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O95197

- RTN3_HUMAN

UniProt

O95197 - RTN3_HUMAN

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Protein
Reticulon-3
Gene
RTN3, ASYIP, NSPL2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. endoplasmic reticulum tubular network organization Source: UniProtKB
  3. response to stress Source: UniProtKB-KW
  4. vesicle-mediated transport Source: UniProtKB-KW
  5. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Apoptosis, ER-Golgi transport, Host-virus interaction, Stress response, Transport

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:RTN3
Synonyms:ASYIP, NSPL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:10469. RTN3.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein 7 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 863862Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei864 – 88724Helical; Reviewed prediction
Add
BLAST
Topological domaini888 – 94760Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei948 – 96821Helical; Reviewed prediction
Add
BLAST
Topological domaini969 – 9724Cytoplasmic Reviewed prediction
Intramembranei973 – 99321Helical; Reviewed prediction
Add
BLAST
Topological domaini994 – 103239Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. endoplasmic reticulum Source: HPA
  3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  4. extracellular space Source: ProtInc
  5. extracellular vesicular exosome Source: UniProt
  6. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34882.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10321031Reticulon-3
PRO_0000168163Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei649 – 6491Phosphoserine1 Publication
Modified residuei650 – 6501Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95197.
PaxDbiO95197.
PRIDEiO95197.

PTM databases

PhosphoSiteiO95197.

Expressioni

Tissue specificityi

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.5 Publications

Inductioni

By endoplasmic reticulum stress (at protein level).1 Publication

Gene expression databases

ArrayExpressiO95197.
BgeeiO95197.
GenevestigatoriO95197.

Organism-specific databases

HPAiHPA015649.
HPA015650.

Interactioni

Subunit structurei

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 ATL2.9 Publications

Protein-protein interaction databases

BioGridi115598. 15 interactions.
IntActiO95197. 12 interactions.
MINTiMINT-5000642.

Structurei

3D structure databases

ProteinModelPortaliO95197.
SMRiO95197. Positions 894-959.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini844 – 1032189Reticulon
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni987 – 103246Interaction with FADD
Add
BLAST
Regioni1000 – 10023Interaction with BACE1

Sequence similaritiesi

Contains 1 reticulon domain.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG303514.
HOVERGENiHBG093922.
InParanoidiO95197.
OMAiRIYKSVV.
OrthoDBiEOG7CZK7J.
PhylomeDBiO95197.
TreeFamiTF105431.

Family and domain databases

InterProiIPR003388. Reticulon.
[Graphical view]
PANTHERiPTHR10994. PTHR10994. 1 hit.
PfamiPF02453. Reticulon. 1 hit.
[Graphical view]
PROSITEiPS50845. RETICULON. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95197-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAEPSAATQS HSISSSSFGA EPSAPGGGGS PGACPALGTK SCSSSCADSF     50
VSSSSSQPVS LFSTSQEGLS SLCSDEPSSE IMTSSFLSSS EIHNTGLTIL 100
HGEKSHVLGS QPILAKEGKD HLDLLDMKKM EKPQGTSNNV SDSSVSLAAG 150
VHCDRPSIPA SFPEHPAFLS KKIGQVEEQI DKETKNPNGV SSREAKTALD 200
ADDRFTLLTA QKPPTEYSKV EGIYTYSLSP SKVSGDDVIE KDSPESPFEV 250
IIDKAAFDKE FKDSYKESTD DFGSWSVHTD KESSEDISET NDKLFPLRNK 300
EAGRYPMSAL LSRQFSHTNA ALEEVSRCVN DMHNFTNEIL TWDLVPQVKQ 350
QTDKSSDCIT KTTGLDMSEY NSEIPVVNLK TSTHQKTPVC SIDGSTPITK 400
STGDWAEASL QQENAITGKP VPDSLNSTKE FSIKGVQGNM QKQDDTLAEL 450
PGSPPEKCDS LGSGVATVKV VLPDDHLKDE MDWQSSALGE ITEADSSGES 500
DDTVIEDITA DTSFENNKIQ AEKPVSIPSA VVKTGEREIK EIPSCEREEK 550
TSKNFEELVS DSELHQDQPD ILGRSPASEA ACSKVPDTNV SLEDVSEVAP 600
EKPITTENPK LPSTVSPNVF NETEFSLNVT TSAYLESLHG KNVKHIDDSS 650
PEDLIAAFTE TRDKGIVDSE RNAFKAISEK MTDFKTTPPV EVLHENESGG 700
SEIKDIGSKY SEQSKETNGS EPLGVFPTQG TPVASLDLEQ EQLTIKALKE 750
LGERQVEKST SAQRDAELPS EEVLKQTFTF APESWPQRSY DILERNVKNG 800
SDLGISQKPI TIRETTRVDA VSSLSKTELV KKHVLARLLT DFSVHDLIFW 850
RDVKKTGFVF GTTLIMLLSL AAFSVISVVS YLILALLSVT ISFRIYKSVI 900
QAVQKSEEGH PFKAYLDVDI TLSSEAFHNY MNAAMVHINR ALKLIIRLFL 950
VEDLVDSLKL AVFMWLMTYV GAVFNGITLL ILAELLIFSV PIVYEKYKTQ 1000
IDHYVGIARD QTKSIVEKIQ AKLPGIAKKK AE 1032
Length:1,032
Mass (Da):112,611
Last modified:March 20, 2007 - v2
Checksum:i26B372B82BFC6361
GO
Isoform 2 (identifier: O95197-2) [UniParc]FASTAAdd to Basket

