Q9NQC3 (RTN4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1192 AA.
Sequence status	Complete.
Protein existence	Evidence 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.29
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 process	Neurogenesis
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: Compara 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: Compara 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 nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome regulation of apoptotic process Non-traceable author statement Ref.3. Source: UniProtKB 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_component	cell projection Inferred from electronic annotation. Source: Compara integral to endoplasmic reticulum membrane Inferred from direct assay Ref.18. Source: UniProtKB neuronal cell body Inferred from electronic annotation. Source: Compara nuclear envelope Inferred from direct assay Ref.3. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATL1	Q8WXF7	2	EBI-715972,EBI-2410266

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1192

1192

Reticulon-4

PRO_0000168165

Regions

Topological domain

1 – 1018

1018

Cytoplasmic Potential

Transmembrane

1019 – 1039

21

Helical; Potential

Topological domain

1040 – 1133

94

Lumenal Potential

Transmembrane

1134 – 1154

21

Helical; Potential

Topological domain

1155 – 1192

38

Cytoplasmic Potential

Domain

1005 – 1192

188

Reticulon

Compositional bias

30 – 47

18

Poly-Glu

Compositional bias

143 – 148

6

Poly-Pro

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.16 Ref.30 Ref.33 Ref.35

Modified residue

7

1

Phosphoserine Ref.23 Ref.33

Modified residue

15

1

Phosphoserine Ref.16 Ref.33 Ref.35

Modified residue

107

1

Phosphoserine Ref.23 Ref.35

Modified residue

152

1

Phosphoserine By similarity

Modified residue

181

1

Phosphoserine Ref.28

Modified residue

182

1

Phosphoserine Ref.28

Modified residue

188

1

Phosphothreonine By similarity

Modified residue

361

1

Phosphoserine By similarity

Modified residue

446

1

Phosphoserine By similarity

Modified residue

860

1

Phosphoserine By similarity

Modified residue

863

1

Phosphoserine By similarity

Modified residue

889

1

Phosphotyrosine By similarity

Modified residue

1104

1

N6-acetyllysine Ref.32

Natural variations

Alternative sequence

1 – 993

993

Missing in isoform 3.

VSP_005652

Alternative sequence

1 – 206

206

Missing in isoform 6.

VSP_037112

Alternative sequence

58 – 289

232

Missing in isoform 4.

VSP_005654

Alternative sequence

186 – 1004

819

Missing in isoform 2.

VSP_005655

Alternative sequence

205 – 1004

800

Missing in isoform 5.

VSP_037113

Alternative sequence

994 – 1004

11

AIFSAELSKTS → MDGQKKNWKDK in isoform 3.

VSP_005653

Natural variant

357

1

D → V.
Corresponds to variant rs11677099 [ dbSNP | Ensembl ].

VAR_053633

Natural variant

429

1

L → V in a colorectal cancer sample; somatic mutation. Ref.36

VAR_035904

Natural variant

899

1

E → Q.
Corresponds to variant rs6757519 [ dbSNP | Ensembl ].

VAR_053634

Natural variant

920

1

S → C.
Corresponds to variant rs6757705 [ dbSNP | Ensembl ].

VAR_053635

Experimental info

Sequence conflict

107

1

S → C in BAA83712. Ref.6

Sequence conflict

135

1

E → Q in BAA83712. Ref.6

Sequence conflict

458

1

S → P in CAB99248. Ref.2

Sequence conflict

564

1

N → S in AAK20831. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

1192

Helix Strand Turn

Details...

