AIFM1_MOUSE - dbPTM
AIFM1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AIFM1_MOUSE
UniProt AC Q9Z0X1
Protein Name Apoptosis-inducing factor 1, mitochondrial
Gene Name Aifm1
Organism Mus musculus (Mouse).
Sequence Length 612
Subcellular Localization Mitochondrion intermembrane space . Mitochondrion inner membrane. Cytoplasm. Cytoplasm, perinuclear region. Nucleus . Proteolytic cleavage during or just after translocation into the mitochondrial intermembrane space (IMS) results in the formation of
Protein 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)..
Protein Sequence MFRCGGLAGAFKQKLVPLVRTVYVQRPKQRNRLPGNLFQQWRVPLELQMARQMASSGSSGGKMDNSVLVLIVGLSTIGAGAYAYKTIKEDQKRYNERVMGLGLSPEEKQRRAIASATEGGSVPQIRAPSHVPFLLIGGGTAAFAAARSIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTKTLQFRQWNGKERSIYFQPPSFYVSAQDLPNIENGGVAVLTGKKVVHLDVRGNMVKLNDGSQITFEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFRKIGDFRALEKISREVKSITVIGGGFLGSELACALGRKSQASGIEVIQLFPEKGNMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVGVSGGRLLIKLKDGRKVETDHIVTAVGLEPNVELAKTGGLEIDSDFGGFRVNAELQARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIPPSAPAVPQVPVEGEDYGKGVIFYLRDKVVVGIVLWNVFNRMPIARKIIKDGEQHEDLNEVAKLFNIHED
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
104PhosphorylationRVMGLGLSPEEKQRR
HHCCCCCCHHHHHHH		28.5929514104
108UbiquitinationLGLSPEEKQRRAIAS
CCCCHHHHHHHHHHH		47.66-
108AcetylationLGLSPEEKQRRAIAS
CCCCHHHHHHHHHHH		47.6623806337
108SuccinylationLGLSPEEKQRRAIAS
CCCCHHHHHHHHHHH		47.6623806337
108MalonylationLGLSPEEKQRRAIAS
CCCCHHHHHHHHHHH		47.6626320211
108SuccinylationLGLSPEEKQRRAIAS
CCCCHHHHHHHHHHH		47.66-
115PhosphorylationKQRRAIASATEGGSV
HHHHHHHHHCCCCCC		29.6125521595
117PhosphorylationRRAIASATEGGSVPQ
HHHHHHHCCCCCCCC		32.4429472430
121PhosphorylationASATEGGSVPQIRAP
HHHCCCCCCCCCCCC		41.2922324799
129PhosphorylationVPQIRAPSHVPFLLI
CCCCCCCCCCCEEEE		35.8123140645
188UbiquitinationSDDPNVTKTLQFRQW
CCCCCCCEEEEEEEC		42.85-
198SuccinylationQFRQWNGKERSIYFQ
EEEECCCCCCEEEEC		46.9023954790
230SuccinylationGVAVLTGKKVVHLDV
EEEEEECCEEEEEEC		36.8423954790
230AcetylationGVAVLTGKKVVHLDV
EEEEEECCEEEEEEC		36.842374687
231AcetylationVAVLTGKKVVHLDVR
EEEEECCEEEEEECC		51.322395425
243AcetylationDVRGNMVKLNDGSQI
ECCCCEEECCCCCEE		30.7023864654
243MalonylationDVRGNMVKLNDGSQI
ECCCCEEECCCCCEE		30.7026320211
248PhosphorylationMVKLNDGSQITFEKC
EEECCCCCEEEEEEE		22.6725159016
255S-nitrosylationSQITFEKCLIATGGT
CEEEEEEEEEECCCC		2.3322178444
255S-nitrosocysteineSQITFEKCLIATGGT
CEEEEEEEEEECCCC		2.33-
265PhosphorylationATGGTPRSLSAIDRA
ECCCCCCCHHHHHHC		28.0726745281
267PhosphorylationGGTPRSLSAIDRAGA
CCCCCCHHHHHHCCC		25.1522942356
277AcetylationDRAGAEVKSRTTLFR
HHCCCCHHCCHHHHH		26.2323864654
278PhosphorylationRAGAEVKSRTTLFRK
HCCCCHHCCHHHHHH		39.7826060331
294MalonylationGDFRALEKISREVKS
CCHHHHHHHCHHCCE		47.0026073543
301PhosphorylationKISREVKSITVIGGG
HHCHHCCEEEEECCC		28.7725777480
303PhosphorylationSREVKSITVIGGGFL
CHHCCEEEEECCCHH		17.1125777480
312PhosphorylationIGGGFLGSELACALG
