Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q13490

- BIRC2_HUMAN

UniProt

Q13490 - BIRC2_HUMAN

Protein

Baculoviral IAP repeat-containing protein 2

Gene

BIRC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. 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. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle.6 Publications

    Enzyme regulationi

    The CARD domain inhibits the activation of E3 ubiquitin ligase activity by preventing RING domain dimerization and E2 ubiquitin donor binding and activation. The CARD domain-mediated autoinhibition of the E3 ubiquitin-protein ligase activity suppresses cell proliferation and migration. USP19 regulates the stability of BIRC2/c-IAP1 by preventing its ubiquitination.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi306 – 3061Zinc
    Metal bindingi309 – 3091Zinc
    Metal bindingi326 – 3261Zinc
    Metal bindingi333 – 3331Zinc

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri571 – 60636RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein N-terminus binding Source: UniProtKB
    4. transcription coactivator activity Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. cell surface receptor signaling pathway Source: ProtInc
    3. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    4. innate immune response Source: Reactome
    5. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    6. necroptotic process Source: Ensembl
    7. negative regulation of apoptotic process Source: UniProtKB
    8. NIK/NF-kappaB signaling Source: UniProtKB
    9. placenta development Source: Ensembl
    10. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    11. positive regulation of protein K48-linked ubiquitination Source: UniProtKB
    12. positive regulation of protein K63-linked ubiquitination Source: UniProtKB
    13. positive regulation of protein monoubiquitination Source: UniProtKB
    14. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    15. protein heterooligomerization Source: Ensembl
    16. protein polyubiquitination Source: UniProtKB
    17. regulation of apoptotic process Source: UniProtKB
    18. regulation of cell cycle Source: UniProtKB
    19. regulation of cell differentiation Source: UniProtKB
    20. regulation of cell proliferation Source: UniProtKB
    21. regulation of cysteine-type endopeptidase activity Source: UniProtKB
    22. regulation of inflammatory response Source: UniProtKB
    23. regulation of innate immune response Source: UniProtKB
    24. regulation of necroptotic process Source: UniProtKB
    25. regulation of nucleotide-binding oligomerization domain containing signaling pathway Source: UniProtKB
    26. regulation of RIG-I signaling pathway Source: UniProtKB
    27. regulation of toll-like receptor signaling pathway Source: UniProtKB
    28. regulation of transcription, DNA-templated Source: UniProtKB-KW
    29. response to cAMP Source: Ensembl
    30. response to ethanol Source: Ensembl
    31. response to hypoxia Source: Ensembl
    32. toll-like receptor 3 signaling pathway Source: Reactome
    33. toll-like receptor 4 signaling pathway Source: Reactome
    34. toll-like receptor signaling pathway Source: Reactome
    35. transcription, DNA-templated Source: UniProtKB-KW
    36. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Activator, Ligase

    Keywords - Biological processi

    Apoptosis, Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinkiQ13490.

    Protein family/group databases

    MEROPSiI32.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Baculoviral IAP repeat-containing protein 2 (EC:6.3.2.-)
    Alternative name(s):
    C-IAP1
    IAP homolog B
    Inhibitor of apoptosis protein 2
    Short name:
    IAP-2
    Short name:
    hIAP-2
    Short name:
    hIAP2
    RING finger protein 48
    TNFR2-TRAF-signaling complex protein 2
    Gene namesi
    Name:BIRC2
    Synonyms:API1, IAP2, MIHB, RNF48
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:590. BIRC2.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Agents that induce either the extrinsic or intrinsic apoptotic pathways promote its redistribution from the nuclear compartment to the cytoplasmic compartment. Associated with the midbody in telophase cells, and found diffusely in the nucleus of interphase cells.

    GO - Cellular componenti

    1. CD40 receptor complex Source: BHF-UCL
    2. cytoplasmic side of plasma membrane Source: BHF-UCL
    3. cytosol Source: Reactome
    4. membrane raft Source: Ensembl
    5. nucleus Source: UniProtKB
    6. XY body Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25359.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 618618Baculoviral IAP repeat-containing protein 2PRO_0000122347Add
    BLAST

    Post-translational modificationi

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

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ13490.
    PaxDbiQ13490.
    PRIDEiQ13490.

