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UniProtKB/Swiss-Prot entry O95831


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AIFM1_HUMAN
Primary accession number O95831
Secondary accession numbers B2RB08 Q5JUZ7 Q6I9X6 Q9Y3I3 Q9Y3I4
Integrated into Swiss-Prot on April 27, 2001
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 94)
Name and origin of the protein
Protein name Apoptosis-inducing factor 1, mitochondrial [Precursor]
Synonyms EC 1.-.-.-
Programmed cell death protein 8
Gene name
Name: AIFM1
Synonyms: AIF, PDCD8
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1038/17135; PubMed=9989411 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Molecular characterization of mitochondrial apoptosis-inducing factor.";
Nature 397:441-446(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
Rhodes S.;
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Kidney;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-613.
TISSUE=Brain;
Mei G., Yu W., Gibbs R.A.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[8]
REVIEW.
DOI=10.1016/S0014-5793(00)01731-2; PubMed=10913597 [NCBI, ExPASy, EBI, Israel, Japan]
Daugas E., Nochy D., Ravagnan L., Loeffler M., Susin S.A., Zamzami N., Kroemer G.;
"Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis.";
FEBS Lett. 476:118-123(2000).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-105 AND SER-268, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
INTERACTION WITH XIAP.
DOI=10.1128/MCB.01065-07; PubMed=17967870 [NCBI, ExPASy, EBI, Israel, Japan]
Wilkinson J.C., Wilkinson A.S., Galban S., Csomos R.A., Duckett C.S.;
"Apoptosis-inducing factor is a target for ubiquitination through interaction with XIAP.";
Mol. Cell. Biol. 28:237-247(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[13]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 121-613 IN COMPLEX WITH FAD, SUBCELLULAR LOCATION, AND DNA-BINDING.
DOI=10.1038/nsb836; PubMed=12198487 [NCBI, ExPASy, EBI, Israel, Japan]
Ye H., Cande C., Stephanou N.C., Jiang S., Gurbuxani S., Larochette N., Daugas E., Garrido C., Kroemer G., Wu H.;
"DNA binding is required for the apoptogenic action of apoptosis inducing factor.";
Nat. Struct. Biol. 9:680-684(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF100928; AAD16436.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049703; CAB41267.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049704; CAB41268.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK314446; BAG37055.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR457379; CAG33660.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139234; CAI42778.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139234; CAI42780.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC111065; AAI11066.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF131759; AAD20036.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00000690; -.
IPI00157908; -.
IPI00300018; -.
RefSeq NP_004199.1; -.
NP_665811.1; -.
NP_665812.1; -.
UniGene Hs.424932
3D structure databases
PDB
1M6I; X-ray; 1.80 A; A=121-613.[ExPASy / RCSB / EBI]
PDBsum 1M6I; -.
ModBase O95831.
Protein-protein interaction databases
IntAct O95831; 21.
PTM databases
PhosphoSite O95831; -.
Enzyme and pathway databases
Pathway_Interaction_DB ceramidepathway; Ceramide signaling pathway.
2D gel databases
REPRODUCTION-2DPAGE IPI00157908; -.
Organism-specific databases
GeneCards GC0XM129092; -.
HGNC HGNC:8768; AIFM1.
GenAtlas AIFM1.
HPA CAB003764; -.
MIM 300169; gene. [NCBI / EBI]
Gene expression databases
ArrayExpress O95831; -.
Bgee O95831; -.
CleanEx HS_AIFM1; -.
GermOnline ENSG00000156709; Homo sapiens.
Ontologies
GO
