SubmitCancel

Skip Header

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

O95831

- AIFM1_HUMAN

UniProt

O95831 - AIFM1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Apoptosis-inducing factor 1, mitochondrial
Gene
AIFM1, AIF, PDCD8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Functions both as NADH oxidoreductase and as regulator of apoptosis. 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. In contrast, functions as an antiapoptotic factor in normal mitochondria via its NADH oxidoreductase activity. The soluble form (AIFsol) found in the nucleus induces 'parthanatos' i.e. caspase-independent fragmentation of chromosomal DNA. Interacts with EIF3G,and thereby inhibits the EIF3 machinery and protein synthesis, and activates casapse-7 to amplify apoptosis. Plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells. Binds to DNA in a sequence-independent manner.4 Publications

Cofactori

FAD.1 Publication

Kineticsi

  1. KM=1.53 mM for NADH1 Publication
  2. KM=26 µM for cytochrome c

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei172 – 1721FAD
Binding sitei177 – 1771FAD
Binding sitei233 – 2331FAD; via amide nitrogen and carbonyl oxygen
Binding sitei285 – 2851FAD
Binding sitei438 – 4381FAD
Binding sitei483 – 4831FAD; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi138 – 1425FAD
Nucleotide bindingi164 – 1652FAD
Nucleotide bindingi454 – 4552FAD

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. NAD(P)H oxidase activity Source: UniProtKB
  3. electron carrier activity Source: ProtInc
  4. flavin adenine dinucleotide binding Source: InterPro
  5. oxidoreductase activity, acting on NAD(P)H Source: UniProtKB
  6. protein binding Source: UniProtKB

GO - Biological processi

  1. DNA catabolic process Source: UniProtKB
  2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  3. apoptotic DNA fragmentation Source: ProtInc
  4. apoptotic process Source: UniProtKB
  5. cell redox homeostasis Source: InterPro
  6. chromosome condensation Source: UniProtKB
  7. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
  8. mitochondrial respiratory chain complex I assembly Source: UniProtKB
  9. neuron apoptotic process Source: Ensembl
  10. neuron differentiation Source: UniProtKB
  11. positive regulation of apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

DNA-binding, FAD, Flavoprotein, NAD

Enzyme and pathway databases

SignaLinkiO95831.

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis-inducing factor 1, mitochondrial (EC:1.1.1.-)
Alternative name(s):
Programmed cell death protein 8
Gene namesi
Name:AIFM1
Synonyms:AIF, PDCD8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8768. AIFM1.

Subcellular locationi

Mitochondrion intermembrane space. Mitochondrion inner membrane. Cytoplasm. Nucleus. Cytoplasmperinuclear region
Note: Proteolytic cleavage during or just after translocation into the mitochondrial intermembrane space (IMS) results in the formation of an inner-membrane-anchored mature form (AIFmit). During apoptosis, further proteolytic processing leads to a 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. Colocalizes with EIF3G in the nucleus and perinuclear region.6 Publications
Isoform 3 : Mitochondrion intermembrane space. Mitochondrion inner membrane
Note: Has a stronger membrane anchorage than isoform 1.6 Publications
Isoform 5 : Cytoplasm 6 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. mitochondrial inner membrane Source: UniProtKB
  3. mitochondrial intermembrane space Source: UniProtKB
  4. mitochondrion Source: UniProt
  5. nucleus Source: UniProtKB
  6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Combined oxidative phosphorylation deficiency 6 (COXPD6) [MIM:300816]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti201 – 2011Missing in COXPD6; higher DNA binding affinity, partially impaired flavin binding and association with increased parthanatos-linked cell death. 1 Publication
VAR_063827
Natural varianti308 – 3081G → E in COXPD6; with prenatal ventriculomegaly and severe postnatal encephalomyopathy. 1 Publication
VAR_067334
Cowchock syndrome (COWCK) [MIM:310490]: An X-linked recessive neuromuscular disorder characterized by early childhood onset of a slowly progressive axonal sensorimotor neuropathy associated in some patients with sensorineural deafness and cognitive impairment.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti493 – 4931E → V in COWCK; increases affinity for NADH and electron transfer activity. Increases affinity for DNA, resulting in increased apoptosis. 1 Publication
VAR_069468

