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Q13489

- BIRC3_HUMAN

UniProt

Q13489 - BIRC3_HUMAN

Protein

Baculoviral IAP repeat-containing protein 3

Gene

BIRC3

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 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8.2 Publications

    Enzyme regulationi

    USP19 regulates the stability of BIRC3/c-IAP2 by preventing its ubiquitination.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi292 – 2921ZincPROSITE-ProRule annotation
    Metal bindingi295 – 2951ZincPROSITE-ProRule annotation
    Metal bindingi312 – 3121ZincPROSITE-ProRule annotation
    Metal bindingi319 – 3191ZincPROSITE-ProRule annotation
    Sitei442 – 4432Breakpoint for translocation to form BIRC3-MALT1

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri557 – 59236RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. ubiquitin-protein transferase activity Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cell surface receptor signaling pathway Source: ProtInc
    3. innate immune response Source: Reactome
    4. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    5. necroptotic process Source: Ensembl
    6. negative regulation of apoptotic process Source: ProtInc
    7. negative regulation of necroptotic process Source: Ensembl
    8. negative regulation of phosphorylation Source: Ensembl
    9. negative regulation of reactive oxygen species metabolic process Source: Ensembl
    10. NIK/NF-kappaB signaling Source: UniProtKB
    11. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    12. positive regulation of protein ubiquitination Source: UniProtKB
    13. protein heterooligomerization Source: Ensembl
    14. protein ubiquitination Source: GOC
    15. regulation of apoptotic process Source: UniProtKB
    16. regulation of cysteine-type endopeptidase activity Source: UniProtKB
    17. regulation of inflammatory response Source: UniProtKB
    18. regulation of innate immune response Source: UniProtKB
    19. regulation of necroptotic process Source: UniProtKB
    20. regulation of nucleotide-binding oligomerization domain containing signaling pathway Source: UniProtKB
    21. regulation of RIG-I signaling pathway Source: UniProtKB
    22. regulation of toll-like receptor signaling pathway Source: UniProtKB
    23. spermatogenesis Source: Ensembl
    24. toll-like receptor 3 signaling pathway Source: Reactome
    25. toll-like receptor 4 signaling pathway Source: Reactome
    26. toll-like receptor signaling pathway Source: Reactome
    27. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Apoptosis, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinkiQ13489.

    Protein family/group databases

    MEROPSiI32.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Baculoviral IAP repeat-containing protein 3 (EC:6.3.2.-)
    Alternative name(s):
    Apoptosis inhibitor 2
    Short name:
    API2
    C-IAP2
    IAP homolog C
    Inhibitor of apoptosis protein 1
    Short name:
    IAP-1
    Short name:
    hIAP-1
    Short name:
    hIAP1
    RING finger protein 49
    TNFR2-TRAF-signaling complex protein 1
    Gene namesi
    Name:BIRC3
    Synonyms:API2, IAP1, MIHC, RNF49
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:591. BIRC3.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. membrane raft Source: Ensembl
    4. nucleus Source: UniProtKB
    5. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving BIRC3 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with MALT1. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma.

    Organism-specific databases

    Orphaneti52417. MALT lymphoma.
    PharmGKBiPA25360.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 604604Baculoviral IAP repeat-containing protein 3PRO_0000122349Add
    BLAST

    Post-translational modificationi

    Auto-ubiquitinated and degraded by the proteasome in apoptotic cells.

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ13489.
    PaxDbiQ13489.
    PRIDEiQ13489.

    PTM databases

    PhosphoSiteiQ13489.

    Miscellaneous databases

    PMAP-CutDBQ13489.

    Expressioni

    Tissue specificityi

    Highly expressed in fetal lung, and kidney. In the adult, expression is mainly seen in lymphoid tissues, including spleen, thymus and peripheral blood lymphocytes.

    Gene expression databases

    ArrayExpressiQ13489.
    BgeeiQ13489.
    CleanExiHS_BIRC3.
    GenevestigatoriQ13489.

    Organism-specific databases

    HPAiHPA002317.

    Interactioni

    Subunit structurei

    Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. The BIR motifs region interacts with TNF receptor associated factors 1 and 2 (TRAF1 and TRAF2) to form a heteromeric complex, which is then recruited to the tumor necrosis factor receptor 2 (TNFR2). Interaction with TRAF2 is required for ubiquitination of IKBKE, degradation of NFKBIA and activation of NF-kappa-B. Interacts with RIP1, RIP2, RIP3, RIP4 and USP19.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASP9P552112EBI-517709,EBI-516799
    RIPK1Q135463EBI-517709,EBI-358507
    RIPK2O433533EBI-517709,EBI-358522
    RIPK3Q9Y5723EBI-517709,EBI-298250
    RIPK4P570783EBI-517709,EBI-4422308
    TRAF1Q130772EBI-517709,EBI-359224
    TRAF2Q129337EBI-517709,EBI-355744

    Protein-protein interaction databases

    BioGridi106827. 68 interactions.
    DIPiDIP-33720N.
    IntActiQ13489. 36 interactions.
    MINTiMINT-216139.
    STRINGi9606.ENSP00000263464.

    Structurei

    Secondary structure

    1
    604
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi28 – 347
    Helixi35 – 384
    Helixi47 – 526
    Beta strandi55 – 573
    Beta strandi64 – 663
    Turni67 – 693
    Helixi82 – 898
    Turni94 – 974
    Helixi250 – 2523
    Helixi255 – 2606
    Helixi261 – 2644
    Helixi273 – 2786
    Beta strandi281 – 2855
    Turni286 – 2883
    Beta strandi289 – 2924
    Turni293 – 2953
    Beta strandi298 – 3014
    Helixi308 – 3158
    Helixi320 – 33415
    Helixi544 – 55512
    Turni558 – 5603
    Beta strandi561 – 5644
    Beta strandi567 – 5704
    Beta strandi575 – 5773
    Turni579 – 5813
    Helixi582 – 5843
    Beta strandi589 – 5913
    Beta strandi597 – 6004

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2UVLX-ray1.91A/B244-337[»]
    3EB5X-ray2.00A536-604[»]
    3EB6X-ray3.40A536-604[»]
    3M0AX-ray2.61D26-99[»]
    3M0DX-ray2.80D26-99[»]
    ProteinModelPortaliQ13489.
    SMRiQ13489. Positions 26-98, 165-235, 244-604.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13489.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati29 – 9668BIR 1Add
    BLAST
    Repeati169 – 23567BIR 2Add
    BLAST
    Repeati255 – 32268BIR 3Add
    BLAST
    Domaini439 – 52991CARDPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the IAP family.Curated
    Contains 3 BIR repeats.PROSITE-ProRule annotation
    Contains 1 CARD domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri557 – 59236RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG243347.
    HOGENOMiHOG000232059.
    HOVERGENiHBG004848.
    InParanoidiQ13489.
    KOiK16060.
    OMAiENSGYFS.
    OrthoDBiEOG78H3TF.
    PhylomeDBiQ13489.
    TreeFamiTF105356.

    Family and domain databases

    Gene3Di1.10.1170.10. 4 hits.
    1.10.533.10. 1 hit.
    InterProiIPR001370. BIR.
    IPR001315. CARD.
    IPR011029. DEATH-like_dom.
    IPR001841. Znf_RING.
    [Graphical view]
    PfamiPF00653. BIR. 3 hits.
    PF00619. CARD. 1 hit.
    [Graphical view]
    SMARTiSM00238. BIR. 3 hits.
    SM00114. CARD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    PROSITEiPS01282. BIR_REPEAT_1. 3 hits.
    PS50143. BIR_REPEAT_2. 3 hits.
    PS50209. CARD. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q13489-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIVENSIFL SNLMKSANTF ELKYDLSCEL YRMSTYSTFP AGVPVSERSL    50
    ARAGFYYTGV NDKVKCFCCG LMLDNWKRGD SPTEKHKKLY PSCRFVQSLN 100
    SVNNLEATSQ PTFPSSVTNS THSLLPGTEN SGYFRGSYSN SPSNPVNSRA 150
    NQDFSALMRS SYHCAMNNEN ARLLTFQTWP LTFLSPTDLA KAGFYYIGPG 200
    DRVACFACGG KLSNWEPKDN AMSEHLRHFP KCPFIENQLQ DTSRYTVSNL 250
    SMQTHAARFK TFFNWPSSVL VNPEQLASAG FYYVGNSDDV KCFCCDGGLR 300
    CWESGDDPWV QHAKWFPRCE YLIRIKGQEF IRQVQASYPH LLEQLLSTSD 350
    SPGDENAESS IIHFEPGEDH SEDAIMMNTP VINAAVEMGF SRSLVKQTVQ 400
    RKILATGENY RLVNDLVLDL LNAEDEIREE ERERATEEKE SNDLLLIRKN 450
    RMALFQHLTC VIPILDSLLT AGIINEQEHD VIKQKTQTSL QARELIDTIL 500
    VKGNIAATVF RNSLQEAEAV LYEHLFVQQD IKYIPTEDVS DLPVEEQLRR 550
    LQEERTCKVC MDKEVSIVFI PCGHLVVCKD CAPSLRKCPI CRSTIKGTVR 600
    TFLS 604
    Length:604
    Mass (Da):68,372
    Last modified:November 1, 1997 - v2
    Checksum:i8581A00BA9AAB4A7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181N → Y in AAC83232. (PubMed:10233894)Curated
    Sequence conflicti119 – 1191N → H in AAC50371. (PubMed:8552191)Curated
    Sequence conflicti153 – 1531D → E in AAC50371. (PubMed:8552191)Curated
    Sequence conflicti163 – 1631H → P in AAC50371. (PubMed:8552191)Curated
    Sequence conflicti165 – 1651A → P in AAC50371. (PubMed:8552191)Curated
    Sequence conflicti191 – 1911K → R in AAC50371. (PubMed:8552191)Curated
    Sequence conflicti364 – 3641F → L in AAC50371. (PubMed:8552191)Curated
    Sequence conflicti552 – 5521Q → P in AAC50371. (PubMed:8552191)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti260 – 2601K → R.1 Publication
    Corresponds to variant rs2276113 [ dbSNP | Ensembl ].
    VAR_021069
    Natural varianti386 – 3861V → M.
    Corresponds to variant rs12222256 [ dbSNP | Ensembl ].
    VAR_049536
    Natural varianti401 – 4011R → K.1 Publication
    Corresponds to variant rs17881197 [ dbSNP | Ensembl ].
    VAR_021070

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L49432 mRNA. Translation: AAC41943.1.
    U45878 mRNA. Translation: AAC50371.1.
    U37546 mRNA. Translation: AAC50507.1.
    AF070674 mRNA. Translation: AAC83232.1.
    AY764389 Genomic DNA. Translation: AAU88144.1.
    BC037420 mRNA. Translation: AAH37420.1.
    AF178945 Genomic DNA. Translation: AAG09369.1.
    CCDSiCCDS8315.1.
    PIRiS68449.
    RefSeqiNP_001156.1. NM_001165.4.
    NP_892007.1. NM_182962.2.
    UniGeneiHs.127799.

    Genome annotation databases

    EnsembliENST00000263464; ENSP00000263464; ENSG00000023445.
    ENST00000532808; ENSP00000432907; ENSG00000023445.
    GeneIDi330.
    KEGGihsa:330.
    UCSCiuc001pgx.3. human.

    Polymorphism databases

    DMDMi2497236.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L49432 mRNA. Translation: AAC41943.1 .
    U45878 mRNA. Translation: AAC50371.1 .
    U37546 mRNA. Translation: AAC50507.1 .
    AF070674 mRNA. Translation: AAC83232.1 .
    AY764389 Genomic DNA. Translation: AAU88144.1 .
    BC037420 mRNA. Translation: AAH37420.1 .
    AF178945 Genomic DNA. Translation: AAG09369.1 .
    CCDSi CCDS8315.1.
    PIRi S68449.
    RefSeqi NP_001156.1. NM_001165.4.
    NP_892007.1. NM_182962.2.
    UniGenei Hs.127799.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2UVL X-ray 1.91 A/B 244-337 [» ]
    3EB5 X-ray 2.00 A 536-604 [» ]
    3EB6 X-ray 3.40 A 536-604 [» ]
    3M0A X-ray 2.61 D 26-99 [» ]
    3M0D X-ray 2.80 D 26-99 [» ]
    ProteinModelPortali Q13489.
    SMRi Q13489. Positions 26-98, 165-235, 244-604.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106827. 68 interactions.
    DIPi DIP-33720N.
    IntActi Q13489. 36 interactions.
    MINTi MINT-216139.
    STRINGi 9606.ENSP00000263464.

    Chemistry

    BindingDBi Q13489.
    ChEMBLi CHEMBL3038465.

    Protein family/group databases

    MEROPSi I32.003.

    PTM databases

    PhosphoSitei Q13489.

    Polymorphism databases

    DMDMi 2497236.

    Proteomic databases

    MaxQBi Q13489.
    PaxDbi Q13489.
    PRIDEi Q13489.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263464 ; ENSP00000263464 ; ENSG00000023445 .
    ENST00000532808 ; ENSP00000432907 ; ENSG00000023445 .
    GeneIDi 330.
    KEGGi hsa:330.
    UCSCi uc001pgx.3. human.

    Organism-specific databases

    CTDi 330.
    GeneCardsi GC11P102188.
    HGNCi HGNC:591. BIRC3.
    HPAi HPA002317.
    MIMi 601721. gene.
    neXtProti NX_Q13489.
    Orphaneti 52417. MALT lymphoma.
    PharmGKBi PA25360.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG243347.
    HOGENOMi HOG000232059.
    HOVERGENi HBG004848.
    InParanoidi Q13489.
    KOi K16060.
    OMAi ENSGYFS.
    OrthoDBi EOG78H3TF.
    PhylomeDBi Q13489.
    TreeFami TF105356.

    Enzyme and pathway databases

    Reactomei REACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinki Q13489.

    Miscellaneous databases

    ChiTaRSi BIRC3. human.
    EvolutionaryTracei Q13489.
    GeneWikii Baculoviral_IAP_repeat-containing_protein_3.
    GenomeRNAii 330.
    NextBioi 1359.
    PMAP-CutDB Q13489.
    PROi Q13489.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13489.
    Bgeei Q13489.
    CleanExi HS_BIRC3.
    Genevestigatori Q13489.

    Family and domain databases

    Gene3Di 1.10.1170.10. 4 hits.
    1.10.533.10. 1 hit.
    InterProi IPR001370. BIR.
    IPR001315. CARD.
    IPR011029. DEATH-like_dom.
    IPR001841. Znf_RING.
    [Graphical view ]
    Pfami PF00653. BIR. 3 hits.
    PF00619. CARD. 1 hit.
    [Graphical view ]
    SMARTi SM00238. BIR. 3 hits.
    SM00114. CARD. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    PROSITEi PS01282. BIR_REPEAT_1. 3 hits.
    PS50143. BIR_REPEAT_2. 3 hits.
    PS50209. CARD. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins."
      Rothe M., Pan M.-G., Henzel W.J., Ayres T.M., Goeddel D.V.
      Cell 83:1243-1252(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes."
      Liston P., Roy N., Tamai K., Lefebvre C., Baird S., Cherton-Horvat G., Farahani R., McLean M., Ikeda J., Mackenzie A., Korneluk R.G.
      Nature 379:349-353(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. "Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors."
      Uren A.G., Pakusch M., Hawkins C.J., Puls K.L., Vaux D.L.
      Proc. Natl. Acad. Sci. U.S.A. 93:4974-4978(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal liver.
    4. "Vascular endothelial genes that are responsive to tumor necrosis factor-alpha in vitro are expressed in atherosclerotic lesions, including inhibitor of apoptosis protein-1, stannin, and two novel genes."
      Horrevoets A.J.G., Fontijn R.D., van Zonneveld A.J., de Vries C.J.M., ten Cate J.W., Pannekoek H.
      Blood 93:3418-3431(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. NIEHS SNPs program
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-260 AND LYS-401.
    6. "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: Lymph.
    7. "Structure of the MLT gene and molecular characterization of the genomic breakpoint junctions in the t(11;18)(q21;q21) of marginal zone B-cell lymphomas of MALT type."
      Baens M., Steyls A., Dierlamm J., De Wolf-Peeters C., Marynen P.
      Genes Chromosomes Cancer 29:281-291(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-441.
    8. "cIAP1 Localizes to the nuclear compartment and modulates the cell cycle."
      Samuel T., Okada K., Hyer M., Welsh K., Zapata J.M., Reed J.C.
      Cancer Res. 65:210-218(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "IAPs: more than just inhibitors of apoptosis proteins."
      Dubrez-Daloz L., Dupoux A., Cartier J.
      Cell Cycle 7:1036-1046(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    10. "To fight or die - inhibitor of apoptosis proteins at the crossroad of innate immunity and death."
      Lopez J., Meier P.
      Curr. Opin. Cell Biol. 22:872-881(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    11. "IAPs: from caspase inhibitors to modulators of NF-kappaB, inflammation and cancer."
      Gyrd-Hansen M., Meier P.
      Nat. Rev. Cancer 10:561-574(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    12. "Inhibitor of apoptosis (IAP) proteins in regulation of inflammation and innate immunity."
      Damgaard R.B., Gyrd-Hansen M.
      Discov. Med. 11:221-231(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    13. "The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2."
      Mei Y., Hahn A.A., Hu S., Yang X.
      J. Biol. Chem. 286:35380-35387(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, INTERACTION WITH USP19.
    14. "cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4)."
      Bertrand M.J., Lippens S., Staes A., Gilbert B., Roelandt R., De Medts J., Gevaert K., Declercq W., Vandenabeele P.
      PLoS ONE 6:E22356-E22356(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE UBIQUITINATION OF RIPK1; RIPK2; RIPK3 AND RIPK4, INTERACTION WITH RIPK1; RIPK2; RIPK3 AND RIPK4.
    15. Cited for: REVIEW ON FUNCTION.
    16. "IKKepsilon-mediated tumorigenesis requires K63-linked polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase complex."
      Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.
      Cell Rep. 3:724-733(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN IKBKE UBIQUITINATION.

    Entry informationi

    Entry nameiBIRC3_HUMAN
    AccessioniPrimary (citable) accession number: Q13489
    Secondary accession number(s): Q16628, Q9HC27, Q9UP46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    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, Reference proteome

    Documents

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

    External Data

    Dasty 3