Details for: XIAP

Gene ID: 331

Symbol: XIAP

Ensembl ID: ENSG00000101966

Description: X-linked inhibitor of apoptosis

Associated with

Other Information

Genular Protein ID: 456314144

Symbol: XIAP_HUMAN

Name: E3 ubiquitin-protein ligase XIAP

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 8654366

Title: A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors.

PubMed ID: 8654366

DOI: 10.1002/j.1460-2075.1996.tb00629.x

PubMed ID: 8552191

Title: Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes.

PubMed ID: 8552191

DOI: 10.1038/379349a0

PubMed ID: 15772651

Title: The DNA sequence of the human X chromosome.

PubMed ID: 15772651

DOI: 10.1038/nature03440

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9230442

Title: X-linked IAP is a direct inhibitor of cell-death proteases.

PubMed ID: 9230442

DOI: 10.1038/40901

PubMed ID: 11447297

Title: 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.

PubMed ID: 11447297

DOI: 10.1073/pnas.161506698

PubMed ID: 11604410

Title: HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins.

PubMed ID: 11604410

DOI: 10.1074/jbc.m109891200

PubMed ID: 12121969

Title: Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro.

PubMed ID: 12121969

DOI: 10.1074/jbc.m200317200

PubMed ID: 12747801

Title: Identification of ubiquitination sites on the X-linked inhibitor of apoptosis protein.

PubMed ID: 12747801

DOI: 10.1042/bj20030583

PubMed ID: 14685266

Title: A novel role for XIAP in copper homeostasis through regulation of MURR1.

PubMed ID: 14685266

DOI: 10.1038/sj.emboj.7600031

PubMed ID: 15029247

Title: The mitochondrial ARTS protein promotes apoptosis through targeting XIAP.

PubMed ID: 15029247

DOI: 10.1038/sj.emboj.7600155

PubMed ID: 14645242

Title: Akt phosphorylation and stabilization of X-linked inhibitor of apoptosis protein (XIAP).

PubMed ID: 14645242

DOI: 10.1074/jbc.m312044200

PubMed ID: 27825084

Title:

PubMed ID: 27825084

DOI: 10.1074/jbc.a116.312044

PubMed ID: 15665297

Title: cIAP1 Localizes to the nuclear compartment and modulates the cell cycle.

PubMed ID: 15665297

DOI: 10.1158/0008-5472.210.65.1

PubMed ID: 16352606

Title: Caspase-7 is directly activated by the approximately 700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 approximately 200-kDa complex.

PubMed ID: 16352606

DOI: 10.1074/jbc.m507393200

PubMed ID: 17080092

Title: XIAP deficiency in humans causes an X-linked lymphoproliferative syndrome.

PubMed ID: 17080092

DOI: 10.1038/nature05257

PubMed ID: 16916640

Title: Engineered hybrid dimers: tracking the activation pathway of caspase-7.

PubMed ID: 16916640

DOI: 10.1016/j.molcel.2006.06.020

PubMed ID: 17382285

Title: XIAP: cell death regulation meets copper homeostasis.

PubMed ID: 17382285

DOI: 10.1016/j.abb.2007.01.033

PubMed ID: 18068114

Title: Nuclear localized protein-1 (Nulp1) increases cell death of human osteosarcoma cells and binds the X-linked inhibitor of apoptosis protein.

PubMed ID: 18068114

DOI: 10.1016/j.bbrc.2007.11.146

PubMed ID: 18414036

Title: IAPs: more than just inhibitors of apoptosis proteins.

PubMed ID: 18414036

DOI: 10.4161/cc.7.8.5783

PubMed ID: 19012568

Title: Binding properties of the C-terminal domain of VIAF.

PubMed ID: 19012568

DOI: 10.1111/j.1747-0285.2008.00719.x

PubMed ID: 17967870

Title: Apoptosis-inducing factor is a target for ubiquitination through interaction with XIAP.

PubMed ID: 17967870

DOI: 10.1128/mcb.01065-07

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19473982

Title: X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN ubiquitination, content, and compartmentalization.

PubMed ID: 19473982

DOI: 10.1074/jbc.c109.009522

PubMed ID: 19667203

Title: XIAP mediates NOD signaling via interaction with RIP2.