    PTM databases

    PhosphoSiteiQ13490.

    Miscellaneous databases

    PMAP-CutDBQ13490.

    Expressioni

    Tissue specificityi

    Present in many fetal and adult tissues. Mainly expressed in adult skeletal muscle, thymus, testis, ovary, and pancreas, low or absent in brain and peripheral blood leukocytes.

    Gene expression databases

    ArrayExpressiQ13490.
    BgeeiQ13490.
    CleanExiHS_BIRC2.
    GenevestigatoriQ13490.

    Organism-specific databases

    HPAiCAB020661.
    HPA005513.

    Interactioni

    Subunit structurei

    Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with CASP9. Interacts (via BIR domains) with TRAF2; the interaction is required for IKBKE ubiquitination. Interacts with E2F1, RIPK1, RIPK2, RIPK3, RIPK4, BIRC5/survivin and USP19.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASP7P552102EBI-514538,EBI-523958
    CASP9P552114EBI-514538,EBI-516799
    DIABLOQ9NR285EBI-514538,EBI-517508
    OTUB1Q96FW13EBI-514538,EBI-1058491
    RAC1P630002EBI-514538,EBI-413628
    RIPK1Q135463EBI-514538,EBI-358507
    RIPK2O433533EBI-514538,EBI-358522
    RIPK3Q9Y5723EBI-514538,EBI-298250
    RIPK4P570783EBI-514538,EBI-4422308
    TNFRSF12AQ9NP842EBI-514538,EBI-2851995
    TRAF2Q1293310EBI-514538,EBI-355744

    Protein-protein interaction databases

    BioGridi106826. 94 interactions.
    IntActiQ13490. 55 interactions.
    MINTiMINT-216174.
    STRINGi9606.ENSP00000227758.

    Structurei

    Secondary structure

    1
    618
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 519
    Helixi52 – 554
    Helixi64 – 696
    Beta strandi72 – 743
    Beta strandi81 – 833
    Turni84 – 863
    Helixi99 – 1068
    Helixi111 – 1177
    Helixi264 – 2663
    Helixi269 – 2746
    Turni275 – 2784
    Beta strandi279 – 2824
    Beta strandi283 – 2853
    Helixi287 – 2926
    Beta strandi295 – 2973
    Beta strandi304 – 3063
    Turni307 – 3093
    Beta strandi312 – 3143
    Helixi322 – 3298
    Helixi334 – 3407
    Helixi342 – 3487
    Helixi355 – 3617
    Helixi389 – 3913
    Helixi394 – 4018
    Helixi406 – 42015
    Helixi427 – 45024
    Turni451 – 4533
    Helixi456 – 4638
    Helixi465 – 4717
    Helixi476 – 4849
    Beta strandi485 – 4873
    Helixi490 – 4978
    Helixi502 – 51615
    Helixi518 – 53114
    Helixi533 – 5408
    Helixi553 – 5553
    Helixi558 – 5669
    Turni572 – 5743
    Beta strandi575 – 5784
    Beta strandi581 – 5844
    Beta strandi589 – 5913
    Turni593 – 5953
    Helixi596 – 5983
    Turni603 – 6053
    Beta strandi611 – 6144

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QBHNMR-A266-363[»]
    2L9MNMR-A435-562[»]
    3D9TX-ray1.50A/B260-352[»]
    3D9UX-ray2.30A260-352[»]
    3M1DX-ray2.00A/B40-119[»]
    3MUPX-ray2.60A/B/C/D251-363[»]
    3OZ1X-ray3.00A/B/C/D251-363[»]
    3T6PX-ray1.90A265-618[»]
    3UW4X-ray1.79A266-343[»]
    4EB9X-ray2.60A/B/C/D251-363[»]
    4HY4X-ray1.25A/B260-352[»]
    4HY5X-ray1.75A/B260-352[»]
    4KMNX-ray1.52A260-357[»]
    4LGEX-ray1.55A/B260-352[»]
    4LGUX-ray2.00A/B260-352[»]
    4MTIX-ray2.15A/B260-352[»]
    4MU7X-ray1.79A/B260-352[»]
    ProteinModelPortaliQ13490.
    SMRiQ13490. Positions 41-118, 180-250, 260-616.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13490.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati46 – 11368BIR 1Add
    BLAST
    Repeati184 – 25067BIR 2Add
    BLAST
    Repeati269 – 33668BIR 3Add
    BLAST
    Domaini453 – 54391CARDPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The BIR domains mediate nuclear localization.1 Publication
    The CARD domain is necessary to stabilize the protein and inhibit the activation of E3 ubiquitin-protein ligase activity of BIRC2/c-IAP1 by preventing RING domain dimerization and E2 ubiquitin donor binding and activation.1 Publication

    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 fingeri571 – 60636RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG243347.
    HOGENOMiHOG000232059.
    HOVERGENiHBG004848.
    InParanoidiQ13490.
    KOiK16060.
    OMAiTYHMWPL.
    OrthoDBiEOG78H3TF.
    PhylomeDBiQ13490.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13490-1) [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

    MHKTASQRLF PGPSYQNIKS IMEDSTILSD WTNSNKQKMK YDFSCELYRM    50
    STYSTFPAGV PVSERSLARA GFYYTGVNDK VKCFCCGLML DNWKLGDSPI 100
    QKHKQLYPSC SFIQNLVSAS LGSTSKNTSP MRNSFAHSLS PTLEHSSLFS 150
    GSYSSLSPNP LNSRAVEDIS SSRTNPYSYA MSTEEARFLT YHMWPLTFLS 200
    PSELARAGFY YIGPGDRVAC FACGGKLSNW EPKDDAMSEH RRHFPNCPFL 250
    ENSLETLRFS ISNLSMQTHA ARMRTFMYWP SSVPVQPEQL ASAGFYYVGR 300
    NDDVKCFCCD GGLRCWESGD DPWVEHAKWF PRCEFLIRMK GQEFVDEIQG 350
    RYPHLLEQLL STSDTTGEEN ADPPIIHFGP GESSSEDAVM MNTPVVKSAL 400
    EMGFNRDLVK QTVQSKILTT GENYKTVNDI VSALLNAEDE KREEEKEKQA 450
    EEMASDDLSL IRKNRMALFQ QLTCVLPILD NLLKANVINK QEHDIIKQKT 500
    QIPLQARELI DTILVKGNAA ANIFKNCLKE IDSTLYKNLF VDKNMKYIPT 550
    EDVSGLSLEE QLRRLQEERT CKVCMDKEVS VVFIPCGHLV VCQECAPSLR 600
    KCPICRGIIK GTVRTFLS 618
    Length:618
    Mass (Da):69,900
    Last modified:November 1, 1997 - v2
    Checksum:iC1778D328063586D
    GO
    Isoform 2 (identifier: Q13490-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-49: Missing.

    Show »
    Length:569
    Mass (Da):64,098
    Checksum:iB678A4C2069F0A22
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti157 – 1571S → P in AAC50372. (PubMed:8552191)Curated
    Sequence conflicti308 – 3081C → G in AAC50372. (PubMed:8552191)Curated
    Sequence conflicti414 – 4141Q → L in AAC50372. (PubMed:8552191)Curated
    Sequence conflicti514 – 5141L → W in AAC50372. (PubMed:8552191)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti453 – 4531M → I.
    Corresponds to variant rs34749508 [ dbSNP | Ensembl ].
    VAR_049535
    Natural varianti453 – 4531M → V.1 Publication
    VAR_025016
    Natural varianti506 – 5061A → V.1 Publication
    Corresponds to variant rs34510872 [ dbSNP | Ensembl ].
    VAR_025017
    Natural varianti549 – 5491P → S.1 Publication
    Corresponds to variant rs35494784 [ dbSNP | Ensembl ].
    VAR_025018

