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Entry version 217 (08 May 2019)
Sequence version 3 (21 Mar 2012)
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Protein

Baculoviral IAP repeat-containing protein 5

Gene

BIRC5

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

Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (PubMed:9859993, PubMed:21364656, PubMed:20627126). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (PubMed:16322459). Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules (PubMed:20826784). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (PubMed:20929775). The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (PubMed:18591255). May counteract a default induction of apoptosis in G2/M phase (PubMed:9859993). The acetylated form represses STAT3 transactivation of target gene promoters (PubMed:20826784). May play a role in neoplasia (PubMed:10626797). Inhibitor of CASP3 and CASP7 (PubMed:21536684). Isoform 2 and isoform 3 do not appear to play vital roles in mitosis (PubMed:12773388, PubMed:16291752). Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform (PubMed:10626797).11 Publications

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 bindingi57ZincCombined sources1 Publication1
Metal bindingi60ZincCombined sources1 Publication1
Metal bindingi77ZincCombined sources1 Publication1
Metal bindingi84ZincCombined sources1 Publication1

<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, Repressor, Thiol protease inhibitor
Biological processApoptosis, Cell cycle, Cell division, Chromosome partition, Mitosis, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6803205 TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain
R-HSA-68877 Mitotic Prometaphase
R-HSA-8951664 Neddylation

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

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SignaLinki
O15392

SIGNOR Signaling Network Open Resource

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SIGNORi
O15392

Protein family/group databases

MEROPS protease database

More...
MEROPSi
I32.005

<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:
Baculoviral IAP repeat-containing protein 5
Alternative name(s):
Apoptosis inhibitor 4
Apoptosis inhibitor survivin
<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:BIRC5
Synonyms:API4, IAP4
<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 17

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:593 BIRC5

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
603352 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O15392

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, 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

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>Mutagenesisi18R → A: Disrupts interaction with histone H3pT3, no effect on interaction with INCENP. 1 Publication1
Mutagenesisi23K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-62; R-78 and R-79. 1 Publication1
Mutagenesisi25W → A: Disrupts interaction with histone H3pT3, no effect on interaction with INCENP. 1 Publication1
Mutagenesisi33C → R: Disrupts interaction with histone H3pT3, no effect on interaction with INCENP. 1 Publication1
Mutagenesisi34T → A: Loss of LAMTOR5 binding. 1 Publication1
Mutagenesisi34T → E: Higher affinity for LAMTOR5 binding. 1 Publication1
Mutagenesisi48T → A or E: Localizes normally during mitosis but cannot support cell proliferation. Increased affinity for CDCA8/borealin. 1 Publication1
Mutagenesisi57C → A: Disrupts interaction with histone H3pT3, no effect on interaction with INCENP. 1 Publication1
Mutagenesisi62K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-78 and R-79. 1 Publication1
Mutagenesisi65E → A: Almost abolishes RAN-binding. Does not disrupt binding to AURKB or CDCA8. Disrupts mitotic spindle assembly. Does not disrupt nuclear export. 1 Publication1
Mutagenesisi67W → A: Disrupts interaction with histone H3pT3, no effect on interaction with INCENP. 1 Publication1
Mutagenesisi70D → A: No change. Loss of interaction with AURKB; when associated with A-71. 1 Publication1
Mutagenesisi71D → A: No change. Loss of interaction with AURKB; when associated with A-70. 1 Publication1
Mutagenesisi78K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-79. 1 Publication1
Mutagenesisi79K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-78. 1 Publication1
Mutagenesisi84C → A: Loss of cytoprotection. 1
Mutagenesisi117T → A: Prevents phosphorylation by AURKB. Still able to localize correctly but prevents interaction with INCENP. 1 Publication1
Mutagenesisi117T → E: Mimics phosphorylation. Disrupts subcellular localization during mitosis and prevents interaction with INCENP. 1 Publication1
Mutagenesisi129K → A or Q: Mimics acetylation. Localization primarily within the nucleus. 1 Publication1
Mutagenesisi129K → R: Loss of acetylation. Localization primarily within the cytoplasm. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
332

Open Targets

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OpenTargetsi
ENSG00000089685

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA25362

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5989

Drug and drug target database

More...
DrugBanki
DB05141 LY2181308

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2795

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
BIRC5

<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_00001223561 – 142Baculoviral IAP repeat-containing protein 5Add BLAST142

