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Protein

E3 ubiquitin-protein ligase XIAP

Gene

XIAP

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • 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. EC:2.3.2.27

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi300ZincPROSITE-ProRule annotation1
Metal bindingi303ZincPROSITE-ProRule annotation1
Metal bindingi320ZincPROSITE-ProRule annotation1
Metal bindingi327ZincPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri450 – 485RING-typePROSITE-ProRule annotationAdd BLAST36

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-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-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P98170

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P98170

SIGNOR Signaling Network Open Resource

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SIGNORi
P98170

Protein family/group databases

MEROPS protease database

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MEROPSi
I32.007

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P98170 Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:XIAP
Synonyms:API3, BIRC4, IAP3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000101966.12

Human Gene Nomenclature Database

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HGNCi
HGNC:592 XIAP

Online Mendelian Inheritance in Man (OMIM)

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MIMi
300079 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P98170

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

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DisGeNETi
331

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
XIAP

MalaCards human disease database

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MalaCardsi
XIAP
MIMi300635 phenotype

Open Targets

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OpenTargetsi
ENSG00000101966

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
2442 X-linked lymphoproliferative disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA25361

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4198

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2790

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
XIAP

Domain mapping of disease mutations (DMDM)

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DMDMi
12643387

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001223521 – 497E3 ubiquitin-protein ligase XIAPAdd BLAST497

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei87Phosphoserine; by PKB2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
P98170

MaxQB - The MaxQuant DataBase

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MaxQBi
P98170

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P98170

PeptideAtlas

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PeptideAtlasi
P98170

PRoteomics IDEntifications database

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PRIDEi
P98170

ProteomicsDB human proteome resource

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ProteomicsDBi
57803

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P98170

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P98170

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P98170

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous, except peripheral blood leukocytes.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000101966 Expressed in 211 organ(s), highest expression level in quadriceps femoris

CleanEx database of gene expression profiles

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CleanExi
HS_XIAP

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P98170 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P98170 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB009203
HPA042428

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106828, 172 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P98170

Database of interacting proteins

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DIPi
DIP-27626N

Protein interaction database and analysis system

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IntActi
P98170, 82 interactors

Molecular INTeraction database

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MINTi
P98170

STRING: functional protein association networks

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STRINGi
9606.ENSP00000347858

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P98170

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P98170

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P98170

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P98170

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati26 – 93BIR 1Add BLAST68
Repeati163 – 230BIR 2Add BLAST68
Repeati265 – 330BIR 3Add BLAST66

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni141 – 149Interaction with caspase-79

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1101 Eukaryota
ENOG410YPNM LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158743

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000232059

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004848

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P98170

KEGG Orthology (KO)

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KOi
K04725

Identification of Orthologs from Complete Genome Data

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OMAi
CSMVLAP

Database of Orthologous Groups

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OrthoDBi
EOG091G0CXH

Database for complete collections of gene phylogenies

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PhylomeDBi
P98170

TreeFam database of animal gene trees

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TreeFami
TF105356

Family and domain databases

Conserved Domains Database

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CDDi
cd00022 BIR, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001370 BIR_rpt
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD

Pfam protein domain database

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Pfami
View protein in Pfam
PF00653 BIR, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00238 BIR, 3 hits
SM00184 RING, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS01282 BIR_REPEAT_1, 3 hits
PS50143 BIR_REPEAT_2, 3 hits
PS50089 ZF_RING_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
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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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9D394C16D45EB635
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>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:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B1AKU3B1AKU3_HUMAN
E3 ubiquitin-protein ligase XIAP
XIAP
16Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti162S → C in AAC50373 (PubMed:8552191).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS14606.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S69544

NCBI Reference Sequences

More...
RefSeqi
NP_001158.2, NM_001167.3
NP_001191330.1, NM_001204401.1
XP_006724817.1, XM_006724754.2
XP_011529631.1, XM_011531329.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.356076
Hs.736565

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000355640; ENSP00000347858; ENSG00000101966
ENST00000371199; ENSP00000360242; ENSG00000101966
ENST00000434753; ENSP00000395230; ENSG00000101966

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
331

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:331

UCSC genome browser

More...
UCSCi
uc004etx.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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, 172 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

The DNASU plasmid repository

More...
DNASUi
331
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
331
DisGeNETi331
EuPathDBiHostDB:ENSG00000101966.12

GeneCards: human genes, protein and diseases

More...
GeneCardsi
XIAP
GeneReviewsiXIAP
HGNCiHGNC:592 XIAP
HPAiCAB009203
HPA042428
MalaCardsiXIAP
MIMi300079 gene
300635 phenotype
neXtProtiNX_P98170
OpenTargetsiENSG00000101966
Orphaneti2442 X-linked lymphoproliferative disease
PharmGKBiPA25361

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1101 Eukaryota
ENOG410YPNM LUCA
GeneTreeiENSGT00940000158743
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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
XIAP human
EvolutionaryTraceiP98170

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
XIAP

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
331
PMAP-CutDBiP98170

Protein Ontology

More...
PROi
PR:P98170

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiXIAP_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P98170
Secondary accession number(s): D3DTF2, Q9NQ14
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 24, 2001
Last modified: December 5, 2018
This is version 206 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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