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Q9NQC3

- RTN4_HUMAN

UniProt

Q9NQC3 - RTN4_HUMAN

Protein

Reticulon-4

Gene

RTN4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (16 Nov 2001)
      Previous versions | rss
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    Functioni

    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.By similarity3 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. angiogenesis Source: Ensembl
    2. apoptotic process Source: UniProtKB
    3. axonal fasciculation Source: UniProtKB
    4. cardiac epithelial to mesenchymal transition Source: Ensembl
    5. cerebral cortex radial glia guided migration Source: UniProtKB
    6. endoplasmic reticulum tubular network organization Source: UniProtKB
    7. negative regulation of axon extension Source: UniProtKB
    8. negative regulation of axonogenesis Source: Reactome
    9. negative regulation of cell growth Source: DFLAT
    10. neurotrophin TRK receptor signaling pathway Source: Reactome
    11. regulation of apoptotic process Source: UniProtKB
    12. regulation of axonogenesis Source: Reactome
    13. regulation of branching morphogenesis of a nerve Source: UniProtKB
    14. regulation of cell migration Source: MGI

    Keywords - Biological processi

    Neurogenesis

    Enzyme and pathway databases

    ReactomeiREACT_13815. Axonal growth inhibition (RHOA activation).

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:RTN4
    Synonyms:KIAA0886, NOGO
    ORF Names:My043, SP1507
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:14085. RTN4.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cell projection Source: Ensembl
    2. endoplasmic reticulum Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. integral component of endoplasmic reticulum membrane Source: UniProtKB
    5. intracellular Source: UniProtKB
    6. neuronal cell body Source: Ensembl
    7. nuclear envelope Source: UniProtKB
    8. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34883.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11921192Reticulon-4PRO_0000168165Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine6 Publications
    Modified residuei7 – 71Phosphoserine2 Publications
    Modified residuei15 – 151Phosphoserine3 Publications
    Modified residuei107 – 1071Phosphoserine2 Publications
    Modified residuei152 – 1521PhosphoserineBy similarity
    Modified residuei181 – 1811Phosphoserine1 Publication
    Modified residuei182 – 1821Phosphoserine1 Publication
    Modified residuei361 – 3611PhosphoserineBy similarity
    Modified residuei511 – 5111PhosphoserineBy similarity
    Modified residuei1104 – 11041N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NQC3.
    PaxDbiQ9NQC3.
    PRIDEiQ9NQC3.

    PTM databases

    PhosphoSiteiQ9NQC3.

    Miscellaneous databases

    PMAP-CutDBQ9NQC3.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiQ9NQC3.
    BgeeiQ9NQC3.
    GenevestigatoriQ9NQC3.

    Organism-specific databases

    HPAiCAB005388.
    HPA023977.

    Interactioni

    Subunit structurei

    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 ATL1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATL1Q8WXF72EBI-715972,EBI-2410266
    NCK2O436392EBI-715945,EBI-713635

    Protein-protein interaction databases

    BioGridi121400. 48 interactions.
    IntActiQ9NQC3. 26 interactions.
    MINTiMINT-154434.

    Structurei

    Secondary structure

    1
    1192
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni1059 – 10624
    Helixi1063 – 10708
    Helixi1074 – 109421
    Helixi1095 – 10973
    Helixi1100 – 11078

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2G31NMR-A1055-1114[»]
    2JV5NMR-A1055-1108[»]
    DisProtiDP00524.
    ProteinModelPortaliQ9NQC3.
    SMRiQ9NQC3. Positions 1055-1114.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NQC3.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 10181018CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1040 – 113394LumenalSequence AnalysisAdd
    BLAST
    Topological domaini1155 – 119238CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1019 – 103921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1134 – 115421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1005 – 1192188ReticulonPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi30 – 4718Poly-GluAdd
    BLAST
    Compositional biasi143 – 1486Poly-Pro

