Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 211 (07 Oct 2020)
Sequence version 1 (01 May 1999)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Apoptosis-inducing factor 1, mitochondrial

Gene

AIFM1

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

Functions both as NADH oxidoreductase and as regulator of apoptosis (PubMed:20362274, PubMed:23217327, PubMed:17094969). In response to apoptotic stimuli, it is released from the mitochondrion intermembrane space into the cytosol and to the nucleus, where it functions as a proapoptotic factor in a caspase-independent pathway. The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA (By similarity). Binds to DNA in a sequence-independent manner (PubMed:27178839). Interacts with EIF3G, and thereby inhibits the EIF3 machinery and protein synthesis, and activates caspase-7 to amplify apoptosis (PubMed:17094969). Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells (PubMed:19418225). In contrast, participates in normal mitochondrial metabolism. Plays an important role in the regulation of respiratory chain biogenesis by interacting with CHCHD4 and controlling CHCHD4 mitochondrial import (PubMed:26004228).By similarity6 Publications
Has NADH oxidoreductase activity. Does not induce nuclear apoptosis.1 Publication
Pro-apoptotic isoform.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD4 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 86 min(-1) for dichlorophenolindophenol reduction and 24 min(-1) for cytochrom c reduction (PubMed:27178839). kcat is 1.5 sec(-1) for dichlorophenolindophenol reduction, 3.1 sec(-1) for ferricyanide and 0.6 sec(-1) for cytochrom c reduction (PubMed:24914854).2 Publications
  1. KM=1.53 mM for NADH1 Publication
  2. KM=26 µM for cytochrome c (at pH 7.4 and 25 degrees Celsius)2 Publications
  3. KM=138 µM for dichlorophenolindophenol (at pH 7.4 and 25 degrees Celsius)1 Publication
  4. KM=0.51 mM for NADH (at pH 7.4 and 25 degrees Celsius)1 Publication
  5. KM=896 µM for NADPH1 Publication
    1. KM=102.6 µM for NADH1 Publication
    2. KM=45.3 µM for NADPH1 Publication

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei172FADCombined sources5 Publications1
      Binding sitei177FADCombined sources4 Publications1
      Binding sitei196NAD 2Combined sources1 Publication1
      Binding sitei233FAD; via amide nitrogen and carbonyl oxygenCombined sources5 Publications1
      Binding sitei285FADCombined sources5 Publications1
      Binding sitei336NAD 1Combined sources1 Publication1
      Binding sitei342NAD 1By similarity1
      Binding sitei399NAD 1; via amide nitrogenCombined sources1 Publication1
      Binding sitei438FADCombined sources5 Publications1
      Binding sitei483FAD; via carbonyl oxygenCombined sources5 Publications1
      Binding sitei483NAD 1; via carbonyl oxygenCombined sources1 Publication1
      Binding sitei493NAD 2Combined sources1 Publication1
      Binding sitei583NAD 2Combined sources1 Publication1

      Regions

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi138 – 142FADCombined sources5 Publications5
      Nucleotide bindingi164 – 165FADCombined sources5 Publications2
      Nucleotide bindingi308 – 311NAD 1Combined sources1 Publication4
      Nucleotide bindingi453 – 454NAD 1Combined sources1 Publication2
      Nucleotide bindingi454 – 455FADCombined sources4 Publications2

      <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 functionDNA-binding, Oxidoreductase
      Biological processApoptosis
      LigandFAD, Flavoprotein, NAD

      Enzyme and pathway databases

      Pathway Commons web resource for biological pathway data

      More...
      PathwayCommonsi
      O95831

      SABIO-RK: Biochemical Reaction Kinetics Database

      More...
      SABIO-RKi
      O95831

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

      More...
      SignaLinki
      O95831

      SIGNOR Signaling Network Open Resource

      More...
      SIGNORi
      O95831

      <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%5Fand%5Ftaxonomy%5Fsection">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:
      Apoptosis-inducing factor 1, mitochondrialCurated (EC:1.6.99.-3 Publications)
      Alternative name(s):
      Programmed cell death protein 8
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:AIFM1Imported
      Synonyms:AIF, PDCD8
      <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

      More...
      EuPathDBi
      HostDB:ENSG00000156709.13

      Human Gene Nomenclature Database

      More...
      HGNCi
      HGNC:8768, AIFM1

      Online Mendelian Inheritance in Man (OMIM)