Keywords - Diseasei

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

Organism-specific databases

MIMi300816. phenotype.
310490. phenotype.
Orphaneti238329. Severe X-linked mitochondrial encephalomyopathy.
101078. X-linked Charcot-Marie-Tooth disease type 4.
PharmGKBiPA162376129.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5454Mitochondrion2 Publications
Add
BLAST
Propeptidei55 – 10147Removed in mature form
PRO_0000401935Add
BLAST
Chaini102 – 613512Apoptosis-inducing factor 1, mitochondrial
PRO_0000022030Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051Phosphothreonine1 Publication
Modified residuei109 – 1091N6-succinyllysine By similarity
Cross-linki255 – 255Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei268 – 2681Phosphoserine1 Publication
Modified residuei388 – 3881N6-acetyllysine By similarity
Modified residuei593 – 5931N6-acetyllysine By similarity

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.
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.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO95831.
PaxDbiO95831.
PRIDEiO95831.

2D gel databases

REPRODUCTION-2DPAGEIPI00157908.
UCD-2DPAGEO95831.

PTM databases

PhosphoSiteiO95831.

Expressioni

Tissue specificityi

Detected in muscle and skin fibroblasts (at protein level). Isoform 5 is frequently down-regulated in human cancers.2 Publications

Gene expression databases

ArrayExpressiO95831.
BgeeiO95831.
CleanExiHS_AIFM1.
GenevestigatoriO95831.

Organism-specific databases

HPAiCAB003764.
HPA030611.

Interactioni

Subunit structurei

Monomer (oxidized form). Homodimer (reduced form). Also dimerizes with isoform 3 preventing its release from mitochondria. Interacts with XIAP/BIRC4. Interacts (via N-terminus) with EIF3G (via C-terminus). Interacts with PRELID1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF3GO758219EBI-356440,EBI-366632
KANK2Q63ZY32EBI-356440,EBI-2556193
KANK2Q63ZY3-24EBI-356440,EBI-6244894
TSC22D4Q9Y3Q82EBI-356440,EBI-739485

Protein-protein interaction databases

BioGridi114579. 58 interactions.
119252. 8 interactions.
IntActiO95831. 29 interactions.
MINTiMINT-209209.
STRINGi9606.ENSP00000287295.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi130 – 1389
Helixi141 – 15313
Beta strandi158 – 16710
Helixi173 – 1764
Helixi178 – 1803
Helixi187 – 1904
Beta strandi192 – 1943
Beta strandi200 – 2067
Helixi208 – 2103
Turni214 – 2196
Beta strandi224 – 2296
Beta strandi233 – 2375
Turni238 – 2414
Beta strandi242 – 2454
Beta strandi250 – 2589
Beta strandi262 – 2643
Helixi268 – 2714
Helixi275 – 2795
Beta strandi281 – 2833
Helixi287 – 29913
Beta strandi301 – 3066
Helixi310 – 32617
Beta strandi329 – 3335
Beta strandi335 – 3384
Turni339 – 3435
Helixi346 – 35712
Turni358 – 3603
Beta strandi362 – 3643
Beta strandi369 – 3757
Beta strandi378 – 3836
Beta strandi388 – 3969
Beta strandi400 – 4023
Helixi407 – 4104
Turni416 – 4183
Beta strandi420 – 4223
Beta strandi428 – 4303
Beta strandi433 – 4353
Helixi437 – 4393
Beta strandi440 – 4445
Turni445 – 4473
Beta strandi448 – 4503
Helixi455 – 46915
Beta strandi481 – 4877
Beta strandi491 – 4966
Beta strandi504 – 5096
Helixi517 – 5248
Helixi529 – 5324
Beta strandi562 – 5698
Beta strandi572 – 5809
Helixi585 – 59410
Helixi604 – 6074

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M6IX-ray1.80A121-613[»]
4FDCX-ray2.40B103-613[»]
4LIIX-ray1.88A100-611[»]
ProteinModelPortaliO95831.
SMRiO95831. Positions 125-611.

Miscellaneous databases

EvolutionaryTraceiO95831.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 483350FAD-dependent oxidoreductase By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi446 – 4516Nuclear localization signal Reviewed prediction

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0446.
HOGENOMiHOG000124580.
HOVERGENiHBG053538.
InParanoidiO95831.
KOiK04727.
OMAiKDGEEHA.
OrthoDBiEOG7C2R0V.
PhylomeDBiO95831.
TreeFamiTF314028.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR029324. AIF_C.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view]
PfamiPF14721. AIF_C. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF55424. SSF55424. 1 hit.

Sequences (6)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95831-1) [UniParc]FASTAAdd to Basket

Also known as: AIF

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.

