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Q13114

- TRAF3_HUMAN

UniProt

Q13114 - TRAF3_HUMAN

Protein

TNF receptor-associated factor 3

Gene

TRAF3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Regulates pathways leading to the activation of NF-kappa-B and MAP kinases, and plays a central role in the regulation of B-cell survival. Part of signaling pathways leading to the production of cytokines and interferon. Required for normal antibody isotype switching from IgM to IgG. Plays a role T-cell dependent immune responses. Plays a role in the regulation of antiviral responses. Is an essential constituent of several E3 ubiquitin-protein ligase complexes. May have E3 ubiquitin-protein ligase activity and promote 'Lys-63'-linked ubiquitination of target proteins. Inhibits activation of NF-kappa-B in response to LTBR stimulation. Inhibits TRAF2-mediated activation of NF-kappa-B. Down-regulates proteolytic processing of NFKB2, and thereby inhibits non-canonical activation of NF-kappa-B. Promotes ubiquitination and proteasomal degradation of MAP3K14.6 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri68 – 7710RING-typePROSITE-ProRule annotation
    Zinc fingeri135 – 19056TRAF-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri191 – 24959TRAF-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. signal transducer activity Source: ProtInc
    4. thioesterase binding Source: UniProtKB
    5. tumor necrosis factor receptor binding Source: UniProt
    6. ubiquitin protein ligase binding Source: UniProtKB
    7. ubiquitin-protein transferase activity Source: InterPro
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. innate immune response Source: Reactome
    3. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    4. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    5. negative regulation of type I interferon production Source: Reactome
    6. regulation of apoptotic process Source: InterPro
    7. regulation of cytokine production Source: UniProtKB
    8. regulation of defense response to virus Source: UniProtKB
    9. regulation of interferon-beta production Source: UniProtKB
    10. regulation of proteolysis Source: UniProtKB
    11. signal transduction Source: ProtInc
    12. toll-like receptor 3 signaling pathway Source: Reactome
    13. toll-like receptor 4 signaling pathway Source: Reactome
    14. toll-like receptor signaling pathway Source: UniProtKB
    15. Toll signaling pathway Source: InterPro
    16. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    17. tumor necrosis factor-mediated signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Apoptosis, Immunity, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    SignaLinkiQ13114.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TNF receptor-associated factor 3 (EC:6.3.2.-)
    Alternative name(s):
    CAP-1
    CD40 receptor-associated factor 1
    Short name:
    CRAF1
    CD40-binding protein
    Short name:
    CD40BP
    LMP1-associated protein 1
    Short name:
    LAP1
    Gene namesi
    Name:TRAF3
    Synonyms:CAP1, CRAF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:12033. TRAF3.

    Subcellular locationi

    Cytoplasm Curated. Endosome By similarity. Mitochondrion
    Note: Undergoes endocytosis together with TLR4 upon LPS signaling By similarity. Associated with mitochondria in response to virus.By similarity

    GO - Cellular componenti

    1. CD40 receptor complex Source: BHF-UCL
    2. cytoplasmic side of plasma membrane Source: BHF-UCL
    3. cytosol Source: Reactome
    4. endosome Source: UniProtKB-SubCell
    5. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Herpes simplex encephalitis 3 (HSE3) [MIM:614849]: A rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. HSE is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti118 – 1181R → W in HSE3. 1 Publication
    VAR_069081