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 residuei20Phosphoserine; by AURKC1 Publication1
Modified residuei23N6-acetyllysine1 Publication1
Modified residuei34Phosphothreonine; by CDK1 and CDK15Combined sources2 Publications1
Modified residuei48Phosphothreonine; by CK2; in vitro1 Publication1
Modified residuei90N6-acetyllysine1 Publication1
Modified residuei110N6-acetyllysine1 Publication1
Modified residuei112N6-acetyllysine1 Publication1
Modified residuei115N6-acetyllysine1 Publication1
Modified residuei117Phosphothreonine; by AURKB1 Publication1
Modified residuei121N6-acetyllysine1 Publication1
Modified residuei129N6-acetyllysine1 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

Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting.2 Publications
In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes (PubMed:14610074). Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities (PubMed:21252625). Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity (PubMed:24866247). Phosphorylation at Ser-20 by AURKC is critical for regulation of proper chromosome alignment and segregation, and possibly cytokinesis.5 Publications
Acetylation at Lys-129 by CBP results in its homodimerization, while deacetylation promotes the formation of monomers which heterodimerize with XPO1/CRM1 which facilitates its nuclear export. The acetylated form represses STAT3 transactivation. The dynamic equilibrium between its acetylation and deacetylation at Lys-129 determines its interaction with XPO1/CRM1, its subsequent subcellular localization, and its ability to inhibit STAT3 transactivation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O15392

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O15392

MaxQB - The MaxQuant DataBase

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MaxQBi
O15392

PeptideAtlas

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PeptideAtlasi
O15392

PRoteomics IDEntifications database

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PRIDEi
O15392

ProteomicsDB human proteome resource

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ProteomicsDBi
48627
48628 [O15392-2]
48629 [O15392-3]
48630 [O15392-4]
48631 [O15392-5]
48632 [O15392-6]
48633 [O15392-7]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O15392

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

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PhosphoSitePlusi
O15392

<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

Expressed only in fetal kidney and liver, and to lesser extent, lung and brain (PubMed:10626797). Abundantly expressed in adenocarcinoma (lung, pancreas, colon, breast, and prostate) and in high-grade lymphomas (PubMed:14741722, PubMed:16329164). Also expressed in various renal cell carcinoma cell lines (PubMed:10626797). Expressed in cochlea including the organ of Corti, the lateral wall, the interdental cells of the Limbus as well as in Schwann cells and cells of the cochlear nerve and the spiral ganglions (at protein level). Not expressed in cells of the inner and outer sulcus or the Reissner's membrane (at protein level) (PubMed:21364656, PubMed:20627126).5 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expression is cell cycle-dependent and peaks at mitosis.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by COMP.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000089685 Expressed in 135 organ(s), highest expression level in vagina

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O15392 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O15392 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB004270
HPA002830

<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 or homodimer. Exists as a homodimer in the apo state and as a monomer in the CPC-bound state. The monomer protects cells against apoptosis more efficiently than the dimer. Only the dimeric form is capable of enhancing tubulin stability in cells. When phosphorylated, interacts with LAMTOR5/HBXIP; the resulting complex binds pro-CASP9, as well as active CASP9, but much less efficiently. Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the complex forms a triple-helix bundle-based subcomplex with INCENP and CDCA8 (PubMed:17956729). Interacts with JTB. Interacts (via BIR domain) with histone H3 phosphorylated at 'Thr-3' (H3pT3). Interacts with EVI5. Interacts with GTP-bound RAN in both the S and M phases of the cell cycle. Interacts with USP9X. Interacts with tubulin. Interacts with BIRC2/c-IAP1. The acetylated form at Lys-129 interacts with STAT3. The monomeric form deacetylated at Lys-129 interacts with XPO1/CRM1. The monomeric form interacts with XIAP/BIRC4. Both the dimeric and monomeric form can interact with DIABLO/SMAC. Interacts with BIRC6/bruce.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
106829, 61 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-111 Survivin homodimer complex
CPX-116 Chromosomal passenger complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O15392

Database of interacting proteins

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DIPi
DIP-34662N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
O15392

Protein interaction database and analysis system

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IntActi
O15392, 19 interactors

Molecular INTeraction database

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MINTi
O15392

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O15392

<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

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E31X-ray2.71A/B1-142[»]
1F3HX-ray2.58A/B1-142[»]
1XOXNMR-A/B1-117[»]
2QFAX-ray1.40A1-142[»]
2RAWX-ray2.40A1-142[»]
2RAXX-ray3.30A/E/X1-120[»]
3UECX-ray2.18A1-142[»]
3UEDX-ray2.70A/C1-142[»]
3UEEX-ray2.61A/C1-142[»]
3UEFX-ray2.45A/C1-142[»]
3UEGX-ray2.80A/B1-142[»]
3UEHX-ray2.60A/B1-142[»]
3UEIX-ray2.70A/B1-142[»]
3UIGX-ray2.40A/B1-142[»]
3UIHX-ray2.40A/B1-142[»]
3UIIX-ray2.60A/B1-142[»]
3UIJX-ray2.70A/B1-142[»]
3UIKX-ray2.70A/B1-142[»]
4A0IX-ray2.60A/B1-142[»]
4A0JX-ray2.80A/B1-142[»]
4A0NX-ray2.74A1-142[»]