« Hide

MFRCGGLAAG ALKQKLVPLV RTVCVRSPRQ RNRLPGNLFQ RWHVPLELQM    50
TRQMASSGAS GGKIDNSVLV LIVGLSTVGA GAYAYKTMKE DEKRYNERIS 100
GLGLTPEQKQ KKAALSASEG EEVPQDKAPS HVPFLLIGGG TAAFAAARSI 150
RARDPGARVL IVSEDPELPY MRPPLSKELW FSDDPNVTKT LRFKQWNGKE 200
RSIYFQPPSF YVSAQDLPHI ENGGVAVLTG KKVVQLDVRD NMVKLNDGSQ 250
ITYEKCLIAT GGTPRSLSAI DRAGAEVKSR TTLFRKIGDF RSLEKISREV 300
KSITIIGGGF LGSELACALG RKARALGTEV IQLFPEKGNM GKILPEYLSN 350
WTMEKVRREG VKVMPNAIVQ SVGVSSGKLL IKLKDGRKVE TDHIVAAVGL 400
EPNVELAKTG GLEIDSDFGG FRVNAELQAR SNIWVAGDAA CFYDIKLGRR 450
RVEHHDHAVV SGRLAGENMT GAAKPYWHQS MFWSDLGPDV GYEAIGLVDS 500
SLPTVGVFAK ATAQDNPKSA TEQSGTGIRS ESETESEASE ITIPPSTPAV 550
PQAPVQGEDY GKGVIFYLRD KVVVGIVLWN IFNRMPIARK IIKDGEQHED 600
LNEVAKLFNI HED 613
Length:613
Mass (Da):66,901
Last modified:May 1, 1999 - v1
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

Note: Brain-specific.

Show »
Length:609
Mass (Da):66,295
Checksum:i313ADD6FA4E5D61A
GO
Isoform 4 (identifier: O95831-4) [UniParc]FASTAAdd to Basket

Also known as: AIFsh2

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

Note: Does not induce nuclear apoptosis.

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.

Note: Pro-apoptotic isoform, strongly down-regulated in many tumor cells, up-regulated by gamma-irradiation.

Show »
Length:261
Mass (Da):28,404
Checksum:iB05C9E9F3AA3F2E3
GO
Isoform 6 (identifier: O95831-6) [UniParc]FASTAAdd to Basket

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti201 – 2011Missing in COXPD6; higher DNA binding affinity, partially impaired flavin binding and association with increased parthanatos-linked cell death. 1 Publication
VAR_063827
Natural varianti308 – 3081G → E in COXPD6; with prenatal ventriculomegaly and severe postnatal encephalomyopathy. 1 Publication
VAR_067334
Natural varianti493 – 4931E → V in COWCK; increases affinity for NADH and electron transfer activity. Increases affinity for DNA, resulting in increased apoptosis. 1 Publication
VAR_069468

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 352352Missing in isoform 5.
VSP_046248Add
BLAST
Alternative sequencei1 – 8787Missing in isoform 6.
VSP_047646Add
BLAST
Alternative sequencei36 – 322287Missing in isoform 2.
VSP_004357Add
BLAST
Alternative sequencei36 – 8247GNLFQ…VGAGA → VVQSHHLGSPSRSLASTGAS GKDGSNLVYFLIVGATVTGA GVY in isoform 3.
VSP_022953Add
BLAST
Alternative sequencei323 – 3242AR → DI in isoform 4 and isoform 6.
VSP_043637
Alternative sequencei325 – 613289Missing in isoform 4 and isoform 6.
VSP_043638Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. Translation: CAI42778.1.
AL139234 Genomic DNA. Translation: CAI42779.1.
AL139234 Genomic DNA. Translation: CAI42780.1.
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]
CCDS48166.1. [O95831-5]
CCDS48167.1. [O95831-4]
RefSeqiNP_001124318.1. NM_001130846.2. [O95831-5]
NP_001124319.1. NM_001130847.3. [O95831-4]
NP_004199.1. NM_004208.3. [O95831-1]
NP_665811.1. NM_145812.2. [O95831-3]
NP_665812.1. NM_145813.2. [O95831-2]
UniGeneiHs.424932.

