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O95197 (RTN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Reticulon-3
Alternative name(s):
Homolog of ASY protein
Short name=HAP
Neuroendocrine-specific protein-like 2
Short name=NSP-like protein 2
Neuroendocrine-specific protein-like II
Short name=NSP-like protein II
Short name=NSPLII
Gene names
Name:RTN3
Synonyms:ASYIP, NSPL2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1032 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in membrane trafficking in the early secretory pathway. Inhibits BACE1 activity and amyloid precursor protein processing. May induce caspase-8 cascade and apoptosis. May favor BCL2 translocation to the mitochondria upon endoplasmic reticulum stress. In case of enteroviruses infection, RTN3 may be involved in the viral replication or pathogenesis. Ref.12 Ref.13 Ref.15 Ref.19

Subunit structure

Homodimer. Interacts with ATL1 By similarity. Interacts with RTN4. Isoform 3 interacts with BACE1, BACE2, BCL2 and FADD. Interacts with Coxsackievirus A16, enterovirus 71 and poliovirus P2C proteins. Interacts with ATL2. Ref.2 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Ref.20 Ref.24

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein Ref.2 Ref.12 Ref.13 Ref.15 Ref.18 Ref.19 Ref.20.

Tissue specificity

Isoform 3 is widely expressed, with highest levels in brain, where it is enriched in neuronal cell bodies from gray matter (at protein level). Three times more abundant in macula than in peripheral retina. Isoform 1 is expressed at high levels in brain and at low levels in skeletal muscle. Isoform 2 is only found in melanoma. Ref.1 Ref.2 Ref.3 Ref.4 Ref.12

Induction

By endoplasmic reticulum stress (at protein level). Ref.19

Sequence similarities

Contains 1 reticulon domain.

Sequence caution

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

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95197-1)

Also known as: A1; A4b;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O95197-2)

Also known as: A2; A3b;

The sequence of this isoform differs from the canonical sequence as follows:
     48-66: Missing.
Isoform 3 (identifier: O95197-3)

Also known as: B1; A1;

The sequence of this isoform differs from the canonical sequence as follows:
     48-66: Missing.
     67-843: Missing.
Isoform 4 (identifier: O95197-4)

Also known as: B2; A2;

The sequence of this isoform differs from the canonical sequence as follows:
     67-843: Missing.
Isoform 5 (identifier: O95197-5)

The sequence of this isoform differs from the canonical sequence as follows:
     48-66: Missing.
     67-843: Missing.
     999-1032: TQIDHYVGIARDQTKSIVEKIQAKLPGIAKKKAE → DPSKTPWNRQKKGRISTWKPEMQQLLKHHLIVITSLLVL
Note: No experimental confirmation available.
Isoform 6 (identifier: O95197-6)

The sequence of this isoform differs from the canonical sequence as follows:
     48-843: Missing.
     914-1032: AYLDVDITLS...LPGIAKKKAE → PRLITMLASP...PQYQAQKLMD
Isoform 7 (identifier: O95197-7)

The sequence of this isoform differs from the canonical sequence as follows:
     48-159: Missing.
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.23
Chain2 – 10321031Reticulon-3
PRO_0000168163

Regions

Topological domain2 – 863862Cytoplasmic Potential
Intramembrane864 – 88724Helical; Potential
Topological domain888 – 94760Cytoplasmic Potential
Intramembrane948 – 96821Helical; Potential
Topological domain969 – 9724Cytoplasmic Potential
Intramembrane973 – 99321Helical; Potential
Topological domain994 – 103239Cytoplasmic Potential
Domain844 – 1032189Reticulon
Region987 – 103246Interaction with FADD
Region1000 – 10023Interaction with BACE1

Amino acid modifications

Modified residue21N-acetylalanine Ref.23 Ref.25 Ref.27 Ref.28
Modified residue6491Phosphoserine Ref.22
Modified residue6501Phosphoserine Ref.22