      More...
      MIMi
      300169, gene

      neXtProt; the human protein knowledge platform

      More...
      neXtProti
      NX_O95831

      <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

      Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, 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

      Combined oxidative phosphorylation deficiency 6 (COXPD6)6 Publications
      The disease is caused by mutations affecting the gene represented in this entry.
      Disease descriptionA mitochondrial disease resulting in a neurodegenerative disorder characterized by psychomotor delay, hypotonia, areflexia, muscle weakness and wasting. Some patients manifest prenatal ventriculomegaly and severe postnatal encephalomyopathy.
      Related information in OMIM
      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_063827201Missing in COXPD6; higher DNA binding affinity, partially impaired flavin binding and association with increased parthanatos-linked cell death. 1 Publication1
      Natural variantiVAR_072791243V → L in COXPD6; reduced protein amount in muscle compared to controls; no effect on reduction with NADH; strongly decreased NADH oxidase activity; no effect on dimerization; no effect on DNA-binding. 2 Publications1
      Natural variantiVAR_067334308G → E in COXPD6; with prenatal ventriculomegaly and severe postnatal encephalomyopathy; no effect on redox potential; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding; decreased interaction with CHCHDE. 3 Publications1
      Natural variantiVAR_083068338G → E in COXPD6; with early-onset severe motor neuron involvement; decreased protein levels; decreased oxidoreductase activity on cytochrome C; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding. 2 Publications1
      Charcot-Marie-Tooth disease, X-linked recessive, 4, with or without cerebellar ataxia (CMTX4)2 Publications
      The disease is caused by mutations affecting the gene represented in this entry.
      Disease descriptionA neuromuscular disorder characterized by progressive sensorimotor axonal neuropathy, distal sensory impairment, difficulty walking due to peripheral neuropathy and/or cerebellar ataxia, and deafness due to auditory neuropathy. Additional features include cognitive impairment, cerebellar atrophy, dysarthria, abnormal extraocular movements, tremor, dysmetria and spasticity. The age at onset ranges from infancy to young adulthood.
      Related information in OMIM
      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Natural variantiVAR_069468493E → V in CMTX4; increases affinity for NADH and electron transfer activity; increases affinity for DNA, resulting in increased apoptosis; no effect on interaction with CHCHD4. 2 PublicationsCorresponds to variant dbSNP:rs281864468EnsemblClinVar.1
      Deafness, X-linked, 5, with peripheral neuropathy (DFNX5)1 Publication
      The disease is caused by mutations affecting the gene represented in this entry.
      Disease descriptionA form of hearing loss characterized by absent or severely abnormal auditory brainstem response, abnormal middle ear reflexes, abnormal speech discrimination, loss of outer hair cell function, and cochlear nerve hypoplasia. DFNX5 patients manifest auditory neuropathy with childhood onset, associated with distal sensory impairment affecting the peripheral nervous system.
      Related information in OMIM
      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Natural variantiVAR_076211260T → A in DFNX5. 1 PublicationCorresponds to variant dbSNP:rs863225432EnsemblClinVar.1
      Natural variantiVAR_076212344L → F in DFNX5; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs184474885EnsemblClinVar.1
      Natural variantiVAR_076213360G → R in DFNX5; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs724160026EnsemblClinVar.1
      Natural variantiVAR_076214422R → Q in DFNX5. 1 PublicationCorresponds to variant dbSNP:rs724160021EnsemblClinVar.1
      Natural variantiVAR_076215422R → W in DFNX5. 1 PublicationCorresponds to variant dbSNP:rs724160020EnsemblClinVar.1
      Natural variantiVAR_076216430R → C in DFNX5; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1223488720Ensembl.1
      Natural variantiVAR_076217451R → Q in DFNX5. 1 PublicationCorresponds to variant dbSNP:rs863225431EnsemblClinVar.1
      Natural variantiVAR_076218472A → V in DFNX5; unknown pathological significance. 1 Publication1
      Natural variantiVAR_076219475P → L in DFNX5; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs724160022EnsemblClinVar.1
      Natural variantiVAR_076220498V → M in DFNX5; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs724160023EnsemblClinVar.1
      Natural variantiVAR_076221591I → M in DFNX5; unknown pathological significance. 1 Publication1
      Spondyloepimetaphyseal dysplasia, X-linked, with hypomyelinating leukodystrophy (SEMDHL)1 Publication
      The disease is caused by mutations affecting the gene represented in this entry.
      Disease descriptionAn X-linked recessive developmental disorder characterized by slowly progressive skeletal and neurologic abnormalities, including short stature, large and deformed joints, significant motor impairment, visual defects, and sometimes cognitive deficits. Affected individuals typically have normal early development in the first year or so of life, followed by development regression and the development of symptoms. Brain imaging shows white matter abnormalities consistent with hypomyelinating leukodystrophy.
      Related information in OMIM
      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Natural variantiVAR_083739235Q → H in SEMDHL; severe decrease of protein expression. 1 Publication1
      Natural variantiVAR_083740237D → G in SEMDHL. 1 Publication1
      Natural variantiVAR_083741237D → V in SEMDHL. 1 Publication1

