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E3 ubiquitin-protein ligase XIAP (EC 2.3.2.27) (Baculoviral IAP repeat-containing protein 4) (IAP-like protein) (ILP) (hILP) (Inhibitor of apoptosis protein 3) (IAP-3) (hIAP-3) (hIAP3) (RING-type E3 ubiquitin transferase XIAP) (X-linked inhibitor of apoptosis protein) (X-linked IAP)

 XIAP_HUMAN              Reviewed;         497 AA.
P98170; D3DTF2; Q9NQ14;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 2.
27-SEP-2017, entry version 192.
RecName: Full=E3 ubiquitin-protein ligase XIAP;
EC=2.3.2.27;
AltName: Full=Baculoviral IAP repeat-containing protein 4;
AltName: Full=IAP-like protein;
Short=ILP;
Short=hILP;
AltName: Full=Inhibitor of apoptosis protein 3;
Short=IAP-3;
Short=hIAP-3;
Short=hIAP3;
AltName: Full=RING-type E3 ubiquitin transferase XIAP;
AltName: Full=X-linked inhibitor of apoptosis protein;
Short=X-linked IAP;
Name=XIAP; Synonyms=API3, BIRC4, IAP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-423.
TISSUE=Fetal heart;
PubMed=8654366;
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.;
"A conserved family of cellular genes related to the baculovirus iap
gene and encoding apoptosis inhibitors.";
EMBO J. 15:2685-2694(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal brain;
PubMed=8552191; DOI=10.1038/379349a0;
Liston P., Roy N., Tamai K., Lefebvre C., Baird S., Cherton-Horvat G.,
Farahani R., McLean M., Ikeda J., Mackenzie A., Korneluk R.G.;
"Suppression of apoptosis in mammalian cells by NAIP and a related
family of IAP genes.";
Nature 379:349-353(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-107; PHE-133;
GLU-242 AND PRO-423.
NIEHS SNPs program;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
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.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION.
PubMed=9230442; DOI=10.1038/40901;
Deveraux Q.L., Takahashi R., Salvesen G.S., Reed J.C.;
"X-linked IAP is a direct inhibitor of cell-death proteases.";
Nature 388:300-304(1997).
[8]
FUNCTION, AND MUTAGENESIS OF CYS-450.
PubMed=11447297; DOI=10.1073/pnas.161506698;
Suzuki Y., Nakabayashi Y., Takahashi R.;
"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.";
Proc. Natl. Acad. Sci. U.S.A. 98:8662-8667(2001).
[9]
MUTAGENESIS OF ASP-148; ASP-214; ASN-259; TRP-310 AND GLU-314.
PubMed=11604410; DOI=10.1074/jbc.M109891200;
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.;
"HtrA2 promotes cell death through its serine protease activity and
its ability to antagonize inhibitor of apoptosis proteins.";
J. Biol. Chem. 277:445-454(2002).
[10]
FUNCTION.
PubMed=12121969; DOI=10.1074/jbc.M200317200;
MacFarlane M., Merrison W., Bratton S.B., Cohen G.M.;
"Proteasome-mediated degradation of Smac during apoptosis: XIAP
promotes Smac ubiquitination in vitro.";
J. Biol. Chem. 277:36611-36616(2002).
[11]
AUTOUBIQUITINATION AT LYS-322 AND LYS-328.
PubMed=12747801; DOI=10.1042/BJ20030583;
Shin H., Okada K., Wilkinson J.C., Solomon K.M., Duckett C.S.,
Reed J.C., Salvesen G.S.;
"Identification of ubiquitination sites on the X-linked inhibitor of
apoptosis protein.";
Biochem. J. 373:965-971(2003).
[12]
INTERACTION WITH COMMD1, AND FUNCTION.
PubMed=14685266; DOI=10.1038/sj.emboj.7600031;
Burstein E., Ganesh L., Dick R.D., van De Sluis B., Wilkinson J.C.,
Klomp L.W., Wijmenga C., Brewer G.J., Nabel G.J., Duckett C.S.;
"A novel role for XIAP in copper homeostasis through regulation of
MURR1.";
EMBO J. 23:244-254(2004).
[13]
INTERACTION WITH SEPT4.
PubMed=15029247; DOI=10.1038/sj.emboj.7600155;
Gottfried Y., Rotem A., Lotan R., Steller H., Larisch S.;
"The mitochondrial ARTS protein promotes apoptosis through targeting
XIAP.";
EMBO J. 23:1627-1635(2004).
[14]
FUNCTION, PHOSPHORYLATION AT SER-87, UBIQUITINATION, AND PROTEASOMAL
DEGRADATION.
PubMed=14645242; DOI=10.1074/jbc.M312044200;
Dan H.C., Sun M., Kaneko S., Feldman R.I., Nicosia S.V., Wang H.-G.,
Tsang B.K., Cheng J.Q.;
"Akt phosphorylation and stabilization of X-linked inhibitor of
apoptosis protein (XIAP).";
J. Biol. Chem. 279:5405-5412(2004).
[15]
SUBCELLULAR LOCATION.
PubMed=15665297;
Samuel T., Okada K., Hyer M., Welsh K., Zapata J.M., Reed J.C.;
"cIAP1 Localizes to the nuclear compartment and modulates the cell
cycle.";
Cancer Res. 65:210-218(2005).
[16]
INVOLVEMENT IN XLP2.