Also known as: A2, A3b

The sequence of this isoform differs from the canonical sequence as follows:
     48-66: Missing.

Show »
Length:1,013
Mass (Da):110,652
Checksum:i26EBCFC7BF6351FC
GO
Isoform 3 (identifier: O95197-3) [UniParc]FASTAAdd to Basket

Also known as: B1, A1

The sequence of this isoform differs from the canonical sequence as follows:
     48-66: Missing.
     67-843: Missing.

Show »
Length:236
Mass (Da):25,609
Checksum:iDDC6A4544ABCDFB7
GO
Isoform 4 (identifier: O95197-4) [UniParc]FASTAAdd to Basket

Also known as: B2, A2

The sequence of this isoform differs from the canonical sequence as follows:
     67-843: Missing.

Show »
Length:255
Mass (Da):27,568
Checksum:iA1EB93C4659AD832
GO
Isoform 5 (identifier: O95197-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:241
Mass (Da):26,452
Checksum:i12919C71F2208160
GO
Isoform 6 (identifier: O95197-6) [UniParc]FASTAAdd to Basket

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

Show »
Length:214
Mass (Da):23,489
Checksum:iD066FBEA9D48E49C
GO
Isoform 7 (identifier: O95197-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     48-159: Missing.

Note: Gene prediction based on EST data.

Show »
Length:920
Mass (Da):100,824
Checksum:i5C36B72E4243492C
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61A → E.1 Publication
Corresponds to variant rs11551944 [ dbSNP | Ensembl ].
VAR_031164
Natural varianti501 – 5011D → H.
Corresponds to variant rs7936660 [ dbSNP | Ensembl ].
VAR_057713

