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P98170

- XIAP_HUMAN

UniProt

P98170 - XIAP_HUMAN

Protein

E3 ubiquitin-protein ligase XIAP

Gene

XIAP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (24 Jan 2001)
      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, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis. Acts as a direct caspase inhibitor. Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry. Inactivates CASP9 by keeping it in a monomeric, inactive state. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8, CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin. Ubiquitinion of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation. Plays a role in copper homeostasis by ubiquitinationg COMMD1 and promoting its proteasomal degradation. Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation. Acts as an important regulator of innate immune signaling via regulation of Nodlike receptors (NLRs). 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. Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program.12 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi300 – 3001ZincPROSITE-ProRule annotation
    Metal bindingi303 – 3031ZincPROSITE-ProRule annotation
    Metal bindingi320 – 3201ZincPROSITE-ProRule annotation
    Metal bindingi327 – 3271ZincPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri450 – 48536RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: ProtInc
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. ubiquitin-protein transferase activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. copper ion homeostasis Source: UniProtKB
    4. intrinsic apoptotic signaling pathway Source: Reactome
    5. negative regulation of apoptotic process Source: UniProtKB
    6. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    7. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
    8. positive regulation of protein linear polyubiquitination Source: UniProtKB
    9. positive regulation of protein ubiquitination Source: UniProtKB
    10. protein ubiquitination Source: GOC
    11. regulation of BMP signaling pathway Source: UniProtKB
    12. regulation of cell proliferation Source: UniProtKB
    13. regulation of inflammatory response Source: UniProtKB
    14. regulation of innate immune response Source: UniProtKB
    15. regulation of nucleotide-binding oligomerization domain containing signaling pathway Source: UniProtKB
    16. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase, Protease inhibitor, Thiol protease inhibitor

    Keywords - Biological processi

    Apoptosis, Ubl conjugation pathway, Wnt signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200731. deactivation of the beta-catenin transactivating complex.
    SABIO-RKP98170.
    SignaLinkiP98170.

    Protein family/group databases

    MEROPSiI32.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase XIAP (EC:6.3.2.-)
    Alternative name(s):
    Baculoviral IAP repeat-containing protein 4
    IAP-like protein
    Short name:
    ILP
    Short name:
    hILP
    Inhibitor of apoptosis protein 3
    Short name:
    IAP-3
    Short name:
    hIAP-3
    Short name:
    hIAP3
    X-linked inhibitor of apoptosis protein
    Short name:
    X-linked IAP
    Gene namesi
    Name:XIAP
    Synonyms:API3, BIRC4, IAP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:592. XIAP.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: TLE3 promotes its nuclear localization.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Lymphoproliferative syndrome, X-linked, 2 (XLP2) [MIM:300635]: A rare immunodeficiency characterized by extreme susceptibility to infection with Epstein-Barr virus (EBV). Symptoms include severe or fatal mononucleosis, acquired hypogammaglobulinemia, pancytopenia and malignant lymphoma.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi75 – 751Y → G: Loss of interaction with TAB1/MAP3K7IP1; when associated with G-75. 1 Publication
    Mutagenesisi80 – 801V → A: Strongly reduced interaction with TAB1/MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Reduced activation of NF-kappa-B. 1 Publication
    Mutagenesisi80 – 801V → D: Loss of interaction with TAB1/MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Strongly reduced activation of NF-kappa-B. 1 Publication
    Mutagenesisi86 – 861V → E: Loss of dimerization. Reduces activation of NF-kappa-B. 1 Publication
    Mutagenesisi87 – 871S → A: No effect on dimerization. 1 Publication
    Mutagenesisi87 – 871S → D or E: Abolishes dimerization. Interferes with ubiquitination. 1 Publication
    Mutagenesisi98 – 981L → G: Loss of interaction with TAB1/MAP3K7IP1; when associated with G-75. 1 Publication
    Mutagenesisi141 – 1411L → A: Reduced inhibition of caspase-3. 1 Publication
    Mutagenesisi147 – 1471V → A: Reduced inhibition of caspase-3. 1 Publication
    Mutagenesisi148 – 1481D → A: Abolishes inhibition of caspase-3. Reduced interaction with PRSS25; when associated with S-214. 2 Publications
    Mutagenesisi149 – 1491I → A: Reduced inhibition of caspase-3. 1 Publication
    Mutagenesisi151 – 1511D → A: Reduced inhibition of caspase-3. 1 Publication
    Mutagenesisi167 – 1671L → A: Reduced inhibition of caspase-3. 1 Publication
    Mutagenesisi196 – 1961D → A: Reduced inhibition of caspase-3. May affect protein folding and stability. 1 Publication
    Mutagenesisi214 – 2141D → S: Reduced interaction with PRSS25. Reduced interaction with PRSS25; when associated with A-148. 1 Publication
    Mutagenesisi259 – 2591N → D: Reduced interaction with PRSS25; when associated with S-314. 1 Publication
    Mutagenesisi310 – 3101W → R: Reduced interaction with PRSS25; when associated with S-314. 1 Publication
    Mutagenesisi314 – 3141E → S: Decreased interaction with DIABLO/SMAC and with PRSS25. Decreases interaction with PRSS25; when associated with D-259 or A-310. 1 Publication
    Mutagenesisi450 – 4501C → A or S: Inhibits degradation of active caspase-3. 1 Publication
    Mutagenesisi467 – 4671H → A: Loss of E3 ubiquitin-protein ligase activity. 1 Publication