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi441 – 4411Y → A: Abolishes interaction with RNF216; when associated with A-443. 1 Publication
    Mutagenesisi443 – 4431Q → A: Abolishes interaction with RNF216; when associated with A-441. 1 Publication
    Mutagenesisi459 – 4591Y → A: Abolishes interaction with LTBR, CD40 and TANK. 1 Publication
    Mutagenesisi512 – 5121F → E: Abolishes interaction with LTBR, CD40 and TANK. 1 Publication
    Mutagenesisi521 – 5211F → A: Abolishes interaction with LTBR, CD40 and TANK. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614849. phenotype.
    Orphaneti1930. Herpetic encephalitis.
    PharmGKBiPA36710.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 568568TNF receptor-associated factor 3PRO_0000056401Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki107 – 107Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki156 – 156Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Undergoes 'Lys-48'-linked polyubiquitination, leading to its proteasomal degradation in response to signaling by TNFSF13B, TLR4 or through CD40. 'Lys-48'-linked polyubiquitinated form is deubiquitinated by OTUD7B, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Undergoes 'Lys-63'-linked ubiquitination during early stages of virus infection, and 'Lys-48'-linked ubiquitination during later stages. Undergoes both 'Lys-48'-linked and 'Lys-63'-linked ubiquitination in response to TLR3 and TLR4 signaling. Deubiquitinated by OTUB1, OTUB2 and OTUD5.5 Publications

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ13114.
    PaxDbiQ13114.
    PRIDEiQ13114.

    PTM databases

    PhosphoSiteiQ13114.

    Miscellaneous databases

    PMAP-CutDBQ13114.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13114.
    BgeeiQ13114.
    CleanExiHS_CAP1.
    HS_TRAF3.
    GenevestigatoriQ13114.

    Organism-specific databases

    HPAiHPA002933.

    Interactioni

    Subunit structurei

    Homotrimer. Heterotrimer with TRAF2 and TRAF5. Interacts with LTBR/TNFRSF3, TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF13C TNFRSF17/BCMA, TLR4 and EDAR. Interacts with MAP3K5, MAP3K14, TRAIP/TRIP, TDP2/TTRAP, TANK/ITRAF and TRAF3IP1. Interaction with TNFRSF5/CD40 is modulated by TANK/ITRAF, which competes for the same binding site. Interacts with TICAM1. Interacts with TRAFD1. Interacts with OTUB1, OTUB2 and OTUD5. Interacts with RNF216, MAVS, OPTN and TBK1. Identified in a complex with TRAF2, MAP3K14 and BIRC3. Interacts with BIRC2 and BIRC3. Upon exposure to bacterial lipopolysaccharide (LPS), recruited to a transient complex containing TLR4, TRAF3, TRAF6, IKBKG, MAP3K7, MYD88, TICAM1, BIRC2, BIRC3 and UBE2N By similarity. Interacts with Epstein-Barr virus protein LMP1. Interacts (via RING-type zinc finger domain) with SRC. Interacts with CARD14.By similarity35 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Azi2Q9QYP62EBI-357631,EBI-6115874From a different organism.
    BRAFP150562EBI-357631,EBI-365980
    CD40P259423EBI-357631,EBI-525714
    Irf1P153142EBI-357631,EBI-6115486From a different organism.
    RIPK2O433535EBI-357631,EBI-358522
    TANKQ928444EBI-357631,EBI-356349
    TRAF3IP1Q8TDR08EBI-357631,EBI-928811
    Zbp1A2APF72EBI-357631,EBI-6115394From a different organism.
    ZMYND11Q153262EBI-357631,EBI-2623509

    Protein-protein interaction databases

    BioGridi113039. 100 interactions.
    DIPiDIP-6222N.
    IntActiQ13114. 32 interactions.
    MINTiMINT-1144408.
    STRINGi9606.ENSP00000332468.

    Structurei

    Secondary structure

    1
    568
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni54 – 563
    Beta strandi59 – 624
    Beta strandi67 – 693
    Helixi74 – 818
    Turni89 – 913
    Turni97 – 993
    Turni365 – 3739
    Turni375 – 3773
    Helixi378 – 41033
    Beta strandi415 – 4239
    Helixi425 – 4339
    Beta strandi438 – 4414
    Beta strandi445 – 4484
    Beta strandi453 – 4597
    Helixi464 – 4663
    Turni467 – 4693
    Beta strandi470 – 4789
    Helixi483 – 4853
    Beta strandi494 – 4985
    Beta strandi502 – 5043
    Beta strandi508 – 5125
    Beta strandi521 – 5233
    Beta strandi525 – 5284
    Beta strandi532 – 5398
    Helixi540 – 5456
    Beta strandi553 – 5608
    Beta strandi563 – 5653