Turn

1059 – 1062

4

Helix

1063 – 1070

8

Helix

1074 – 1094

21

Helix

1095 – 1097

3

Helix

1100 – 1107

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (RTN 4A) (Nogo-A) (RTN-xL) [UniParc]. Last modified November 16, 2001. Version 2. Checksum: CDE239BBF31589CA	FASTA	1,192	129,931
	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
	Isoform 2 (RTN 4B) (ASY) (Nogo-B) (RTN-xS) (Foocen-M) [UniParc]. Checksum: 8A19379EF91A59B4	FASTA	373	40,318
	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 SSGSVVVDLL YWRDIKKTGV VFGASLFLLL SLTVFSIVSV TAYIALALLS VTISFRIYKG 250 260 270 280 290 300 VIQAIQKSDE GHPFRAYLES EVAISEELVQ KYSNSALGHV NCTIKELRRL FLVDDLVDSL 310 320 330 340 350 360 KFAVLMWVFT YVGALFNGLT LLILALISLF SVPVIYERHQ AQIDHYLGLA NKNVKDAMAK 370 IQAKIPGLKR KAE
	Isoform 3 (RTN 4C) (Nogo-C) (Foocen-S) [UniParc]. Checksum: C60161DF3FB34D80	FASTA	199	22,395
	10 20 30 40 50 60 MDGQKKNWKD KVVDLLYWRD IKKTGVVFGA SLFLLLSLTV FSIVSVTAYI ALALLSVTIS 70 80 90 100 110 120 FRIYKGVIQA IQKSDEGHPF RAYLESEVAI SEELVQKYSN SALGHVNCTI KELRRLFLVD 130 140 150 160 170 180 DLVDSLKFAV LMWVFTYVGA LFNGLTLLIL ALISLFSVPV IYERHQAQID HYLGLANKNV 190 KDAMAKIQAK IPGLKRKAE
	Isoform 4 [UniParc]. Checksum: 51B5E94CF103BA74	FASTA	960	106,360
	10 20 30 40 50 60 MEDLDQSPLV SSSDSPPRPQ PAFKYQFVRE PEDEEEEEEE EEEDEDEDLE ELEVLERTEF 70 80 90 100 110 120 SELEYSEMGS SFSVSPKAES AVIVANPREE IIVKNKDEEE KLVSNNILHN QQELPTALTK 130 140 150 160 170 180 LVKEDEVVSS EKAKDSFNEK RVAVEAPMRE EYADFKPFER VWEVKDSKED SDMLAAGGKI 190 200 210 220 230 240 ESNLESKVDK KCFADSLEQT NHEKDSESSN DDTSFPSTPE GIKDRSGAYI TCAPFNPAAT 250 260 270 280 290 300 ESIATNIFPL LGDPTSENKT DEKKIEEKKA QIVTEKNTST KTSNPFLVAA QDSETDYVTT 310 320 330 340 350 360 DNLTKVTEEV VANMPEGLTP DLVQEACESE LNEVTGTKIA YETKMDLVQT SEVMQESLYP 370 380 390 400 410 420 AAQLCPSFEE SEATPSPVLP DIVMEAPLNS AVPSAGASVI QPSSSPLEAS SVNYESIKHE 430 440 450 460 470 480 PENPPPYEEA MSVSLKKVSG IKEEIKEPEN INAALQETEA PYISIACDLI KETKLSAEPA 490 500 510 520 530 540 PDFSDYSEMA KVEQPVPDHS ELVEDSSPDS EPVDLFSDDS IPDVPQKQDE TVMLVKESLT 550 560 570 580 590 600 ETSFESMIEY ENKEKLSALP PEGGKPYLES FKLSLDNTKD TLLPDEVSTL SKKEKIPLQM 610 620 630 640 650 660 EELSTAVYSN DDLFISKEAQ IRETETFSDS SPIEIIDEFP TLISSKTDSF SKLAREYTDL 670 680 690 700 710 720 EVSHKSEIAN APDGAGSLPC TELPHDLSLK NIQPKVEEKI SFSDDFSKNG SATSKVLLLP 730 740 750 760 770 780 PDVSALATQA EIESIVKPKV LVKEAEKKLP SDTEKEDRSP SAIFSAELSK TSVVDLLYWR 790 800 810 820 830 840 DIKKTGVVFG ASLFLLLSLT VFSIVSVTAY IALALLSVTI SFRIYKGVIQ AIQKSDEGHP 850 860 870 880 890 900 FRAYLESEVA ISEELVQKYS NSALGHVNCT IKELRRLFLV DDLVDSLKFA VLMWVFTYVG 910 920 930 940 950 960 ALFNGLTLLI LALISLFSVP VIYERHQAQI DHYLGLANKN VKDAMAKIQA KIPGLKRKAE
	Isoform 5 (RTN4-B2) [UniParc]. Checksum: D7B2AA5E839E58AD	FASTA	392	42,274
	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 RSSAVVDLLY WRDIKKTGVV FGASLFLLLS LTVFSIVSVT 250 260 270 280 290 300 AYIALALLSV TISFRIYKGV IQAIQKSDEG HPFRAYLESE VAISEELVQK YSNSALGHVN 310 320 330 340 350 360 CTIKELRRLF LVDDLVDSLK FAVLMWVFTY VGALFNGLTL LILALISLFS VPVIYERHQA 370 380 390 QIDHYLGLAN KNVKDAMAKI QAKIPGLKRK AE
	Isoform 6 (Rtn-T) [UniParc]. Checksum: 0CDE8F647036415A	FASTA	986	108,450
	10 20 30 40 50 60 MDLKEQPGNT ISAGQEDFPS VLLETAASLP SLSPLSAASF KEHEYLGNLS TVLPTEGTLQ 70 80 90 100 110 120 ENVSEASKEV SEKAKTLLID RDLTEFSELE YSEMGSSFSV SPKAESAVIV ANPREEIIVK 130 140 150 160 170 180 NKDEEEKLVS NNILHNQQEL PTALTKLVKE DEVVSSEKAK DSFNEKRVAV EAPMREEYAD 190 200 210 220 230 240 FKPFERVWEV KDSKEDSDML AAGGKIESNL ESKVDKKCFA DSLEQTNHEK DSESSNDDTS 250 260 270 280 290 300 FPSTPEGIKD RSGAYITCAP FNPAATESIA TNIFPLLGDP TSENKTDEKK IEEKKAQIVT 310 320 330 340 350 360 EKNTSTKTSN PFLVAAQDSE TDYVTTDNLT KVTEEVVANM PEGLTPDLVQ EACESELNEV 370 380 390 400 410 420 TGTKIAYETK MDLVQTSEVM QESLYPAAQL CPSFEESEAT PSPVLPDIVM EAPLNSAVPS 430 440 450 460 470 480 AGASVIQPSS SPLEASSVNY ESIKHEPENP PPYEEAMSVS LKKVSGIKEE IKEPENINAA 490 500 510 520 530 540 LQETEAPYIS IACDLIKETK LSAEPAPDFS DYSEMAKVEQ PVPDHSELVE DSSPDSEPVD 550 560 570 580 590 600 LFSDDSIPDV PQKQDETVML VKESLTETSF ESMIEYENKE KLSALPPEGG KPYLESFKLS 610 620 630 640 650 660 LDNTKDTLLP DEVSTLSKKE KIPLQMEELS TAVYSNDDLF ISKEAQIRET ETFSDSSPIE 670 680 690 700 710 720 IIDEFPTLIS SKTDSFSKLA REYTDLEVSH KSEIANAPDG AGSLPCTELP HDLSLKNIQP 730 740 750 760 770 780 KVEEKISFSD DFSKNGSATS KVLLLPPDVS ALATQAEIES IVKPKVLVKE AEKKLPSDTE 790 800 810 820 830 840 KEDRSPSAIF SAELSKTSVV DLLYWRDIKK TGVVFGASLF LLLSLTVFSI VSVTAYIALA 850 860 870 880 890 900 LLSVTISFRI YKGVIQAIQK SDEGHPFRAY LESEVAISEE LVQKYSNSAL GHVNCTIKEL 910 920 930 940 950 960 RRLFLVDDLV DSLKFAVLMW VFTYVGALFN GLTLLILALI SLFSVPVIYE RHQAQIDHYL 970 980 GLANKNVKDA MAKIQAKIPG LKRKAE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"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.
[30]	"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, MASS SPECTROMETRY.
[31]	"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.
[32]	"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, MASS SPECTROMETRY.
[33]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[34]	"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].
[35]	"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, MASS SPECTROMETRY.
[36]	"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. , 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.