PubMed ID: 19667203

DOI: 10.1073/pnas.0907131106

PubMed ID: 20171186

Title: Molecular interaction between HAX-1 and XIAP inhibits apoptosis.

PubMed ID: 20171186

DOI: 10.1016/j.bbrc.2010.02.084

PubMed ID: 20888210

Title: To fight or die - inhibitor of apoptosis proteins at the crossroad of innate immunity and death.

PubMed ID: 20888210

DOI: 10.1016/j.ceb.2010.08.025

PubMed ID: 20670888

Title: Transnitrosylation of XIAP regulates caspase-dependent neuronal cell death.

PubMed ID: 20670888

DOI: 10.1016/j.molcel.2010.07.002

PubMed ID: 21145488

Title: Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3 ligases.

PubMed ID: 21145488

DOI: 10.1016/j.molcel.2010.11.011

PubMed ID: 20154138

Title: Regulation of the copper chaperone CCS by XIAP-mediated ubiquitination.

PubMed ID: 20154138

DOI: 10.1128/mcb.00900-09

PubMed ID: 20651737

Title: IAPs: from caspase inhibitors to modulators of NF-kappaB, inflammation and cancer.

PubMed ID: 20651737

DOI: 10.1038/nrc2889

PubMed ID: 21695558

Title: ARTS binds to a distinct domain in XIAP-BIR3 and promotes apoptosis by a mechanism that is different from other IAP-antagonists.

PubMed ID: 21695558

DOI: 10.1007/s10495-011-0622-0

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22103349

Title: Nondegradative ubiquitination of apoptosis inducing factor (AIF) by X-linked inhibitor of apoptosis at a residue critical for AIF-mediated chromatin degradation.

PubMed ID: 22103349

DOI: 10.1021/bi201483g

PubMed ID: 21447281

Title: Inhibitor of apoptosis (IAP) proteins in regulation of inflammation and innate immunity.

PubMed ID: 21447281

PubMed ID: 21536684

Title: Survivin monomer plays an essential role in apoptosis regulation.

PubMed ID: 21536684

DOI: 10.1074/jbc.m111.237586

PubMed ID: 21849505

Title: The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2.

PubMed ID: 21849505

DOI: 10.1074/jbc.m111.282020

PubMed ID: 21931591

Title: cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).

PubMed ID: 21931591

DOI: 10.1371/journal.pone.0022356

PubMed ID: 22095281

Title: IAPs: guardians of RIPK1.

PubMed ID: 22095281

DOI: 10.1038/cdd.2011.163

PubMed ID: 22607974

Title: The ubiquitin ligase XIAP recruits LUBAC for NOD2 signaling in inflammation and innate immunity.

PubMed ID: 22607974

DOI: 10.1016/j.molcel.2012.04.014

PubMed ID: 30389919

Title: ARTS mediates apoptosis and regeneration of the intestinal stem cell niche.

PubMed ID: 30389919

DOI: 10.1038/s41467-018-06941-4

PubMed ID: 22304967

Title: XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt signaling.

PubMed ID: 22304967

DOI: 10.1016/j.molcel.2011.12.032

PubMed ID: 29020630

Title: Degradation of Bcl-2 by XIAP and ARTS Promotes Apoptosis.

PubMed ID: 29020630

DOI: 10.1016/j.celrep.2017.09.052

PubMed ID: 30026309

Title: Small molecule inhibitors reveal an indispensable scaffolding role of RIPK2 in NOD2 signaling.

PubMed ID: 30026309

DOI: 10.15252/embj.201899372

PubMed ID: 29452636

Title: Disruption of XIAP-RIP2 association blocks NOD2-mediated inflammatory signaling.

PubMed ID: 29452636

DOI: 10.1016/j.molcel.2018.01.016

PubMed ID: 10548111

Title: NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP.

PubMed ID: 10548111

DOI: 10.1038/44617

PubMed ID: 11140637

Title: Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain.

PubMed ID: 11140637

DOI: 10.1038/35050006

PubMed ID: 11257230

Title: Structural basis of caspase-7 inhibition by XIAP.

PubMed ID: 11257230

DOI: 10.1016/s0092-8674(01)00272-0

PubMed ID: 11257231

Title: Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain.

PubMed ID: 11257231

DOI: 10.1016/s0092-8674(02)02075-5

PubMed ID: 12620238

Title: Mechanism of XIAP-mediated inhibition of caspase-9.