Genome annotation databases

EnsembliENST00000287295; ENSP00000287295; ENSG00000156709. [O95831-1]
ENST00000319908; ENSP00000315122; ENSG00000156709. [O95831-3]
ENST00000346424; ENSP00000316320; ENSG00000156709. [O95831-2]
ENST00000416073; ENSP00000402535; ENSG00000156709. [O95831-4]
ENST00000440263; ENSP00000405879; ENSG00000156709. [O95831-5]
ENST00000535724; ENSP00000446113; ENSG00000156709. [O95831-6]
GeneIDi9131.
KEGGihsa:9131.
UCSCiuc004evg.3. human. [O95831-1]
uc004evh.3. human. [O95831-3]
uc004evi.3. human. [O95831-2]
uc004evk.3. human.
uc011mus.2. human. [O95831-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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. Translation: CAI42778.1 .
AL139234 Genomic DNA. Translation: CAI42779.1 .
AL139234 Genomic DNA. Translation: CAI42780.1 .
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 .
CCDSi CCDS14618.1. [O95831-1 ]
CCDS14619.1. [O95831-3 ]
CCDS48166.1. [O95831-5 ]
CCDS48167.1. [O95831-4 ]
RefSeqi NP_001124318.1. NM_001130846.2. [O95831-5 ]
NP_001124319.1. NM_001130847.3. [O95831-4 ]
NP_004199.1. NM_004208.3. [O95831-1 ]
NP_665811.1. NM_145812.2. [O95831-3 ]
NP_665812.1. NM_145813.2. [O95831-2 ]
UniGenei Hs.424932.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M6I X-ray 1.80 A 121-613 [» ]
4FDC X-ray 2.40 B 103-613 [» ]
4LII X-ray 1.88 A 100-611 [» ]
ProteinModelPortali O95831.
SMRi O95831. Positions 125-611.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114579. 58 interactions.
119252. 8 interactions.
IntActi O95831. 29 interactions.
MINTi MINT-209209.
STRINGi 9606.ENSP00000287295.

PTM databases

PhosphoSitei O95831.

2D gel databases

REPRODUCTION-2DPAGE IPI00157908.
UCD-2DPAGE O95831.

Proteomic databases

MaxQBi O95831.
PaxDbi O95831.
PRIDEi O95831.

Protocols and materials databases

DNASUi 51060.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000287295 ; ENSP00000287295 ; ENSG00000156709 . [O95831-1 ]
ENST00000319908 ; ENSP00000315122 ; ENSG00000156709 . [O95831-3 ]
ENST00000346424 ; ENSP00000316320 ; ENSG00000156709 . [O95831-2 ]
ENST00000416073 ; ENSP00000402535 ; ENSG00000156709 . [O95831-4 ]
ENST00000440263 ; ENSP00000405879 ; ENSG00000156709 . [O95831-5 ]
ENST00000535724 ; ENSP00000446113 ; ENSG00000156709 . [O95831-6 ]
GeneIDi 9131.
KEGGi hsa:9131.
UCSCi uc004evg.3. human. [O95831-1 ]
uc004evh.3. human. [O95831-3 ]
uc004evi.3. human. [O95831-2 ]
uc004evk.3. human.
uc011mus.2. human. [O95831-4 ]

Organism-specific databases

CTDi 9131.
GeneCardsi GC0XM129263.
HGNCi HGNC:8768. AIFM1.
HPAi CAB003764.
HPA030611.
MIMi 300169. gene.
300816. phenotype.
310490. phenotype.
neXtProti NX_O95831.
Orphaneti 238329. Severe X-linked mitochondrial encephalomyopathy.
101078. X-linked Charcot-Marie-Tooth disease type 4.
PharmGKBi PA162376129.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0446.
HOGENOMi HOG000124580.
HOVERGENi HBG053538.
InParanoidi O95831.
KOi K04727.
OMAi KDGEEHA.
OrthoDBi EOG7C2R0V.
PhylomeDBi O95831.
TreeFami TF314028.

Enzyme and pathway databases

SignaLinki O95831.