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FLKX-ray2.80A/B341-568[»]
    1FLLX-ray3.50A/B341-568[»]
    1KZZX-ray3.50A377-568[»]
    1L0AX-ray2.90A377-568[»]
    1RF3X-ray3.50A377-568[»]
    1ZMSX-ray2.80A377-568[»]
    2ECYNMR-A43-101[»]
    2GKWX-ray2.70A377-568[»]
    ProteinModelPortaliQ13114.
    SMRiQ13114. Positions 38-198, 364-568.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13114.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini415 – 560146MATHPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili267 – 33872Sequence AnalysisAdd
    BLAST

    Domaini

    The MATH/TRAF domain binds to receptor cytoplasmic domains.
    The Ring-type zinc finger domain is required for its function in down-regulation of NFKB2 proteolytic processing.By similarity

    Sequence similaritiesi

    Contains 1 MATH domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 2 TRAF-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri68 – 7710RING-typePROSITE-ProRule annotation
    Zinc fingeri135 – 19056TRAF-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri191 – 24959TRAF-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG239194.
    HOVERGENiHBG058222.
    InParanoidiQ13114.
    KOiK03174.
    OMAiYGCTFQG.
    OrthoDBiEOG7966G5.
    PhylomeDBiQ13114.
    TreeFamiTF321154.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    3.90.890.10. 1 hit.
    InterProiIPR002083. MATH.
    IPR013323. SIAH-type.
    IPR012227. TNF_rcpt--assoc_TRAF.
    IPR008974. TRAF-like.
    IPR027128. TRAF3.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    IPR001293. Znf_TRAF.
    [Graphical view]
    PANTHERiPTHR10131:SF72. PTHR10131:SF72. 1 hit.
    PfamiPF00917. MATH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015614. TRAF. 1 hit.
    SMARTiSM00061. MATH. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF49599. SSF49599. 3 hits.
    PROSITEiPS50144. MATH. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    PS50145. ZF_TRAF. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13114-1) [UniParc]FASTAAdd to Basket

    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

    MESSKKMDSP GALQTNPPLK LHTDRSAGTP VFVPEQGGYK EKFVKTVEDK    50
    YKCEKCHLVL CSPKQTECGH RFCESCMAAL LSSSSPKCTA CQESIVKDKV 100
    FKDNCCKREI LALQIYCRNE SRGCAEQLML GHLLVHLKND CHFEELPCVR 150
    PDCKEKVLRK DLRDHVEKAC KYREATCSHC KSQVPMIALQ KHEDTDCPCV 200
    VVSCPHKCSV QTLLRSELSA HLSECVNAPS TCSFKRYGCV FQGTNQQIKA 250
    HEASSAVQHV NLLKEWSNSL EKKVSLLQNE SVEKNKSIQS LHNQICSFEI 300
    EIERQKEMLR NNESKILHLQ RVIDSQAEKL KELDKEIRPF RQNWEEADSM 350
    KSSVESLQNR VTELESVDKS AGQVARNTGL LESQLSRHDQ MLSVHDIRLA 400
    DMDLRFQVLE TASYNGVLIW KIRDYKRRKQ EAVMGKTLSL YSQPFYTGYF 450
    GYKMCARVYL NGDGMGKGTH LSLFFVIMRG EYDALLPWPF KQKVTLMLMD 500
    QGSSRRHLGD AFKPDPNSSS FKKPTGEMNI ASGCPVFVAQ TVLENGTYIK 550
    DDTIFIKVIV DTSDLPDP 568
    Length:568
    Mass (Da):64,490
    Last modified:October 17, 2006 - v2
    Checksum:i9456E440C0A90FBF
    GO
    Isoform 2 (identifier: Q13114-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         191-273: Missing.

    Show »
    Length:485
    Mass (Da):55,306
    Checksum:i1280A3E1B054768D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti134 – 1341Missing in AAA56753. (PubMed:7533327)Curated
    Sequence conflicti158 – 1581L → F in BAH13910. (PubMed:14702039)Curated
    Sequence conflicti218 – 24225Missing in AAA68195. (PubMed:7530216)CuratedAdd
    BLAST
    Sequence conflicti339 – 3391P → S in AAA68195. (PubMed:7530216)Curated
    Sequence conflicti405 – 4051R → G in AAA56753. (PubMed:7533327)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti118 – 1181R → W in HSE3. 1 Publication
    VAR_069081
    Natural varianti129 – 1291M → T.2 Publications
    Corresponds to variant rs1131877 [ dbSNP | Ensembl ].
    VAR_052149

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei191 – 27383Missing in isoform 2. 1 PublicationVSP_040040Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15637 mRNA. Translation: AAA56753.1.
    U19260 mRNA. Translation: AAA65732.1.
    L38509 mRNA. Translation: AAA68195.1.
    U21092 mRNA. Translation: AAC50112.1.
    BX247977 mRNA. Translation: CAD62311.1.
    AK303172 mRNA. Translation: BAH13910.1.
    AL117209 Genomic DNA. No translation available.
    BC075087 mRNA. Translation: AAH75087.1.
    BC075086 mRNA. Translation: AAH75086.1.
    AF110908 mRNA. Translation: AAD29276.1.
    CCDSiCCDS55946.1. [Q13114-2]
    CCDS9975.1. [Q13114-1]
    PIRiA55960.
    S68467.
    RefSeqiNP_001186356.1. NM_001199427.1. [Q13114-2]
    NP_003291.2. NM_003300.3. [Q13114-1]
    NP_663777.1. NM_145725.2. [Q13114-1]
    NP_663778.1. NM_145726.2.
    UniGeneiHs.510528.

    Genome annotation databases

    EnsembliENST00000392745; ENSP00000376500; ENSG00000131323. [Q13114-1]
    ENST00000539721; ENSP00000445998; ENSG00000131323. [Q13114-2]
    ENST00000560371; ENSP00000454207; ENSG00000131323. [Q13114-1]
    GeneIDi7187.
    KEGGihsa:7187.
    UCSCiuc001ymc.2. human. [Q13114-1]
    uc010txy.2. human. [Q13114-2]

    Polymorphism databases

    DMDMi116242824.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U15637 mRNA. Translation: AAA56753.1 .
    U19260 mRNA. Translation: AAA65732.1 .
    L38509 mRNA. Translation: AAA68195.1 .
    U21092 mRNA. Translation: AAC50112.1 .
    BX247977 mRNA. Translation: CAD62311.1 .
    AK303172 mRNA. Translation: BAH13910.1 .
    AL117209 Genomic DNA. No translation available.
    BC075087 mRNA. Translation: AAH75087.1 .
    BC075086 mRNA. Translation: AAH75086.1 .
    AF110908 mRNA. Translation: AAD29276.1 .
    CCDSi CCDS55946.1. [Q13114-2 ]
    CCDS9975.1. [Q13114-1 ]
    PIRi A55960.
    S68467.
    RefSeqi NP_001186356.1. NM_001199427.1. [Q13114-2 ]
    NP_003291.2. NM_003300.3. [Q13114-1 ]
    NP_663777.1. NM_145725.2. [Q13114-1 ]
    NP_663778.1. NM_145726.2.
    UniGenei Hs.510528.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FLK X-ray 2.80 A/B 341-568 [» ]
    1FLL X-ray 3.50 A/B 341-568 [» ]
    1KZZ X-ray 3.50 A 377-568 [» ]
    1L0A X-ray 2.90 A 377-568 [» ]
    1RF3 X-ray 3.50 A 377-568 [» ]
    1ZMS X-ray 2.80 A 377-568 [» ]
    2ECY NMR - A 43-101 [» ]
    2GKW X-ray 2.70 A 377-568 [» ]
    ProteinModelPortali Q13114.
    SMRi Q13114. Positions 38-198, 364-568.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113039. 100 interactions.
    DIPi DIP-6222N.
    IntActi Q13114. 32 interactions.
    MINTi MINT-1144408.
    STRINGi 9606.ENSP00000332468.