      Mutagenesis

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi196W → A: Increases protein dimerization at lower NADH levels. 1 Publication1
      Mutagenesisi413 – 430EIDSD…ELQAR → AIDSDFGGFAVNAELQAA: Disrupts dimerization. Lower efficiency in stabilizing charge-transfer complexes upon coenzyme reduction. 1 PublicationAdd BLAST18
      Mutagenesisi443 – 445YDI → ADA: Disrupts dimerization. Disrupts dimerization; when associated with A-477. 1 Publication3
      Mutagenesisi454H → A: Allows dimerization in absence of NADH. 1 Publication1
      Mutagenesisi477W → A: Disrupts dimerization; when associated with A-443--445-A. 1 Publication1
      Mutagenesisi480S → A: Allows dimerization in absence of NADH. 1 Publication1
      Mutagenesisi485D → A: Increases protein dimerization at lower NADH levels. 1 Publication1
      Mutagenesisi529R → A: Increases protein dimerization at lower NADH levels. 1 Publication1
      Mutagenesisi531E → A: Increases protein dimerization at lower NADH levels. 1 Publication1
      Mutagenesisi533E → A: Increases protein dimerization at lower NADH levels. 1 Publication1
      Mutagenesisi535E → A: Increases protein dimerization at lower NADH levels. 1 Publication1

      Keywords - Diseasei

      Charcot-Marie-Tooth disease, Deafness, Disease mutation, Dwarfism, Mental retardation, Neurodegeneration, Neuropathy, Primary mitochondrial disease

      Organism-specific databases

      DisGeNET

      More...
      DisGeNETi
      9131

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

      More...
      GeneReviewsi
      AIFM1

      MalaCards human disease database

      More...
      MalaCardsi
      AIFM1
      MIMi300232, phenotype
      300614, phenotype
      300816, phenotype
      310490, phenotype

      Open Targets

      More...
      OpenTargetsi
      ENSG00000156709

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

      More...
      Orphaneti
      83629, Leukoencephalopathy-spondylometaphyseal dysplasia syndrome
      238329, Severe X-linked mitochondrial encephalomyopathy
      101078, X-linked Charcot-Marie-Tooth disease type 4
      139583, X-linked hereditary sensory and autonomic neuropathy with deafness

      The Pharmacogenetics and Pharmacogenomics Knowledge Base

      More...
      PharmGKBi
      PA162376129

      Miscellaneous databases

      Pharos NIH Druggable Genome Knowledgebase

      More...
      Pharosi
      O95831, Tbio

      Chemistry databases

      ChEMBL database of bioactive drug-like small molecules

      More...
      ChEMBLi
      CHEMBL4295688

      Drug and drug target database

      More...
      DrugBanki
      DB03147, Flavin adenine dinucleotide
      DB05282, MCC

      Polymorphism and mutation databases

      BioMuta curated single-nucleotide variation and disease association database

      More...
      BioMutai
      AIFM1

      <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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 54MitochondrionCombined sources2 PublicationsAdd BLAST54
      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000040193555 – 101Removed in mature form1 PublicationAdd BLAST47
      <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000022030102 – 613Apoptosis-inducing factor 1, mitochondrialAdd BLAST512

      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 residuei105PhosphothreonineCombined sources1
      Modified residuei109N6-succinyllysineBy similarity1
      Modified residuei116PhosphoserineCombined sources1
      Modified residuei118PhosphoserineCombined sources1
      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
      Modified residuei268PhosphoserineCombined sources1
      Modified residuei292PhosphoserineCombined sources1
      Modified residuei371PhosphoserineCombined sources1
      Modified residuei388N6-acetyllysineBy similarity1
      Modified residuei521PhosphothreonineCombined sources1
      Modified residuei524PhosphoserineCombined sources1
      Modified residuei530PhosphoserineCombined sources1
      Modified residuei593N6-acetyllysineBy similarity1

      <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

      Under normal conditions, a 54-residue N-terminal segment is first proteolytically removed during or just after translocation into the mitochondrial intermembrane space (IMS) by the mitochondrial processing peptidase (MPP) to form the inner-membrane-anchored mature form (AIFmit). During apoptosis, it is further proteolytically processed at amino-acid position 101 leading to the generation of the mature form, which is confined to the mitochondrial IMS in a soluble form (AIFsol). AIFsol is released to the cytoplasm in response to specific death signals, and translocated to the nucleus, where it induces nuclear apoptosis in a caspase-independent manner.1 Publication
      Ubiquitination by XIAP/BIRC4 does not lead to proteasomal degradation. Ubiquitination at Lys-255 by XIAP/BIRC4 blocks its ability to bind DNA and induce chromatin degradation, thereby inhibiting its ability to induce cell death.2 Publications

      Keywords - PTMi

      Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

      Proteomic databases

      Encyclopedia of Proteome Dynamics

      More...
      EPDi
      O95831

      jPOST - Japan Proteome Standard Repository/Database

      More...
      jPOSTi
      O95831

      MassIVE - Mass Spectrometry Interactive Virtual Environment

      More...
      MassIVEi
      O95831

      MaxQB - The MaxQuant DataBase

      More...
      MaxQBi
      O95831

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

      More...
      PaxDbi
      O95831

      PeptideAtlas

      More...
      PeptideAtlasi
      O95831

      PRoteomics IDEntifications database

      More...
      PRIDEi
      O95831

      ProteomicsDB: a multi-organism proteome resource

      More...
      ProteomicsDBi
      51073 [O95831-1]
      51074 [O95831-2]
      51075 [O95831-3]
      51076 [O95831-4]
      61222
      61439

      2D gel databases

      REPRODUCTION-2DPAGE

      More...
      REPRODUCTION-2DPAGEi
      IPI00157908

      University College Dublin 2-DE Proteome Database

      More...
      UCD-2DPAGEi
      O95831

      PTM databases

      CarbonylDB database of protein carbonylation sites

      More...
      CarbonylDBi
      O95831

      iPTMnet integrated resource for PTMs in systems biology context

      More...
      iPTMneti
      O95831

      MetOSite database of methionine sulfoxide sites

      More...
      MetOSitei
      O95831

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

      More...
      PhosphoSitePlusi
      O95831

      SwissPalm database of S-palmitoylation events

      More...
      SwissPalmi
      O95831

      <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 in all tested tissues (PubMed:16644725). Detected in muscle and skin fibroblasts (at protein level) (PubMed:23217327). Expressed in osteoblasts (at protein level) (PubMed:28842795).3 Publications
      Brain specific.1 Publication
      Expressed in all tested tissues except brain.1 Publication
      Isoform 5 is frequently down-regulated in human cancers.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

      Strongly down-regulated in many tumor cells, up-regulated by gamma-irradiation.1 Publication

      Gene expression databases

      Bgee dataBase for Gene Expression Evolution

      More...
      Bgeei
      ENSG00000156709, Expressed in adult mammalian kidney and 227 other tissues

      ExpressionAtlas, Differential and Baseline Expression

      More...
      ExpressionAtlasi
      O95831, baseline and differential

      Genevisible search portal to normalized and curated expression data from Genevestigator

      More...
      Genevisiblei
      O95831, HS

      Organism-specific databases

      Human Protein Atlas

      More...
      HPAi
      ENSG00000156709, Tissue enhanced (kidney)

      <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

      Monomer (oxidized form). Homodimer (reduced form). Upon reduction with NADH, undergoes dimerization and forms tight, long-lived FADH2-NAD charge transfer complexes (CTC) resistant to oxidation (PubMed:24914854, PubMed:20111043, PubMed:23217327, PubMed:27818101). Also dimerizes with isoform 3 preventing its release from mitochondria (PubMed:20111043).

      Interacts with XIAP/BIRC4 (PubMed:17967870).

      Interacts (via N-terminus) with EIF3G (via C-terminus) (PubMed:17094969).

      Interacts with PRELID1 (PubMed:21364629).

      Interacts with CHCHD4; the interaction increases in presence of NADH (PubMed:26004228).

