CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024073
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Apoptosis-inducing factor 1, mitochondrial 
Protein Synonyms/Alias
 Programmed cell death protein 8 
Gene Name
 Aifm1 
Gene Synonyms/Alias
 Aif; Pdcd8 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
108LGLSPEEKQRRAIASubiquitination[1]
188SDDPNVTKTLQFRQWubiquitination[1]
243DVRGNMVKLNDGSQIacetylation[2]
381SGGRLLIKLKDGRKVacetylation[2]
445AACFYDIKLGRRRVEacetylation[2]
517ATAQDNPKSATEQSGubiquitination[1]
592PIARKIIKDGEQHEDacetylation[2, 3]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647
Functional Description
 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 (By similarity). 
Sequence Annotation
 NP_BIND 137 141 FAD.
 NP_BIND 163 164 FAD.
 NP_BIND 453 454 FAD.
 REGION 133 482 FAD-dependent oxidoreductase.
 MOTIF 445 450 Nuclear localization signal (Potential).
 BINDING 171 171 FAD.
 BINDING 176 176 FAD.
 BINDING 232 232 FAD; via amide nitrogen and carbonyl
 BINDING 284 284 FAD.
 BINDING 437 437 FAD.
 BINDING 482 482 FAD; via carbonyl oxygen.
 MOD_RES 267 267 Phosphoserine (By similarity).
 MOD_RES 592 592 N6-acetyllysine.
 CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Apoptosis; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; FAD; Flavoprotein; Isopeptide bond; Membrane; Mitochondrion; Mitochondrion inner membrane; NAD; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 612 AA 
Protein Sequence
MFRCGGLAGA FKQKLVPLVR TVYVQRPKQR NRLPGNLFQQ WRVPLELQMA RQMASSGSSG 60
GKMDNSVLVL IVGLSTIGAG AYAYKTIKED QKRYNERVMG LGLSPEEKQR RAIASATEGG 120
SVPQIRAPSH VPFLLIGGGT AAFAAARSIR ARDPGARVLI VSEDPELPYM RPPLSKELWF 180
SDDPNVTKTL QFRQWNGKER SIYFQPPSFY VSAQDLPNIE NGGVAVLTGK KVVHLDVRGN 240
MVKLNDGSQI TFEKCLIATG GTPRSLSAID RAGAEVKSRT TLFRKIGDFR ALEKISREVK 300
SITVIGGGFL GSELACALGR KSQASGIEVI QLFPEKGNMG KILPQYLSNW TMEKVKREGV 360
KVMPNAIVQS VGVSGGRLLI KLKDGRKVET DHIVTAVGLE PNVELAKTGG LEIDSDFGGF 420
RVNAELQARS NIWVAGDAAC FYDIKLGRRR VEHHDHAVVS GRLAGENMTG AAKPYWHQSM 480
FWSDLGPDVG YEAIGLVDSS LPTVGVFAKA TAQDNPKSAT EQSGTGIRSE SETESEASEI 540
TIPPSAPAVP QVPVEGEDYG KGVIFYLRDK VVVGIVLWNV FNRMPIARKI IKDGEQHEDL 600
NEVAKLFNIH ED 612 
Gene Ontology
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
 GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
 GO:0005741; C:mitochondrial outer membrane; TAS:MGI.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; TAS:MGI.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
 GO:0006309; P:apoptotic DNA fragmentation; IGI:MGI.
 GO:0008637; P:apoptotic mitochondrial changes; TAS:MGI.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB.
 GO:0032981; P:mitochondrial respiratory chain complex I assembly; IEA:Compara.
 GO:0051402; P:neuron apoptotic process; IGI:MGI.
 GO:0030182; P:neuron differentiation; IEA:Compara. 
Interpro
 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. 
Pfam
 PF00070; Pyr_redox
 PF07992; Pyr_redox_2 
SMART
  
PROSITE
  
PRINTS
 PR00368; FADPNR.