Skip Header

Contribute Send feedback
Read comments (?) or add your own

O95831 (AIFM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apoptosis-inducing factor 1, mitochondrial
EC=1.-.-.-
Alternative name(s):
Programmed cell death protein 8
Gene names
Name:AIFM1
Synonyms:AIF, PDCD8
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length613 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable oxidoreductase that has a dual role in controlling cellular life and death; during apoptosis, it is translocated from the mitochondria to the nucleus to function as a proapoptotic factor in a caspase-independent pathway, while in normal mitochondria, it functions as an antiapoptotic factor via its 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. Ref.11 Ref.15 Ref.19

Cofactor

FAD.

Subunit structure

Interacts with XIAP. Interacts (via N-terminus) with EIF3G (via C-terminus). Ref.11 Ref.13

Subcellular location

Mitochondrion intermembrane space. Mitochondrion inner membrane. Cytoplasm. Nucleus. Cytoplasm › perinuclear 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. Ref.8 Ref.11 Ref.18

Post-translational modification

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.

Involvement in disease

Defects in AIFM1 are the cause of combined oxidative phosphorylation deficiency type 6 (COXPD6) [MIM:300816]. It is a mitochondrial disease resulting in a neurodegenerative disorder characterized by psychomotor delay, hypotonia, areflexia, muscle weakness and wasting. Ref.19

Sequence similarities

Belongs to the FAD-dependent oxidoreductase family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Membrane
Mitochondrion
Mitochondrion inner membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainTransit peptide
   LigandDNA-binding
FAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processDNA fragmentation involved in apoptotic nuclear change

Traceable author statement. Source: ProtInc

activation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay Ref.11. Source: UniProtKB

apoptosis in response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial intermembrane space

Inferred from direct assay Ref.8. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

electron carrier activity

Traceable author statement. Source: ProtInc

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TSC22D4Q9Y3Q82EBI-356440,EBI-739485

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95831-1)

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.
Isoform 2 (identifier: O95831-2)

The sequence of this isoform differs from the canonical sequence as follows:
     36-322: Missing.
Isoform 3 (identifier: O95831-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5454Mitochondrion Ref.8
Propeptide55 – 10147Removed in mature form
PRO_0000401935
Chain102 – 613512Apoptosis-inducing factor 1, mitochondrial
PRO_0000022030

Regions

Nucleotide binding138 – 1425FAD
Nucleotide binding164 – 1652FAD
Nucleotide binding454 – 4552FAD
Region134 – 483350FAD-dependent oxidoreductase By similarity
Motif446 – 4516Nuclear localization signal Potential

Sites

Binding site1721FAD
Binding site1771FAD
Binding site2331FAD; via amide nitrogen and carbonyl oxygen
Binding site2851FAD
Binding site4381FAD
Binding site4831FAD; via carbonyl oxygen

Amino acid modifications

Modified residue1051Phosphothreonine Ref.12
Modified residue2681Phosphoserine Ref.12 Ref.14
Modified residue2951N6-acetyllysine Ref.16
Modified residue5931N6-acetyllysine By similarity

Natural variations

Alternative sequence36 – 322287Missing in isoform 2.
VSP_004357
Alternative sequence36 – 8247GNLFQ…VGAGA → VVQSHHLGSPSRSLASTGAS GKDGSNLVYFLIVGATVTGA GVY in isoform 3.
VSP_022953
Natural variant2011Missing in COXPD6; higher DNA binding affinity, partially impaired flavin binding and association with increased parthanatos-linked cell death.
VAR_063827

Secondary structure

1 ................................................................................................ 613
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: A156762BC64E6340

FASTA61366,901
        10         20         30         40         50         60 
MFRCGGLAAG ALKQKLVPLV RTVCVRSPRQ RNRLPGNLFQ RWHVPLELQM TRQMASSGAS 

        70         80         90        100        110        120 
GGKIDNSVLV LIVGLSTVGA GAYAYKTMKE DEKRYNERIS GLGLTPEQKQ KKAALSASEG 

       130        140        150        160        170        180 
EEVPQDKAPS HVPFLLIGGG TAAFAAARSI RARDPGARVL IVSEDPELPY MRPPLSKELW 

       190        200        210        220        230        240 
FSDDPNVTKT LRFKQWNGKE RSIYFQPPSF YVSAQDLPHI ENGGVAVLTG KKVVQLDVRD 

       250        260        270        280        290        300 
NMVKLNDGSQ ITYEKCLIAT GGTPRSLSAI DRAGAEVKSR TTLFRKIGDF RSLEKISREV 

       310        320        330        340        350        360 
KSITIIGGGF LGSELACALG RKARALGTEV IQLFPEKGNM GKILPEYLSN WTMEKVRREG 

