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Protein

Death domain-containing membrane protein NRADD

Gene

Nradd

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

Functioni

Modulates NTRK1 signaling. Can activate several intracellular signaling pathways, leading to activation of JUN. Promotes apoptosis. Promotes translocation of SORT1 to the cell membrane, and thereby hinders lysosomal degradation of SOTR1 and promotes its interaction with NGFR.3 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Names & Taxonomyi

Protein namesi
Recommended name:
Death domain-containing membrane protein NRADD
Alternative name(s):
Neurotrophin receptor homolog-2
Short name:
NRH2
Neurotrophin receptor-alike death domain protein
Gene namesi
Name:Nradd
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1914419. Nradd.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5252ExtracellularCuratedAdd
BLAST
Transmembranei53 – 7321Helical; Signal-anchor for type III membrane proteinSequence analysisAdd
BLAST
Topological domaini74 – 228155CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

  • cell body membrane Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • lamellipodium Source: MGI
  • membrane Source: MGI
  • neuron projection membrane Source: Ensembl
  • nuclear envelope lumen Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 228228Death domain-containing membrane protein NRADDPRO_0000415383Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi4 – 41N-linked (GlcNAc...)1 Publication
Glycosylationi37 – 371N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8CJ26.
PaxDbiQ8CJ26.
PRIDEiQ8CJ26.

PTM databases

iPTMnetiQ8CJ26.
PhosphoSiteiQ8CJ26.
SwissPalmiQ8CJ26.

Expressioni

Tissue specificityi

Detected in lung and testis.

Gene expression databases

BgeeiQ8CJ26.
ExpressionAtlasiQ8CJ26. baseline and differential.
GenevisibleiQ8CJ26. MM.

Interactioni

Subunit structurei

Interacts with NGFR. Interacts with NTRK1. Interacts with SORT1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Sort1Q6PHU55EBI-6985725,EBI-6985663

Protein-protein interaction databases

IntActiQ8CJ26. 2 interactions.
MINTiMINT-7290501.
STRINGi10090.ENSMUSP00000035069.

Structurei

Secondary structure

1
228
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi140 – 1434Combined sources
Helixi146 – 1494Combined sources
Helixi158 – 1658Combined sources
Helixi169 – 1757Combined sources
Helixi181 – 1888Combined sources
Beta strandi191 – 1955Combined sources
Helixi201 – 2077Combined sources
Turni208 – 2103Combined sources
Helixi212 – 2187Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IB1NMR-A138-228[»]
ProteinModelPortaliQ8CJ26.
SMRiQ8CJ26. Positions 48-85, 138-228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8CJ26.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini143 – 22280DeathPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi139 – 1424Poly-Gln

Sequence similaritiesi

Contains 1 death domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J99A. Eukaryota.
ENOG4111D5W. LUCA.
GeneTreeiENSGT00730000110974.
HOGENOMiHOG000147886.
HOVERGENiHBG071107.
InParanoidiQ8CJ26.
OMAiAFKCWRS.
OrthoDBiEOG7FFMSW.
PhylomeDBiQ8CJ26.
TreeFamiTF106466.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
[Graphical view]
PfamiPF00531. Death. 1 hit.
[Graphical view]
SMARTiSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CJ26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLYNVSKGVV YSDTALQGQD GDREGMWVGA GGALAPNTSS LFPPEPPGAS
60 70 80 90 100
SNIIPVYCAL LATVILGLLA YVAFKCWRSH KQRQQLAKAR TVELGDPDRD
110 120 130 140 150
QRRGDSNVFV DSPPSLEPCI PSQGPHPDLG CQLYLHIPQQ QQEEVQRLLM
160 170 180 190 200
MGEPAKGWQE LAGHLGYQAE AVETMACDQM PAYTLLRNWA AQEGNRATLR
210 220
VLEDALAAIG REDVVQVLSS PAESSSVV
Length:228
Mass (Da):24,727
Last modified:March 1, 2003 - v1
Checksum:iD46B7402D8362FDF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211P → H in BAE35698 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF534394 mRNA. Translation: AAN05631.1.
AK160222 mRNA. Translation: BAE35698.1.
AC132103 Genomic DNA. No translation available.
BC069856 mRNA. Translation: AAH69856.1.
CCDSiCCDS23569.1.
RefSeqiNP_080288.1. NM_026012.2.
UniGeneiMm.46680.