    Organism-specific databases

    MIMi300635. phenotype.
    Orphaneti2442. X-linked lymphoproliferative disease.
    PharmGKBiPA25361.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 497497E3 ubiquitin-protein ligase XIAPPRO_0000122352Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei87 – 871Phosphoserine; by PKB2 Publications
    Cross-linki322 – 322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Cross-linki328 – 328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Modified residuei450 – 4501S-nitrosocysteine1 Publication

    Post-translational modificationi

    S-Nitrosylation down-regulates its E3 ubiquitin-protein ligase activity.3 Publications
    Autoubiquitinated and degraded by the proteasome in apoptotic cells.2 Publications
    Phosphorylation by PKB/AKT protects XIAP against ubiquitination and protects the protein against proteasomal degradation.3 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    MaxQBiP98170.
    PaxDbiP98170.
    PeptideAtlasiP98170.
    PRIDEiP98170.

    PTM databases

    PhosphoSiteiP98170.

    Miscellaneous databases

    PMAP-CutDBP98170.

    Expressioni

    Tissue specificityi

    Ubiquitous, except peripheral blood leukocytes.

    Gene expression databases

    ArrayExpressiP98170.
    BgeeiP98170.
    CleanExiHS_XIAP.
    GenevestigatoriP98170.

    Organism-specific databases

    HPAiCAB009203.

    Interactioni

    Subunit structurei

    Monomer, and homodimer. Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with TAB1/MAP3K7IP1 and AIFM1. Interaction with SMAC hinders binding of TAB1/MAP3K7IP1 and AIFM1. Interacts with TCF25 and COMMD1. Interacts with SEPT4 isoform 6, but not with other SEPT4 isoforms. Interacts with RIP1, RIP2, RIP3, RIP4, CCS and USP19. Interacts (via BIR 2 domain and BIR 3 domain) with HAX1 (via C-terminus) and this interaction blocks ubiquitination of XIAP/BIRC4. Interacts with the monomeric form of BIRC5/survivin. Interacts with TLE3 and TCF7L2/TCF4.16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASP3P425742EBI-517127,EBI-524064
    CASP7P552102EBI-517127,EBI-523958
    CASP9P552116EBI-517127,EBI-516799
    DIABLOQ9NR288EBI-517127,EBI-517508
    HTRA2O4346418EBI-517127,EBI-517086
    Htra2Q9JIY54EBI-517127,EBI-2365838From a different organism.
    NOTCH1P465314EBI-517127,EBI-636374
    RAC1P630003EBI-517127,EBI-413628
    RIPK4P570782EBI-517127,EBI-4422308
    SEPT4O43236-64EBI-517127,EBI-4372019
    SIAH1Q8IUQ43EBI-517127,EBI-747107
    TRAF6Q9Y4K32EBI-517127,EBI-359276
    UBCP0CG483EBI-517127,EBI-3390054
    UBE2D1P516683EBI-517127,EBI-743540
    UBE2D2P628372EBI-517127,EBI-347677
    UBE2D3P610772EBI-517127,EBI-348268
    UBE2NP610882EBI-517127,EBI-1052908
    UBE2V1Q134042EBI-517127,EBI-1050671