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

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SMRi
O15392

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
O15392

<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>Repeati18 – 88BIRAdd BLAST71

<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 BIR repeat is necessary and sufficient for LAMTOR5 binding.1 Publication

<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

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00510000047537

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000172188

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O15392

KEGG Orthology (KO)

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KOi
K08731

Database of Orthologous Groups

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OrthoDBi
1404665at2759

Family and domain databases

Conserved Domains Database

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CDDi
cd00022 BIR, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001370 BIR_rpt

Pfam protein domain database

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Pfami
View protein in Pfam
PF00653 BIR, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00238 BIR, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50143 BIR_REPEAT_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>Sequences (7+)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 describes 7 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 7 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O15392-1) [UniParc]FASTAAdd to basket
Also known as: Alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN
60 70 80 90 100
EPDLAQCFFC FKELEGWEPD DDPIEEHKKH SSGCAFLSVK KQFEELTLGE
110 120 130 140
FLKLDRERAK NKIAKETNNK KKEFEETAKK VRRAIEQLAA MD
Length:142
Mass (Da):16,389
Last modified:March 21, 2012 - v3
<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:i9E7CADCDF2822286
GO
Isoform 2 (identifier: O15392-2) [UniParc]FASTAAdd to basket
Also known as: 2B, Beta

The sequence of this isoform differs from the canonical sequence as follows:
     74-74: I → IGPGTVAYACNTSTLGGRGGRITR

Show »
Length:165
Mass (Da):18,636
Checksum:iD1E961E51ADDD01E
GO
Isoform 3 (identifier: O15392-3) [UniParc]FASTAAdd to basket
Also known as: DeltaEx3

The sequence of this isoform differs from the canonical sequence as follows:
     74-142: IEEHKKHSSG...RAIEQLAAMD → MQRKPTIRRK...SLPVGPLAMS

Show »
Length:137
Mass (Da):15,622
Checksum:i38C82D22E46BFF7C
GO
Isoform 4 (identifier: O15392-4) [UniParc]FASTAAdd to basket
Also known as: 3B

The sequence of this isoform differs from the canonical sequence as follows:
     114-142: AKETNNKKKEFEETAKKVRRAIEQLAAMD → ERALLAE

Show »
Length:120
Mass (Da):13,812
Checksum:i3904E8C8AF6945F7
GO
Isoform 5 (identifier: O15392-5) [UniParc]FASTAAdd to basket
Also known as: SI

The sequence of this isoform differs from the canonical sequence as follows:
     105-142: DRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD → VRETLPPPRSFIR

Show »
Length:117
Mass (Da):13,467
Checksum:i82FC6A9B55F06876
GO
Isoform 6 (identifier: O15392-6) [UniParc]FASTAAdd to basket
Also known as: 3 alpha

The sequence of this isoform differs from the canonical sequence as follows:
     74-142: IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD → MRELC

Show »
Length:78
Mass (Da):8,991
Checksum:iD06E2937DCAC8283
GO
Isoform 7 (identifier: O15392-7) [UniParc]FASTAAdd to basket
Also known as: 2 alpha

The sequence of this isoform differs from the canonical sequence as follows:
     74-142: IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD → M

Show »
Length:74
Mass (Da):8,490
Checksum:i8CAC8283CD371FD9
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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BLT4H3BLT4_HUMAN
Baculoviral IAP repeat-containing p...
BIRC5
165Annotation score:

Annotation score:2 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>
A0A0B4J1S3A0A0B4J1S3_HUMAN
Baculoviral IAP repeat-containing p...
BIRC5
142Annotation 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>
K7EMW2K7EMW2_HUMAN
Baculoviral IAP repeat-containing p...
BIRC5
121Annotation 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>
K7EP76K7EP76_HUMAN
Baculoviral IAP repeat-containing p...
BIRC5
52Annotation 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>
K7ELG2K7ELG2_HUMAN
Baculoviral IAP repeat-containing p...
BIRC5
83Annotation 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 conflicti57 – 58CF → WV in AAW22624 (PubMed:16329164).Curated2
Sequence conflicti58F → L in BAD97148 (Ref. 11) Curated1
Sequence conflicti128A → V in CAG46540 (Ref. 9) 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_021071129K → E Loss of acetylation; localization primarily within the cytoplasm; increased likelihood of existing as monomer; stronger binding to XPO1/CRM1. 2 PublicationsCorresponds to variant dbSNP:rs2071214Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_02033874 – 142IEEHK…LAAMD → MQRKPTIRRKNLRKLRRKCA VPSSSWLPWIEASGRSCLVP EWLHHFQGLFPGATSLPVGP LAMS in isoform 3. 1 PublicationAdd BLAST69
Alternative sequenceiVSP_02033974 – 142IEEHK…LAAMD → MRELC in isoform 6. 1 PublicationAdd BLAST69
Alternative sequenceiVSP_02034074 – 142IEEHK…LAAMD → M in isoform 7. 1 PublicationAdd BLAST69
Alternative sequenceiVSP_00245474I → IGPGTVAYACNTSTLGGRGG RITR in isoform 2. 2 Publications1
Alternative sequenceiVSP_020341105 – 142DRERA…LAAMD → VRETLPPPRSFIR in isoform 5. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_020342114 – 142AKETN…LAAMD → ERALLAE in isoform 4. 1 PublicationAdd BLAST29

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U75285 Genomic DNA Translation: AAC51660.1
AF077350 mRNA Translation: AAD34226.1
AB154416 mRNA Translation: BAD11155.1
AY830084 mRNA Translation: AAW22624.1
AB028869 mRNA Translation: BAA93676.1
AY927772 mRNA Translation: AAY15202.1
DQ227257 mRNA Translation: ABB76601.1
DQ310375 mRNA Translation: ABC42341.1
DQ310376 mRNA Translation: ABC42342.1
DQ310377 mRNA Translation: ABC42343.1
DQ310378 mRNA Translation: ABC42344.1
DQ310379 mRNA Translation: ABC42345.1
CR541740 mRNA Translation: CAG46540.1
AK223428 mRNA Translation: BAD97148.1
AK311917 mRNA Translation: BAG34858.1
AY795969 Genomic DNA Translation: AAV40840.1
AC087645 Genomic DNA No translation available.
CH471099 Genomic DNA Translation: EAW89514.1
BC008718 mRNA Translation: AAH08718.1
BC034148 mRNA Translation: AAH34148.1
BC065497 mRNA Translation: AAH65497.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11755.1 [O15392-1]
CCDS32751.1 [O15392-3]
CCDS32752.1 [O15392-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001012270.1, NM_001012270.1 [O15392-3]
NP_001012271.1, NM_001012271.1
NP_001159.2, NM_001168.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000374948; ENSP00000364086; ENSG00000089685 [O15392-3]
ENST00000590449; ENSP00000465868; ENSG00000089685 [O15392-7]
ENST00000590925; ENSP00000467336; ENSG00000089685 [O15392-4]
ENST00000592734; ENSP00000466617; ENSG00000089685 [O15392-6]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
332

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:332

UCSC genome browser

More...
UCSCi
uc002jvh.4 human [O15392-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75285 Genomic DNA Translation: AAC51660.1
AF077350 mRNA Translation: AAD34226.1
AB154416 mRNA Translation: BAD11155.1
AY830084 mRNA Translation: AAW22624.1
AB028869 mRNA Translation: BAA93676.1
AY927772 mRNA Translation: AAY15202.1
DQ227257 mRNA Translation: ABB76601.1
DQ310375 mRNA Translation: ABC42341.1
DQ310376 mRNA Translation: ABC42342.1
DQ310377 mRNA Translation: ABC42343.1
DQ310378 mRNA Translation: ABC42344.1
DQ310379 mRNA Translation: ABC42345.1
CR541740 mRNA Translation: CAG46540.1
AK223428 mRNA Translation: BAD97148.1
AK311917 mRNA Translation: BAG34858.1
AY795969 Genomic DNA Translation: AAV40840.1
AC087645 Genomic DNA No translation available.
CH471099 Genomic DNA Translation: EAW89514.1
BC008718 mRNA Translation: AAH08718.1
BC034148 mRNA Translation: AAH34148.1
BC065497 mRNA Translation: AAH65497.1
CCDSiCCDS11755.1 [O15392-1]
CCDS32751.1 [O15392-3]
CCDS32752.1 [O15392-2]
RefSeqiNP_001012270.1, NM_001012270.1 [O15392-3]
NP_001012271.1, NM_001012271.1
NP_001159.2, NM_001168.2