ECCCHHHHHHHHHHC		31.4225777480
316S-nitrosylationFLGSELACALGRKSQ
HHHHHHHHHHCCCHH		5.1321278135
316GlutathionylationFLGSELACALGRKSQ
HHHHHHHHHHCCCHH		5.1324333276
316S-nitrosocysteineFLGSELACALGRKSQ
HHHHHHHHHHCCCHH		5.13-
336MalonylationVIQLFPEKGNMGKIL
EEECCCCCCCHHHCH		56.6826320211
336AcetylationVIQLFPEKGNMGKIL
EEECCCCCCCHHHCH		56.6823864654
341AcetylationPEKGNMGKILPQYLS
CCCCCHHHCHHHHHH		30.2423864654
361AcetylationKVKREGVKVMPNAIV
HHHHCCCEECCCEEE		43.6123864654
370PhosphorylationMPNAIVQSVGVSGGR
CCCEEEEEECEECCE		15.2229472430
374PhosphorylationIVQSVGVSGGRLLIK
EEEEECEECCEEEEE		29.6029472430
381AcetylationSGGRLLIKLKDGRKV
ECCEEEEEECCCCEE		49.8323864654
387AcetylationIKLKDGRKVETDHIV
EEECCCCEEECCEEE		50.3723576753
387MalonylationIKLKDGRKVETDHIV
EEECCCCEEECCEEE		50.3726320211
407AcetylationEPNVELAKTGGLEID
CCCCEEHHHCCEEEC		61.4023864654
408PhosphorylationPNVELAKTGGLEIDS
CCCEEHHHCCEEECC		30.7629472430
415PhosphorylationTGGLEIDSDFGGFRV
HCCEEECCCCCCEEE		40.2719060867
440S-nitrosocysteineWVAGDAACFYDIKLG
EEEECCEEEEECEEC		3.30-
440S-nitrosylationWVAGDAACFYDIKLG
EEEECCEEEEECEEC		3.3021278135
445AcetylationAACFYDIKLGRRRVE
CEEEEECEECCCCCC		41.8323201123
499PhosphorylationEAIGLVDSSLPTVGV
HHHHCCCCCCCCCEE		26.71-
500PhosphorylationAIGLVDSSLPTVGVF
HHHCCCCCCCCCEEE		33.63-
503PhosphorylationLVDSSLPTVGVFAKA
CCCCCCCCCEEEEEE		34.87-
517MalonylationATAQDNPKSATEQSG
EECCCCCCCHHHCCC		60.0026320211
517UbiquitinationATAQDNPKSATEQSG
EECCCCCCCHHHCCC		60.00-
518PhosphorylationTAQDNPKSATEQSGT
ECCCCCCCHHHCCCC		41.5025619855
520PhosphorylationQDNPKSATEQSGTGI
CCCCCCHHHCCCCCC		41.4725619855
523PhosphorylationPKSATEQSGTGIRSE
CCCHHHCCCCCCCCC		31.9023140645
529PhosphorylationQSGTGIRSESETESE
CCCCCCCCCCCCCCC		43.48-
533PhosphorylationGIRSESETESEASEI
CCCCCCCCCCCCCCC		54.83-
589MalonylationNRMPIARKIIKDGEQ
CCCHHHHHHHCCCCC		39.5026320211
589AcetylationNRMPIARKIIKDGEQ
CCCHHHHHHHCCCCC		39.5023576753
592MalonylationPIARKIIKDGEQHED
HHHHHHHCCCCCCCC		64.2526320211
592AcetylationPIARKIIKDGEQHED
HHHHHHHCCCCCCCC		64.2523576753
592SuccinylationPIARKIIKDGEQHED
HHHHHHHCCCCCCCC		64.2523954790
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of AIFM1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
254Kubiquitylation

-
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of AIFM1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BAG6_MOUSEBag6physical
18056262
KAD2_HUMANAK2physical
26496610
CLUS_HUMANCLUphysical
26496610
CX6B1_HUMANCOX6B1physical
26496610
HMGB1_HUMANHMGB1physical
26496610
PHB_HUMANPHBphysical
26496610
VDAC1_HUMANVDAC1physical
26496610
NUDC_HUMANNUDCphysical
26496610
MIC60_HUMANIMMTphysical
26496610
PHB2_HUMANPHB2physical
26496610
STML2_HUMANSTOML2physical
26496610
MIC19_HUMANCHCHD3physical
26496610
MIC25_HUMANCHCHD6physical
26496610
MIA40_HUMANCHCHD4physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AIFM1_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-592, AND MASS SPECTROMETRY.

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