Genome annotation databases

EnsembliENSMUST00000035069; ENSMUSP00000035069; ENSMUSG00000032491.
GeneIDi67169.
KEGGimmu:67169.
UCSCiuc009ruk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF534394 mRNA. Translation: AAN05631.1.
AK160222 mRNA. Translation: BAE35698.1.
AC132103 Genomic DNA. No translation available.
BC069856 mRNA. Translation: AAH69856.1.
CCDSiCCDS23569.1.
RefSeqiNP_080288.1. NM_026012.2.
UniGeneiMm.46680.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IB1NMR-A138-228[»]
ProteinModelPortaliQ8CJ26.
SMRiQ8CJ26. Positions 48-85, 138-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8CJ26. 2 interactions.
MINTiMINT-7290501.
STRINGi10090.ENSMUSP00000035069.

PTM databases

iPTMnetiQ8CJ26.
PhosphoSiteiQ8CJ26.
SwissPalmiQ8CJ26.

Proteomic databases

MaxQBiQ8CJ26.
PaxDbiQ8CJ26.
PRIDEiQ8CJ26.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035069; ENSMUSP00000035069; ENSMUSG00000032491.
GeneIDi67169.
KEGGimmu:67169.
UCSCiuc009ruk.1. mouse.

Organism-specific databases

CTDi67169.
MGIiMGI:1914419. Nradd.

Phylogenomic databases

eggNOGiENOG410J99A. Eukaryota.
ENOG4111D5W. LUCA.
GeneTreeiENSGT00730000110974.
HOGENOMiHOG000147886.
HOVERGENiHBG071107.
InParanoidiQ8CJ26.
OMAiAFKCWRS.
OrthoDBiEOG7FFMSW.
PhylomeDBiQ8CJ26.
TreeFamiTF106466.

Miscellaneous databases

EvolutionaryTraceiQ8CJ26.
PROiQ8CJ26.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CJ26.
ExpressionAtlasiQ8CJ26. baseline and differential.
GenevisibleiQ8CJ26. MM.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
[Graphical view]
PfamiPF00531. Death. 1 hit.
[Graphical view]
SMARTiSM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "NRADD, a novel membrane protein with a death domain involved in mediating apoptosis in response to ER stress."
    Wang X., Shao Z., Zetoune F.S., Zeidler M.G., Gowrishankar K., Vincenz C.
    Cell Death Differ. 10:580-591(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION.
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
    Tissue: Eye.
  5. "Proteolytic processing of the p75 neurotrophin receptor and two homologs generates C-terminal fragments with signaling capability."
    Kanning K.C., Hudson M., Amieux P.S., Wiley J.C., Bothwell M., Schecterson L.C.
    J. Neurosci. 23:5425-5436(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GLYCOSYLATION, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
  6. "Neurotrophin receptor homolog-2 regulates nerve growth factor signaling."
    Wong A.W., Willingham M., Xiao J., Kilpatrick T.J., Murray S.S.
    J. Neurochem. 106:1964-1976(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NTRK1.
  7. "NRH2 is a trafficking switch to regulate sortilin localization and permit proneurotrophin-induced cell death."
    Kim T., Hempstead B.L.
    EMBO J. 28:1612-1623(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NGFR AND SORT1, SUBCELLULAR LOCATION, GLYCOSYLATION.
  8. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-4.
    Tissue: Myoblast.
  9. "Solution structure of p45 death domain."
    Vilar M., Sung T.C., Lee K.F., Riek R.
    Submitted (SEP-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 138-228.

Entry informationi

Entry nameiNRADD_MOUSE
AccessioniPrimary (citable) accession number: Q8CJ26
Secondary accession number(s): Q3TVC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.