      8 Publications

      <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

      Hide details

      GO - Molecular functioni

      Protein-protein interaction databases

      The Biological General Repository for Interaction Datasets (BioGRID)

      More...
      BioGRIDi
      114579, 333 interactors

      CORUM comprehensive resource of mammalian protein complexes

      More...
      CORUMi
      O95831

      Database of interacting proteins

      More...
      DIPi
      DIP-32975N

      Protein interaction database and analysis system

      More...
      IntActi
      O95831, 269 interactors

      Molecular INTeraction database

      More...
      MINTi
      O95831

      STRING: functional protein association networks

      More...
      STRINGi
      9606.ENSP00000287295

      Miscellaneous databases

      RNAct, Protein-RNA interaction predictions for model organisms.

      More...
      RNActi
      O95831, protein

      <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

      1613
      Legend: HelixTurnBeta strandPDB Structure known for this area
      Show more details

      3D structure databases

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

      More...
      SMRi
      O95831

      Database of comparative protein structure models

      More...
      ModBasei
      Search...

      Protein Data Bank in Europe - Knowledge Base

      More...
      PDBe-KBi
      Search...

      Miscellaneous databases

      Relative evolutionary importance of amino acids within a protein sequence

      More...
      EvolutionaryTracei
      O95831

      <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

      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>Regioni134 – 483FAD-dependent oxidoreductaseBy similarityAdd BLAST350

      Motif

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1 – 31Mitochondrial localization signalBy similarityAdd BLAST31
      Motifi63 – 89Mitochondrial localization signalBy similarityAdd BLAST27
      Motifi446 – 451Nuclear localization signalSequence analysis6

      <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

      Keywords - Domaini

      Transit peptide

      Phylogenomic databases

      evolutionary genealogy of genes: Non-supervised Orthologous Groups

      More...
      eggNOGi
      KOG1346, Eukaryota

      Ensembl GeneTree

      More...
      GeneTreei
      ENSGT00940000156455

      The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

      More...
      HOGENOMi
      CLU_1059750_0_0_1

      InParanoid: Eukaryotic Ortholog Groups

      More...
      InParanoidi
      O95831

      KEGG Orthology (KO)

      More...
      KOi
      K04727

      Identification of Orthologs from Complete Genome Data

      More...
      OMAi
      EVRYERC

      Database of Orthologous Groups

      More...
      OrthoDBi
      830428at2759

      Database for complete collections of gene phylogenies

      More...
      PhylomeDBi
      O95831

      TreeFam database of animal gene trees

      More...
      TreeFami
      TF314028

      Family and domain databases

      Gene3D Structural and Functional Annotation of Protein Families

      More...
      Gene3Di
      3.30.390.30, 1 hit
      3.50.50.60, 2 hits

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR029324, AIF_C
      IPR036188, FAD/NAD-bd_sf
      IPR023753, FAD/NAD-binding_dom
      IPR016156, FAD/NAD-linked_Rdtase_dimer_sf

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF14721, AIF_C, 1 hit
      PF07992, Pyr_redox_2, 1 hit

      Superfamily database of structural and functional annotation

      More...
      SUPFAMi
      SSF51905, SSF51905, 2 hits
      SSF55424, SSF55424, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6+)i

      <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

      <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

      This entry describes 6 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

      This entry has 6 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

      Isoform 1 (identifier: O95831-1) [UniParc]FASTAAdd to basket
      Also known as: AIF

      This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

      « Hide
              10         20         30         40         50
      MFRCGGLAAG ALKQKLVPLV RTVCVRSPRQ RNRLPGNLFQ RWHVPLELQM
      60 70 80 90 100
      TRQMASSGAS GGKIDNSVLV LIVGLSTVGA GAYAYKTMKE DEKRYNERIS
      110 120 130 140 150
      GLGLTPEQKQ KKAALSASEG EEVPQDKAPS HVPFLLIGGG TAAFAAARSI
      160 170 180 190 200
      RARDPGARVL IVSEDPELPY MRPPLSKELW FSDDPNVTKT LRFKQWNGKE
      210 220 230 240 250
      RSIYFQPPSF YVSAQDLPHI ENGGVAVLTG KKVVQLDVRD NMVKLNDGSQ
      260 270 280 290 300
      ITYEKCLIAT GGTPRSLSAI DRAGAEVKSR TTLFRKIGDF RSLEKISREV
      310 320 330 340 350
      KSITIIGGGF LGSELACALG RKARALGTEV IQLFPEKGNM GKILPEYLSN
      360 370 380 390 400
      WTMEKVRREG VKVMPNAIVQ SVGVSSGKLL IKLKDGRKVE TDHIVAAVGL
      410 420 430 440 450
      EPNVELAKTG GLEIDSDFGG FRVNAELQAR SNIWVAGDAA CFYDIKLGRR
      460 470 480 490 500
      RVEHHDHAVV SGRLAGENMT GAAKPYWHQS MFWSDLGPDV GYEAIGLVDS
      510 520 530 540 550
      SLPTVGVFAK ATAQDNPKSA TEQSGTGIRS ESETESEASE ITIPPSTPAV
      560 570 580 590 600
      PQAPVQGEDY GKGVIFYLRD KVVVGIVLWN IFNRMPIARK IIKDGEQHED
      610
      LNEVAKLFNI HED
      Length:613
      Mass (Da):66,901
      Last modified:May 1, 1999 - v1
      <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:iA156762BC64E6340
      GO
      Isoform 2 (identifier: O95831-2) [UniParc]FASTAAdd to basket