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E31X-ray2.71A/B1-142[»]
1F3HX-ray2.58A/B1-142[»]
1XOXNMR-A/B1-117[»]
2QFAX-ray1.40A1-142[»]
2RAWX-ray2.40A1-142[»]
2RAXX-ray3.30A/E/X1-120[»]
3UECX-ray2.18A1-142[»]
3UEDX-ray2.70A/C1-142[»]
3UEEX-ray2.61A/C1-142[»]
3UEFX-ray2.45A/C1-142[»]
3UEGX-ray2.80A/B1-142[»]
3UEHX-ray2.60A/B1-142[»]
3UEIX-ray2.70A/B1-142[»]
3UIGX-ray2.40A/B1-142[»]
3UIHX-ray2.40A/B1-142[»]
3UIIX-ray2.60A/B1-142[»]
3UIJX-ray2.70A/B1-142[»]
3UIKX-ray2.70A/B1-142[»]
4A0IX-ray2.60A/B1-142[»]
4A0JX-ray2.80A/B1-142[»]
4A0NX-ray2.74A1-142[»]
SMRiO15392
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106829, 61 interactors
ComplexPortaliCPX-111 Survivin homodimer complex
CPX-116 Chromosomal passenger complex
CORUMiO15392
DIPiDIP-34662N
ELMiO15392
IntActiO15392, 19 interactors
MINTiO15392

Chemistry databases

BindingDBiO15392
ChEMBLiCHEMBL5989
DrugBankiDB05141 LY2181308
GuidetoPHARMACOLOGYi2795

Protein family/group databases

MEROPSiI32.005

PTM databases

iPTMnetiO15392
PhosphoSitePlusiO15392

Polymorphism and mutation databases

BioMutaiBIRC5

Proteomic databases

EPDiO15392
jPOSTiO15392
MaxQBiO15392
PeptideAtlasiO15392
PRIDEiO15392
ProteomicsDBi48627
48628 [O15392-2]
48629 [O15392-3]
48630 [O15392-4]
48631 [O15392-5]
48632 [O15392-6]
48633 [O15392-7]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
332
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374948; ENSP00000364086; ENSG00000089685 [O15392-3]
ENST00000590449; ENSP00000465868; ENSG00000089685 [O15392-7]
ENST00000590925; ENSP00000467336; ENSG00000089685 [O15392-4]
ENST00000592734; ENSP00000466617; ENSG00000089685 [O15392-6]
GeneIDi332
KEGGihsa:332
UCSCiuc002jvh.4 human [O15392-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
332
DisGeNETi332

GeneCards: human genes, protein and diseases

More...
GeneCardsi
BIRC5
HGNCiHGNC:593 BIRC5
HPAiCAB004270
HPA002830
MIMi603352 gene
neXtProtiNX_O15392
OpenTargetsiENSG00000089685
PharmGKBiPA25362

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

GeneTreeiENSGT00510000047537
HOGENOMiHOG000172188
InParanoidiO15392
KOiK08731
OrthoDBi1404665at2759

Enzyme and pathway databases

ReactomeiR-HSA-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-4615885 SUMOylation of DNA replication proteins
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6803205 TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain
R-HSA-68877 Mitotic Prometaphase
R-HSA-8951664 Neddylation
SignaLinkiO15392
SIGNORiO15392

Miscellaneous databases

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

More...
ChiTaRSi
BIRC5 human
EvolutionaryTraceiO15392

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Survivin

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

More...
GenomeRNAii
332

Protein Ontology

More...
PROi
PR:O15392

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000089685 Expressed in 135 organ(s), highest expression level in vagina
ExpressionAtlasiO15392 baseline and differential
GenevisibleiO15392 HS

Family and domain databases

CDDicd00022 BIR, 1 hit
InterProiView protein in InterPro
IPR001370 BIR_rpt
PfamiView protein in Pfam
PF00653 BIR, 1 hit
SMARTiView protein in SMART
SM00238 BIR, 1 hit
PROSITEiView protein in PROSITE
PS50143 BIR_REPEAT_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 nameiBIRC5_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: O15392
Secondary accession number(s): A2SUH6
, B2R4R1, Q2I3N8, Q4VGX0, Q53F61, Q5MGC6, Q6FHL2, Q75SP2, Q9P2W8
<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: May 30, 2000
Last sequence update: March 21, 2012
Last modified: May 8, 2019
This is version 217 of the entry and version 3 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 17
    Human chromosome 17: 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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