IPI

IPI00021766.
IPI00219207.
IPI00298289.
IPI00477663.
IPI00478442.
IPI00894213.

RefSeq

NP_008939.1. NM_007008.2.
NP_065393.1. NM_020532.4.
NP_722550.1. NM_153828.2.
NP_997403.1. NM_207520.1.
NP_997404.1. NM_207521.1.

UniGene

Hs.741208.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2G31	NMR	-	A	1055-1114	[»]
2JV5	NMR	-	A	1055-1108	[»]

ProteinModelPortal

Q9NQC3.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NQC3. 21 interactions.

MINT

MINT-154434.

PTM databases

PhosphoSite

Q9NQC3.

Polymorphism databases

DMDM

17369290.

Proteomic databases

PaxDb

Q9NQC3.

PRIDE

Q9NQC3.

Protocols and materials databases

DNASU

57142.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000317610; ENSP00000322147; ENSG00000115310.
ENST00000337526; ENSP00000337838; ENSG00000115310.
ENST00000357376; ENSP00000349944; ENSG00000115310.
ENST00000357732; ENSP00000350365; ENSG00000115310.
ENST00000394609; ENSP00000378107; ENSG00000115310.
ENST00000394611; ENSP00000378109; ENSG00000115310.
ENST00000404909; ENSP00000385650; ENSG00000115310.
ENST00000405240; ENSP00000384471; ENSG00000115310.

GeneID

57142.

KEGG

hsa:57142.

UCSC

uc002ryd.3. human.
uc002ryf.3. human.

Organism-specific databases

CTD

57142.

GeneCards

GC02M055199.

H-InvDB

HIX0002059.

HGNC

HGNC:14085. RTN4.

HPA

CAB005388.
HPA023977.

MIM

604475. gene.

neXtProt

NX_Q9NQC3.

PharmGKB

PA34883.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG306139.

HOVERGEN

HBG023134.

InParanoid

Q9NQC3.

Enzyme and pathway databases

Pathway_Interaction_DB

p75ntrpathway. p75(NTR)-mediated signaling.

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q9NQC3.

Bgee

Q9NQC3.

Genevestigator

Q9NQC3.

GermOnline

ENSG00000115310. Homo sapiens.

Family and domain databases

InterPro

IPR003388. Reticulon.
[Graphical view]

PANTHER

PTHR10994. PTHR10994. 1 hit.

Pfam

PF02453. Reticulon. 1 hit.
[Graphical view]

PROSITE

PS50845. RETICULON. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

RTN4. human.

EvolutionaryTrace

Q9NQC3.

GenomeRNAi

57142.

NextBio

63075.

PMAP-CutDB

Q9NQC3.

SOURCE

Search...

Entry information

Entry name

RTN4_HUMAN

Accession

Primary (citable) accession number: Q9NQC3
Secondary accession number(s): O94962 , 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:	May 1, 2013
This is version 135 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.