    PTM databases

    PhosphoSitei Q13114.

    Polymorphism databases

    DMDMi 116242824.

    Proteomic databases

    MaxQBi Q13114.
    PaxDbi Q13114.
    PRIDEi Q13114.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000392745 ; ENSP00000376500 ; ENSG00000131323 . [Q13114-1 ]
    ENST00000539721 ; ENSP00000445998 ; ENSG00000131323 . [Q13114-2 ]
    ENST00000560371 ; ENSP00000454207 ; ENSG00000131323 . [Q13114-1 ]
    GeneIDi 7187.
    KEGGi hsa:7187.
    UCSCi uc001ymc.2. human. [Q13114-1 ]
    uc010txy.2. human. [Q13114-2 ]

    Organism-specific databases

    CTDi 7187.
    GeneCardsi GC14P103243.
    HGNCi HGNC:12033. TRAF3.
    HPAi HPA002933.
    MIMi 601896. gene.
    614849. phenotype.
    neXtProti NX_Q13114.
    Orphaneti 1930. Herpetic encephalitis.
    PharmGKBi PA36710.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239194.
    HOVERGENi HBG058222.
    InParanoidi Q13114.
    KOi K03174.
    OMAi YGCTFQG.
    OrthoDBi EOG7966G5.
    PhylomeDBi Q13114.
    TreeFami TF321154.

    Enzyme and pathway databases

    Reactomei REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    SignaLinki Q13114.