PubMed=17080092; DOI=10.1038/nature05257;
Rigaud S., Fondaneche M.-C., Lambert N., Pasquier B., Mateo V.,
Soulas P., Galicier L., Le Deist F., Rieux-Laucat F., Revy P.,
Fischer A., de Saint Basile G., Latour S.;
"XIAP deficiency in humans causes an X-linked lymphoproliferative
syndrome.";
Nature 444:110-114(2006).
[17]
REVIEW ON FUNCTION.
PubMed=17382285; DOI=10.1016/j.abb.2007.01.033;
Mufti A.R., Burstein E., Duckett C.S.;
"XIAP: cell death regulation meets copper homeostasis.";
Arch. Biochem. Biophys. 463:168-174(2007).
[18]
INTERACTION WITH TCF25.
PubMed=18068114; DOI=10.1016/j.bbrc.2007.11.146;
Steen H., Lindholm D.;
"Nuclear localized protein-1 (Nulp1) increases cell death of human
osteosarcoma cells and binds the X-linked inhibitor of apoptosis
protein.";
Biochem. Biophys. Res. Commun. 366:432-437(2008).
[19]
REVIEW ON FUNCTION.
PubMed=18414036; DOI=10.4161/cc.7.8.5783;
Dubrez-Daloz L., Dupoux A., Cartier J.;
"IAPs: more than just inhibitors of apoptosis proteins.";
Cell Cycle 7:1036-1046(2008).
[20]
FUNCTION, MUTAGENESIS OF HIS-467, AND INTERACTION WITH AIFM1.
PubMed=17967870; DOI=10.1128/MCB.01065-07;
Wilkinson J.C., Wilkinson A.S., Galban S., Csomos R.A., Duckett C.S.;
"Apoptosis-inducing factor is a target for ubiquitination through
interaction with XIAP.";
Mol. Cell. Biol. 28:237-247(2008).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
FUNCTION IN THE UBIQUITINATION OF PTEN, AND INTERACTION WITH PTEN.
PubMed=19473982; DOI=10.1074/jbc.C109.009522;
Van Themsche C., Leblanc V., Parent S., Asselin E.;
"X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN
ubiquitination, content, and compartmentalization.";
J. Biol. Chem. 284:20462-20466(2009).
[23]
INTERACTION WITH HAX1.
PubMed=20171186; DOI=10.1016/j.bbrc.2010.02.084;
Kang Y.J., Jang M., Park Y.K., Kang S., Bae K.H., Cho S., Lee C.K.,
Park B.C., Chi S.W., Park S.G.;
"Molecular interaction between HAX-1 and XIAP inhibits apoptosis.";
Biochem. Biophys. Res. Commun. 393:794-799(2010).
[24]
REVIEW ON FUNCTION.
PubMed=20888210; DOI=10.1016/j.ceb.2010.08.025;
Lopez J., Meier P.;
"To fight or die - inhibitor of apoptosis proteins at the crossroad of
innate immunity and death.";
Curr. Opin. Cell Biol. 22:872-881(2010).
[25]
S-NITROSYLATION AT CYS-450.
PubMed=20670888; DOI=10.1016/j.molcel.2010.07.002;
Nakamura T., Wang L., Wong C.C., Scott F.L., Eckelman B.P., Han X.,
Tzitzilonis C., Meng F., Gu Z., Holland E.A., Clemente A.T.,
Okamoto S., Salvesen G.S., Riek R., Yates J.R. III, Lipton S.A.;
"Transnitrosylation of XIAP regulates caspase-dependent neuronal cell
death.";
Mol. Cell 39:184-195(2010).
[26]
FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE OF THE NEDD8 CONJUGATION
PATHWAY.
PubMed=21145488; DOI=10.1016/j.molcel.2010.11.011;
Broemer M., Tenev T., Rigbolt K.T., Hempel S., Blagoev B., Silke J.,
Ditzel M., Meier P.;
"Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3
ligases.";
Mol. Cell 40:810-822(2010).
[27]
FUNCTION IN THE UBIQUITINATION OF CCS, AND INTERACTION WITH CCS.
PubMed=20154138; DOI=10.1128/MCB.00900-09;
Brady G.F., Galban S., Liu X., Basrur V., Gitlin J.D.,
Elenitoba-Johnson K.S., Wilson T.E., Duckett C.S.;
"Regulation of the copper chaperone CCS by XIAP-mediated
ubiquitination.";
Mol. Cell. Biol. 30:1923-1936(2010).
[28]
REVIEW ON FUNCTION.
PubMed=20651737; DOI=10.1038/nrc2889;
Gyrd-Hansen M., Meier P.;
"IAPs: from caspase inhibitors to modulators of NF-kappaB,
inflammation and cancer.";
Nat. Rev. Cancer 10:561-574(2010).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
FUNCTION IN THE UBIQUITINATION OF AIFM1.
PubMed=22103349; DOI=10.1021/bi201483g;
Lewis E.M., Wilkinson A.S., Davis N.Y., Horita D.A., Wilkinson J.C.;
"Nondegradative ubiquitination of apoptosis inducing factor (AIF) by
X-linked inhibitor of apoptosis at a residue critical for AIF-mediated
chromatin degradation.";
Biochemistry 50:11084-11096(2011).
[31]
REVIEW ON FUNCTION.
PubMed=21447281;
Damgaard R.B., Gyrd-Hansen M.;
"Inhibitor of apoptosis (IAP) proteins in regulation of inflammation
and innate immunity.";
Discov. Med. 11:221-231(2011).