    Protein-protein interaction databases

    BioGridi106828. 108 interactions.
    DIPiDIP-27626N.
    IntActiP98170. 42 interactions.
    MINTiMINT-141734.
    STRINGi9606.ENSP00000347858.

    Structurei

    Secondary structure

    1
    497
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi26 – 305
    Helixi31 – 333
    Beta strandi40 – 423
    Helixi44 – 496
    Beta strandi52 – 543
    Beta strandi61 – 633
    Turni64 – 663
    Helixi79 – 868
    Turni91 – 977
    Turni128 – 1303
    Helixi136 – 1427
    Helixi150 – 1523
    Helixi158 – 1614
    Helixi163 – 1686
    Turni169 – 1724
    Beta strandi175 – 1795
    Helixi181 – 1866
    Beta strandi189 – 1913
    Beta strandi198 – 2003
    Turni201 – 2033
    Beta strandi206 – 2083
    Helixi216 – 2238
    Helixi228 – 2325
    Helixi244 – 2463
    Beta strandi249 – 2513
    Beta strandi254 – 2563
    Helixi260 – 2623
    Helixi265 – 2706
    Turni271 – 2744
    Beta strandi277 – 2793
    Helixi281 – 2866
    Beta strandi289 – 2913
    Beta strandi293 – 2964
    Beta strandi298 – 3003
    Turni301 – 3033
    Beta strandi306 – 3094
    Beta strandi311 – 3133
    Helixi316 – 3238
    Helixi328 – 3336
    Helixi336 – 3427
    Turni343 – 3453
    Helixi347 – 3526
    Helixi354 – 3563
    Helixi368 – 3725
    Helixi375 – 3817
    Helixi386 – 40015
    Helixi407 – 41913
    Helixi437 – 44711
    Turni451 – 4533
    Beta strandi454 – 4574
    Beta strandi460 – 4634
    Helixi472 – 4754
    Turni482 – 4843
    Beta strandi489 – 4935