Natural variations

Alternative sequence48 – 843796Missing in isoform 6.
VSP_045319
Alternative sequence48 – 159112Missing in isoform 7.
VSP_047008
Alternative sequence48 – 6619Missing in isoform 2, isoform 3 and isoform 5.
VSP_023759
Alternative sequence67 – 843777Missing in isoform 3, isoform 4 and isoform 5.
VSP_023760
Alternative sequence914 – 1032119AYLDV…KKKAE → PRLITMLASPEIRPSQLLKR SKQNSLESPKKRQNKYMETR NATVTKTPFNSYNVVTCTMK ENTQCQLEPAFQAFFLIWCF LPSFPFNPQYQAQKLMD in isoform 6.
VSP_045320
Alternative sequence999 – 103234TQIDH…KKKAE → DPSKTPWNRQKKGRISTWKP EMQQLLKHHLIVITSLLVL in isoform 5.
VSP_023761
Natural variant61A → E. Ref.4
Corresponds to variant rs11551944 [ dbSNP | Ensembl ].
VAR_031164
Natural variant5011D → H.
Corresponds to variant rs7936660 [ dbSNP | Ensembl ].
VAR_057713

Experimental info

Sequence conflict8711A → V in BAD93008. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A1) (A4b) [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: 26B372B82BFC6361

FASTA1,032112,611
        10         20         30         40         50         60 
MAEPSAATQS HSISSSSFGA EPSAPGGGGS PGACPALGTK SCSSSCADSF VSSSSSQPVS 

        70         80         90        100        110        120 
LFSTSQEGLS SLCSDEPSSE IMTSSFLSSS EIHNTGLTIL HGEKSHVLGS QPILAKEGKD 

       130        140        150        160        170        180 
HLDLLDMKKM EKPQGTSNNV SDSSVSLAAG VHCDRPSIPA SFPEHPAFLS KKIGQVEEQI 

       190        200        210        220        230        240 
DKETKNPNGV SSREAKTALD ADDRFTLLTA QKPPTEYSKV EGIYTYSLSP SKVSGDDVIE 

       250        260        270        280        290        300 
KDSPESPFEV IIDKAAFDKE FKDSYKESTD DFGSWSVHTD KESSEDISET NDKLFPLRNK 

       310        320        330        340        350        360 
EAGRYPMSAL LSRQFSHTNA ALEEVSRCVN DMHNFTNEIL TWDLVPQVKQ QTDKSSDCIT 

       370        380        390        400        410        420 
KTTGLDMSEY NSEIPVVNLK TSTHQKTPVC SIDGSTPITK STGDWAEASL QQENAITGKP 

       430        440        450        460        470        480 
VPDSLNSTKE FSIKGVQGNM QKQDDTLAEL PGSPPEKCDS LGSGVATVKV VLPDDHLKDE 

       490        500        510        520        530        540 
MDWQSSALGE ITEADSSGES DDTVIEDITA DTSFENNKIQ AEKPVSIPSA VVKTGEREIK 

       550        560        570        580        590        600 
EIPSCEREEK TSKNFEELVS DSELHQDQPD ILGRSPASEA ACSKVPDTNV SLEDVSEVAP 

       610        620        630        640        650        660 
EKPITTENPK LPSTVSPNVF NETEFSLNVT TSAYLESLHG KNVKHIDDSS PEDLIAAFTE 

       670        680        690        700        710        720 
TRDKGIVDSE RNAFKAISEK MTDFKTTPPV EVLHENESGG SEIKDIGSKY SEQSKETNGS 

       730        740        750        760        770        780 
EPLGVFPTQG TPVASLDLEQ EQLTIKALKE LGERQVEKST SAQRDAELPS EEVLKQTFTF 

       790        800        810        820        830        840 
APESWPQRSY DILERNVKNG SDLGISQKPI TIRETTRVDA VSSLSKTELV KKHVLARLLT 

       850        860        870        880        890        900 
DFSVHDLIFW RDVKKTGFVF GTTLIMLLSL AAFSVISVVS YLILALLSVT ISFRIYKSVI 

       910        920        930        940        950        960 
QAVQKSEEGH PFKAYLDVDI TLSSEAFHNY MNAAMVHINR ALKLIIRLFL VEDLVDSLKL 

       970        980        990       1000       1010       1020 
AVFMWLMTYV GAVFNGITLL ILAELLIFSV PIVYEKYKTQ IDHYVGIARD QTKSIVEKIQ 

      1030 
AKLPGIAKKK AE 

« Hide

Isoform 2 (A2) (A3b) [UniParc].

Checksum: 26EBCFC7BF6351FC
Show »

FASTA1,013110,652
Isoform 3 (B1) (A1) [UniParc].

Checksum: DDC6A4544ABCDFB7
Show »

FASTA23625,609
Isoform 4 (B2) (A2) [UniParc].

Checksum: A1EB93C4659AD832
Show »

FASTA25527,568
Isoform 5 [UniParc].

Checksum: 12919C71F2208160
Show »

FASTA24126,452
Isoform 6 [UniParc].

Checksum: D066FBEA9D48E49C
Show »

FASTA21423,489
Isoform 7 [UniParc].

Checksum: 5C36B72E4243492C
Show »

FASTA920100,824

References

« Hide 'large scale' references
[1]"Cloning of a novel member of the reticulon gene family (RTN3): gene structure and chromosomal localization to 11q13."
Moreira E.F., Jaworski C.J., Rodriguez I.R.
Genomics 58:73-81(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
Tissue: Retina.
[2]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), HOMODIMERIZATION, INTERACTION WITH RTN4, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[3]"Overexpression of human reticulon 3 (hRTN3) in astrocytoma."
Huang X., Yang H., Zhou Y., Liu J., Yin B., Peng X., Qiang B., Yuan J.
Clin. Neuropathol. 23:1-7(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
[4]"Identification of a new RTN3 transcript, RTN3-A1, and its distribution in adult mouse brain."
Cai Y., Saiyin H., Lin Q., Zhang P., Tang L., Pan X., Yu L.
Brain Res. Mol. Brain Res. 138:236-243(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, VARIANT GLU-6.
Tissue: Brain.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
Tissue: Brain and Corpus callosum.
[6]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Kidney.
[7]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[8]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain, Eye and Lymph.
[11]"A reticular rhapsody: phylogenic evolution and nomenclature of the RTN/Nogo gene family."
Oertle T., Klinger M., Stuermer C.A.O., Schwab M.E.
FASEB J. 17:1238-1247(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION (ISOFORMS 3; 4 AND 5).
[12]"Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation."
He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.
Nat. Med. 10:959-965(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BACE1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
[13]"Reticulon 3 is involved in membrane trafficking between the endoplasmic reticulum and Golgi."
Wakana Y., Koyama S., Nakajima K., Hatsuzawa K., Nagahama M., Tani K., Hauri H.-P., Melancon P., Tagaya M.
Biochem. Biophys. Res. Commun. 334:1198-1205(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION, SUBCELLULAR LOCATION, FUNCTION.
[14]"Tissue specificity and regulation of the N-terminal diversity of reticulon 3."
Di Scala F., Dupuis L., Gaiddon C., De Tapia M., Jokic N., Gonzalez de Aguilar J.-L., Raul J.-S., Ludes B., Loeffler J.-P.
Biochem. J. 385:125-134(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3 AND 4).
[15]"Adaptor FADD is recruited by RTN3/HAP in ER-bound signaling complexes."
Xiang R., Liu Y., Zhu L., Dong W., Qi Y.
Apoptosis 11:1923-1932(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FADD, SUBCELLULAR LOCATION, FUNCTION.
[16]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid beta-protein."
Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.
Eur. J. Neurosci. 24:1237-1244(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BACE1 AND BACE2.
[18]"Mapping of interaction domains mediating binding between BACE1 and RTN/Nogo proteins."
He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.
J. Mol. Biol. 363:625-634(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION, INTERACTION WITH BACE1 AND RTN4, SUBCELLULAR LOCATION.
[19]"Reticulon 3 mediates Bcl-2 accumulation in mitochondria in response to endoplasmic reticulum stress."
Wan Q., Kuang E., Dong W., Zhou S., Xu H., Qi Y., Liu Y.
Apoptosis 12:319-328(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY ER STRESS, INTERACTION WITH BCL2, SUBCELLULAR LOCATION, FUNCTION.
[20]"Reticulon 3 binds the 2C protein of enterovirus 71 and is required for viral replication."
Tang W.-F., Yang S.-Y., Wu B.-W., Jheng J.-R., Chen Y.-L., Shih C.-H., Lin K.-H., Lai H.-C., Tang P., Horng J.-T.
J. Biol. Chem. 282:5888-5898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COXSACKIEVIRUS A16 P2C; POLIOVIRUS P2C AND ENTEROVIRUS 71 P2C, SUBCELLULAR LOCATION.
[21]"The membrane topology of RTN3 and its effect on binding of RTN3 to BACE1."
He W., Shi Q., Hu X., Yan R.
J. Biol. Chem. 282:29144-29151(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY.
[22]"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-649 AND SER-650, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[24]"A class of dynamin-like GTPases involved in the generation of the tubular ER network."
Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A., Rapoport T.A., Blackstone C.
Cell 138:549-561(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATL2.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"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].
[27]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF059524 mRNA. Translation: AAC99319.1.
AF059529 expand/collapse EMBL AC list , AF059525, AF059526, AF059527, AF059528 Genomic DNA. Translation: AAD20951.1.
AF119297 mRNA. Translation: AAD26810.1.
AY427821 mRNA. Translation: AAR02474.1.
AY750848 mRNA. Translation: AAU81930.1.
AP000753 Genomic DNA. No translation available.
AP006289 Genomic DNA. No translation available.
AK297529 mRNA. Translation: BAH12606.1.
AB209771 mRNA. Translation: BAD93008.1. Different initiation.
AK075412 mRNA. Translation: BAG52134.1.
AK222898 mRNA. Translation: BAD96618.1.
AK295361 mRNA. Translation: BAH12044.1.
CH471076 Genomic DNA. Translation: EAW74170.1.
BC000634 mRNA. Translation: AAH00634.1.
BC010556 mRNA. Translation: AAH10556.1.
BC011394 mRNA. Translation: AAH11394.1.
BC022993 mRNA. Translation: AAH22993.1.
BC100822 mRNA. Translation: AAI00823.1.
BC100823 mRNA. Translation: AAI00824.1.
BC105981 mRNA. Translation: AAI05982.1.
BC105982 mRNA. Translation: AAI05983.1.
BC118628 mRNA. Translation: AAI18629.1.
BC118550 mRNA. Translation: AAI18551.1.
BK001685 mRNA. Translation: DAA01931.1.
BK001681 mRNA. Translation: DAA01941.1.
BK001684 mRNA. Translation: DAA01943.1.
RefSeqNP_001252518.1. NM_001265589.1.
NP_001252519.1. NM_001265590.1.
NP_001252520.1. NM_001265591.1.
NP_006045.1. NM_006054.3.
NP_958831.1. NM_201428.2.
NP_958832.1. NM_201429.2.
NP_958833.1. NM_201430.2.
UniGeneHs.743229.

