Reviewed, UniProtKB/Swiss-Prot O95831 (AIFM1_HUMAN)

Names and origin

Protein names

Recommended name:
    Apoptosis-inducing factor 1, mitochondrial
    EC=1.-.-.-
Alternative name(s):
    Programmed cell death protein 8

Gene names

Name:	AIFM1
Synonyms:	AIF, PDCD8

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	613 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probable oxidoreductase that acts as a caspase-independent mitochondrial effector of apoptotic cell death. Extramitochondrial AIF induces nuclear chromatin condensation and large scale DNA fragmentation (in vitro). Binds to DNA in a sequence-independent manner.
Cofactor	FAD.
Subunit structure	Interacts with XIAP. Ref.10
Subcellular location	Mitochondrion intermembrane space. Nucleus. Note: Translocated to the nucleus upon induction of apoptosis. Ref.13
Sequence similarities	Belongs to the FAD-dependent oxidoreductase family.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	DNA-binding FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction resulting in induction of apoptosis Ref.1 Traceable author statement. Source: ProtInc DNA fragmentation involved in apoptosis Ref.1 Traceable author statement. Source: ProtInc cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial intermembrane space Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Ref.1 Traceable author statement. Source: ProtInc
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Ref.1 Traceable author statement. Source: ProtInc oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRF2	Q9HAW0	1	EBI-356440,EBI-1055224
C20orf24	Q9BUV8	1	EBI-356440,EBI-1050079
MLF2	Q15773	1	EBI-356440,EBI-1051875
PELO	Q9BRX2	1	EBI-356440,EBI-1043580
PTP4A3	O75365	1	EBI-356440,EBI-1043866
TSC22D4	Q9Y3Q8	1	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 102

102

Mitochondrion By similarity

Chain

103 – 613

511

Apoptosis-inducing factor 1, mitochondrial

PRO_0000022030

Regions

Nucleotide binding

138 – 142

5

FAD By similarity

Nucleotide binding

164 – 165

2

FAD By similarity

Nucleotide binding

454 – 455

2

FAD By similarity

Region

134 – 483

350

FAD-dependent oxidoreductase By similarity

Motif

446 – 451

6

Nuclear localization signal Potential

Sites

Binding site

172

1

FAD By similarity

Binding site

177

1

FAD By similarity

Binding site

233

1

FAD; via amide nitrogen and carbonyl oxygen By similarity

Binding site

285

1

FAD By similarity

Binding site

438

1

FAD By similarity

Binding site

483

1

FAD; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue

105

1

Phosphothreonine Ref.9

Modified residue

268

1

Phosphoserine Ref.9 Ref.11

Modified residue

593

1

N6-acetyllysine By similarity

Natural variations

Alternative sequence

36 – 322

287

Missing in isoform 2.

VSP_004357

Alternative sequence

36 – 82

47

GNLFQ…VGAGA → VVQSHHLGSPSRSLASTGAS GKDGSNLVYFLIVGATVTGA GVY in isoform 3.

VSP_022953

Secondary structure

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613

Helix Strand Turn

Details...