PubMed ID: 12620238

DOI: 10.1016/s1097-2765(03)00054-6

PubMed ID: 15317454

Title: Discovery of potent antagonists of the antiapoptotic protein XIAP for the treatment of cancer.

PubMed ID: 15317454

DOI: 10.1021/jm040037k

PubMed ID: 17336535

Title: Structure-activity based study of the Smac-binding pocket within the BIR3 domain of XIAP.

PubMed ID: 17336535

DOI: 10.1016/j.bmc.2007.02.010

PubMed ID: 17698078

Title: Crystal structure of the BIR1 domain of XIAP in two crystal forms.

PubMed ID: 17698078

DOI: 10.1016/j.jmb.2007.07.019

PubMed ID: 17560374

Title: XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1 dimerization.

PubMed ID: 17560374

DOI: 10.1016/j.molcel.2007.05.006

PubMed ID: 20489057

Title: XIAP deficiency: a unique primary immunodeficiency best classified as X-linked familial hemophagocytic lymphohistiocytosis and not as X-linked lymphoproliferative disease.

PubMed ID: 20489057

DOI: 10.1182/blood-2010-01-256099

PubMed ID: 21119115

Title: Clinical similarities and differences of patients with X-linked lymphoproliferative syndrome type 1 (XLP-1/SAP deficiency) versus type 2 (XLP-2/XIAP deficiency).

PubMed ID: 21119115

DOI: 10.1182/blood-2010-07-298372

Sequence Information:

  • Length: 497
  • Mass: 56685
  • Checksum: 9D394C16D45EB635
  • Sequence:
  • MTFNSFEGSK TCVPADINKE EEFVEEFNRL KTFANFPSGS PVSASTLARA GFLYTGEGDT 
    VRCFSCHAAV DRWQYGDSAV GRHRKVSPNC RFINGFYLEN SATQSTNSGI QNGQYKVENY 
    LGSRDHFALD RPSETHADYL LRTGQVVDIS DTIYPRNPAM YSEEARLKSF QNWPDYAHLT 
    PRELASAGLY YTGIGDQVQC FCCGGKLKNW EPCDRAWSEH RRHFPNCFFV LGRNLNIRSE 
    SDAVSSDRNF PNSTNLPRNP SMADYEARIF TFGTWIYSVN KEQLARAGFY ALGEGDKVKC 
    FHCGGGLTDW KPSEDPWEQH AKWYPGCKYL LEQKGQEYIN NIHLTHSLEE CLVRTTEKTP 
    SLTRRIDDTI FQNPMVQEAI RMGFSFKDIK KIMEEKIQIS GSNYKSLEVL VADLVNAQKD 
    SMQDESSQTS LQKEISTEEQ LRRLQEEKLC KICMDRNIAI VFVPCGHLVT CKQCAEAVDK 
    CPMCYTVITF KQKIFMS

Genular Protein ID: 3300899479

Symbol: B2R9R2_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 497
  • Mass: 56624
  • Checksum: 6EE3E5338BF55CCB
  • Sequence:
  • MTFNSFEGSK TCVPADINKE EEFVEEFNRL KTFANFPSGS PVSASTLARA GFLYTGEGDT 
    VRCFSCHAAV DRWQYGDSAV GRHRKVSPNC RFINGFYLEN SATQSTNSGI QNGQYKVENY 
    LGSRDHFALD RPSEAHADYL LRTGQVVDIS DTIYPRNPAM YSEEARLKSF QNWPDYAHLT 
    PRELASAGLY YTGIGDQVQC FCCGGKLKNW EPCDRAWSEH RRHFPNCFFV LGRNLNIRSE 
    SDAVSSDRNF PNSTNLPRNP SMADYEARIF TFGTWIYSVN KEQLARAGFY ALGEGDKVKC 
    FHCGGGLTDW KPSEDPWEQH AKWYPGCKYL LEQKGQEYIN NIHLTHSLEE CLVRTTEKTP 
    SLTRRIDDTI FQNPMVQEAI RMGFSFKDIK KIMEEKIQIS GSNYKSLEVL VADLVNAQKD 
    SMPDESSQTS LQKEISTEEQ LRRLQEEKLC KICMDRNIAI VFVPCGHLVT CKQCAEAVDK 
    CPMCYTVITF KQKIFMS

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.