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C9QNMR-A124-240[»]
    1F9XNMR-A241-356[»]
    1G3FNMR-A241-356[»]
    1G73X-ray2.00C/D238-358[»]
    1I3OX-ray2.70E/F124-240[»]
    1I4OX-ray2.40C/D120-260[»]
    1I51X-ray2.45E/F124-240[»]
    1KMCX-ray2.90C/D124-242[»]
    1NW9X-ray2.40A253-350[»]
    1TFQNMR-A241-356[»]
    1TFTNMR-A241-356[»]
    2ECGNMR-A430-497[»]
    2JK7X-ray2.82A241-356[»]
    2KNANMR-A357-449[»]
    2OPYX-ray2.80A249-354[»]
    2OPZX-ray3.00A/B/C/D249-357[»]
    2POIX-ray1.80A10-99[»]
    2POPX-ray3.10B/D10-100[»]
    2QRAX-ray2.50A/B/C/D10-99[»]
    2VSLX-ray2.10A250-345[»]
    3CLXX-ray2.70A/B/C/D241-356[»]
    3CM2X-ray2.50A/B/C/D/E/F/G/H/I/J241-356[»]
    3CM7X-ray3.10A/B/C/D241-356[»]
    3EYLX-ray3.00A/B241-356[»]
    3G76X-ray3.00A/B/C/D/E/F/G/H241-356[»]
    3HL5X-ray1.80A/B256-346[»]
    3UW4X-ray1.79A338-348[»]
    3UW5X-ray1.71A/B336-348[»]
    4EC4X-ray3.30A/B/C/D/E/F/G/J/K/L241-356[»]
    4HY0X-ray2.84A/B/C/D/E/F/G/H238-357[»]
    4IC2X-ray2.20A/B429-497[»]
    4IC3X-ray1.78A/B429-497[»]
    4J3YX-ray1.45A/C152-236[»]
    4J44X-ray1.30A/C152-236[»]
    4J45X-ray1.48A/C152-236[»]
    4J46X-ray1.42A/C152-236[»]
    4J47X-ray1.35A/C152-236[»]
    4J48X-ray2.10A/C152-236[»]
    4KJUX-ray1.60A/C152-236[»]
    4KJVX-ray1.70A/C152-236[»]
    4KMPX-ray1.95A/B256-348[»]
    ProteinModelPortaliP98170.
    SMRiP98170. Positions 20-99, 124-240, 256-345, 357-497.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP98170.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati26 – 9368BIR 1Add
    BLAST
    Repeati163 – 23068BIR 2Add
    BLAST
    Repeati265 – 33066BIR 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni141 – 1499Interaction with caspase-7

    Domaini

    The first BIR domain is involved in interaction with TAB1/MAP3K7IP1 and is important for dimerization. The second BIR domain is sufficient to inhibit CASP3 and CASP7, while the third BIR is involved in CASP9 inhibition. The interactions with DIABLO/SMAC and PRSS25 are mediated by the second and third BIR domains.

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri450 – 48536RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG243347.
    HOGENOMiHOG000232059.
    HOVERGENiHBG004848.
    InParanoidiP98170.
    KOiK04725.
    OMAiAMYSEEA.
    PhylomeDBiP98170.
    TreeFamiTF105356.

    Family and domain databases

    Gene3Di1.10.1170.10. 4 hits.
    InterProiIPR001370. BIR.
    IPR001841. Znf_RING.
    [Graphical view]
    PfamiPF00653. BIR. 3 hits.
    [Graphical view]
    SMARTiSM00238. BIR. 3 hits.
    SM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS01282. BIR_REPEAT_1. 3 hits.
    PS50143. BIR_REPEAT_2. 3 hits.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P98170-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTFNSFEGSK TCVPADINKE EEFVEEFNRL KTFANFPSGS PVSASTLARA    50
    GFLYTGEGDT VRCFSCHAAV DRWQYGDSAV GRHRKVSPNC RFINGFYLEN 100
    SATQSTNSGI QNGQYKVENY LGSRDHFALD RPSETHADYL LRTGQVVDIS 150
    DTIYPRNPAM YSEEARLKSF QNWPDYAHLT PRELASAGLY YTGIGDQVQC 200
    FCCGGKLKNW EPCDRAWSEH RRHFPNCFFV LGRNLNIRSE SDAVSSDRNF 250
    PNSTNLPRNP SMADYEARIF TFGTWIYSVN KEQLARAGFY ALGEGDKVKC 300
    FHCGGGLTDW KPSEDPWEQH AKWYPGCKYL LEQKGQEYIN NIHLTHSLEE 350
    CLVRTTEKTP SLTRRIDDTI FQNPMVQEAI RMGFSFKDIK KIMEEKIQIS 400
    GSNYKSLEVL VADLVNAQKD SMQDESSQTS LQKEISTEEQ LRRLQEEKLC 450
    KICMDRNIAI VFVPCGHLVT CKQCAEAVDK CPMCYTVITF KQKIFMS 497
    Length:497
    Mass (Da):56,685
    Last modified:January 24, 2001 - v2
    Checksum:i9D394C16D45EB635
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621S → C in AAC50373. (PubMed:8552191)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071N → S.1 Publication
    Corresponds to variant rs28382721 [ dbSNP | Ensembl ].
    VAR_022282
    Natural varianti133 – 1331S → F.1 Publication
    Corresponds to variant rs28382722 [ dbSNP | Ensembl ].
    VAR_022283
    Natural varianti242 – 2421D → E.1 Publication
    Corresponds to variant rs28382723 [ dbSNP | Ensembl ].
    VAR_022284
    Natural varianti423 – 4231Q → P.2 Publications
    Corresponds to variant rs5956583 [ dbSNP | Ensembl ].
    VAR_022285

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U32974 mRNA. Translation: AAC50518.1.
    U45880 mRNA. Translation: AAC50373.1.
    AY886519 Genomic DNA. Translation: AAW62257.1.
    AL121601 Genomic DNA. Translation: CAB95312.1.
    CH471107 Genomic DNA. Translation: EAX11858.1.
    CH471107 Genomic DNA. Translation: EAX11859.1.
    CH471107 Genomic DNA. Translation: EAX11860.1.
    CH471107 Genomic DNA. Translation: EAX11861.1.
    BC032729 mRNA. Translation: AAH32729.1.
    CCDSiCCDS14606.1.
    PIRiS69544.
    RefSeqiNP_001158.2. NM_001167.3.
    NP_001191330.1. NM_001204401.1.
    XP_006724817.1. XM_006724754.1.
    UniGeneiHs.356076.
    Hs.736565.

    Genome annotation databases

    EnsembliENST00000355640; ENSP00000347858; ENSG00000101966.
    ENST00000371199; ENSP00000360242; ENSG00000101966.
    ENST00000434753; ENSP00000395230; ENSG00000101966.
    GeneIDi331.
    KEGGihsa:331.
    UCSCiuc004etx.3. human.

    Polymorphism databases

    DMDMi12643387.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    BIRC4base

    XIAP mutation db

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U32974 mRNA. Translation: AAC50518.1 .
    U45880 mRNA. Translation: AAC50373.1 .
    AY886519 Genomic DNA. Translation: AAW62257.1 .
    AL121601 Genomic DNA. Translation: CAB95312.1 .
    CH471107 Genomic DNA. Translation: EAX11858.1 .
    CH471107 Genomic DNA. Translation: EAX11859.1 .
    CH471107 Genomic DNA. Translation: EAX11860.1 .
    CH471107 Genomic DNA. Translation: EAX11861.1 .
    BC032729 mRNA. Translation: AAH32729.1 .
    CCDSi CCDS14606.1.
    PIRi S69544.
    RefSeqi NP_001158.2. NM_001167.3.
    NP_001191330.1. NM_001204401.1.
    XP_006724817.1. XM_006724754.1.
    UniGenei Hs.356076.
    Hs.736565.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C9Q NMR - A 124-240 [» ]
    1F9X NMR - A 241-356 [» ]
    1G3F NMR - A 241-356 [» ]
    1G73 X-ray 2.00 C/D 238-358 [» ]
    1I3O X-ray 2.70 E/F 124-240 [» ]
    1I4O X-ray 2.40 C/D 120-260 [» ]
    1I51 X-ray 2.45 E/F 124-240 [» ]
    1KMC X-ray 2.90 C/D 124-242 [» ]
    1NW9 X-ray 2.40 A 253-350 [» ]
    1TFQ NMR - A 241-356 [» ]
    1TFT NMR - A 241-356 [» ]
    2ECG NMR - A 430-497 [» ]
    2JK7 X-ray 2.82 A 241-356 [» ]
    2KNA NMR - A 357-449 [» ]
    2OPY X-ray 2.80 A 249-354 [» ]
    2OPZ X-ray 3.00 A/B/C/D 249-357 [» ]
    2POI X-ray 1.80 A 10-99 [» ]
    2POP X-ray 3.10 B/D 10-100 [» ]
    2QRA X-ray 2.50 A/B/C/D 10-99 [» ]
    2VSL X-ray 2.10 A 250-345 [» ]
    3CLX X-ray 2.70 A/B/C/D 241-356 [» ]
    3CM2 X-ray 2.50 A/B/C/D/E/F/G/H/I/J 241-356 [» ]
    3CM7 X-ray 3.10 A/B/C/D 241-356 [» ]
    3EYL X-ray 3.00 A/B 241-356 [» ]
    3G76 X-ray 3.00 A/B/C/D/E/F/G/H 241-356 [» ]
    3HL5 X-ray 1.80 A/B 256-346 [» ]
    3UW4 X-ray 1.79 A 338-348 [» ]
    3UW5 X-ray 1.71 A/B 336-348 [» ]
    4EC4 X-ray 3.30 A/B/C/D/E/F/G/J/K/L 241-356 [» ]
    4HY0 X-ray 2.84 A/B/C/D/E/F/G/H 238-357 [» ]
    4IC2 X-ray 2.20 A/B 429-497 [» ]
    4IC3 X-ray 1.78 A/B 429-497 [» ]
    4J3Y X-ray 1.45 A/C 152-236 [» ]
    4J44 X-ray 1.30 A/C 152-236 [» ]
    4J45 X-ray 1.48 A/C 152-236 [» ]
    4J46 X-ray 1.42 A/C 152-236 [» ]
    4J47 X-ray 1.35 A/C 152-236 [» ]
    4J48 X-ray 2.10 A/C 152-236 [» ]
    4KJU X-ray 1.60 A/C 152-236 [» ]
    4KJV X-ray 1.70 A/C 152-236 [» ]
    4KMP X-ray 1.95 A/B 256-348 [» ]
    ProteinModelPortali P98170.
    SMRi P98170. Positions 20-99, 124-240, 256-345, 357-497.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106828. 108 interactions.
    DIPi DIP-27626N.
    IntActi P98170. 42 interactions.
    MINTi MINT-141734.
    STRINGi 9606.ENSP00000347858.

    Chemistry

    BindingDBi P98170.
    ChEMBLi CHEMBL4198.

    Protein family/group databases

    MEROPSi I32.004.

    PTM databases

    PhosphoSitei P98170.

    Polymorphism databases

    DMDMi 12643387.

    Proteomic databases

    MaxQBi P98170.
    PaxDbi P98170.
    PeptideAtlasi P98170.
    PRIDEi P98170.

    Protocols and materials databases

    DNASUi 331.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355640 ; ENSP00000347858 ; ENSG00000101966 .
    ENST00000371199 ; ENSP00000360242 ; ENSG00000101966 .
    ENST00000434753 ; ENSP00000395230 ; ENSG00000101966 .
    GeneIDi 331.
    KEGGi hsa:331.
    UCSCi uc004etx.3. human.

    Organism-specific databases

    CTDi 331.
    GeneCardsi GC0XP122993.
    GeneReviewsi XIAP.
    HGNCi HGNC:592. XIAP.
    HPAi CAB009203.
    MIMi 300079. gene.
    300635. phenotype.
    neXtProti NX_P98170.
    Orphaneti 2442. X-linked lymphoproliferative disease.
    PharmGKBi PA25361.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG243347.
    HOGENOMi HOG000232059.
    HOVERGENi HBG004848.
    InParanoidi P98170.
    KOi K04725.
    OMAi AMYSEEA.
    PhylomeDBi P98170.
    TreeFami TF105356.

    Enzyme and pathway databases

    Reactomei REACT_200731. deactivation of the beta-catenin transactivating complex.
    SABIO-RK P98170.
    SignaLinki P98170.