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei48 – 843796Missing in isoform 6.
VSP_045319Add
BLAST
Alternative sequencei48 – 159112Missing in isoform 7.
VSP_047008Add
BLAST
Alternative sequencei48 – 6619Missing in isoform 2, isoform 3 and isoform 5.
VSP_023759Add
BLAST
Alternative sequencei67 – 843777Missing in isoform 3, isoform 4 and isoform 5.
VSP_023760Add
BLAST
Alternative sequencei914 – 1032119AYLDV…KKKAE → PRLITMLASPEIRPSQLLKR SKQNSLESPKKRQNKYMETR NATVTKTPFNSYNVVTCTMK ENTQCQLEPAFQAFFLIWCF LPSFPFNPQYQAQKLMD in isoform 6.
VSP_045320Add
BLAST
Alternative sequencei999 – 103234TQIDH…KKKAE → DPSKTPWNRQKKGRISTWKP EMQQLLKHHLIVITSLLVL in isoform 5.
VSP_023761Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti871 – 8711A → V in BAD93008. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF059524 mRNA. Translation: AAC99319.1.
AF059529
, 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.
CCDSiCCDS41664.1. [O95197-4]
CCDS58141.1. [O95197-1]
CCDS58142.1. [O95197-7]
CCDS58143.1. [O95197-6]
CCDS8048.1. [O95197-5]
CCDS8049.1. [O95197-3]
CCDS8050.1. [O95197-2]
RefSeqiNP_001252518.1. NM_001265589.1. [O95197-1]
NP_001252519.1. NM_001265590.1. [O95197-7]
NP_001252520.1. NM_001265591.1. [O95197-6]
NP_006045.1. NM_006054.3. [O95197-3]
NP_958831.1. NM_201428.2. [O95197-2]
NP_958832.1. NM_201429.2. [O95197-4]
NP_958833.1. NM_201430.2. [O95197-5]
UniGeneiHs.743229.

Genome annotation databases

EnsembliENST00000339997; 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]
GeneIDi10313.
KEGGihsa:10313.
UCSCiuc001nxm.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.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF059524 mRNA. Translation: AAC99319.1 .
AF059529
, 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 .
CCDSi CCDS41664.1. [O95197-4 ]
CCDS58141.1. [O95197-1 ]
CCDS58142.1. [O95197-7 ]
CCDS58143.1. [O95197-6 ]
CCDS8048.1. [O95197-5 ]
CCDS8049.1. [O95197-3 ]
CCDS8050.1. [O95197-2 ]
RefSeqi NP_001252518.1. NM_001265589.1. [O95197-1 ]
NP_001252519.1. NM_001265590.1. [O95197-7 ]
NP_001252520.1. NM_001265591.1. [O95197-6 ]
NP_006045.1. NM_006054.3. [O95197-3 ]
NP_958831.1. NM_201428.2. [O95197-2 ]
NP_958832.1. NM_201429.2. [O95197-4 ]
NP_958833.1. NM_201430.2. [O95197-5 ]
UniGenei Hs.743229.

3D structure databases

ProteinModelPortali O95197.
SMRi O95197. Positions 894-959.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115598. 15 interactions.
IntActi O95197. 12 interactions.
MINTi MINT-5000642.

PTM databases

PhosphoSitei O95197.

Proteomic databases

MaxQBi O95197.
PaxDbi O95197.
PRIDEi O95197.

Protocols and materials databases

DNASUi 10313.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339997 ; 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 ]
GeneIDi 10313.
KEGGi hsa:10313.
UCSCi uc001nxm.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

CTDi 10313.
GeneCardsi GC11P063448.
H-InvDB HIX0021346.
HGNCi HGNC:10469. RTN3.
HPAi HPA015649.
HPA015650.
MIMi 604249. gene.
neXtProti NX_O95197.
PharmGKBi PA34882.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG303514.
HOVERGENi HBG093922.
InParanoidi O95197.
OMAi RIYKSVV.
OrthoDBi EOG7CZK7J.
PhylomeDBi O95197.
TreeFami TF105431.

Miscellaneous databases

ChiTaRSi RTN3. human.
GeneWikii RTN3.
GenomeRNAii 10313.
NextBioi 39085.
PROi O95197.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95197.
Bgeei O95197.
Genevestigatori O95197.

Family and domain databases

InterProi IPR003388. Reticulon.
[Graphical view ]
PANTHERi PTHR10994. PTHR10994. 1 hit.
Pfami PF02453. Reticulon. 1 hit.
[Graphical view ]
PROSITEi PS50845. RETICULON. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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. 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.
    , 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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. 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. 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. 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. 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].

Entry informationi

Entry nameiRTN3_HUMAN
AccessioniPrimary (citable) accession number: O95197
Secondary accession number(s): B3KQS2
, B7Z308, B7Z4M0, F5H774, Q147U9, Q496K2, Q53GN3, Q59EP0, Q5UEP2, Q6T930, Q7RTM7, Q7RTM8, Q7RTN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 20, 2007
Last modified: September 3, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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