Beta strand

130 – 138

9

Helix

141 – 153

13

Beta strand

158 – 167

10

Helix

173 – 176

4

Helix

178 – 180

3

Helix

187 – 190

4

Beta strand

192 – 194

3

Beta strand

200 – 206

7

Helix

208 – 210

3

Turn

214 – 219

6

Beta strand

224 – 229

6

Beta strand

233 – 237

5

Turn

238 – 241

4

Beta strand

242 – 245

4

Beta strand

250 – 258

9

Beta strand

262 – 264

3

Helix

268 – 271

4

Helix

275 – 279

5

Beta strand

281 – 283

3

Helix

287 – 299

13

Beta strand

301 – 306

6

Helix

310 – 326

17

Beta strand

329 – 333

5

Beta strand

335 – 338

4

Turn

339 – 343

5

Helix

346 – 357

12

Turn

358 – 360

3

Beta strand

362 – 364

3

Beta strand

369 – 375

7

Beta strand

378 – 383

6

Beta strand

388 – 396

9

Beta strand

400 – 402

3

Helix

407 – 410

4

Turn

416 – 418

3

Beta strand

420 – 422

3

Beta strand

428 – 430

3

Beta strand

433 – 435

3

Helix

437 – 439

3

Beta strand

440 – 444

5

Turn

445 – 447

3

Beta strand

448 – 450

3

Helix

455 – 469

15

Beta strand

481 – 487

7

Beta strand

491 – 496

6

Beta strand

504 – 509

6

Helix

517 – 524

8

Helix

529 – 532

4

Beta strand

562 – 569

8

Beta strand

572 – 580

9

Helix

585 – 594

10

Helix

604 – 607

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: A156762BC64E6340	FASTA	613	66,901
	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
	Isoform 2. Checksum: A87ACDC0A0556040	FASTA	326	35,638
	10 20 30 40 50 60 MFRCGGLAAG ALKQKLVPLV RTVCVRSPRQ RNRLPARALG TEVIQLFPEK GNMGKILPEY 70 80 90 100 110 120 LSNWTMEKVR REGVKVMPNA IVQSVGVSSG KLLIKLKDGR KVETDHIVAA VGLEPNVELA 130 140 150 160 170 180 KTGGLEIDSD FGGFRVNAEL QARSNIWVAG DAACFYDIKL GRRRVEHHDH AVVSGRLAGE 190 200 210 220 230 240 NMTGAAKPYW HQSMFWSDLG PDVGYEAIGL VDSSLPTVGV FAKATAQDNP KSATEQSGTG 250 260 270 280 290 300 IRSESETESE ASEITIPPST PAVPQAPVQG EDYGKGVIFY LRDKVVVGIV LWNIFNRMPI 310 320 ARKIIKDGEQ HEDLNEVAKL FNIHED
	Isoform 3. Checksum: 313ADD6FA4E5D61A	FASTA	609	66,295
	10 20 30 40 50 60 MFRCGGLAAG ALKQKLVPLV RTVCVRSPRQ RNRLPVVQSH HLGSPSRSLA STGASGKDGS 70 80 90 100 110 120 NLVYFLIVGA TVTGAGVYYA YKTMKEDEKR YNERISGLGL TPEQKQKKAA LSASEGEEVP 130 140 150 160 170 180 QDKAPSHVPF LLIGGGTAAF AAARSIRARD PGARVLIVSE DPELPYMRPP LSKELWFSDD 190 200 210 220 230 240 PNVTKTLRFK QWNGKERSIY FQPPSFYVSA QDLPHIENGG VAVLTGKKVV QLDVRDNMVK 250 260 270 280 290 300 LNDGSQITYE KCLIATGGTP RSLSAIDRAG AEVKSRTTLF RKIGDFRSLE KISREVKSIT 310 320 330 340 350 360 IIGGGFLGSE LACALGRKAR ALGTEVIQLF PEKGNMGKIL PEYLSNWTME KVRREGVKVM 370 380 390 400 410 420 PNAIVQSVGV SSGKLLIKLK DGRKVETDHI VAAVGLEPNV ELAKTGGLEI DSDFGGFRVN 430 440 450 460 470 480 AELQARSNIW VAGDAACFYD IKLGRRRVEH HDHAVVSGRL AGENMTGAAK PYWHQSMFWS 490 500 510 520 530 540 DLGPDVGYEA IGLVDSSLPT VGVFAKATAQ DNPKSATEQS GTGIRSESET ESEASEITIP 550 560 570 580 590 600 PSTPAVPQAP VQGEDYGKGV IFYLRDKVVV GIVLWNIFNR MPIARKIIKD GEQHEDLNEV AKLFNIHED

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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] (ISOFORM 3). Tissue: Brain.
[7]	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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBLGenBankDDBJ

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: CAI42780.1.
BC111065 mRNA. Translation: AAI11066.1.
AF131759 mRNA. Translation: AAD20036.1.

IPI

IPI00000690.
IPI00157908.
IPI00300018.

RefSeq

NP_004199.1.
NP_665811.1.
NP_665812.1.

UniGene

Hs.424932

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1M6I	X-ray	1.80	A	121-613	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O95831. 21 interactions.

PTM databases

PhosphoSite

O95831.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00157908.

Proteomic databases

PRIDE

O95831.

Genome annotation databases

Ensembl

ENSG00000156709. Homo sapiens. [Contig view]

GeneID

9131.

Organism-specific databases

GeneCards

GC0XM129092.

HGNC

HGNC:8768. AIFM1.

HPA

CAB003764.

MIM

300169. gene.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O95831.

OMA

O95831. VTETLRF.

Enzyme and pathway databases

Pathway_Interaction_DB

ceramidepathway. Ceramide signaling pathway.

Gene expression databases

ArrayExpress

O95831.

Bgee

O95831.

CleanEx

HS_AIFM1.

GermOnline

ENSG00000156709. Homo sapiens.

Family and domain databases

InterPro

IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]

Gene3D

G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.

Pfam

PF00070. Pyr_redox. 2 hits.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.

ProDom

PD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Other Resources

NextBio

34229.

SOURCE

Search...

Entry information

Entry name

AIFM1_HUMAN

Accession

Primary (citable) accession number: O95831
Secondary accession number(s): B2RB08 , Q5JUZ7, Q6I9X6, Q9Y3I3, Q9Y3I4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)