[32]
INTERACTION WITH BIRC5/SURVIVIN.
PubMed=21536684; DOI=10.1074/jbc.M111.237586;
Pavlyukov M.S., Antipova N.V., Balashova M.V., Vinogradova T.V.,
Kopantzev E.P., Shakhparonov M.I.;
"Survivin monomer plays an essential role in apoptosis regulation.";
J. Biol. Chem. 286:23296-23307(2011).
[33]
INTERACTION WITH USP19.
PubMed=21849505; DOI=10.1074/jbc.M111.282020;
Mei Y., Hahn A.A., Hu S., Yang X.;
"The USP19 deubiquitinase regulates the stability of c-IAP1 and c-
IAP2.";
J. Biol. Chem. 286:35380-35387(2011).
[34]
INTERACTION WITH RIPK1; RIPK2; RIPK3 AND RIPK4.
PubMed=21931591; DOI=10.1371/journal.pone.0022356;
Bertrand M.J., Lippens S., Staes A., Gilbert B., Roelandt R.,
De Medts J., Gevaert K., Declercq W., Vandenabeele P.;
"cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin
chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).";
PLoS ONE 6:E22356-E22356(2011).
[35]
REVIEW ON FUNCTION.
PubMed=22095281; DOI=10.1038/cdd.2011.163;
Darding M., Meier P.;
"IAPs: guardians of RIPK1.";
Cell Death Differ. 19:58-66(2012).
[36]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TLE3 AND
TCF7L2/TCF4.
PubMed=22304967; DOI=10.1016/j.molcel.2011.12.032;
Hanson A.J., Wallace H.A., Freeman T.J., Beauchamp R.D., Lee L.A.,
Lee E.;
"XIAP monoubiquitylates Groucho/TLE to promote canonical Wnt
signaling.";
Mol. Cell 45:619-628(2012).
[37]
STRUCTURE BY NMR OF 124-240, AND MUTAGENESIS OF LEU-141; VAL-147;
ASP-148; ILE-149; ASP-151; LEU-167 AND ASP-196.
PubMed=10548111; DOI=10.1038/44617;
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.;
"NMR structure and mutagenesis of the inhibitor-of-apoptosis protein
XIAP.";
Nature 401:818-822(1999).
[38]
STRUCTURE BY NMR OF 238-358 IN COMPLEX WITH DIABLO/SMAC.
PubMed=11140637; DOI=10.1038/35050006;
Liu Z., Sun C., Olejniczak E.T., Meadows R.P., Betz S.F., Oost T.,
Herrmann J., Wu J.C., Fesik S.W.;
"Structural basis for binding of Smac/DIABLO to the XIAP BIR3
domain.";
Nature 408:1004-1008(2000).
[39]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 120-260 IN COMPLEX WITH
CASP7.
PubMed=11257231; DOI=10.1016/S0092-8674(02)02075-5;
Huang Y., Park Y.C., Rich R.L., Segal D., Myszka D.G., Wu H.;
"Structural basis of caspase inhibition by XIAP: differential roles of
the linker versus the BIR domain.";
Cell 104:781-790(2001).
[40]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 253-350 IN COMPLEX WITH
CASP9.
PubMed=12620238; DOI=10.1016/S1097-2765(03)00054-6;
Shiozaki E.N., Chai J., Rigotti D.J., Riedl S.J., Li P.,
Srinivasula S.M., Alnemri E.S., Fairman R., Shi Y.;
"Mechanism of XIAP-mediated inhibition of caspase-9.";
Mol. Cell 11:519-527(2003).
[41]
STRUCTURE BY NMR OF 241-356.
PubMed=15317454; DOI=10.1021/jm040037k;
Oost T.K., Sun C., Armstrong R.C., Al-Assaad A.-S., Betz S.F.,
Deckwerth T.L., Ding H., Elmore S.W., Meadows R.P., Olejniczak E.T.,
Oleksijew A., Oltersdorf T., Rosenberg S.H., Shoemaker A.R.,
Tomaselli K.J., Zou H., Fesik S.W.;
"Discovery of potent antagonists of the antiapoptotic protein XIAP for
the treatment of cancer.";
J. Med. Chem. 47:4417-4426(2004).
[42]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 249-354.
PubMed=17336535; DOI=10.1016/j.bmc.2007.02.010;
Wist A.D., Gu L., Riedl S.J., Shi Y., McLendon G.L.;
"Structure-activity based study of the Smac-binding pocket within the
BIR3 domain of XIAP.";
Bioorg. Med. Chem. 15:2935-2943(2007).
[43]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-99, PHOSPHORYLATION AT
SER-87, MUTAGENESIS OF SER-87, AND SUBUNIT.
PubMed=17698078; DOI=10.1016/j.jmb.2007.07.019;
Lin S.-C., Huang Y., Lo Y.-C., Lu M., Wu H.;
"Crystal structure of the BIR1 domain of XIAP in two crystal forms.";
J. Mol. Biol. 372:847-854(2007).
[44]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-99 IN COMPLEX WITH TAB1,
FUNCTION, AND MUTAGENESIS OF TYR-75; VAL-80; VAL-86 AND LEU-98.
PubMed=17560374; DOI=10.1016/j.molcel.2007.05.006;
Lu M., Lin S.-C., Huang Y., Kang Y.J., Rich R., Lo Y.-C., Myszka D.,
Han J., Wu H.;
"XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and
BIR1 dimerization.";
Mol. Cell 26:689-702(2007).