    Miscellaneous databases

    ChiTaRSi TRAF3. human.
    EvolutionaryTracei Q13114.
    GeneWikii TRAF3.
    GenomeRNAii 7187.
    NextBioi 28176.
    PMAP-CutDB Q13114.
    PROi Q13114.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13114.
    Bgeei Q13114.
    CleanExi HS_CAP1.
    HS_TRAF3.
    Genevestigatori Q13114.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    3.90.890.10. 1 hit.
    InterProi IPR002083. MATH.
    IPR013323. SIAH-type.
    IPR012227. TNF_rcpt--assoc_TRAF.
    IPR008974. TRAF-like.
    IPR027128. TRAF3.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    IPR001293. Znf_TRAF.
    [Graphical view ]
    PANTHERi PTHR10131:SF72. PTHR10131:SF72. 1 hit.
    Pfami PF00917. MATH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015614. TRAF. 1 hit.
    SMARTi SM00061. MATH. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49599. SSF49599. 3 hits.
    PROSITEi PS50144. MATH. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    PS50145. ZF_TRAF. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel RING finger protein interacts with the cytoplasmic domain of CD40."
      Hu H.M., O'Rourke K., Boguski M.S., Dixit V.M.
      J. Biol. Chem. 269:30069-30072(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TNFRSF5.
    2. "The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family."
      Mosialos G., Birkenbach M., Yalamanchili R., VanArsdale T., Ware C., Kieff E.
      Cell 80:389-399(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, INTERACTION WITH EBV LMP-1.
      Tissue: Lymphoma.
    3. "A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40."
      Sato T., Irie S., Reed J.C.
      FEBS Lett. 358:113-118(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TNFRSF5, VARIANT THR-129.
      Tissue: Fetal brain.
    4. "Involvement of CRAF1, a relative of TRAF, in CD40 signaling."
      Cheng G., Cleary A.M., Ye Z.S., Hong D.I., Lederman S., Baltimore D.
      Science 267:1494-1498(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TNFRSF5, VARIANT THR-129.
    5. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    6. "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] (ISOFORM 2).
      Tissue: Thymus.
    7. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 1).
      Tissue: Brain.
    9. "A single gene for human TRAF-3 at chromosome 14q32.3 encodes a variety of mRNA species by alternative polyadenylation, mRNA splicing and transcription initiation."
      van Eyndhoven W.G., Frank D., Kalachikov S., Cleary A.M., Hong D.I., Cho E., Nasr S., Perez A.J., Mackus W.J.M., Cayanis E., Wellington S., Fischer S.G., Warburton D., Lederman S.
      Mol. Immunol. 35:1189-1206(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 536-568.
    10. "TRAF5, an activator of NF-kappaB and putative signal transducer for the lymphotoxin-beta receptor."
      Nakano H., Oshima H., Chung W., Williams-Abbott L., Ware C.F., Yagita H., Okumura K.
      J. Biol. Chem. 271:14661-14664(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LTBR.
    11. "I-TRAF is a novel TRAF-interacting protein that regulates TRAF-mediated signal transduction."
      Rothe M., Xiong J., Shu H.-B., Williamson K., Goddard A., Goeddel D.V.
      Proc. Natl. Acad. Sci. U.S.A. 93:8241-8246(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TANK.
    12. "Binding sites of cytoplasmic effectors TRAF1, 2, and 3 on CD30 and other members of the TNF receptor superfamily."
      Boucher L.-M., Marengere L.E., Lu Y., Thukral S., Mak T.W.
      Biochem. Biophys. Res. Commun. 233:592-600(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF8.
    13. "Herpesvirus entry mediator, a member of the tumor necrosis factor receptor (TNFR) family, interacts with members of the TNFR-associated factor family and activates the transcription factors NF-kappaB and AP-1."
      Marsters S.A., Ayres T.M., Skubatch M., Gray C.L., Rothe M., Ashkenazi A.
      J. Biol. Chem. 272:14029-14032(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF14.
    14. "Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2."
      Song H.Y., Regnier C.H., Kirschning C.J., Goeddel D.V., Rothe M.
      Proc. Natl. Acad. Sci. U.S.A. 94:9792-9796(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K14.
    15. "CD40-tumor necrosis factor receptor-associated factor (TRAF) interactions: regulation of CD40 signaling through multiple TRAF binding sites and TRAF hetero-oligomerization."
      Pullen S.S., Miller H.G., Everdeen D.S., Dang T.T., Crute J.J., Kehry M.R.
