Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

E3 ubiquitin-protein ligase XIAP

Gene

XIAP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi300ZincPROSITE-ProRule annotation1
Metal bindingi303ZincPROSITE-ProRule annotation1
Metal bindingi320ZincPROSITE-ProRule annotation1
Metal bindingi327ZincPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri450 – 485RING-typePROSITE-ProRule annotationAdd BLAST36

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionProtease inhibitor, Thiol protease inhibitor, Transferase
Biological processApoptosis, Ubl conjugation pathway, Wnt signaling pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-111463 SMAC binds to IAPs
R-HSA-111464 SMAC-mediated dissociation of IAP:caspase complexes
R-HSA-3769402 Deactivation of the beta-catenin transactivating complex
R-HSA-5213460 RIPK1-mediated regulated necrosis
R-HSA-5357905 Regulation of TNFR1 signaling
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5675482 Regulation of necroptotic cell death
R-HSA-8948747 Regulation of PTEN localization
R-HSA-8948751 Regulation of PTEN stability and activity
SABIO-RKiP98170
SignaLinkiP98170
SIGNORiP98170

Protein family/group databases

MEROPSiI32.007
MoonDBiP98170 Predicted

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase XIAP (EC:2.3.2.27)
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
RING-type E3 ubiquitin transferase XIAP
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
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

EuPathDBiHostDB:ENSG00000101966.12
HGNCiHGNC:592 XIAP
MIMi300079 gene
neXtProtiNX_P98170

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Lymphoproliferative syndrome, X-linked, 2 (XLP2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:300635

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi75Y → G: Loss of interaction with TAB1/MAP3K7IP1; when associated with G-75. 1 Publication1
Mutagenesisi80V → A: Strongly reduced interaction with TAB1/MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Reduced activation of NF-kappa-B. 1 Publication1
Mutagenesisi80V → D: Loss of interaction with TAB1/MAP3K7IP1. Reduced activation of MAP3K7/TAK1. Strongly reduced activation of NF-kappa-B. 1 Publication1
Mutagenesisi86V → E: Loss of dimerization. Reduces activation of NF-kappa-B. 1 Publication1
Mutagenesisi87S → A: No effect on dimerization. 1 Publication1
Mutagenesisi87S → D or E: Abolishes dimerization. Interferes with ubiquitination. 1 Publication1
Mutagenesisi98L → G: Loss of interaction with TAB1/MAP3K7IP1; when associated with G-75. 1 Publication1
Mutagenesisi141L → A: Reduced inhibition of caspase-3. 1 Publication1
Mutagenesisi147V → A: Reduced inhibition of caspase-3. 1 Publication1
Mutagenesisi148D → A: Abolishes inhibition of caspase-3. Reduced interaction with PRSS25; when associated with S-214. 2 Publications1
Mutagenesisi149I → A: Reduced inhibition of caspase-3. 1 Publication1
Mutagenesisi151D → A: Reduced inhibition of caspase-3. 1 Publication1
Mutagenesisi167L → A: Reduced inhibition of caspase-3. 1 Publication1
Mutagenesisi196D → A: Reduced inhibition of caspase-3. May affect protein folding and stability. 1 Publication1
Mutagenesisi214D → S: Reduced interaction with PRSS25. Reduced interaction with PRSS25; when associated with A-148. 1 Publication1
Mutagenesisi259N → D: Reduced interaction with PRSS25; when associated with S-314. 1 Publication1
Mutagenesisi310W → R: Reduced interaction with PRSS25; when associated with S-314. 1 Publication1
Mutagenesisi314E → S: Decreased interaction with DIABLO/SMAC and with PRSS25. Decreases interaction with PRSS25; when associated with D-259 or A-310. 1 Publication1
Mutagenesisi450C → A or S: Inhibits degradation of active caspase-3. 1 Publication1
Mutagenesisi467H → A: Loss of E3 ubiquitin-protein ligase activity. 1 Publication1

Organism-specific databases

DisGeNETi331
GeneReviewsiXIAP
MalaCardsiXIAP
MIMi300635 phenotype
OpenTargetsiENSG00000101966
Orphaneti2442 X-linked lymphoproliferative disease
PharmGKBiPA25361

Chemistry databases

ChEMBLiCHEMBL4198
GuidetoPHARMACOLOGYi2790

Polymorphism and mutation databases

BioMutaiXIAP
DMDMi12643387

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001223521 – 497E3 ubiquitin-protein ligase XIAPAdd BLAST497

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei87Phosphoserine; by PKB2 Publications1
Cross-linki322Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki328Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei450S-nitrosocysteine1 Publication1

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

EPDiP98170
MaxQBiP98170
PaxDbiP98170
PeptideAtlasiP98170
PRIDEiP98170
ProteomicsDBi57803

PTM databases

iPTMnetiP98170
PhosphoSitePlusiP98170

Miscellaneous databases

PMAP-CutDBiP98170

Expressioni

Tissue specificityi

Ubiquitous, except peripheral blood leukocytes.

Gene expression databases

BgeeiENSG00000101966 Expressed in 211 organ(s), highest expression level in quadriceps femoris
CleanExiHS_XIAP
ExpressionAtlasiP98170 baseline and differential
GenevisibleiP98170 HS

Organism-specific databases

HPAiCAB009203
HPA042428

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi106828, 169 interactors
CORUMiP98170
DIPiDIP-27626N
IntActiP98170, 82 interactors
MINTiP98170
STRINGi9606.ENSP00000347858

Chemistry databases

BindingDBiP98170

Structurei

Secondary structure

1497
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP98170
SMRiP98170
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP98170

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati26 – 93BIR 1Add BLAST68
Repeati163 – 230BIR 2Add BLAST68
Repeati265 – 330BIR 3Add BLAST66

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni141 – 149Interaction with caspase-79

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri450 – 485RING-typePROSITE-ProRule annotationAdd BLAST36

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1101 Eukaryota
ENOG410YPNM LUCA
GeneTreeiENSGT00500000044782
HOGENOMiHOG000232059
HOVERGENiHBG004848
InParanoidiP98170
KOiK04725
OMAiCSMVLAP
OrthoDBiEOG091G0CXH
PhylomeDBiP98170
TreeFamiTF105356

Family and domain databases

CDDicd00022 BIR, 3 hits
Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001370 BIR_rpt
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF00653 BIR, 3 hits
SMARTiView protein in SMART
SM00238 BIR, 3 hits
SM00184 RING, 1 hit
PROSITEiView protein in PROSITE
PS01282 BIR_REPEAT_1, 3 hits
PS50143 BIR_REPEAT_2, 3 hits
PS50089 ZF_RING_2, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1AKU2B1AKU2_HUMAN
E3 ubiquitin-protein ligase XIAP
XIAP
156Annotation score:
B1AKU3B1AKU3_HUMAN
E3 ubiquitin-protein ligase XIAP
XIAP
16Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti162S → C in AAC50373 (PubMed:8552191).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_022282107N → S1 PublicationCorresponds to variant dbSNP:rs28382721Ensembl.1
Natural variantiVAR_022283133S → F1 PublicationCorresponds to variant dbSNP:rs28382722Ensembl.1
Natural variantiVAR_022284242D → E1 PublicationCorresponds to variant dbSNP:rs28382723Ensembl.1
Natural variantiVAR_022285423Q → P2 PublicationsCorresponds to variant dbSNP:rs5956583EnsemblClinVar.1

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 No translation available.
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_006724754.2
XP_011529631.1, XM_011531329.2
UniGeneiHs.356076
Hs.736565

Genome annotation databases

EnsembliENST00000355640; ENSP00000347858; ENSG00000101966
ENST00000371199; ENSP00000360242; ENSG00000101966
ENST00000434753; ENSP00000395230; ENSG00000101966
GeneIDi331
KEGGihsa:331
UCSCiuc004etx.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

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 No translation available.
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_006724754.2
XP_011529631.1, XM_011531329.2
UniGeneiHs.356076
Hs.736565

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4OXCX-ray2.90A/B/C/D10-99[»]
4WVSX-ray2.09A156-231[»]
4WVTX-ray1.96A/B156-231[»]
4WVUX-ray2.02A156-231[»]
5C0KX-ray2.20A249-354[»]
5C0LX-ray2.60A246-354[»]
5C3HX-ray2.65A249-354[»]
5C3KX-ray2.02A249-354[»]
5C7AX-ray2.36A249-354[»]
5C7BX-ray2.68A249-354[»]
5C7CX-ray2.32A249-354[»]
5C7DX-ray2.25A249-354[»]
5C83X-ray2.33A249-354[»]
5C84X-ray2.36A249-354[»]
5M6EX-ray2.32A249-354[»]
5M6FX-ray2.39A249-354[»]
5M6HX-ray2.50A249-354[»]
5M6LX-ray2.61A249-354[»]
5M6MX-ray2.37A249-354[»]
5O6TX-ray1.57A/B434-497[»]
5OQWX-ray2.31A/B249-354[»]
6EY2X-ray2.70A/B/C/D/E/F/G/H241-356[»]
ProteinModelPortaliP98170
SMRiP98170
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106828, 169 interactors
CORUMiP98170
DIPiDIP-27626N
IntActiP98170, 82 interactors
MINTiP98170
STRINGi9606.ENSP00000347858

Chemistry databases

BindingDBiP98170
ChEMBLiCHEMBL4198
GuidetoPHARMACOLOGYi2790

Protein family/group databases

MEROPSiI32.007
MoonDBiP98170 Predicted

PTM databases

iPTMnetiP98170
PhosphoSitePlusiP98170

Polymorphism and mutation databases

BioMutaiXIAP
DMDMi12643387

Proteomic databases

EPDiP98170
MaxQBiP98170
PaxDbiP98170
PeptideAtlasiP98170
PRIDEiP98170
ProteomicsDBi57803

Protocols and materials databases

DNASUi331
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355640; ENSP00000347858; ENSG00000101966
ENST00000371199; ENSP00000360242; ENSG00000101966
ENST00000434753; ENSP00000395230; ENSG00000101966
GeneIDi331
KEGGihsa:331
UCSCiuc004etx.4 human

Organism-specific databases

CTDi331
DisGeNETi331
EuPathDBiHostDB:ENSG00000101966.12
GeneCardsiXIAP
GeneReviewsiXIAP
HGNCiHGNC:592 XIAP
HPAiCAB009203
HPA042428
MalaCardsiXIAP
MIMi300079 gene
300635 phenotype
neXtProtiNX_P98170
OpenTargetsiENSG00000101966
Orphaneti2442 X-linked lymphoproliferative disease
PharmGKBiPA25361
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1101 Eukaryota
ENOG410YPNM LUCA
GeneTreeiENSGT00500000044782
HOGENOMiHOG000232059
HOVERGENiHBG004848
InParanoidiP98170
KOiK04725
OMAiCSMVLAP
OrthoDBiEOG091G0CXH
PhylomeDBiP98170
TreeFamiTF105356

Enzyme and pathway databases

ReactomeiR-HSA-111463 SMAC binds to IAPs
R-HSA-111464 SMAC-mediated dissociation of IAP:caspase complexes
R-HSA-3769402 Deactivation of the beta-catenin transactivating complex
R-HSA-5213460 RIPK1-mediated regulated necrosis
R-HSA-5357905 Regulation of TNFR1 signaling
R-HSA-5357956 TNFR1-induced NFkappaB signaling pathway
R-HSA-5675482 Regulation of necroptotic cell death
R-HSA-8948747 Regulation of PTEN localization
R-HSA-8948751 Regulation of PTEN stability and activity
SABIO-RKiP98170
SignaLinkiP98170
SIGNORiP98170

Miscellaneous databases

ChiTaRSiXIAP human
EvolutionaryTraceiP98170
GeneWikiiXIAP
GenomeRNAii331
PMAP-CutDBiP98170
PROiPR:P98170
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101966 Expressed in 211 organ(s), highest expression level in quadriceps femoris
CleanExiHS_XIAP
ExpressionAtlasiP98170 baseline and differential
GenevisibleiP98170 HS

Family and domain databases

CDDicd00022 BIR, 3 hits
Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR001370 BIR_rpt
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF00653 BIR, 3 hits
SMARTiView protein in SMART
SM00238 BIR, 3 hits
SM00184 RING, 1 hit
PROSITEiView protein in PROSITE
PS01282 BIR_REPEAT_1, 3 hits
PS50143 BIR_REPEAT_2, 3 hits
PS50089 ZF_RING_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiXIAP_HUMAN
AccessioniPrimary (citable) accession number: P98170
Secondary accession number(s): D3DTF2, Q9NQ14
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 24, 2001
Last modified: November 7, 2018
This is version 205 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again