3D structure databases

ProteinModelPortalO95197.
SMRO95197. Positions 894-959.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115598. 15 interactions.
IntActO95197. 12 interactions.
MINTMINT-5000642.

PTM databases

PhosphoSiteO95197.

Proteomic databases

PaxDbO95197.
PRIDEO95197.

Protocols and materials databases

DNASU10313.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339997; ENSP00000344106; ENSG00000133318. [O95197-2]
ENST00000341307; ENSP00000340903; ENSG00000133318. [O95197-5]
ENST00000354497; ENSP00000346492; ENSG00000133318. [O95197-6]
ENST00000356000; ENSP00000348279; ENSG00000133318. [O95197-4]
ENST00000377819; ENSP00000367050; ENSG00000133318. [O95197-1]
ENST00000537981; ENSP00000440874; ENSG00000133318. [O95197-3]
ENST00000540798; ENSP00000442733; ENSG00000133318. [O95197-7]
GeneID10313.
KEGGhsa:10313.
UCSCuc001nxm.3. human. [O95197-4]
uc001nxn.3. human. [O95197-2]
uc001nxo.3. human. [O95197-3]
uc001nxp.3. human. [O95197-5]
uc001nxq.3. human. [O95197-1]
uc010rmu.2. human.

Organism-specific databases

CTD10313.
GeneCardsGC11P063448.
H-InvDBHIX0021346.
HGNCHGNC:10469. RTN3.
HPAHPA015649.
HPA015650.
MIM604249. gene.
neXtProtNX_O95197.
PharmGKBPA34882.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303514.
HOVERGENHBG093922.
InParanoidO95197.
OMAKGRISTW.
OrthoDBEOG7CZK7J.
PhylomeDBO95197.
TreeFamTF105431.

Gene expression databases

ArrayExpressO95197.
BgeeO95197.
GenevestigatorO95197.

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

ChiTaRSRTN3. human.
GeneWikiRTN3.
GenomeRNAi10313.
NextBio39085.
PROO95197.
SOURCESearch...

Entry information

Entry nameRTN3_HUMAN
AccessionPrimary (citable) accession number: O95197
Secondary accession number(s): B3KQS2 expand/collapse secondary AC list , B7Z308, B7Z4M0, F5H774, Q147U9, Q496K2, Q53GN3, Q59EP0, Q5UEP2, Q6T930, Q7RTM7, Q7RTM8, Q7RTN3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 20, 2007
Last modified: April 16, 2014
This is version 125 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

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 11

Human chromosome 11: entries, gene names and cross-references to MIM