      Biochemistry 37:11836-11845(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF5 AND TRAF5.
    16. "Activation of OX40 signal transduction pathways leads to tumor necrosis factor receptor-associated factor (TRAF) 2- and TRAF5-mediated NF-kappaB activation."
      Kawamata S., Hori T., Imura A., Takaori-Kondo A., Uchiyama T.
      J. Biol. Chem. 273:5808-5814(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF4.
    17. "The TRAF family of signal transducers mediates NF-kappaB activation by the TRANCE receptor."
      Wong B.R., Josien R., Lee S.Y., Vologodskaia M., Steinman R.M., Choi Y.
      J. Biol. Chem. 273:28355-28359(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF11A.
    18. Cited for: INTERACTION WITH MAP3K5.
    19. "4-1BB and Ox40 are members of a tumor necrosis factor (TNF)-nerve growth factor receptor subfamily that bind TNF receptor-associated factors and activate nuclear factor kappaB."
      Arch R.H., Thompson C.B.
      Mol. Cell. Biol. 18:558-565(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF4 AND TNFRSF9.
    20. "Identification of a novel activation-inducible protein of the tumor necrosis factor receptor superfamily and its ligand."
      Kwon B., Yu K.-Y., Ni J., Yu G.-L., Jang I.-K., Kim Y.-J., Xing L., Liu D., Wang S.-X., Kwon B.S.
      J. Biol. Chem. 274:6056-6061(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF18.
      Tissue: T-cell.
    21. "Mediation of TNF receptor-associated factor effector functions by apoptosis signal-regulating kinase-1 (ASK1)."
      Hoeflich K.P., Yeh W.C., Yao Z., Mak T.W., Woodgett J.R.
      Oncogene 18:5814-5820(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP3K5.
    22. "TAJ, a novel member of the tumor necrosis factor receptor family, activates the c-Jun N-terminal kinase pathway and mediates caspase-independent cell death."
      Eby M.T., Jasmin A., Kumar A., Sharma K., Chaudhary P.M.
      J. Biol. Chem. 275:15336-15342(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF19.
    23. "TTRAP, a novel protein that associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor-associated factors (TRAFs), and that inhibits nuclear factor-kappa B activation."
      Pype S., Declercq W., Ibrahimi A., Michiels C., Van Rietschoten J.G.I., Dewulf N., de Boer M., Vandenabeele P., Huylebroeck D., Remacle J.E.
      J. Biol. Chem. 275:18586-18593(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TTRAP.
    24. "MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule network."
      Ling L., Goeddel D.V.
      J. Biol. Chem. 275:23852-23860(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF3IP1.
    25. "TNF receptor family member BCMA (B cell maturation) associates with TNF receptor-associated factor (TRAF) 1, TRAF2, and TRAF3 and activates NF-kappa B, elk-1, c-Jun N-terminal kinase, and p38 mitogen-activated protein kinase."
      Hatzoglou A., Roussel J., Bourgeade M.-F., Rogier E., Madry C., Inoue J., Devergne O., Tsapis A.
      J. Immunol. 165:1322-1330(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNFRSF17.
    26. "The ectodermal dysplasia receptor activates the nuclear factor-kappaB, JNK, and cell death pathways and binds to ectodysplasin A."
      Kumar A., Eby M.T., Sinha S., Jasmin A., Chaudhary P.M.
      J. Biol. Chem. 276:2668-2677(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EDAR.
    27. "TRAF3 forms heterotrimers with TRAF2 and modulates its ability to mediate NF-{kappa}B activation."
      He L., Grammer A.C., Wu X., Lipsky P.E.
      J. Biol. Chem. 279:55855-55865(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    28. "Regulation of the NF-kappaB-inducing kinase by tumor necrosis factor receptor-associated factor 3-induced degradation."
      Liao G., Zhang M., Harhaj E.W., Sun S.C.
      J. Biol. Chem. 279:26243-26250(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PROTEASOMAL DEGRADATION, INTERACTION WITH MAP3K14.
    29. Cited for: INTERACTION WITH OTUD5 AND TBK1, FUNCTION AS E3 PROTEIN-UBIQUITIN LIGASE, UBIQUITINATION.
    30. "The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling."
      Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A., Anthonsen M.W.
      J. Biol. Chem. 284:19122-19131(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRC.
    31. "The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS signaling pathway by targeting TRAF3 for degradation."
      Nakhaei P., Mesplede T., Solis M., Sun Q., Zhao T., Yang L., Chuang T.H., Ware C.F., Lin R., Hiscott J.
      PLoS Pathog. 5:E1000650-E1000650(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, MUTAGENESIS OF TYR-441 AND GLN-443, INTERACTION WITH RNF216 AND MAVS.
    32. "Regulation of virus-triggered signaling by OTUB1- and OTUB2-mediated deubiquitination of TRAF3 and TRAF6."
      Li S., Zheng H., Mao A.P., Zhong B., Li Y., Liu Y., Gao Y., Ran Y., Tien P., Shu H.B.
      J. Biol. Chem. 285:4291-4297(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH OTUB1 AND OTUB2.
    33. "Virus-triggered ubiquitination of TRAF3/6 by cIAP1/2 is essential for induction of interferon-beta (IFN-beta) and cellular antiviral response."
      Mao A.P., Li S., Zhong B., Li Y., Yan J., Li Q., Teng C., Shu H.B.
      J. Biol. Chem. 285:9470-9476(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BIRC2 AND BIRC3, SUBCELLULAR LOCATION, UBIQUITINATION.
    34. "TRAF3 controls activation of the canonical and alternative NFkappaB by the lymphotoxin beta receptor."
      Bista P., Zeng W., Ryan S., Bailly V., Browning J.L., Lukashev M.E.
      J. Biol. Chem. 285:12971-12978(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    35. "Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation."
      Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P., Xing G., He F., Zhang L.
      Mol. Cell. Biochem. 338:11-17(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, FUNCTION.
    36. "Optineurin negatively regulates the induction of IFNbeta in response to RNA virus infection."
      Mankouri J., Fragkoudis R., Richards K.H., Wetherill L.F., Harris M., Kohl A., Elliott R.M., Macdonald A.
      PLoS Pathog. 6:E1000778-E1000778(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH OPTN AND TBK1.
    37. "Alternative splicing of CARMA2/CARD14 transcripts generates protein variants with differential effect on NF-kappaB activation and endoplasmic reticulum stress-induced cell death."
      Scudiero I., Zotti T., Ferravante A., Vessichelli M., Vito P., Stilo R.
      J. Cell. Physiol. 226:3121-3131(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CARD14.
    38. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 341-568, X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 341-568 IN COMPLEX WITH TNFRSF5.
    39. "Downstream regulator TANK binds to the CD40 recognition site on TRAF3."
      Li C., Ni C.Z., Havert M.L., Cabezas E., He J., Kaiser D., Reed J.C., Satterthwait A.C., Cheng G., Ely K.R.
      Structure 10:403-411(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 377-568 IN COMPLEX WITH TANK, X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 377-568 IN COMPLEX WITH TNFRSF5.
    40. "Structurally distinct recognition motifs in lymphotoxin-beta receptor and CD40 for tumor necrosis factor receptor-associated factor (TRAF)-mediated signaling."
      Li C., Norris P.S., Ni C.Z., Havert M.L., Chiong E.M., Tran B.R., Cabezas E., Reed J.C., Satterthwait A.C., Ware C.F., Ely K.R.
      J. Biol. Chem. 278:50523-50529(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 377-568 IN COMPLEX WITH LTBR, MUTAGENESIS OF TYR-459; PHE-512 AND PHE-521, INTERACTION WITH TANK AND CD40, SUBUNIT.
    41. "Key molecular contacts promote recognition of the BAFF receptor by TNF receptor-associated factor 3: implications for intracellular signaling regulation."
      Ni C.Z., Oganesyan G., Welsh K., Zhu X., Reed J.C., Satterthwait A.C., Cheng G., Ely K.R.
      J. Immunol. 173:7394-7400(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 377-568 IN COMPLEX WITH TNFRSF13C PEPTIDE, SUBUNIT, INTERACTION WITH TNFRSF13C.
    42. "LMP1 protein from the Epstein-Barr virus is a structural CD40 decoy in B lymphocytes for binding to TRAF3."
      Wu S., Xie P., Welsh K., Li C., Ni C.Z., Zhu X., Reed J.C., Satterthwait A.C., Bishop G.A., Ely K.R.
      J. Biol. Chem. 280:33620-33626(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 377-568 IN COMPLEX WITH EPSTEIN-BARR VIRUS PROTEIN LMP1, SUBUNIT.
    43. "Solution structure of the zinc finger, C3HC4 type (RING finger) domain of TNF receptor-associated factor 3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 43-101.
    44. Cited for: VARIANT HSE3 TRP-118.

    Entry informationi

    Entry nameiTRAF3_HUMAN
    AccessioniPrimary (citable) accession number: Q13114
    Secondary accession number(s): B7Z8C4
    , Q12990, Q13076, Q13947, Q6AZX1, Q9UNL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 169 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, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3