    Miscellaneous databases

    ChiTaRSi XIAP. human.
    EvolutionaryTracei P98170.
    GeneWikii XIAP.
    GenomeRNAii 331.
    NextBioi 1365.
    PMAP-CutDB P98170.
    PROi P98170.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P98170.
    Bgeei P98170.
    CleanExi HS_XIAP.
    Genevestigatori P98170.

    Family and domain databases

    Gene3Di 1.10.1170.10. 4 hits.
    InterProi IPR001370. BIR.
    IPR001841. Znf_RING.
    [Graphical view ]
    Pfami PF00653. BIR. 3 hits.
    [Graphical view ]
    SMARTi SM00238. BIR. 3 hits.
    SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS01282. BIR_REPEAT_1. 3 hits.
    PS50143. BIR_REPEAT_2. 3 hits.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors."
      Duckett C.S., Nava V.E., Gedrich R.W., Clem R.J., van Dongen J.L., Gilfillan M.C., Shiels H., Hardwick J.M., Thompson C.B.
      EMBO J. 15:2685-2694(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-423.
      Tissue: Fetal heart.
    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: Fetal brain.
    3. NIEHS SNPs program
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-107; PHE-133; GLU-242 AND PRO-423.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Uterus.
    7. "X-linked IAP is a direct inhibitor of cell-death proteases."
      Deveraux Q.L., Takahashi R., Salvesen G.S., Reed J.C.
      Nature 388:300-304(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death."
      Suzuki Y., Nakabayashi Y., Takahashi R.
      Proc. Natl. Acad. Sci. U.S.A. 98:8662-8667(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-450.
    9. "HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins."
      Verhagen A.M., Silke J., Ekert P.G., Pakusch M., Kaufmann H., Connolly L.M., Day C.L., Tikoo A., Burke R., Wrobel C., Moritz R.L., Simpson R.J., Vaux D.L.
      J. Biol. Chem. 277:445-454(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-148; ASP-214; ASN-259; TRP-310 AND GLU-314.
    10. "Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro."
      MacFarlane M., Merrison W., Bratton S.B., Cohen G.M.
      J. Biol. Chem. 277:36611-36616(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Identification of ubiquitination sites on the X-linked inhibitor of apoptosis protein."
      Shin H., Okada K., Wilkinson J.C., Solomon K.M., Duckett C.S., Reed J.C., Salvesen G.S.
      Biochem. J. 373:965-971(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOUBIQUITINATION AT LYS-322 AND LYS-328.
    12. Cited for: INTERACTION WITH COMMD1, FUNCTION.
    13. "The mitochondrial ARTS protein promotes apoptosis through targeting XIAP."
      Gottfried Y., Rotem A., Lotan R., Steller H., Larisch S.
      EMBO J. 23:1627-1635(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEPT4.
    14. "Akt phosphorylation and stabilization of X-linked inhibitor of apoptosis protein (XIAP)."
      Dan H.C., Sun M., Kaneko S., Feldman R.I., Nicosia S.V., Wang H.-G., Tsang B.K., Cheng J.Q.
      J. Biol. Chem. 279:5405-5412(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-87, UBIQUITINATION, PROTEASOMAL DEGRADATION.
    15. "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.
    16. Cited for: INVOLVEMENT IN XLP2.
    17. "XIAP: cell death regulation meets copper homeostasis."
      Mufti A.R., Burstein E., Duckett C.S.
      Arch. Biochem. Biophys. 463:168-174(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    18. "Nuclear localized protein-1 (Nulp1) increases cell death of human osteosarcoma cells and binds the X-linked inhibitor of apoptosis protein."
      Steen H., Lindholm D.
      Biochem. Biophys. Res. Commun. 366:432-437(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TCF25.
    19. "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.
    20. "Apoptosis-inducing factor is a target for ubiquitination through interaction with XIAP."
      Wilkinson J.C., Wilkinson A.S., Galban S., Csomos R.A., Duckett C.S.
      Mol. Cell. Biol. 28:237-247(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF HIS-467, INTERACTION WITH AIFM1.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN ubiquitination, content, and compartmentalization."
      Van Themsche C., Leblanc V., Parent S., Asselin E.
      J. Biol. Chem. 284:20462-20466(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE UBIQUITINATION OF PTEN, INTERACTION WITH PTEN.
    23. Cited for: INTERACTION WITH HAX1.
    24. "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.
    25. Cited for: S-NITROSYLATION AT CYS-450.
    26. "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.
    27. Cited for: FUNCTION IN THE UBIQUITINATION OF CCS, INTERACTION WITH CCS.
    28. "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.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Nondegradative ubiquitination of apoptosis inducing factor (AIF) by X-linked inhibitor of apoptosis at a residue critical for AIF-mediated chromatin degradation."
      Lewis E.M., Wilkinson A.S., Davis N.Y., Horita D.A., Wilkinson J.C.
      Biochemistry 50:11084-11096(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE UBIQUITINATION OF AIFM1.
    31. "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.
    32. Cited for: INTERACTION WITH BIRC5/SURVIVIN.
    33. "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: INTERACTION WITH USP19.
    34. "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: INTERACTION WITH RIPK1; RIPK2; RIPK3 AND RIPK4.
    35. Cited for: REVIEW ON FUNCTION.
    36. "XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling."
      Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A., Lee E.
      Mol. Cell 45:619-628(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TLE3 AND TCF7L2/TCF4.
    37. "NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP."
      Sun C., Cai M., Gunasekera A.H., Meadows R.P., Wang H., Chen J., Zhang H., Wu W., Xu N., Ng S.-C., Fesik S.W.
      Nature 401:818-822(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 124-240, MUTAGENESIS OF LEU-141; VAL-147; ASP-148; ILE-149; ASP-151; LEU-167 AND ASP-196.
    38. "Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain."
      Liu Z., Sun C., Olejniczak E.T., Meadows R.P., Betz S.F., Oost T., Herrmann J., Wu J.C., Fesik S.W.
      Nature 408:1004-1008(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 238-358 IN COMPLEX WITH DIABLO/SMAC.
    39. "Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain."
      Huang Y., Park Y.C., Rich R.L., Segal D., Myszka D.G., Wu H.
      Cell 104:781-790(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 120-260 IN COMPLEX WITH CASP7.
    40. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 253-350 IN COMPLEX WITH CASP9.
    41. Cited for: STRUCTURE BY NMR OF 241-356.
    42. "Structure-activity based study of the Smac-binding pocket within the BIR3 domain of XIAP."
      Wist A.D., Gu L., Riedl S.J., Shi Y., McLendon G.L.
      Bioorg. Med. Chem. 15:2935-2943(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 249-354.
    43. "Crystal structure of the BIR1 domain of XIAP in two crystal forms."
      Lin S.-C., Huang Y., Lo Y.-C., Lu M., Wu H.
      J. Mol. Biol. 372:847-854(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-99, PHOSPHORYLATION AT SER-87, MUTAGENESIS OF SER-87, SUBUNIT.
    44. "XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1 dimerization."
      Lu M., Lin S.-C., Huang Y., Kang Y.J., Rich R., Lo Y.-C., Myszka D., Han J., Wu H.
      Mol. Cell 26:689-702(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-99 IN COMPLEX WITH TAB1, FUNCTION, MUTAGENESIS OF TYR-75; VAL-80; VAL-86 AND LEU-98.
    45. "Solution structure of the RING domain of the baculoviral IAP repeat-containing protein 4 from Homo sapiens."
      RIKEN structural genomics initiative (RSGI)
      Submitted (MAR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 427-497.

    Entry informationi

    Entry nameiXIAP_HUMAN
    AccessioniPrimary (citable) accession number: P98170
    Secondary accession number(s): D3DTF2, Q9NQ14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 24, 2001
    Last modified: October 1, 2014
    This is version 161 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 X
      Human chromosome X: 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