Reviewed, UniProtKB/Swiss-Prot P98170 (XIAP_HUMAN)

Names and origin

Protein names

Recommended name:
    Baculoviral IAP repeat-containing protein 4
    EC=6.3.2.-
Alternative name(s):
    E3 ubiquitin-protein ligase XIAP
    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
    IAP-like protein
      Short name=ILP
      Short name=hILP

Gene names

Name:	XIAP
Synonyms:	API3, BIRC4, IAP3

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	497 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Apoptotic suppressor. Has E3 ubiquitin-protein ligase activity. Mediates the proteasomal degradation of target proteins, such as caspase-3, SMAC or AIFM1. Inhibitor of caspase-3, -7 and -9. Mediates activation of MAP3K7/TAK1, leading to the activation of NF-kappa-B. Ref.6 Ref.7 Ref.9 Ref.11 Ref.15 Ref.24
Subunit structure	Monomer, and homodimer. Interacts with SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with MAP3K7IP1 and AIFM1. Interaction with SMAC hinders binding of MAP3K7IP1 and AIFM1. Interacts with TCF25. Interacts with SEPT4 isoform 6, but not with other SEPT4 isoforms. Ref.15 Ref.10 Ref.14 Ref.23
Subcellular location	Cytoplasm.
Tissue specificity	Ubiquitous, except peripheral blood leukocytes.
Domain	The first BIR domain is involved in interaction with MAP3K7IP1 and is important for dimerization. The second BIR domain is sufficient to inhibit caspase-3 and caspase-7, while the third BIR is involved in caspase-9 inhibition. The interactions with SMAC and PRSS25 are mediated by the second and third BIR domains.
Post-translational modification	Ubiquitinated and degraded by the proteasome in apoptotic cells. Ref.11 Phosphorylation by PKB/AKT protects XIAP against ubiquitination and protects the protein against proteasomal degradation.
Involvement in disease	Defects in XIAP are the cause of lymphoproliferative syndrome X-linked type 2 (XLP2) [MIM:300635]. XLP is 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. Ref.13
Sequence similarities	Belongs to the IAP family. Contains 3 BIR repeats. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Apoptosis Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase Protease inhibitor Thiol protease inhibitor
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Ref.1 Inferred from mutant phenotype. Source: UniProtKB apoptosis Inferred from electronic annotation. Source: UniProtKB-KW modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW response to DNA damage stimulus Inferred from expression pattern. Source: UniProtKB
Cellular component	cytosol Ref.1 Ref.19 Inferred from Experiment. Source: Reactome
Molecular function	caspase inhibitor activity Ref.6 Inferred from direct assay. Source: ProtInc ligase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CASP9	P55211	4	EBI-517127,EBI-516799
DIABLO	Q9NR28	5	EBI-517127,EBI-517508
HTRA2	O43464	3	EBI-517127,EBI-517086
TBK1	Q9UHD2	1	EBI-517127,EBI-356402
UBE2D1	P51668	1	EBI-517127,EBI-743540
UBE2D2	P62837	1	EBI-517127,EBI-347677
UBE2D3	P61077	1	EBI-517127,EBI-348268
UBE2E1	P51965	1	EBI-517127,EBI-348546
UBE2N	P61088	1	EBI-517127,EBI-1052908

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 497

497

Baculoviral IAP repeat-containing protein 4

PRO_0000122352

Regions

Repeat

26 – 93

68

BIR 1

Repeat

163 – 230

68

BIR 2

Repeat

265 – 330

66

BIR 3

Zinc finger

450 – 485

36

RING-type

Region

141 – 149

9

Interaction with caspase-7

Sites

Metal binding

300

1

Zinc By similarity

Metal binding

303

1

Zinc By similarity

Metal binding

320

1

Zinc By similarity

Metal binding

327

1

Zinc By similarity

Amino acid modifications

Modified residue

87

1

Phosphoserine; by PKB Ref.11 Ref.23

Modified residue

139

1

Phosphotyrosine Ref.12

Natural variations

Natural variant

107

1

N → S: dbSNP rs28382721. Ref.3

VAR_022282

Natural variant

133

1

S → F: dbSNP rs28382722. Ref.3

VAR_022283

Natural variant

242

1

D → E: dbSNP rs28382723. Ref.3

VAR_022284

Natural variant

423

1

Q → P: dbSNP rs5956583. Ref.3 Ref.1

VAR_022285

Experimental info

Mutagenesis

75

1

Y → G: Loss of interaction with MAP3K7IP1; when associated with G-75. Ref.24

Mutagenesis

80

1

V → A: Strongly reduced interaction with MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Reduced activation of NF-kappa-B. Ref.24

Mutagenesis

80

1

V → D: Loss of interaction with MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Strongly reduced activation of NF-kappa-B. Ref.24

Mutagenesis

86

1

V → E: Loss of dimerization. Reduces activation of NF-kappa-B. Ref.24

Mutagenesis

87

1

S → A: No effect on dimerization. Ref.23

Mutagenesis

87

1

S → D or E: Abolishes dimerization. Interferes with ubiquitination. Ref.23

Mutagenesis

98

1

L → G: Loss of interaction with MAP3K7IP1; when associated with G-75. Ref.24

Mutagenesis

141

1

L → A: Reduced inhibition of caspase-3. Ref.17

Mutagenesis

147

1

V → A: Reduced inhibition of caspase-3. Ref.17

Mutagenesis

148

1

D → A: Abolishes inhibition of caspase-3. Reduced interaction with PRSS25; when associated with S-214. Ref.17 Ref.8

Mutagenesis

149

1

I → A: Reduced inhibition of caspase-3. Ref.17

Mutagenesis

151

1

D → A: Reduced inhibition of caspase-3. Ref.17

Mutagenesis

167

1

L → A: Reduced inhibition of caspase-3. Ref.17

Mutagenesis

196

1

D → A: Reduced inhibition of caspase-3. May affect protein folding and stability. Ref.17

Mutagenesis

214

1

D → S: Reduced interaction with PRSS25. Reduced interaction with PRSS25; when associated with A-148. Ref.8

Mutagenesis

259

1

N → D: Reduced interaction with PRSS25; when associated with S-314. Ref.8

Mutagenesis

310

1

W → R: Reduced interaction with PRSS25; when associated with S-314. Ref.8

Mutagenesis

314

1

E → S: Decreased interaction with SMAC and with PRSS25. Decreases interaction with PRSS25; when associated with D-259 or A-310. Ref.8

Mutagenesis

450

1

C → A or S: Inhibits degradation of active caspase-3. Ref.7

Mutagenesis

467

1

H → A: Loss of E3 ubiquitin-protein ligase activity. Ref.15

Sequence conflict

162

1

S → C in AAC50373. Ref.2

Secondary structure

1

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497

Helix Strand Turn

Details...

Helix

26 – 30

5

Helix

31 – 33

3

Beta strand

40 – 42

3

Helix

44 – 49

6

Beta strand

52 – 54

3

Beta strand

61 – 63

3

Turn

64 – 66

3

Helix

79 – 86

8

Turn

91 – 97

7

Helix

136 – 142

7

Helix

260 – 262

3

Helix

265 – 270

6

Turn

271 – 274

4

Beta strand

277 – 279

3

Helix

281 – 286

6

Beta strand

289 – 291

3

Beta strand

298 – 300

3

Turn

301 – 303

3

Beta strand

306 – 309

4

Helix

316 – 323

8

Helix

328 – 342

15

Sequences

	Sequence		Length	Mass (Da)
	P98170-1 [UniParc]. Last modified January 24, 2001. Version 2. Checksum: 9D394C16D45EB635	FASTA	497	56,685
	10 20 30 40 50 60 MTFNSFEGSK TCVPADINKE EEFVEEFNRL KTFANFPSGS PVSASTLARA GFLYTGEGDT 70 80 90 100 110 120 VRCFSCHAAV DRWQYGDSAV GRHRKVSPNC RFINGFYLEN SATQSTNSGI QNGQYKVENY 130 140 150 160 170 180 LGSRDHFALD RPSETHADYL LRTGQVVDIS DTIYPRNPAM YSEEARLKSF QNWPDYAHLT 190 200 210 220 230 240 PRELASAGLY YTGIGDQVQC FCCGGKLKNW EPCDRAWSEH RRHFPNCFFV LGRNLNIRSE 250 260 270 280 290 300 SDAVSSDRNF PNSTNLPRNP SMADYEARIF TFGTWIYSVN KEQLARAGFY ALGEGDKVKC 310 320 330 340 350 360 FHCGGGLTDW KPSEDPWEQH AKWYPGCKYL LEQKGQEYIN NIHLTHSLEE CLVRTTEKTP 370 380 390 400 410 420 SLTRRIDDTI FQNPMVQEAI RMGFSFKDIK KIMEEKIQIS GSNYKSLEVL VADLVNAQKD 430 440 450 460 470 480 SMQDESSQTS LQKEISTEEQ LRRLQEEKLC KICMDRNIAI VFVPCGHLVT CKQCAEAVDK 490 CPMCYTVITF KQKIFMS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8654366] [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: 8552191] [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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Uterus.
[6]	"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: 9230442] [Abstract] Cited for: FUNCTION.
[7]	"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: 11447297] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-450.
[8]	"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: 11604410] [Abstract] Cited for: MUTAGENESIS OF ASP-148; ASP-214; ASN-259; TRP-310 AND GLU-314.
[9]	"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: 12121969] [Abstract] Cited for: FUNCTION.
[10]	"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: 15029247] [Abstract] Cited for: INTERACTION WITH SEPT4.
[11]	"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: 14645242] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-87, UBIQUITINATION, PROTEASOMAL DEGRADATION.
[12]	"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling." Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z. EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-139, MASS SPECTROMETRY.
[13]	"XIAP deficiency in humans causes an X-linked lymphoproliferative syndrome." 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. Nature 444:110-114(2006) [PubMed: 17080092] [Abstract] Cited for: INVOLVEMENT IN XLP2.
[14]	"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: 18068114] [Abstract] Cited for: INTERACTION WITH TCF25.
[15]	"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: 17967870] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF HIS-467, INTERACTION WITH AIFM1.
[16]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[17]	"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: 10548111] [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.
[18]	"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: 11140637] [Abstract] Cited for: STRUCTURE BY NMR OF 238-358 IN COMPLEX WITH SMAC.
[19]	"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: 11257231] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 120-260 IN COMPLEX WITH CASP7.
[20]	"Mechanism of XIAP-mediated inhibition of caspase-9." Shiozaki E.N., Chai J., Rigotti D.J., Riedl S.J., Li P., Srinivasula S.M., Alnemri E.S., Fairman R., Shi Y. Mol. Cell 11:519-527(2003) [PubMed: 12620238] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 253-350 IN COMPLEX WITH CASP9.
[21]	"Discovery of potent antagonists of the antiapoptotic protein XIAP for the treatment of cancer." 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. J. Med. Chem. 47:4417-4426(2004) [PubMed: 15317454] [Abstract] Cited for: STRUCTURE BY NMR OF 241-356.
[22]	"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: 17336535] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 249-354.
[23]	"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: 17698078] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-99, PHOSPHORYLATION AT SER-87, MUTAGENESIS OF SER-87, SUBUNIT.
[24]	"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: 17560374] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 10-99 IN COMPLEX WITH MAP3K7IP1, FUNCTION, MUTAGENESIS OF TYR-75; VAL-80; VAL-86 AND LEU-98.
[25]	"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.
+	Additional computationally mapped references.

Web resources

GeneReviews

BIRC4base

XIAP mutation db

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U32974 mRNA. Translation: AAC50518.1.
U45880 mRNA. Translation: AAC50373.1.
AY886519 Genomic DNA. Translation: AAW62257.1.
AL121601 Genomic DNA. Translation: CAB95312.1.
BC032729 mRNA. Translation: AAH32729.1.

IPI

IPI00303890.

PIR

S69544.

RefSeq

NP_001158.2.

UniGene

Hs.356076

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
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	[»]

SMR

P98170. Positions 154-285, 208-332.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27626N.

IntAct

P98170. 22 interactions.

STRING

P98170.

Protein family/group databases

MEROPS

I32.001.
I32.004.

PTM databases

PhosphoSite

P98170.

Proteomic databases

PeptideAtlas

P98170.

PRIDE

P98170.

Genome annotation databases

Ensembl

ENST00000355640; ENSP00000347858; ENSG00000101966; Homo sapiens. [Genome view]
ENST00000371199; ENSP00000360242; ENSG00000101966; Homo sapiens. [Genome view]

GeneID

331.

KEGG

hsa:331.

UCSC

uc004etx.1. human.

Organism-specific databases

CTD

331.

GeneCards

GC0XP122823.

H-InvDB

HIX0017033.
HIX0030550.

HGNC

HGNC:592. XIAP.

HPA

CAB009203.

MIM

300079. gene.
300635. phenotype.

Orphanet

2442. X-linked lymphoproliferative disease.

PharmGKB

PA25361.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12867.

HOGENOM

HBG714776.

HOVERGEN

P98170.

InParanoid

P98170.

OMA

VLGRNVN.

PhylomeDB

P98170.

Enzyme and pathway databases

Pathway_Interaction_DB

bmppathway. BMP receptor signaling.
caspase_pathway. Caspase cascade in apoptosis.
p75ntrpathway. p75(NTR)-mediated signaling.
tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P98170.

Bgee

P98170.

CleanEx

HS_XIAP.

Genevestigator

P98170.

GermOnline

ENSG00000101966. Homo sapiens.

Family and domain databases

InterPro

IPR001370. Prot_inh_I32_IAP.
IPR001841. Znf_RING.
[Graphical view]

Pfam

PF00653. BIR. 3 hits.
[Graphical view]

SMART

SM00238. BIR. 3 hits.
SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS01282. BIR_REPEAT_1. 3 hits.
PS50143. BIR_REPEAT_2. 3 hits.
PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

P98170.

NextBio

1365.

PMAP-CutDB

P98170.

SOURCE

Search...

Entry information

Entry name

XIAP_HUMAN

Accession

Primary (citable) accession number: P98170
Secondary accession number(s): Q9NQ14

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 24, 2001
Last modified:	February 9, 2010
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.