      The sequence of this isoform differs from the canonical sequence as follows:
           36-322: Missing.

      Show »
      Length:326
      Mass (Da):35,638
      Checksum:iA87ACDC0A0556040
      GO
      Isoform 3 (identifier: O95831-3) [UniParc]FASTAAdd to basket
      Also known as: AIF-exB, AIF2

      The sequence of this isoform differs from the canonical sequence as follows:
           36-82: GNLFQRWHVP...VGLSTVGAGA → VVQSHHLGSP...GATVTGAGVY

      Show »
      Length:609
      Mass (Da):66,295
      Checksum:i313ADD6FA4E5D61A
      GO
      Isoform 4 (identifier: O95831-4) [UniParc]FASTAAdd to basket
      Also known as: AIFsh21 Publication

      The sequence of this isoform differs from the canonical sequence as follows:
           323-324: AR → DI
           325-613: Missing.

      Show »
      Length:324
      Mass (Da):35,384
      Checksum:i259AA55812C2F07E
      GO
      Isoform 5 (identifier: O95831-5) [UniParc]FASTAAdd to basket
      Also known as: AIFsh

      The sequence of this isoform differs from the canonical sequence as follows:
           1-352: Missing.

      Show »
      Length:261
      Mass (Da):28,404
      Checksum:iB05C9E9F3AA3F2E3
      GO
      Isoform 6 (identifier: O95831-6) [UniParc]FASTAAdd to basket
      Also known as: AIFsh31 Publication

      The sequence of this isoform differs from the canonical sequence as follows:
           1-87: Missing.
           323-324: AR → DI
           325-613: Missing.

      Show »
      Length:237
      Mass (Da):26,033
      Checksum:iC1DDF16F42339374
      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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
      EntryEntry nameProtein names
      Gene namesLengthAnnotation
      E9PMA0E9PMA0_HUMAN
      Apoptosis-inducing factor 1, mitoch...
      AIFM1
      274Annotation 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>
      E9PMQ8E9PMQ8_HUMAN
      Apoptosis-inducing factor 1, mitoch...
      AIFM1
      89Annotation 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>
      E9PRR0E9PRR0_HUMAN
      Apoptosis-inducing factor 1, mitoch...
      AIFM1
      43Annotation 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>

      Natural variant

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Natural variantiVAR_063827201Missing in COXPD6; higher DNA binding affinity, partially impaired flavin binding and association with increased parthanatos-linked cell death. 1 Publication1
      Natural variantiVAR_083739235Q → H in SEMDHL; severe decrease of protein expression. 1 Publication1
      Natural variantiVAR_083740237D → G in SEMDHL. 1 Publication1
      Natural variantiVAR_083741237D → V in SEMDHL. 1 Publication1
      Natural variantiVAR_072791243V → L in COXPD6; reduced protein amount in muscle compared to controls; no effect on reduction with NADH; strongly decreased NADH oxidase activity; no effect on dimerization; no effect on DNA-binding. 2 Publications1
      Natural variantiVAR_076211260T → A in DFNX5. 1 PublicationCorresponds to variant dbSNP:rs863225432EnsemblClinVar.1
      Natural variantiVAR_083067262G → S Probable disease-associated variant found in patient with mitochondrial encephalomyopathy with moderate clinical severity and slow progressive course despite early onset as well as and cerebellar involvement; decreased protein level; strongly decreased redox potential; strongly decreased NADH oxidase activity; no effect on DNA-binding. 2 Publications1
      Natural variantiVAR_067334308G → E in COXPD6; with prenatal ventriculomegaly and severe postnatal encephalomyopathy; no effect on redox potential; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding; decreased interaction with CHCHDE. 3 Publications1
      Natural variantiVAR_083068338G → E in COXPD6; with early-onset severe motor neuron involvement; decreased protein levels; decreased oxidoreductase activity on cytochrome C; slowered reduction with NADH; strongly decreased NADH oxidase activity; strongly decreased NADH oxidase activity; no effect on DNA-binding. 2 Publications1
      Natural variantiVAR_076212344L → F in DFNX5; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs184474885EnsemblClinVar.1
      Natural variantiVAR_076213360G → R in DFNX5; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs724160026EnsemblClinVar.1
      Natural variantiVAR_076214422R → Q in DFNX5. 1 PublicationCorresponds to variant dbSNP:rs724160021EnsemblClinVar.1
      Natural variantiVAR_076215422R → W in DFNX5. 1 PublicationCorresponds to variant dbSNP:rs724160020EnsemblClinVar.1
      Natural variantiVAR_076216430R → C in DFNX5; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1223488720Ensembl.1
      Natural variantiVAR_076217451R → Q in DFNX5. 1 PublicationCorresponds to variant dbSNP:rs863225431EnsemblClinVar.1
      Natural variantiVAR_076218472A → V in DFNX5; unknown pathological significance. 1 Publication1
      Natural variantiVAR_076219475P → L in DFNX5; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs724160022EnsemblClinVar.1
      Natural variantiVAR_069468493E → V in CMTX4; increases affinity for NADH and electron transfer activity; increases affinity for DNA, resulting in increased apoptosis; no effect on interaction with CHCHD4. 2 PublicationsCorresponds to variant dbSNP:rs281864468EnsemblClinVar.1
      Natural variantiVAR_076220498V → M in DFNX5; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs724160023EnsemblClinVar.1
      Natural variantiVAR_076221591I → M in DFNX5; unknown pathological significance. 1 Publication1

      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_0462481 – 352Missing in isoform 5. 1 PublicationAdd BLAST352
      Alternative sequenceiVSP_0476461 – 87Missing in isoform 6. 1 PublicationAdd BLAST87
      Alternative sequenceiVSP_00435736 – 322Missing in isoform 2. 1 PublicationAdd BLAST287
      Alternative sequenceiVSP_02295336 – 82GNLFQ…VGAGA → VVQSHHLGSPSRSLASTGAS GKDGSNLVYFLIVGATVTGA GVY in isoform 3. 3 PublicationsAdd BLAST47
      Alternative sequenceiVSP_043637323 – 324AR → DI in isoform 4 and isoform 6. 1 Publication2
      Alternative sequenceiVSP_043638325 – 613Missing in isoform 4 and isoform 6. 1 PublicationAdd BLAST289

      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
      AF100928 mRNA Translation: AAD16436.1
      DQ016496 mRNA Translation: AAY84737.1
      DQ016498 mRNA Translation: AAY84739.1
      DQ016500 mRNA Translation: AAY84741.1
      AL049703 mRNA Translation: CAB41267.1
      AL049704 mRNA Translation: CAB41268.1
      AK314446 mRNA Translation: BAG37055.1
      CR457379 mRNA Translation: CAG33660.1
      AL139234 Genomic DNA No translation available.
      CH471107 Genomic DNA Translation: EAX11811.1
      CH471107 Genomic DNA Translation: EAX11812.1
      CH471107 Genomic DNA Translation: EAX11810.1
      BC111065 mRNA Translation: AAI11066.1
      BC139738 mRNA Translation: AAI39739.1
      AF131759 mRNA Translation: AAD20036.1

      The Consensus CDS (CCDS) project

      More...
      CCDSi
      CCDS14618.1 [O95831-1]
      CCDS14619.1 [O95831-3]
      CCDS48167.1 [O95831-4]

      NCBI Reference Sequences

      More...
      RefSeqi
      NP_001124318.2, NM_001130846.3
      NP_001124319.1, NM_001130847.3 [O95831-4]
      NP_004199.1, NM_004208.3 [O95831-1]
      NP_665811.1, NM_145812.2 [O95831-3]

      Genome annotation databases

      Ensembl eukaryotic genome annotation project

      More...
      Ensembli
      ENST00000287295; ENSP00000287295; ENSG00000156709 [O95831-1]
      ENST00000319908; ENSP00000315122; ENSG00000156709 [O95831-3]
      ENST00000346424; ENSP00000316320; ENSG00000156709 [O95831-2]
      ENST00000416073; ENSP00000402535; ENSG00000156709 [O95831-4]
      ENST00000535724; ENSP00000446113; ENSG00000156709 [O95831-4]

      Database of genes from NCBI RefSeq genomes

      More...
      GeneIDi
      9131

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...
      KEGGi
      hsa:9131

      UCSC genome browser

      More...
      UCSCi
      uc004evg.4, human [O95831-1]

      Keywords - Coding sequence diversityi

      Alternative splicing

      <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%5Freferences%5Fsection">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

      Atlas of Genetics and Cytogenetics in Oncology and Haematology

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      AF100928 mRNA Translation: AAD16436.1
      DQ016496 mRNA Translation: AAY84737.1
      DQ016498 mRNA Translation: AAY84739.1
      DQ016500 mRNA Translation: AAY84741.1
      AL049703 mRNA Translation: CAB41267.1
      AL049704 mRNA Translation: CAB41268.1
      AK314446 mRNA Translation: BAG37055.1
      CR457379 mRNA Translation: CAG33660.1
      AL139234 Genomic DNA No translation available.
      CH471107 Genomic DNA Translation: EAX11811.1
      CH471107 Genomic DNA Translation: EAX11812.1
      CH471107 Genomic DNA Translation: EAX11810.1
      BC111065 mRNA Translation: AAI11066.1
      BC139738 mRNA Translation: AAI39739.1
      AF131759 mRNA Translation: AAD20036.1
      CCDSiCCDS14618.1 [O95831-1]
      CCDS14619.1 [O95831-3]
      CCDS48167.1 [O95831-4]
      RefSeqiNP_001124318.2, NM_001130846.3
      NP_001124319.1, NM_001130847.3 [O95831-4]
      NP_004199.1, NM_004208.3 [O95831-1]
      NP_665811.1, NM_145812.2 [O95831-3]

      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
      1M6IX-ray1.80A121-613[»]
      4BURX-ray2.88A/B/C/D103-613[»]
      4BV6X-ray1.80A121-613[»]
      4FDCX-ray2.40B103-613[»]
      4LIIX-ray1.88A100-611[»]
      5FMHX-ray1.80A104-613[»]
      5FS6X-ray1.90A/B103-613[»]
      5FS7X-ray1.85A/B103-613[»]
      5FS8X-ray1.40A103-613[»]
      5FS9X-ray1.75A/B103-613[»]
      5KVHX-ray2.27A/B78-613[»]
      5KVIX-ray2.00A78-613[»]
      SMRiO95831
      ModBaseiSearch...
      PDBe-KBiSearch...

      Protein-protein interaction databases

      BioGRIDi114579, 333 interactors
      CORUMiO95831
      DIPiDIP-32975N
      IntActiO95831, 269 interactors
      MINTiO95831
      STRINGi9606.ENSP00000287295

      Chemistry databases

      ChEMBLiCHEMBL4295688
      DrugBankiDB03147, Flavin adenine dinucleotide
      DB05282, MCC

      PTM databases

      CarbonylDBiO95831
      iPTMnetiO95831
      MetOSiteiO95831
      PhosphoSitePlusiO95831
      SwissPalmiO95831

      Polymorphism and mutation databases

      BioMutaiAIFM1

      2D gel databases

      REPRODUCTION-2DPAGEiIPI00157908
      UCD-2DPAGEiO95831

      Proteomic databases

      EPDiO95831
      jPOSTiO95831
      MassIVEiO95831
      MaxQBiO95831
      PaxDbiO95831
      PeptideAtlasiO95831
      PRIDEiO95831
      ProteomicsDBi51073 [O95831-1]
      51074 [O95831-2]
      51075 [O95831-3]
      51076 [O95831-4]
      61222
      61439

      Protocols and materials databases

      ABCD curated depository of sequenced antibodies

      More...
      ABCDi
      O95831, 1 sequenced antibody

      Antibodypedia a portal for validated antibodies

      More...
      Antibodypediai
      3528, 828 antibodies

      The DNASU plasmid repository

      More...
      DNASUi
      51060

      Genome annotation databases

      EnsembliENST00000287295; ENSP00000287295; ENSG00000156709 [O95831-1]
      ENST00000319908; ENSP00000315122; ENSG00000156709 [O95831-3]
      ENST0