    Domaini

    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.By similarity

    Sequence similaritiesi

    Contains 1 reticulon domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG306139.
    HOVERGENiHBG023134.
    InParanoidiQ9NQC3.
    OMAiNIHRVAT.
    OrthoDBiEOG7CZK7J.
    PhylomeDBiQ9NQC3.
    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 (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NQC3-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEDLDQSPLV SSSDSPPRPQ PAFKYQFVRE PEDEEEEEEE EEEDEDEDLE     50
    ELEVLERKPA AGLSAAPVPT APAAGAPLMD FGNDFVPPAP RGPLPAAPPV 100
    APERQPSWDP SPVSSTVPAP SPLSAAAVSP SKLPEDDEPP ARPPPPPPAS 150
    VSPQAEPVWT PPAPAPAAPP STPAAPKRRG SSGSVDETLF ALPAASEPVI 200
    RSSAENMDLK EQPGNTISAG QEDFPSVLLE TAASLPSLSP LSAASFKEHE 250
    YLGNLSTVLP TEGTLQENVS EASKEVSEKA KTLLIDRDLT EFSELEYSEM 300
    GSSFSVSPKA ESAVIVANPR EEIIVKNKDE EEKLVSNNIL HNQQELPTAL 350
    TKLVKEDEVV SSEKAKDSFN EKRVAVEAPM REEYADFKPF ERVWEVKDSK 400
    EDSDMLAAGG KIESNLESKV DKKCFADSLE QTNHEKDSES SNDDTSFPST 450
    PEGIKDRSGA YITCAPFNPA ATESIATNIF PLLGDPTSEN KTDEKKIEEK 500
    KAQIVTEKNT STKTSNPFLV AAQDSETDYV TTDNLTKVTE EVVANMPEGL 550
    TPDLVQEACE SELNEVTGTK IAYETKMDLV QTSEVMQESL YPAAQLCPSF 600
    EESEATPSPV LPDIVMEAPL NSAVPSAGAS VIQPSSSPLE ASSVNYESIK 650
    HEPENPPPYE EAMSVSLKKV SGIKEEIKEP ENINAALQET EAPYISIACD 700
    LIKETKLSAE PAPDFSDYSE MAKVEQPVPD HSELVEDSSP DSEPVDLFSD 750
    DSIPDVPQKQ DETVMLVKES LTETSFESMI EYENKEKLSA LPPEGGKPYL 800
    ESFKLSLDNT KDTLLPDEVS TLSKKEKIPL QMEELSTAVY SNDDLFISKE 850
    AQIRETETFS DSSPIEIIDE FPTLISSKTD SFSKLAREYT DLEVSHKSEI 900
    ANAPDGAGSL PCTELPHDLS LKNIQPKVEE KISFSDDFSK NGSATSKVLL 950
    LPPDVSALAT QAEIESIVKP KVLVKEAEKK LPSDTEKEDR SPSAIFSAEL 1000
    SKTSVVDLLY WRDIKKTGVV FGASLFLLLS LTVFSIVSVT AYIALALLSV 1050
    TISFRIYKGV IQAIQKSDEG HPFRAYLESE VAISEELVQK YSNSALGHVN 1100
    CTIKELRRLF LVDDLVDSLK FAVLMWVFTY VGALFNGLTL LILALISLFS 1150
    VPVIYERHQA QIDHYLGLAN KNVKDAMAKI QAKIPGLKRK AE 1192
    Length:1,192
    Mass (Da):129,931
    Last modified:November 16, 2001 - v2
    Checksum:iCDE239BBF31589CA
    GO
    Isoform 2 (identifier: Q9NQC3-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:373
    Mass (Da):40,318
    Checksum:i8A19379EF91A59B4
    GO
    Isoform 3 (identifier: Q9NQC3-3) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:199
    Mass (Da):22,395
    Checksum:iC60161DF3FB34D80
    GO
    Isoform 4 (identifier: Q9NQC3-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         58-289: Missing.

    Show »
    Length:960
    Mass (Da):106,360
    Checksum:i51B5E94CF103BA74
    GO
    Isoform 5 (identifier: Q9NQC3-5) [UniParc]FASTAAdd to Basket

    Also known as: RTN4-B2

    The sequence of this isoform differs from the canonical sequence as follows:
         205-1004: Missing.

    Show »
    Length:392
    Mass (Da):42,274
    Checksum:iD7B2AA5E839E58AD
    GO
    Isoform 6 (identifier: Q9NQC3-6) [UniParc]FASTAAdd to Basket

    Also known as: Rtn-T

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

    Show »
    Length:986
    Mass (Da):108,450
    Checksum:i0CDE8F647036415A
    GO

    Sequence cautioni

    The sequence AAD39920.1 differs from that shown. Reason: Frameshift at positions 1149 and 1156.
    The sequence AAG43160.1 differs from that shown. Reason: Frameshift at positions 684 and 700.
    The sequence AAG43160.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA74909.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071S → C in BAA83712. 1 PublicationCurated
    Sequence conflicti135 – 1351E → Q in BAA83712. 1 PublicationCurated
    Sequence conflicti458 – 4581S → P in CAB99248. (PubMed:10667780)Curated
    Sequence conflicti564 – 5641N → S in AAK20831. (PubMed:11866689)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti357 – 3571D → V.
    Corresponds to variant rs11677099 [ dbSNP | Ensembl ].
    VAR_053633
    Natural varianti429 – 4291L → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035904
    Natural varianti899 – 8991E → Q.
    Corresponds to variant rs6757519 [ dbSNP | Ensembl ].
    VAR_053634
    Natural varianti920 – 9201S → C.
    Corresponds to variant rs6757705 [ dbSNP | Ensembl ].
    VAR_053635

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 993993Missing in isoform 3. 8 PublicationsVSP_005652Add
    BLAST
    Alternative sequencei1 – 206206Missing in isoform 6. 2 PublicationsVSP_037112Add
    BLAST
    Alternative sequencei58 – 289232Missing in isoform 4. 1 PublicationVSP_005654Add
    BLAST
    Alternative sequencei186 – 1004819Missing in isoform 2. 7 PublicationsVSP_005655Add
    BLAST
    Alternative sequencei205 – 1004800Missing in isoform 5. 2 PublicationsVSP_037113Add
    BLAST
    Alternative sequencei994 – 100411AIFSAELSKTS → MDGQKKNWKDK in isoform 3. 8 PublicationsVSP_005653Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1851.1. [Q9NQC3-2]
    CCDS1852.1. [Q9NQC3-6]
    CCDS42683.1. [Q9NQC3-5]
    CCDS42684.1. [Q9NQC3-1]
    CCDS42685.1. [Q9NQC3-3]
    RefSeqiNP_008939.1. NM_007008.2. [Q9NQC3-3]
    NP_065393.1. NM_020532.4. [Q9NQC3-1]
    NP_722550.1. NM_153828.2. [Q9NQC3-2]
    NP_997403.1. NM_207520.1. [Q9NQC3-5]
    NP_997404.1. NM_207521.1. [Q9NQC3-6]
    XP_005264491.1. XM_005264434.2. [Q9NQC3-6]
    UniGeneiHs.637850.

    Genome annotation databases

    EnsembliENST00000317610; ENSP00000322147; ENSG00000115310. [Q9NQC3-2]
    ENST00000337526; ENSP00000337838; ENSG00000115310. [Q9NQC3-1]
    ENST00000357376; ENSP00000349944; ENSG00000115310. [Q9NQC3-6]
    ENST00000357732; ENSP00000350365; ENSG00000115310. [Q9NQC3-5]
    ENST00000394609; ENSP00000378107; ENSG00000115310. [Q9NQC3-3]
    ENST00000394611; ENSP00000378109; ENSG00000115310. [Q9NQC3-6]
    ENST00000404909; ENSP00000385650; ENSG00000115310. [Q9NQC3-6]
    ENST00000405240; ENSP00000384471; ENSG00000115310. [Q9NQC3-6]
    GeneIDi57142.
    KEGGihsa:57142.
    UCSCiuc002ryc.3. human. [Q9NQC3-3]
    uc002ryd.3. human. [Q9NQC3-1]
    uc002ryf.3. human. [Q9NQC3-5]
    uc002ryg.3. human. [Q9NQC3-2]

    Polymorphism databases

    DMDMi17369290.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS1851.1. [Q9NQC3-2 ]
    CCDS1852.1. [Q9NQC3-6 ]
    CCDS42683.1. [Q9NQC3-5 ]
    CCDS42684.1. [Q9NQC3-1 ]
    CCDS42685.1. [Q9NQC3-3 ]
    RefSeqi NP_008939.1. NM_007008.2. [Q9NQC3-3 ]
    NP_065393.1. NM_020532.4. [Q9NQC3-1 ]
    NP_722550.1. NM_153828.2. [Q9NQC3-2 ]
    NP_997403.1. NM_207520.1. [Q9NQC3-5 ]
    NP_997404.1. NM_207521.1. [Q9NQC3-6 ]
    XP_005264491.1. XM_005264434.2. [Q9NQC3-6 ]
    UniGenei Hs.637850.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2G31 NMR - A 1055-1114 [» ]
    2JV5 NMR - A 1055-1108 [» ]
    DisProti DP00524.
    ProteinModelPortali Q9NQC3.
    SMRi Q9NQC3. Positions 1055-1114.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121400. 48 interactions.
    IntActi Q9NQC3. 26 interactions.
    MINTi MINT-154434.

    PTM databases

    PhosphoSitei Q9NQC3.

    Polymorphism databases

    DMDMi 17369290.

    Proteomic databases

    MaxQBi Q9NQC3.
    PaxDbi Q9NQC3.
    PRIDEi Q9NQC3.