GO:0005758; Cellular component: mitochondrial intermembrane space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634; Cellular component: nucleus (traceable author statement from ProtInc).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055; Molecular function: electron carrier activity (traceable author statement from ProtInc).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0016491; Molecular function: oxidoreductase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0008630; Biological process: DNA damage response, signal transduction resulting in induction of apoptosis (traceable author statement from ProtInc).
GO:0006309; Biological process: DNA fragmentation involved in apoptosis (traceable author statement from ProtInc).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
Pfam PF00070; Pyr_redox; 2.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
Proteomic databases
PRIDE O95831; -.
Genome annotation databases
Ensembl ENSG00000156709; Homo sapiens. [Contig view]
GeneID 9131; -.
Phylogenomic databases
HOVERGEN O95831; -.
OMA O95831; VTETLRF.
Other
NextBio 34229; -.
SOURCE AIFM1; Homo sapiens.
ProtoNet O95831.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Alternative splicing; Apoptosis; DNA-binding; FAD; Flavoprotein; Mitochondrion; Nucleus; Oxidoreductase; Phosphoprotein; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1   102  102     Mitochondrion (By similarity). 
CHAIN   103   613  511     Apoptosis-inducing factor 1, mitochondrial. PRO_0000022030
NP_BIND   138   142  5     FAD (By similarity). 
NP_BIND   164   165  2     FAD (By similarity). 
NP_BIND   454   455  2     FAD (By similarity). 
REGION   134   483  350     FAD-dependent oxidoreductase (By similarity). 
MOTIF   446   451  6     Nuclear localization signal (Potential). 
BINDING   172   172        FAD (By similarity). 
BINDING   177   177        FAD (By similarity). 
BINDING   233   233        FAD; via amide nitrogen and carbonyl oxygen (By similarity). 
BINDING   285   285        FAD (By similarity). 
BINDING   438   438        FAD (By similarity). 
BINDING   483   483        FAD; via carbonyl oxygen (By similarity). 
MOD_RES   105   105        Phosphothreonine. 
MOD_RES   268   268        Phosphoserine. 
MOD_RES   593   593        N6-acetyllysine (By similarity). 
VAR_SEQ   36   322        Missing (in isoform 2). VSP_004357
VAR_SEQ   36    82        GNLFQRWHVPLELQMTRQMASSGASGGKIDNSVLVLIVGL STVGAGA -> VVQSHHLGSPSRSLASTGASGKDGSNLVYFLIVGATVT GAGVY (in isoform 3). VSP_022953
STRAND   130   138  9      
HELIX   141   153  13      
STRAND   158   167  10      
HELIX   173   176  4      
HELIX   178   180  3      
HELIX   187   190  4      
STRAND   192   194  3      
STRAND   200   206  7      
HELIX   208   210  3      
TURN   214   219  6      
STRAND   224   229  6      
STRAND   233   237  5      
TURN   238   241  4      
STRAND   242   245  4      
STRAND   250   258  9      
STRAND   262   264  3      
HELIX   268   271  4      
HELIX   275   279  5      
STRAND   281   283  3      
HELIX   287   299  13      
STRAND   301   306  6      
HELIX   310   326  17      
STRAND   329   333  5      
STRAND   335   338  4      
TURN   339   343  5      
HELIX   346   357  12      
TURN   358   360  3      
STRAND   362   364  3      
STRAND   369   375  7      
STRAND   378   383  6      
STRAND   388   396  9      
STRAND   400   402  3      
HELIX   407   410  4      
TURN   416   418  3      
STRAND   420   422  3      
STRAND   428   430  3      
STRAND   433   435  3      
HELIX   437   439  3      
STRAND   440   444  5      
TURN   445   447  3      
STRAND   448   450  3      
HELIX   455   469  15      
STRAND   481   487  7      
STRAND   491   496  6      
STRAND   504   509  6      
HELIX   517   524  8      
HELIX   529   532  4      
STRAND   562   569  8      
STRAND   572   580  9      
HELIX   585   594  10      
HELIX   604   607  4      
Sequence information
Length: 613 AA [This is the length of the unprocessed precursor] Molecular weight: 66901 Da [This is the MW of the unprocessed precursor] CRC64: A156762BC64E6340 [This is a checksum on the sequence]
        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 

O95831 in FASTA format

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