Miscellaneous databases

ChiTaRSi AIFM1. human.
EvolutionaryTracei O95831.
GeneWikii AIFM1.
GenomeRNAii 9131.
NextBioi 34229.
PROi O95831.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95831.
Bgeei O95831.
CleanExi HS_AIFM1.
Genevestigatori O95831.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
InterProi IPR029324. AIF_C.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
[Graphical view ]
Pfami PF14721. AIF_C. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF55424. SSF55424. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "AIFsh, a novel apoptosis-inducing factor (AIF) pro-apoptotic isoform with potential pathological relevance in human cancer."
    Delettre C., Yuste V.J., Moubarak R.S., Bras M., Lesbordes-Brion J.-C., Petres S., Bellalou J., Susin S.A.
    J. Biol. Chem. 281:6413-6427(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), PROTEIN SEQUENCE OF N-TERMINUS, SUBCELLULAR LOCATION (ISOFORM 5), TISSUE SPECIFICITY.
  3. "Identification and characterization of AIFsh2, a mitochondrial apoptosis-inducing factor (AIF) isoform with NADH oxidase activity."
    Delettre C., Yuste V.J., Moubarak R.S., Bras M., Robert N., Susin S.A.
    J. Biol. Chem. 281:18507-18518(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 6), ALTERNATIVE SPLICING.
  4. Rhodes S.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Kidney.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Brain.
  10. "Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space."
    Otera H., Ohsakaya S., Nagaura Z., Ishihara N., Mihara K.
    EMBO J. 24:1375-1386(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 55-59, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
  11. Mei G., Yu W., Gibbs R.A.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-613.
    Tissue: Brain.
  12. "Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis."
    Daugas E., Nochy D., Ravagnan L., Loeffler M., Susin S.A., Zamzami N., Kroemer G.
    FEBS Lett. 476:118-123(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  13. "Apoptosis-inducing factor (AIF) inhibits protein synthesis by interacting with the eukaryotic translation initiation factor 3 subunit p44 (eIF3g)."
    Kim J.T., Kim K.D., Song E.Y., Lee H.G., Kim J.W., Kim J.W., Chae S.K., Kim E., Lee M.S., Yang Y., Lim J.S.
    FEBS Lett. 580:6375-6383(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF3G.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Apoptosis-inducing factor is a target for ubiquitination through interaction with XIAP."
    Wilkinson J.C., Wilkinson A.S., Galban S., Csomos R.A., Duckett C.S.
    Mol. Cell. Biol. 28:237-247(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY XIAP/BIRC4, INTERACTION WITH XIAP/BIRC4.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Apoptosis-inducing factor plays a critical role in caspase-independent, pyknotic cell death in hydrogen peroxide-exposed cells."
    Son Y.O., Jang Y.S., Heo J.S., Chung W.T., Choi K.C., Lee J.C.
    Apoptosis 14:796-808(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. Cited for: ALTERNATIVE SPLICING (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 3), SUBUNIT.
  19. Cited for: INTERACTION WITH PRELID1.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Nondegradative ubiquitination of apoptosis inducing factor (AIF) by X-linked inhibitor of apoptosis at a residue critical for AIF-mediated chromatin degradation."
    Lewis E.M., Wilkinson A.S., Davis N.Y., Horita D.A., Wilkinson J.C.
    Biochemistry 50:11084-11096(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-255 BY XIAP/BIRC4.
  22. "DNA binding is required for the apoptogenic action of apoptosis inducing factor."
    Ye H., Cande C., Stephanou N.C., Jiang S., Gurbuxani S., Larochette N., Daugas E., Garrido C., Kroemer G., Wu H.
    Nat. Struct. Biol. 9:680-684(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 121-613 IN COMPLEX WITH FAD, SUBCELLULAR LOCATION, DNA-BINDING.
  23. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 103-613 IN COMPLEX WITH FAD, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, DNA-BINDING, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT COWCK VAL-493, CHARACTERIZATION OF VARIANT COWCK VAL-493.
  24. "Severe X-linked mitochondrial encephalomyopathy associated with a mutation in apoptosis-inducing factor."
    Ghezzi D., Sevrioukova I., Invernizzi F., Lamperti C., Mora M., D'Adamo P., Novara F., Zuffardi O., Uziel G., Zeviani M.
    Am. J. Hum. Genet. 86:639-649(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT COXPD6 ARG-201 DEL, CHARACTERIZATION OF VARIANT COXPD6 ARG-201 DEL, FUNCTION.
  25. "Early prenatal ventriculomegaly due to an AIFM1 mutation identified by linkage analysis and whole exome sequencing."
    Berger I., Ben-Neriah Z., Dor-Wolman T., Shaag A., Saada A., Zenvirt S., Raas-Rothschild A., Nadjari M., Kaestner K.H., Elpeleg O.
    Mol. Genet. Metab. 104:517-520(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT COXPD6 GLU-308.

Entry informationi

Entry nameiAIFM1_HUMAN
AccessioniPrimary (citable) accession number: O95831
Secondary accession number(s): A4QPB4
, B1ALN1, B2RB08, D3DTE9, Q1L6K4, Q1L6K6, Q2QKE4, Q5JUZ7, Q6I9X6, Q9Y3I3, Q9Y3I4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi