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P98170

- XIAP_HUMAN

UniProt

P98170 - XIAP_HUMAN

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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

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. ubiquitin-protein transferase activity Source: UniProtKB
  4. 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. inhibition of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
  5. intrinsic apoptotic signaling pathway Source: Reactome
  6. negative regulation of apoptotic process Source: UniProtKB
  7. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  8. negative regulation of neuron apoptotic process Source: Ensembl
  9. neuron apoptotic process Source: Ensembl
  10. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  11. positive regulation of protein linear polyubiquitination Source: UniProtKB
  12. positive regulation of protein ubiquitination Source: UniProtKB
  13. protein ubiquitination Source: GOC
  14. regulation of BMP signaling pathway Source: UniProtKB
  15. regulation of cell proliferation Source: UniProtKB
  16. regulation of inflammatory response Source: UniProtKB
  17. regulation of innate immune response Source: UniProtKB
  18. regulation of nucleotide-binding oligomerization domain containing signaling pathway Source: UniProtKB
  19. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

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
  4. perinuclear region of cytoplasm Source: Ensembl
  5. protein complex Source: Ensembl
Complete GO annotation...

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)1 Publication
Cross-linki328 – 328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
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

BgeeiP98170.
CleanExiHS_XIAP.
ExpressionAtlasiP98170. baseline and differential.
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
DIABLOQ9NR289EBI-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. 120 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 – 305Combined sources
Helixi31 – 333Combined sources
Beta strandi40 – 423Combined sources
Helixi44 – 496Combined sources
Beta strandi52 – 543Combined sources
Beta strandi61 – 633Combined sources
Turni64 – 663Combined sources
Helixi79 – 868Combined sources
Turni91 – 977Combined sources
Turni128 – 1303Combined sources
Helixi136 – 1427Combined sources
Helixi150 – 1523Combined sources
Helixi158 – 1614Combined sources
Helixi163 – 1686Combined sources
Turni169 – 1724Combined sources
Beta strandi175 – 1795Combined sources
Helixi181 – 1866Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi198 – 2003Combined sources
Turni201 – 2033Combined sources
Beta strandi206 – 2083Combined sources
Helixi216 – 2238Combined sources
Helixi228 – 2325Combined sources
Helixi244 – 2463Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi254 – 2563Combined sources
Helixi260 – 2623Combined sources
Helixi265 – 2706Combined sources
Turni271 – 2744Combined sources
Beta strandi277 – 2793Combined sources
Helixi281 – 2866Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi298 – 3003Combined sources
Turni301 – 3033Combined sources
Beta strandi306 – 3094Combined sources
Beta strandi311 – 3133Combined sources
Helixi316 – 3238Combined sources
Helixi328 – 3336Combined sources
Helixi336 – 3427Combined sources
Turni343 – 3453Combined sources
Helixi347 – 3526Combined sources
Helixi354 – 3563Combined sources
Helixi368 – 3725Combined sources
Helixi375 – 3817Combined sources
Helixi386 – 40015Combined sources
Helixi407 – 41913Combined sources
Helixi437 – 44711Combined sources
Turni451 – 4533Combined sources
Beta strandi454 – 4574Combined sources
Beta strandi460 – 4634Combined sources
Helixi472 – 4754Combined sources
Turni482 – 4843Combined sources
Beta strandi489 – 4935Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4MTZX-ray2.10A/B/C/D10-99[»]
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.
GeneTreeiENSGT00500000044782.
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

        10         20         30         40         50
MTFNSFEGSK TCVPADINKE EEFVEEFNRL KTFANFPSGS PVSASTLARA
60 70 80 90 100
GFLYTGEGDT VRCFSCHAAV DRWQYGDSAV GRHRKVSPNC RFINGFYLEN
110 120 130 140 150
SATQSTNSGI QNGQYKVENY LGSRDHFALD RPSETHADYL LRTGQVVDIS
160 170 180 190 200
DTIYPRNPAM YSEEARLKSF QNWPDYAHLT PRELASAGLY YTGIGDQVQC
210 220 230 240 250
FCCGGKLKNW EPCDRAWSEH RRHFPNCFFV LGRNLNIRSE SDAVSSDRNF
260 270 280 290 300
PNSTNLPRNP SMADYEARIF TFGTWIYSVN KEQLARAGFY ALGEGDKVKC
310 320 330 340 350
FHCGGGLTDW KPSEDPWEQH AKWYPGCKYL LEQKGQEYIN NIHLTHSLEE
360 370 380 390 400
CLVRTTEKTP SLTRRIDDTI FQNPMVQEAI RMGFSFKDIK KIMEEKIQIS
410 420 430 440 450
GSNYKSLEVL VADLVNAQKD SMQDESSQTS LQKEISTEEQ LRRLQEEKLC
460 470 480 490
KICMDRNIAI VFVPCGHLVT CKQCAEAVDK CPMCYTVITF KQKIFMS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
4MTZ X-ray 2.10 A/B/C/D 10-99 [» ]
ProteinModelPortali P98170.
SMRi P98170. Positions 20-99, 124-240, 256-345, 357-497.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106828. 120 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.
GeneTreei ENSGT00500000044782.
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

Bgeei P98170.
CleanExi HS_XIAP.
ExpressionAtlasi P98170. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 163 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

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