    Protocols and materials databases

    DNASUi 57142.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317610 ; ENSP00000322147 ; ENSG00000115310 . [Q9NQC3-2 ]
    ENST00000337526 ; ENSP00000337838 ; ENSG00000115310 . [Q9NQC3-1 ]
    ENST00000357376 ; ENSP00000349944 ; ENSG00000115310 . [Q9NQC3-6 ]
    ENST00000357732 ; ENSP00000350365 ; ENSG00000115310 . [Q9NQC3-5 ]
    ENST00000394609 ; ENSP00000378107 ; ENSG00000115310 . [Q9NQC3-3 ]
    ENST00000394611 ; ENSP00000378109 ; ENSG00000115310 . [Q9NQC3-6 ]
    ENST00000404909 ; ENSP00000385650 ; ENSG00000115310 . [Q9NQC3-6 ]
    ENST00000405240 ; ENSP00000384471 ; ENSG00000115310 . [Q9NQC3-6 ]
    GeneIDi 57142.
    KEGGi hsa:57142.
    UCSCi uc002ryc.3. human. [Q9NQC3-3 ]
    uc002ryd.3. human. [Q9NQC3-1 ]
    uc002ryf.3. human. [Q9NQC3-5 ]
    uc002ryg.3. human. [Q9NQC3-2 ]

    Organism-specific databases

    CTDi 57142.
    GeneCardsi GC02M055199.
    H-InvDB HIX0002059.
    HGNCi HGNC:14085. RTN4.
    HPAi CAB005388.
    HPA023977.
    MIMi 604475. gene.
    neXtProti NX_Q9NQC3.
    PharmGKBi PA34883.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG306139.
    HOVERGENi HBG023134.
    InParanoidi Q9NQC3.
    OMAi NIHRVAT.
    OrthoDBi EOG7CZK7J.
    PhylomeDBi Q9NQC3.
    TreeFami TF105431.

    Enzyme and pathway databases

    Reactomei REACT_13815. Axonal growth inhibition (RHOA activation).

    Miscellaneous databases

    ChiTaRSi RTN4. human.
    EvolutionaryTracei Q9NQC3.
    GeneWikii Reticulon_4.
    GenomeRNAii 57142.
    NextBioi 63075.
    PMAP-CutDB Q9NQC3.
    PROi Q9NQC3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NQC3.
    Bgeei Q9NQC3.
    Genevestigatori Q9NQC3.

    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

    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. 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. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    15. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5).
      Tissue: Brain, Eye, Kidney, Ovary, Pancreas, Placenta and Skeletal muscle.
    16. Bienvenut W.V.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-24; 92-104; 1075-1090 AND 1158-1171, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    17. Mao Y.M., Xie Y., Zheng Z.H.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-1192 (ISOFORMS 1/4).
      Tissue: Fetal brain.
    18. "Identification of the Nogo inhibitor of axon regeneration as a Reticulon protein."
      GrandPre T., Nakamura F., Vartanian T., Strittmatter S.M.
      Nature 403:439-444(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY, FUNCTION.
      Tissue: Brain.
    19. "Identification of a receptor mediating Nogo-66 inhibition of axonal regeneration."
      Fournier A.E., GrandPre T., Strittmatter S.M.
      Nature 409:341-346(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Tissue: Brain.
    20. "Nogos and the Nogo-66 receptor: factors inhibiting CNS neuron regeneration."
      Ng C.E.L., Tang B.L.
      J. Neurosci. Res. 67:559-565(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    21. Cited for: INTERACTION WITH RTN3.
    22. "Reticulon family members modulate BACE1 activity and amyloid-beta peptide generation."
      He W., Lu Y., Qahwash I., Hu X.-Y., Chang A., Yan R.
      Nat. Med. 10:959-965(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BACE1.
    23. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid beta-protein."
      Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W.
      Eur. J. Neurosci. 24:1237-1244(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BACE1 AND BACE2, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
    25. "Mapping of interaction domains mediating binding between BACE1 and RTN/Nogo proteins."
      He W., Hu X., Shi Q., Zhou X., Lu Y., Fisher C., Yan R.
      J. Mol. Biol. 363:625-634(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RTN3.
    26. "Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells."
      Miao R.Q., Gao Y., Harrison K.D., Prendergast J., Acevedo L.M., Yu J., Hu F., Strittmatter S.M., Sessa W.C.
      Proc. Natl. Acad. Sci. U.S.A. 103:10997-11002(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NGBR.
    27. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "A class of dynamin-like GTPases involved in the generation of the tubular ER network."
      Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A., Rapoport T.A., Blackstone C.
      Cell 138:549-561(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATL1.
    31. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    33. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    38. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-429.

    Entry informationi

    Entry nameiRTN4_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQC3
    Secondary accession number(s): O94962
    , Q7L7Q5, Q7L7Q6, Q7L7Q8, Q8IUA4, Q96B16, Q9BXG5, Q9H212, Q9H3I3, Q9UQ42, Q9Y293, Q9Y2Y7, Q9Y5U6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: November 16, 2001
    Last modified: October 1, 2014
    This is version 150 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3