[45]
STRUCTURE BY NMR OF 427-497.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RING domain of the baculoviral IAP repeat-
containing protein 4 from Homo sapiens.";
Submitted (MAR-2008) to the PDB data bank.
-!- FUNCTION: 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. {ECO:0000269|PubMed:11447297,
ECO:0000269|PubMed:12121969, ECO:0000269|PubMed:14645242,
ECO:0000269|PubMed:14685266, ECO:0000269|PubMed:17560374,
ECO:0000269|PubMed:17967870, ECO:0000269|PubMed:19473982,
ECO:0000269|PubMed:20154138, ECO:0000269|PubMed:21145488,
ECO:0000269|PubMed:22103349, ECO:0000269|PubMed:22304967,
ECO:0000269|PubMed:9230442}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:11140637, ECO:0000269|PubMed:11257231,
ECO:0000269|PubMed:12620238, ECO:0000269|PubMed:14685266,
ECO:0000269|PubMed:15029247, ECO:0000269|PubMed:17560374,
ECO:0000269|PubMed:17698078, ECO:0000269|PubMed:17967870,
ECO:0000269|PubMed:18068114, ECO:0000269|PubMed:19473982,
ECO:0000269|PubMed:20154138, ECO:0000269|PubMed:20171186,
ECO:0000269|PubMed:21536684, ECO:0000269|PubMed:21849505,
ECO:0000269|PubMed:21931591, ECO:0000269|PubMed:22304967}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-517127, EBI-517127;
Q3E793:BOL1 (xeno); NbExp=3; IntAct=EBI-517127, EBI-2344281;
Q92851:CASP10; NbExp=3; IntAct=EBI-517127, EBI-495095;
Q92851-4:CASP10; NbExp=3; IntAct=EBI-517127, EBI-6621134;
P42574:CASP3; NbExp=3; IntAct=EBI-517127, EBI-524064;
P55210:CASP7; NbExp=3; IntAct=EBI-517127, EBI-523958;
P55211:CASP9; NbExp=17; IntAct=EBI-517127, EBI-516799;
P61024:CKS1B; NbExp=5; IntAct=EBI-517127, EBI-456371;
Q9NR28:DIABLO; NbExp=9; IntAct=EBI-517127, EBI-517508;
Q96FJ2:DYNLL2; NbExp=3; IntAct=EBI-517127, EBI-742371;
P19447:ERCC3; NbExp=3; IntAct=EBI-517127, EBI-1183307;
P32502:GCD7 (xeno); NbExp=3; IntAct=EBI-517127, EBI-6260;
O43464:HTRA2; NbExp=20; IntAct=EBI-517127, EBI-517086;
Q9JIY5:Htra2 (xeno); NbExp=4; IntAct=EBI-517127, EBI-2365838;
Q17RB8:LONRF1; NbExp=5; IntAct=EBI-517127, EBI-2341787;
Q9Y5V3:MAGED1; NbExp=2; IntAct=EBI-517127, EBI-716006;
Q9HC98:NEK6; NbExp=3; IntAct=EBI-517127, EBI-740364;
P46531:NOTCH1; NbExp=4; IntAct=EBI-517127, EBI-636374;
O43447:PPIH; NbExp=4; IntAct=EBI-517127, EBI-1055615;
P63000:RAC1; NbExp=3; IntAct=EBI-517127, EBI-413628;
P40937:RFC5; NbExp=5; IntAct=EBI-517127, EBI-712376;
O43353:RIPK2; NbExp=4; IntAct=EBI-517127, EBI-358522;
P57078:RIPK4; NbExp=2; IntAct=EBI-517127, EBI-4422308;
O43236-6:SEPT4; NbExp=4; IntAct=EBI-517127, EBI-4372019;
Q8IUQ4:SIAH1; NbExp=3; IntAct=EBI-517127, EBI-747107;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-517127, EBI-2212028;
P38340:TAE1 (xeno); NbExp=3; IntAct=EBI-517127, EBI-21116;
Q9Y4K3:TRAF6; NbExp=2; IntAct=EBI-517127, EBI-359276;
P0CG48:UBC; NbExp=3; IntAct=EBI-517127, EBI-3390054;
P51668:UBE2D1; NbExp=7; IntAct=EBI-517127, EBI-743540;
P62837:UBE2D2; NbExp=2; IntAct=EBI-517127, EBI-347677;
P61077:UBE2D3; NbExp=2; IntAct=EBI-517127, EBI-348268;
P61088:UBE2N; NbExp=2; IntAct=EBI-517127, EBI-1052908;
Q13404:UBE2V1; NbExp=3; IntAct=EBI-517127, EBI-1050671;
A5D8V6:VPS37C; NbExp=5; IntAct=EBI-517127, EBI-2559305;
Q96HA8:WDYHV1; NbExp=3; IntAct=EBI-517127, EBI-741158;
Q01976:YSA1 (xeno); NbExp=3; IntAct=EBI-517127, EBI-2344265;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=TLE3 promotes its
nuclear localization.
-!- TISSUE SPECIFICITY: Ubiquitous, except peripheral blood
leukocytes.
-!- DOMAIN: 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.
-!- PTM: S-Nitrosylation down-regulates its E3 ubiquitin-protein
ligase activity. {ECO:0000269|PubMed:12747801,
ECO:0000269|PubMed:14645242, ECO:0000269|PubMed:20670888}.
-!- PTM: Autoubiquitinated and degraded by the proteasome in apoptotic
cells. {ECO:0000269|PubMed:12747801, ECO:0000269|PubMed:14645242}.
-!- PTM: Phosphorylation by PKB/AKT protects XIAP against
ubiquitination and protects the protein against proteasomal
degradation. {ECO:0000269|PubMed:12747801,
ECO:0000269|PubMed:14645242, ECO:0000269|PubMed:17698078}.
-!- DISEASE: 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.
{ECO:0000269|PubMed:17080092}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
-!- WEB RESOURCE: Name=BIRC4base; Note=XIAP mutation db;
URL="http://structure.bmc.lu.se/idbase/BIRC4base/";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/birc4/";
-----------------------------------------------------------------------
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EMBL; U32974; AAC50518.1; -; mRNA.
EMBL; U45880; AAC50373.1; -; mRNA.
EMBL; AY886519; AAW62257.1; -; Genomic_DNA.
EMBL; AL121601; CAB95312.1; -; Genomic_DNA.
EMBL; CH471107; EAX11858.1; -; Genomic_DNA.
EMBL; CH471107; EAX11859.1; -; Genomic_DNA.
EMBL; CH471107; EAX11860.1; -; Genomic_DNA.
EMBL; CH471107; EAX11861.1; -; Genomic_DNA.
EMBL; BC032729; AAH32729.1; -; mRNA.
CCDS; CCDS14606.1; -.
PIR; S69544; S69544.
RefSeq; NP_001158.2; NM_001167.3.
RefSeq; NP_001191330.1; NM_001204401.1.
RefSeq; XP_006724817.1; XM_006724754.2.
RefSeq; XP_011529631.1; XM_011531329.2.
UniGene; Hs.356076; -.
UniGene; Hs.736565; -.
PDB; 1C9Q; NMR; -; A=124-240.
PDB; 1F9X; NMR; -; A=241-356.
PDB; 1G3F; NMR; -; A=241-356.
PDB; 1G73; X-ray; 2.00 A; C/D=238-358.
PDB; 1I3O; X-ray; 2.70 A; E/F=124-240.
PDB; 1I4O; X-ray; 2.40 A; C/D=120-260.
PDB; 1I51; X-ray; 2.45 A; E/F=124-240.
PDB; 1KMC; X-ray; 2.90 A; C/D=124-242.
PDB; 1NW9; X-ray; 2.40 A; A=253-350.
PDB; 1TFQ; NMR; -; A=241-356.
PDB; 1TFT; NMR; -; A=241-356.
PDB; 2ECG; NMR; -; A=430-497.
PDB; 2JK7; X-ray; 2.82 A; A=241-356.
PDB; 2KNA; NMR; -; A=357-449.
PDB; 2OPY; X-ray; 2.80 A; A=249-354.
PDB; 2OPZ; X-ray; 3.00 A; A/B/C/D=249-357.
PDB; 2POI; X-ray; 1.80 A; A=10-99.
PDB; 2POP; X-ray; 3.10 A; B/D=10-100.
PDB; 2QRA; X-ray; 2.50 A; A/B/C/D=10-99.
PDB; 2VSL; X-ray; 2.10 A; A=250-345.
PDB; 3CLX; X-ray; 2.70 A; A/B/C/D=241-356.
PDB; 3CM2; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=241-356.
PDB; 3CM7; X-ray; 3.10 A; A/B/C/D=241-356.
PDB; 3EYL; X-ray; 3.00 A; A/B=241-356.
PDB; 3G76; X-ray; 3.00 A; A/B/C/D/E/F/G/H=241-356.
PDB; 3HL5; X-ray; 1.80 A; A/B=256-346.
PDB; 3UW4; X-ray; 1.79 A; A=338-348.
PDB; 3UW5; X-ray; 1.71 A; A/B=336-348.
PDB; 4EC4; X-ray; 3.30 A; A/B/C/D/E/F/G/J/K/L=241-356.
PDB; 4HY0; X-ray; 2.84 A; A/B/C/D/E/F/G/H=238-357.
PDB; 4IC2; X-ray; 2.20 A; A/B=429-497.
PDB; 4IC3; X-ray; 1.78 A; A/B=429-497.
PDB; 4J3Y; X-ray; 1.45 A; A/C=152-236.
PDB; 4J44; X-ray; 1.30 A; A/C=152-236.
PDB; 4J45; X-ray; 1.48 A; A/C=152-236.
PDB; 4J46; X-ray; 1.42 A; A/C=152-236.
PDB; 4J47; X-ray; 1.35 A; A/C=152-236.
PDB; 4J48; X-ray; 2.10 A; A/C=152-236.
PDB; 4KJU; X-ray; 1.60 A; A/C=152-236.
PDB; 4KJV; X-ray; 1.70 A; A/C=152-236.
PDB; 4KMP; X-ray; 1.95 A; A/B=256-348.
PDB; 4MTZ; X-ray; 2.10 A; A/B/C/D=10-99.
PDB; 4OXC; X-ray; 2.90 A; A/B/C/D=10-99.
PDB; 4WVS; X-ray; 2.09 A; A=156-231.
PDB; 4WVT; X-ray; 1.96 A; A/B=156-231.
PDB; 4WVU; X-ray; 2.02 A; A=156-231.
PDB; 5C0K; X-ray; 2.20 A; A=249-354.
PDB; 5C0L; X-ray; 2.60 A; A=246-354.
PDB; 5C3H; X-ray; 2.65 A; A=249-354.
PDB; 5C3K; X-ray; 2.02 A; A=249-354.
PDB; 5C7A; X-ray; 2.36 A; A=249-354.
PDB; 5C7B; X-ray; 2.68 A; A=249-354.
PDB; 5C7C; X-ray; 2.32 A; A=249-354.
PDB; 5C7D; X-ray; 2.25 A; A=249-354.
PDB; 5C83; X-ray; 2.33 A; A=249-354.
PDB; 5C84; X-ray; 2.36 A; A=249-354.
PDB; 5M6E; X-ray; 2.32 A; A=249-354.
PDB; 5M6F; X-ray; 2.39 A; A=249-354.
PDB; 5M6H; X-ray; 2.50 A; A=249-354.
PDB; 5M6L; X-ray; 2.61 A; A=249-354.
PDB; 5M6M; X-ray; 2.37 A; A=249-354.
PDBsum; 1C9Q; -.
PDBsum; 1F9X; -.
PDBsum; 1G3F; -.
PDBsum; 1G73; -.
PDBsum; 1I3O; -.
PDBsum; 1I4O; -.
PDBsum; 1I51; -.
PDBsum; 1KMC; -.
PDBsum; 1NW9; -.
PDBsum; 1TFQ; -.
PDBsum; 1TFT; -.
PDBsum; 2ECG; -.
PDBsum; 2JK7; -.
PDBsum; 2KNA; -.
PDBsum; 2OPY; -.
PDBsum; 2OPZ; -.
PDBsum; 2POI; -.
PDBsum; 2POP; -.
PDBsum; 2QRA; -.
PDBsum; 2VSL; -.
PDBsum; 3CLX; -.
PDBsum; 3CM2; -.
PDBsum; 3CM7; -.
PDBsum; 3EYL; -.
PDBsum; 3G76; -.
PDBsum; 3HL5; -.
PDBsum; 3UW4; -.
PDBsum; 3UW5; -.
PDBsum; 4EC4; -.
PDBsum; 4HY0; -.
PDBsum; 4IC2; -.
PDBsum; 4IC3; -.
PDBsum; 4J3Y; -.
PDBsum; 4J44; -.
PDBsum; 4J45; -.
PDBsum; 4J46; -.
PDBsum; 4J47; -.
PDBsum; 4J48; -.
PDBsum; 4KJU; -.
PDBsum; 4KJV; -.
PDBsum; 4KMP; -.
PDBsum; 4MTZ; -.
PDBsum; 4OXC; -.
PDBsum; 4WVS; -.
PDBsum; 4WVT; -.
PDBsum; 4WVU; -.
PDBsum; 5C0K; -.
PDBsum; 5C0L; -.
PDBsum; 5C3H; -.
PDBsum; 5C3K; -.
PDBsum; 5C7A; -.
PDBsum; 5C7B; -.
PDBsum; 5C7C; -.
PDBsum; 5C7D; -.
PDBsum; 5C83; -.
PDBsum; 5C84; -.
PDBsum; 5M6E; -.
PDBsum; 5M6F; -.
PDBsum; 5M6H; -.
PDBsum; 5M6L; -.
PDBsum; 5M6M; -.
ProteinModelPortal; P98170; -.
SMR; P98170; -.
BioGrid; 106828; 161.
CORUM; P98170; -.
DIP; DIP-27626N; -.
IntAct; P98170; 85.
MINT; MINT-141734; -.
STRING; 9606.ENSP00000347858; -.
BindingDB; P98170; -.
ChEMBL; CHEMBL4198; -.
GuidetoPHARMACOLOGY; 2790; -.
MEROPS; I32.007; -.
iPTMnet; P98170; -.
PhosphoSitePlus; P98170; -.
BioMuta; XIAP; -.
DMDM; 12643387; -.
EPD; P98170; -.
MaxQB; P98170; -.
PaxDb; P98170; -.
PeptideAtlas; P98170; -.
PRIDE; P98170; -.
DNASU; 331; -.
Ensembl; ENST00000355640; ENSP00000347858; ENSG00000101966.
Ensembl; ENST00000371199; ENSP00000360242; ENSG00000101966.
Ensembl; ENST00000434753; ENSP00000395230; ENSG00000101966.
GeneID; 331; -.
KEGG; hsa:331; -.
UCSC; uc004etx.4; human.
CTD; 331; -.
DisGeNET; 331; -.
EuPathDB; HostDB:ENSG00000101966.12; -.
GeneCards; XIAP; -.
GeneReviews; XIAP; -.
HGNC; HGNC:592; XIAP.
HPA; CAB009203; -.
HPA; HPA042428; -.
MalaCards; XIAP; -.
MIM; 300079; gene.
MIM; 300635; phenotype.
neXtProt; NX_P98170; -.
OpenTargets; ENSG00000101966; -.
Orphanet; 2442; X-linked lymphoproliferative disease.
PharmGKB; PA25361; -.
eggNOG; KOG1101; Eukaryota.
eggNOG; ENOG410YPNM; LUCA.
GeneTree; ENSGT00500000044782; -.
HOGENOM; HOG000232059; -.
HOVERGEN; HBG004848; -.
InParanoid; P98170; -.
KO; K04725; -.
OMA; AMYSEEA; -.
OrthoDB; EOG091G0CXH; -.
PhylomeDB; P98170; -.
TreeFam; TF105356; -.
Reactome; R-HSA-111463; SMAC binds to IAPs.
Reactome; R-HSA-111464; SMAC-mediated dissociation of IAP:caspase complexes.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
Reactome; R-HSA-8948747; Regulation of PTEN localization.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
SABIO-RK; P98170; -.
SignaLink; P98170; -.
SIGNOR; P98170; -.
ChiTaRS; XIAP; human.
EvolutionaryTrace; P98170; -.
GeneWiki; XIAP; -.
GenomeRNAi; 331; -.
PMAP-CutDB; P98170; -.
PRO; PR:P98170; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000101966; -.
CleanEx; HS_XIAP; -.
ExpressionAtlas; P98170; baseline and differential.
Genevisible; P98170; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; EXP:Reactome.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
GO; GO:0055070; P:copper ion homeostasis; TAS:UniProtKB.
GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:1902530; P:positive regulation of protein linear polyubiquitination; IDA:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0030510; P:regulation of BMP signaling pathway; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; TAS:UniProtKB.
GO; GO:0045088; P:regulation of innate immune response; TAS:UniProtKB.
GO; GO:0070424; P:regulation of nucleotide-binding oligomerization domain containing signaling pathway; TAS:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
CDD; cd00022; BIR; 3.
InterPro; IPR001370; BIR_rpt.
InterPro; IPR001841; Znf_RING.
Pfam; PF00653; BIR; 3.
SMART; SM00238; BIR; 3.
SMART; SM00184; RING; 1.
PROSITE; PS01282; BIR_REPEAT_1; 3.
PROSITE; PS50143; BIR_REPEAT_2; 3.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Cytoplasm;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
Protease inhibitor; Reference proteome; Repeat; S-nitrosylation;
Thiol protease inhibitor; Transferase; Ubl conjugation;
Ubl conjugation pathway; Wnt signaling pathway; Zinc; Zinc-finger.
CHAIN 1 497 E3 ubiquitin-protein ligase XIAP.
/FTId=PRO_0000122352.
REPEAT 26 93 BIR 1.
REPEAT 163 230 BIR 2.
REPEAT 265 330 BIR 3.
ZN_FING 450 485 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 141 149 Interaction with caspase-7.
METAL 300 300 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 303 303 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 320 320 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 327 327 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
MOD_RES 87 87 Phosphoserine; by PKB.
{ECO:0000269|PubMed:14645242,
ECO:0000269|PubMed:17698078}.
MOD_RES 450 450 S-nitrosocysteine.
{ECO:0000269|PubMed:20670888}.
CROSSLNK 322 322 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:12747801}.
CROSSLNK 328 328 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:12747801}.
VARIANT 107 107 N -> S (in dbSNP:rs28382721).
{ECO:0000269|Ref.3}.
/FTId=VAR_022282.
VARIANT 133 133 S -> F (in dbSNP:rs28382722).
{ECO:0000269|Ref.3}.
/FTId=VAR_022283.
VARIANT 242 242 D -> E (in dbSNP:rs28382723).
{ECO:0000269|Ref.3}.
/FTId=VAR_022284.
VARIANT 423 423 Q -> P (in dbSNP:rs5956583).
{ECO:0000269|PubMed:8654366,
ECO:0000269|Ref.3}.
/FTId=VAR_022285.
MUTAGEN 75 75 Y->G: Loss of interaction with
TAB1/MAP3K7IP1; when associated with G-
75. {ECO:0000269|PubMed:17560374}.
MUTAGEN 80 80 V->A: Strongly reduced interaction with
TAB1/MAP3K7IP1. Reduced activation of
MAP3K7/TAK1. Reduced activation of NF-
kappa-B. {ECO:0000269|PubMed:17560374}.
MUTAGEN 80 80 V->D: Loss of interaction with
TAB1/MAP3K7IP1. Reduced activation of
MAP3K7/TAK1. Strongly reduced activation
of NF-kappa-B.
{ECO:0000269|PubMed:17560374}.
MUTAGEN 86 86 V->E: Loss of dimerization. Reduces
activation of NF-kappa-B.
{ECO:0000269|PubMed:17560374}.
MUTAGEN 87 87 S->A: No effect on dimerization.
{ECO:0000269|PubMed:17698078}.
MUTAGEN 87 87 S->D,E: Abolishes dimerization.
Interferes with ubiquitination.
{ECO:0000269|PubMed:17698078}.
MUTAGEN 98 98 L->G: Loss of interaction with
TAB1/MAP3K7IP1; when associated with G-
75. {ECO:0000269|PubMed:17560374}.
MUTAGEN 141 141 L->A: Reduced inhibition of caspase-3.
{ECO:0000269|PubMed:10548111}.
MUTAGEN 147 147 V->A: Reduced inhibition of caspase-3.
{ECO:0000269|PubMed:10548111}.
MUTAGEN 148 148 D->A: Abolishes inhibition of caspase-3.
Reduced interaction with PRSS25; when
associated with S-214.
{ECO:0000269|PubMed:10548111,
ECO:0000269|PubMed:11604410}.
MUTAGEN 149 149 I->A: Reduced inhibition of caspase-3.
{ECO:0000269|PubMed:10548111}.
MUTAGEN 151 151 D->A: Reduced inhibition of caspase-3.
{ECO:0000269|PubMed:10548111}.
MUTAGEN 167 167 L->A: Reduced inhibition of caspase-3.
{ECO:0000269|PubMed:10548111}.
MUTAGEN 196 196 D->A: Reduced inhibition of caspase-3.
May affect protein folding and stability.
{ECO:0000269|PubMed:10548111}.
MUTAGEN 214 214 D->S: Reduced interaction with PRSS25.
Reduced interaction with PRSS25; when
associated with A-148.
{ECO:0000269|PubMed:11604410}.
MUTAGEN 259 259 N->D: Reduced interaction with PRSS25;
when associated with S-314.
{ECO:0000269|PubMed:11604410}.
MUTAGEN 310 310 W->R: Reduced interaction with PRSS25;
when associated with S-314.
{ECO:0000269|PubMed:11604410}.
MUTAGEN 314 314 E->S: Decreased interaction with
DIABLO/SMAC and with PRSS25. Decreases
interaction with PRSS25; when associated
with D-259 or A-310.
{ECO:0000269|PubMed:11604410}.
MUTAGEN 450 450 C->A,S: Inhibits degradation of active
caspase-3. {ECO:0000269|PubMed:11447297}.
MUTAGEN 467 467 H->A: Loss of E3 ubiquitin-protein ligase
activity. {ECO:0000269|PubMed:17967870}.
CONFLICT 162 162 S -> C (in Ref. 2; AAC50373).
{ECO:0000305}.
HELIX 26 30 {ECO:0000244|PDB:2POI}.
HELIX 31 33 {ECO:0000244|PDB:2POI}.
STRAND 40 42 {ECO:0000244|PDB:2POI}.
HELIX 44 49 {ECO:0000244|PDB:2POI}.
STRAND 52 54 {ECO:0000244|PDB:2POI}.
STRAND 61 63 {ECO:0000244|PDB:2POI}.
TURN 64 66 {ECO:0000244|PDB:2POI}.
HELIX 79 86 {ECO:0000244|PDB:2POI}.
TURN 91 97 {ECO:0000244|PDB:2POI}.
TURN 128 130 {ECO:0000244|PDB:1I3O}.
HELIX 136 142 {ECO:0000244|PDB:1I4O}.
HELIX 150 152 {ECO:0000244|PDB:1I3O}.
HELIX 158 161 {ECO:0000244|PDB:4J44}.
HELIX 163 168 {ECO:0000244|PDB:4J44}.
TURN 169 172 {ECO:0000244|PDB:4J44}.
HELIX 175 177 {ECO:0000244|PDB:4WVT}.
HELIX 181 186 {ECO:0000244|PDB:4J44}.
STRAND 189 191 {ECO:0000244|PDB:4J44}.
STRAND 198 200 {ECO:0000244|PDB:4J44}.
TURN 201 203 {ECO:0000244|PDB:4J44}.
STRAND 206 208 {ECO:0000244|PDB:4J44}.
HELIX 216 223 {ECO:0000244|PDB:4J44}.
HELIX 228 232 {ECO:0000244|PDB:4J44}.
HELIX 244 246 {ECO:0000244|PDB:1F9X}.
STRAND 249 251 {ECO:0000244|PDB:1F9X}.
STRAND 254 256 {ECO:0000244|PDB:5C3K}.
HELIX 260 262 {ECO:0000244|PDB:3HL5}.
HELIX 265 270 {ECO:0000244|PDB:3HL5}.
TURN 271 274 {ECO:0000244|PDB:3HL5}.
STRAND 277 279 {ECO:0000244|PDB:3HL5}.
HELIX 281 286 {ECO:0000244|PDB:3HL5}.
STRAND 289 291 {ECO:0000244|PDB:3HL5}.
STRAND 293 296 {ECO:0000244|PDB:2OPZ}.
STRAND 298 300 {ECO:0000244|PDB:3HL5}.
TURN 301 303 {ECO:0000244|PDB:3HL5}.
STRAND 306 309 {ECO:0000244|PDB:1G73}.
STRAND 311 313 {ECO:0000244|PDB:1F9X}.
HELIX 316 323 {ECO:0000244|PDB:3HL5}.
HELIX 328 333 {ECO:0000244|PDB:3HL5}.
HELIX 336 342 {ECO:0000244|PDB:3UW5}.
TURN 343 345 {ECO:0000244|PDB:3HL5}.
HELIX 346 353 {ECO:0000244|PDB:1G73}.
HELIX 354 356 {ECO:0000244|PDB:1G73}.
HELIX 368 372 {ECO:0000244|PDB:2KNA}.
HELIX 375 381 {ECO:0000244|PDB:2KNA}.
HELIX 386 400 {ECO:0000244|PDB:2KNA}.
HELIX 407 419 {ECO:0000244|PDB:2KNA}.
HELIX 437 447 {ECO:0000244|PDB:4IC3}.
TURN 451 453 {ECO:0000244|PDB:4IC3}.
STRAND 454 457 {ECO:0000244|PDB:4IC3}.
STRAND 460 463 {ECO:0000244|PDB:4IC3}.
HELIX 472 475 {ECO:0000244|PDB:4IC3}.
TURN 482 484 {ECO:0000244|PDB:4IC3}.
STRAND 489 493 {ECO:0000244|PDB:4IC3}.
SEQUENCE 497 AA; 56685 MW; 9D394C16D45EB635 CRC64;
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


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