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4949Missing in isoform 2. 1 PublicationVSP_045314Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L49431 mRNA. Translation: AAC41942.1.
    U45879 mRNA. Translation: AAC50372.1.
    U37547 mRNA. Translation: AAC50508.1.
    AK303197 mRNA. Translation: BAG64288.1.
    AP000942 Genomic DNA. No translation available.
    DQ068066 Genomic DNA. Translation: AAY46158.1.
    BC016174 mRNA. Translation: AAH16174.1.
    BC028578 mRNA. Translation: AAH28578.1.
    CCDSiCCDS58169.1. [Q13490-2]
    CCDS8316.1. [Q13490-1]
    PIRiS68450.
    RefSeqiNP_001157.1. NM_001166.4. [Q13490-1]
    NP_001243092.1. NM_001256163.1. [Q13490-1]
    NP_001243095.1. NM_001256166.1. [Q13490-2]
    UniGeneiHs.696238.
    Hs.731943.

    Genome annotation databases

    EnsembliENST00000227758; ENSP00000227758; ENSG00000110330. [Q13490-1]
    ENST00000530675; ENSP00000431723; ENSG00000110330. [Q13490-2]
    GeneIDi329.
    KEGGihsa:329.
    UCSCiuc001pgy.4. human. [Q13490-1]

    Polymorphism databases

    DMDMi2497238.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L49431 mRNA. Translation: AAC41942.1 .
    U45879 mRNA. Translation: AAC50372.1 .
    U37547 mRNA. Translation: AAC50508.1 .
    AK303197 mRNA. Translation: BAG64288.1 .
    AP000942 Genomic DNA. No translation available.
    DQ068066 Genomic DNA. Translation: AAY46158.1 .
    BC016174 mRNA. Translation: AAH16174.1 .
    BC028578 mRNA. Translation: AAH28578.1 .
    CCDSi CCDS58169.1. [Q13490-2 ]
    CCDS8316.1. [Q13490-1 ]
    PIRi S68450.
    RefSeqi NP_001157.1. NM_001166.4. [Q13490-1 ]
    NP_001243092.1. NM_001256163.1. [Q13490-1 ]
    NP_001243095.1. NM_001256166.1. [Q13490-2 ]
    UniGenei Hs.696238.
    Hs.731943.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QBH NMR - A 266-363 [» ]
    2L9M NMR - A 435-562 [» ]
    3D9T X-ray 1.50 A/B 260-352 [» ]
    3D9U X-ray 2.30 A 260-352 [» ]
    3M1D X-ray 2.00 A/B 40-119 [» ]
    3MUP X-ray 2.60 A/B/C/D 251-363 [» ]
    3OZ1 X-ray 3.00 A/B/C/D 251-363 [» ]
    3T6P X-ray 1.90 A 265-618 [» ]
    3UW4 X-ray 1.79 A 266-343 [» ]
    4EB9 X-ray 2.60 A/B/C/D 251-363 [» ]
    4HY4 X-ray 1.25 A/B 260-352 [» ]
    4HY5 X-ray 1.75 A/B 260-352 [» ]
    4KMN X-ray 1.52 A 260-357 [» ]
    4LGE X-ray 1.55 A/B 260-352 [» ]
    4LGU X-ray 2.00 A/B 260-352 [» ]
    4MTI X-ray 2.15 A/B 260-352 [» ]
    4MU7 X-ray 1.79 A/B 260-352 [» ]
    ProteinModelPortali Q13490.
    SMRi Q13490. Positions 41-118, 180-250, 260-616.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106826. 94 interactions.
    IntActi Q13490. 55 interactions.
    MINTi MINT-216174.
    STRINGi 9606.ENSP00000227758.

    Chemistry

    BindingDBi Q13490.
    ChEMBLi CHEMBL5462.

    Protein family/group databases

    MEROPSi I32.002.

    PTM databases

    PhosphoSitei Q13490.

    Polymorphism databases

    DMDMi 2497238.

    Proteomic databases

    MaxQBi Q13490.
    PaxDbi Q13490.
    PRIDEi Q13490.

    Protocols and materials databases

    DNASUi 329.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000227758 ; ENSP00000227758 ; ENSG00000110330 . [Q13490-1 ]
    ENST00000530675 ; ENSP00000431723 ; ENSG00000110330 . [Q13490-2 ]
    GeneIDi 329.
    KEGGi hsa:329.
    UCSCi uc001pgy.4. human. [Q13490-1 ]

    Organism-specific databases

    CTDi 329.
    GeneCardsi GC11P102252.
    HGNCi HGNC:590. BIRC2.
    HPAi CAB020661.
    HPA005513.
    MIMi 601712. gene.
    neXtProti NX_Q13490.
    PharmGKBi PA25359.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG243347.
    HOGENOMi HOG000232059.
    HOVERGENi HBG004848.
    InParanoidi Q13490.
    KOi K16060.
    OMAi TYHMWPL.
    OrthoDBi EOG78H3TF.
    PhylomeDBi Q13490.
    TreeFami TF105356.

    Enzyme and pathway databases

    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinki Q13490.

    Miscellaneous databases

    EvolutionaryTracei Q13490.
    GeneWikii BIRC2.
    GenomeRNAii 329.
    NextBioi 1355.
    PMAP-CutDB Q13490.
    PROi Q13490.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13490.
    Bgeei Q13490.
    CleanExi HS_BIRC2.
    Genevestigatori Q13490.

    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] (ISOFORM 1).
    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] (ISOFORM 1).
      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] (ISOFORM 1).
      Tissue: Fetal liver.
    4. NIEHS SNPs program
      Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-453; VAL-506 AND SER-549.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Thymus.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Testis and Uterus.
    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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BIRC5/SURVIVIN.
    9. "c-IAP1 cooperates with Myc by acting as a ubiquitin ligase for Mad1."
      Xu L., Zhu J., Hu X., Zhu H., Kim H.T., LaBaer J., Goldberg A., Yuan J.
      Mol. Cell 28:914-922(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE UBIQUITINATION OF MXD1/MAD1.
    10. "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.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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.
    13. "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.
    14. "Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3 ligases."
      Broemer M., Tenev T., Rigbolt K.T., Hempel S., Blagoev B., Silke J., Ditzel M., Meier P.
      Mol. Cell 40:810-822(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE OF THE NEDD8 CONJUGATION PATHWAY.
    15. "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.
    16. "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.
    17. "Cellular inhibitor of apoptosis protein-1 (cIAP1) can regulate E2F1 transcription factor-mediated control of cyclin transcription."
      Cartier J., Berthelet J., Marivin A., Gemble S., Edmond V., Plenchette S., Lagrange B., Hammann A., Dupoux A., Delva L., Eymin B., Solary E., Dubrez L.
      J. Biol. Chem. 286:26406-26417(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH E2F1 AND TRAF2, SUBCELLULAR LOCATION.
    18. "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.
    19. "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.
    20. Cited for: REVIEW ON FUNCTION.
    21. "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.
    22. "Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat."
      Hinds M.G., Norton R.S., Vaux D.L., Day C.L.
      Nat. Struct. Biol. 6:648-651(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 266-363.
    23. "The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9."
      Kulathila R., Vash B., Sage D., Cornell-Kennon S., Wright K., Koehn J., Stams T., Clark K., Price A.
      Acta Crystallogr. D 65:58-66(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 260-352 IN COMPLEXES WITH ZINC IONS; DIABLO AND CASP9 PEPTIDES, SUBUNIT.
    24. "CARD-mediated autoinhibition of cIAP1's E3 ligase activity suppresses cell proliferation and migration."
      Lopez J., John S.W., Tenev T., Rautureau G.J., Hinds M.G., Francalanci F., Wilson R., Broemer M., Santoro M.M., Day C.L., Meier P.
      Mol. Cell 42:569-583(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 435-562, DOMAIN CARD, ENZYME REGULATION.

    Entry informationi

    Entry nameiBIRC2_HUMAN
    AccessioniPrimary (citable) accession number: Q13490
    Secondary accession number(s): B4E026, Q16516, Q4TTG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 152 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