       370        380        390        400        410        420 
VKVMPNAIVQ SVGVSSGKLL IKLKDGRKVE TDHIVAAVGL EPNVELAKTG GLEIDSDFGG 

       430        440        450        460        470        480 
FRVNAELQAR SNIWVAGDAA CFYDIKLGRR RVEHHDHAVV SGRLAGENMT GAAKPYWHQS 

       490        500        510        520        530        540 
MFWSDLGPDV GYEAIGLVDS SLPTVGVFAK ATAQDNPKSA TEQSGTGIRS ESETESEASE 

       550        560        570        580        590        600 
ITIPPSTPAV PQAPVQGEDY GKGVIFYLRD KVVVGIVLWN IFNRMPIARK IIKDGEQHED 

       610 
LNEVAKLFNI HED

« Hide

Isoform 2 [UniParc].

Checksum: A87ACDC0A0556040
Show »

FASTA32635,638
Isoform 3 [UniParc].

Checksum: 313ADD6FA4E5D61A
Show »

FASTA60966,295

References

« Hide 'large scale' references
[1]"Molecular characterization of mitochondrial apoptosis-inducing factor."
Susin S.A., Lorenzo H.K., Zamzami N., Marzo I., Snow B.E., Brothers G.M., Mangion J., Jacotot E., Costantini P., Loeffler M., Larochette N., Goodlett D.R., Aebersold R., Siderovski D.P., Penninger J.M., Kroemer G.
Nature 397:441-446(1999) [PubMed: 9989411] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]Rhodes S.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
[3]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Kidney.
[4]"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).
[5]"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. expand/collapse author list , 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: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Brain.
[8]"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: 15775970] [Abstract]
Cited for: PROTEIN SEQUENCE OF 55-59, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
[9]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.
[10]"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: 10913597] [Abstract]
Cited for: REVIEW.
[11]"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: 17094969] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF3G.
[12]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-105 AND SER-268, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[13]"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: 17967870] [Abstract]
Cited for: INTERACTION WITH XIAP.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"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: 19418225] [Abstract]
Cited for: FUNCTION.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-295, MASS SPECTROMETRY.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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: 12198487] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 121-613 IN COMPLEX WITH FAD, SUBCELLULAR LOCATION, DNA-BINDING.
[19]"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: 20362274] [Abstract]
Cited for: VARIANT COXPD6 ARG-201 DEL, CHARACTERIZATION OF VARIANT COXPD6 ARG-201 DEL, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF100928 mRNA. Translation: AAD16436.1.
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.
IPIIPI00000690.
IPI00157908.
IPI00300018.
RefSeqNP_001124318.1. NM_001130846.2.
NP_001124319.1. NM_001130847.3.
NP_004199.1. NM_004208.3.
NP_056997.1. NM_015913.2.
NP_665811.1. NM_145812.2.
NP_665812.1. NM_145813.2.
UniGeneHs.424932.
Hs.476033.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M6IX-ray1.80A121-613[»]
ProteinModelPortalO95831.
SMRO95831. Positions 128-608.
ModBaseSearch...

Protein-protein interaction databases

IntActO95831. 17 interactions.
MINTMINT-209209.
STRINGO95831.

PTM databases

PhosphoSiteO95831.

2D gel databases

REPRODUCTION-2DPAGEIPI00157908.
UCD-2DPAGEO95831.

Proteomic databases

PRIDEO95831.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287295; ENSP00000287295; ENSG00000156709.
GeneID51060.
9131.
KEGGhsa:51060.
hsa:9131.
UCSCuc004evg.1. human.
uc004evh.1. human.

Organism-specific databases

CTD51060.
9131.
GeneCardsGC0XM129263.
HGNCHGNC:8768. AIFM1.
HPACAB003764.
MIM300169. gene.
300816. phenotype.
neXtProtNX_O95831.
Orphanet238329. Severe X-linked mitochondrial encephalomyopathy.
PharmGKBPA162376129.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12733.
HOGENOMHBG644911.
HOVERGENHBG053538.
InParanoidO95831.
OMAKIGDFRT.
OrthoDBEOG40S0FD.
PhylomeDBO95831.

Enzyme and pathway databases

Pathway_Interaction_DBceramidepathway. Ceramide signaling pathway.

Gene expression databases

ArrayExpressO95831.
BgeeO95831.
CleanExHS_AIFM1.
GenevestigatorO95831.
GermOnlineENSG00000156709. Homo sapiens.

Family and domain databases

InterProIPR016156. 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]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KOK04727.
K05360.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
ProtoNetSearch...

Other

NextBio34229.
SOURCESearch...

Entry information

Entry nameAIFM1_HUMAN
AccessionPrimary (citable) accession number: O95831
Secondary accession number(s): A4QPB4 expand/collapse secondary AC list , B1ALN1, B2RB08, D3DTE9, Q5JUZ7, Q6I9X6, Q9Y3I3, Q9Y3I4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents