SFSKLAREYT DLEVSHKSEI 

       910        920        930        940        950        960 
ANAPDGAGSL PCTELPHDLS LKNIQPKVEE KISFSDDFSK NGSATSKVLL LPPDVSALAT 

       970        980        990       1000       1010       1020 
QAEIESIVKP KVLVKEAEKK LPSDTEKEDR SPSAIFSAEL SKTSVVDLLY WRDIKKTGVV 

      1030       1040       1050       1060       1070       1080 
FGASLFLLLS LTVFSIVSVT AYIALALLSV TISFRIYKGV IQAIQKSDEG HPFRAYLESE 

      1090       1100       1110       1120       1130       1140 
VAISEELVQK YSNSALGHVN CTIKELRRLF LVDDLVDSLK FAVLMWVFTY VGALFNGLTL 

      1150       1160       1170       1180       1190 
LILALISLFS VPVIYERHQA QIDHYLGLAN KNVKDAMAKI QAKIPGLKRK AE 

« Hide

Isoform 2 (RTN 4B) (ASY) (Nogo-B) (RTN-xS) (Foocen-M) [UniParc].

Checksum: 8A19379EF91A59B4
Show »

FASTA37340,318
Isoform 3 (RTN 4C) (Nogo-C) (Foocen-S) [UniParc].

Checksum: C60161DF3FB34D80
Show »

FASTA19922,395
Isoform 4 [UniParc].

Checksum: 51B5E94CF103BA74
Show »

FASTA960106,360
Isoform 5 (RTN4-B2) [UniParc].

Checksum: D7B2AA5E839E58AD
Show »

FASTA39242,274
Isoform 6 (Rtn-T) [UniParc].

Checksum: 0CDE8F647036415A
Show »

FASTA986108,450

References

« Hide 'large scale' references
[1]"Assignment of the human reticulon 4 gene (RTN4) to chromosome 2p14-->2p13 by radiation hybrid mapping."
Yang J., Yu L., Bi A.D., Zhao S.-Y.
Cytogenet. Cell Genet. 88:101-102(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
[2]"Inhibitor of neurite outgrowth in humans."
Prinjha R., Moore S.E., Vinson M., Blake S., Morrow R., Christie G., Michalovich D., Simmons D.L., Walsh F.S.
Nature 403:383-384(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
[3]"A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity."
Tagami S., Eguchi Y., Kinoshita M., Takeda M., Tsujimoto Y.
Oncogene 19:5736-5746(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[4]"Expression of a novel reticulon-like gene in human testis."
Zhou Z.M., Sha J.H., Li J.M., Lin M., Zhu H., Zhou Y.D., Wang L.R., Zhu H., Wang Y.Q., Zhou K.Y.
Reproduction 123:227-234(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
Tissue: Testis.
[5]"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; 2; 3; 5 AND 6).
[6]"Isolation of a cell death-inducing gene."
Yutsudo M.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Fibroblast.
[7]"Human neuroendocrine-specific protein C (NSP) homolog gene."
Song H., Peng Y., Zhou J., Huang Q., Dai M., Mao Y.M., Yu Y., Xu X., Luo B., Hu R., Chen J.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Pituitary.
[8]"Cloning of a member of the reticulon gene family in human."
Ito T., Schwartz S.M.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Tissue: Placenta and Skeletal muscle.
[9]"Developmentally-regulated alternative splicing in a novel Nogo-A."
Jin W.-L., Ju G.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[10]"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[11]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Umbilical cord blood.
[12]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[13]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]"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] (ISOFORMS 2; 3 AND 5).
Tissue: Brain, Eye, Kidney, Ovary, Pancreas, Placenta and Skeletal muscle.
[16]Bienvenut W.V.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-24; 92-104; 1075-1090 AND 1158-1171, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[17]Mao Y.M., Xie Y., Zheng Z.H.
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-1192 (ISOFORMS 1/4).
Tissue: Fetal brain.
[18]"Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein."
GrandPre T., Nakamura F., Vartanian T., Strittmatter S.M.
Nature 403:439-444(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY, FUNCTION.
Tissue: Brain.
[19]"Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration."
Fournier A.E., GrandPre T., Strittmatter S.M.
Nature 409:341-346(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Tissue: Brain.
[20]"Nogos and the Nogo-66 receptor: factors inhibiting CNS neuron regeneration."
Ng C.E.L., Tang B.L.
J. Neurosci. Res. 67:559-565(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[21]"Pro-apoptotic ASY/Nogo-B protein associates with ASYIP."
Qi B., Qi Y., Watari A., Yoshioka N., Inoue H., Minemoto Y., Yamashita K., Sasagawa T., Yutsudo M.
J. Cell. Physiol. 196:312-318(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RTN3.
[22]"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.
[23]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
[25]"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: INTERACTION WITH RTN3.
[26]"Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells."
Miao R.Q., Gao Y., Harrison K.D., Prendergast J., Acevedo L.M., Yu J., Hu F., Strittmatter S.M., Sessa W.C.
Proc. Natl. Acad. Sci. U.S.A. 103:10997-11002(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NGBR.
[27]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"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 ATL1.
[31]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[33]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[34]"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 MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[35]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[36]"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 MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[37]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-429.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Protein Spotlight

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

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF087901 mRNA. Translation: AAG12205.1.
AF148537 mRNA. Translation: AAG12176.1.
AF148538 mRNA. Translation: AAG12177.1.
AJ251383 mRNA. Translation: CAB99248.1.
AJ251384 mRNA. Translation: CAB99249.1.
AJ251385 mRNA. Translation: CAB99250.1.
AB040462 mRNA. Translation: BAB18927.1.
AB040463 mRNA. Translation: BAB18928.1.
AF333336 mRNA. Translation: AAK20831.1.
AY102285 Genomic DNA. Translation: AAM64240.1.
AY102285 Genomic DNA. Translation: AAM64241.1.
AY102285 Genomic DNA. Translation: AAM64242.1.
AY102285 Genomic DNA. Translation: AAM64243.1.
AY102285 Genomic DNA. Translation: AAM64244.1.
AY102276 mRNA. Translation: AAM64245.1.
AY102277 mRNA. Translation: AAM64246.1.
AY102278 mRNA. Translation: AAM64247.1.
AY102279 mRNA. Translation: AAM64248.1.
AY123245 mRNA. Translation: AAM64249.1.
AY123246 mRNA. Translation: AAM64250.1.
AY123247 mRNA. Translation: AAM64251.1.
AY123248 mRNA. Translation: AAM64252.1.
AY123249 mRNA. Translation: AAM64253.1.
AY123250 mRNA. Translation: AAM64254.1.
AB015639 mRNA. Translation: BAA83712.1.
AF077050 mRNA. Translation: AAD27783.1.
AF132047 mRNA. Translation: AAD31021.1.
AF132048 mRNA. Translation: AAD31022.1.
AF320999 mRNA. Translation: AAG40878.1.
AB020693 mRNA. Translation: BAA74909.2. Different initiation.
AF125103 mRNA. Translation: AAD39920.1. Frameshift.
AF177332 mRNA. Translation: AAG17976.1.
AC013414 Genomic DNA. No translation available.
AC092461 Genomic DNA. No translation available.
AC093165 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00115.1.
CH471053 Genomic DNA. Translation: EAX00116.1.
CH471053 Genomic DNA. Translation: EAX00117.1.
CH471053 Genomic DNA. Translation: EAX00118.1.
CH471053 Genomic DNA. Translation: EAX00119.1.
CH471053 Genomic DNA. Translation: EAX00121.1.
CH471053 Genomic DNA. Translation: EAX00122.1.
CH471053 Genomic DNA. Translation: EAX00123.1.
CH471053 Genomic DNA. Translation: EAX00124.1.
CH471053 Genomic DNA. Translation: EAX00125.1.
CH471053 Genomic DNA. Translation: EAX00127.1.
CH471053 Genomic DNA. Translation: EAX00130.1.
CH471053 Genomic DNA. Translation: EAX00132.1.
BC001035 mRNA. Translation: AAH01035.1.
BC007109 mRNA. Translation: AAH07109.1.
BC010737 mRNA. Translation: AAH10737.1.
BC012619 mRNA. Translation: AAH12619.1.
BC014366 mRNA. Translation: AAH14366.1.
BC016165 mRNA. Translation: AAH16165.1.
BC026788 mRNA. Translation: AAH26788.1.
BC068991 mRNA. Translation: AAH68991.1.
BC150182 mRNA. Translation: AAI50183.1.
BC152425 mRNA. Translation: AAI52426.1.
BC152555 mRNA. Translation: AAI52556.1.
AF063601 mRNA. Translation: AAG43160.1. Sequence problems.
CCDSCCDS1851.1. [Q9NQC3-2]
CCDS1852.1. [Q9NQC3-6]
CCDS42683.1. [Q9NQC3-5]
CCDS42684.1. [Q9NQC3-1]
CCDS42685.1. [Q9NQC3-3]
RefSeqNP_008939.1. NM_007008.2. [Q9NQC3-3]
NP_065393.1. NM_020532.4. [Q9NQC3-1]
NP_722550.1. NM_153828.2. [Q9NQC3-2]
NP_997403.1. NM_207520.1. [Q9NQC3-5]
NP_997404.1. NM_207521.1. [Q9NQC3-6]
XP_005264491.1. XM_005264434.2. [Q9NQC3-6]
UniGeneHs.637850.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G31NMR-A1055-1114[»]
2JV5NMR-A1055-1108[»]
DisProtDP00524.
ProteinModelPortalQ9NQC3.
SMRQ9NQC3. Positions 1055-1114.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121400. 48 interactions.
IntActQ9NQC3. 26 interactions.
MINTMINT-154434.

PTM databases

PhosphoSiteQ9NQC3.

Polymorphism databases

DMDM17369290.

Proteomic databases

MaxQBQ9NQC3.
PaxDbQ9NQC3.
PRIDEQ9NQC3.

Protocols and materials databases

DNASU57142.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317610; ENSP00000322147; ENSG00000115310. [Q9NQC3-2]
ENST00000337526; ENSP00000337838; ENSG00000115310. [Q9NQC3-1]
ENST00000357376; ENSP00000349944; ENSG00000115310. [Q9NQC3-6]
ENST00000357732; ENSP00000350365; ENSG00000115310. [Q9NQC3-5]
ENST00000394609; ENSP00000378107; ENSG00000115310. [Q9NQC3-3]
ENST00000394611; ENSP00000378109; ENSG00000115310. [Q9NQC3-6]
ENST00000404909; ENSP00000385650; ENSG00000115310. [Q9NQC3-6]
ENST00000405240; ENSP00000384471; ENSG00000115310. [Q9NQC3-6]
GeneID57142.
KEGGhsa:57142.
UCSCuc002ryc.3. human. [Q9NQC3-3]
uc002ryd.3. human. [Q9NQC3-1]
uc002ryf.3. human. [Q9NQC3-5]
uc002ryg.3. human. [Q9NQC3-2]

Organism-specific databases

CTD57142.
GeneCardsGC02M055199.
H-InvDBHIX0002059.
HGNCHGNC:14085. RTN4.
HPACAB005388.
HPA023977.
MIM604475. gene.
neXtProtNX_Q9NQC3.
PharmGKBPA34883.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG306139.
HOVERGENHBG023134.
InParanoidQ9NQC3.
OMANIHRVAT.
OrthoDBEOG7CZK7J.
PhylomeDBQ9NQC3.
TreeFamTF105431.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ9NQC3.
BgeeQ9NQC3.
GenevestigatorQ9NQC3.

Family and domain databases

InterProIPR003388. Reticulon.
[Graphical view]
PANTHERPTHR10994. PTHR10994. 1 hit.
PfamPF02453. Reticulon. 1 hit.
[Graphical view]
PROSITEPS50845. RETICULON. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRTN4. human.
EvolutionaryTraceQ9NQC3.
GeneWikiReticulon_4.
GenomeRNAi57142.
NextBio63075.
PMAP-CutDBQ9NQC3.
PROQ9NQC3.
SOURCESearch...

Entry information

Entry nameRTN4_HUMAN
AccessionPrimary (citable) accession number: Q9NQC3
Secondary accession number(s): O94962 expand/collapse secondary AC list , Q7L7Q5, Q7L7Q6, Q7L7Q8, Q8IUA4, Q96B16, Q9BXG5, Q9H212, Q9H3I3, Q9UQ42, Q9Y293, Q9Y2Y7, Q9Y5U6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: November 16, 2001
Last modified: July 9, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM