AFG32_HUMAN - dbPTM
AFG32_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AFG32_HUMAN
UniProt AC Q9Y4W6
Protein Name AFG3-like protein 2
Gene Name AFG3L2
Organism Homo sapiens (Human).
Sequence Length 797
Subcellular Localization Mitochondrion . Mitochondrion inner membrane
Multi-pass membrane protein .
Protein Description ATP-dependent protease which is essential for axonal and neuron development. In neurons, mediates degradation of SMDT1/EMRE before its assembly with the uniporter complex, limiting the availability of SMDT1/EMRE for MCU assembly and promoting efficient assembly of gatekeeper subunits with MCU. [PubMed: 27642048 Required for the maturation of paraplegin (SPG7) after its cleavage by mitochondrial-processing peptidase (MPP), converting it into a proteolytically active mature form (By similarity]
Protein Sequence MAHRCLRLWGRGGCWPRGLQQLLVPGGVGPGEQPCLRTLYRFVTTQARASRNSLLTDIIAAYQRFCSRPPKGFEKYFPNGKNGKKASEPKEVMGEKKESKPAATTRSSGGGGGGGGKRGGKKDDSHWWSRFQKGDIPWDDKDFRMFFLWTALFWGGVMFYLLLKRSGREITWKDFVNNYLSKGVVDRLEVVNKRFVRVTFTPGKTPVDGQYVWFNIGSVDTFERNLETLQQELGIEGENRVPVVYIAESDGSFLLSMLPTVLIIAFLLYTIRRGPAGIGRTGRGMGGLFSVGETTAKVLKDEIDVKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSTLEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDSINQKHFEQAIERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQGDMVLEKPYSEATARLIDDEVRILINDAYKRTVALLTEKKADVEKVALLLLEKEVLDKNDMVELLGPRPFAEKSTYEEFVEGTGSLDEDTSLPEGLKDWNKEREKEKEEPPGEKVAN
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
14S-palmitoylationRLWGRGGCWPRGLQQ
HHHCCCCCCCCCHHH		5.1429575903
99PhosphorylationVMGEKKESKPAATTR
HCCCCCCCCCCCCCC		53.4729083192
100AcetylationMGEKKESKPAATTRS
CCCCCCCCCCCCCCC		39.5020167786
104PhosphorylationKESKPAATTRSSGGG
CCCCCCCCCCCCCCC		25.5029083192
105PhosphorylationESKPAATTRSSGGGG
CCCCCCCCCCCCCCC		24.6729083192
107PhosphorylationKPAATTRSSGGGGGG
CCCCCCCCCCCCCCC		31.1029083192
108PhosphorylationPAATTRSSGGGGGGG
CCCCCCCCCCCCCCC		37.8629083192
117SuccinylationGGGGGGGKRGGKKDD
CCCCCCCCCCCCCCC		51.66-
117SuccinylationGGGGGGGKRGGKKDD
CCCCCCCCCCCCCCC		51.66-
121MalonylationGGGKRGGKKDDSHWW
CCCCCCCCCCCCCCH		56.7230639696
122MalonylationGGKRGGKKDDSHWWS
CCCCCCCCCCCCCHH		70.7826320211
150PhosphorylationFRMFFLWTALFWGGV
HHHHHHHHHHHHHHH		18.6846160193
160PhosphorylationFWGGVMFYLLLKRSG
HHHHHHHHHHHHHCC		4.3746160211
173UbiquitinationSGREITWKDFVNNYL
CCCCCCHHHHHHHHH		32.4121890473
179PhosphorylationWKDFVNNYLSKGVVD
HHHHHHHHHCCCCHH		13.7222817900
182UbiquitinationFVNNYLSKGVVDRLE
HHHHHHCCCCHHHHH		53.8021890473
193UbiquitinationDRLEVVNKRFVRVTF
HHHHHCCCCEEEEEE		35.29-
193AcetylationDRLEVVNKRFVRVTF
HHHHHCCCCEEEEEE		35.2930585747
1932-HydroxyisobutyrylationDRLEVVNKRFVRVTF
HHHHHCCCCEEEEEE		35.29-
218PhosphorylationYVWFNIGSVDTFERN
EEEEEECCHHHHHHH		17.0246160187
221PhosphorylationFNIGSVDTFERNLET
EEECCHHHHHHHHHH		25.8246160199
270PhosphorylationIIAFLLYTIRRGPAG
HHHHHHHHHHHCCCC		14.1524719451
285SulfoxidationIGRTGRGMGGLFSVG
CCCCCCCCCCCEECC		3.5621406390
290PhosphorylationRGMGGLFSVGETTAK
CCCCCCEECCHHHHH		33.9722210691
300AcetylationETTAKVLKDEIDVKF
HHHHHHHHHHCCCCC		57.1926051181
300UbiquitinationETTAKVLKDEIDVKF
HHHHHHHHHHCCCCC		57.19-
306AcetylationLKDEIDVKFKDVAGC
HHHHCCCCCCCCCCC		42.8419608861
308SuccinylationDEIDVKFKDVAGCEE
HHCCCCCCCCCCCHH		45.6427452117
308AcetylationDEIDVKFKDVAGCEE
HHCCCCCCCCCCCHH		45.6426051181
308MalonylationDEIDVKFKDVAGCEE
HHCCCCCCCCCCCHH		45.6430639696
331SuccinylationVNFLKNPKQYQDLGA
HHHHHCHHHHHCCCC		71.6623954790
331UbiquitinationVNFLKNPKQYQDLGA
HHHHHCHHHHHCCCC		71.66-
3312-HydroxyisobutyrylationVNFLKNPKQYQDLGA
HHHHHCHHHHHCCCC		71.66-
331MalonylationVNFLKNPKQYQDLGA
HHHHHCHHHHHCCCC		71.6626320211
331AcetylationVNFLKNPKQYQDLGA
HHHHHCHHHHHCCCC		71.6625953088
342UbiquitinationDLGAKIPKGAILTGP
CCCCCCCCCCEEECC		65.5321890473
352PhosphorylationILTGPPGTGKTLLAK
EEECCCCCCHHHHHH		41.08110761159
354UbiquitinationTGPPGTGKTLLAKAT
ECCCCCCHHHHHHHH		35.52-
402GlutathionylationLARKNAPCILFIDEI
HHHCCCCEEEEEEEC		3.8122555962
425PhosphorylationRGNFGGQSEQENTLN
CCCCCCCCHHHHHHH		44.5124043423
430PhosphorylationGQSEQENTLNQLLVE
CCCHHHHHHHHHHHH		26.7424043423
443PhosphorylationVEMDGFNTTTNVVIL
HHCCCCCCCCCEEEE		32.5124043423
444PhosphorylationEMDGFNTTTNVVILA
HCCCCCCCCCEEEEE		19.9224043423
445PhosphorylationMDGFNTTTNVVILAG
CCCCCCCCCEEEEEC		24.7924043423
453PhosphorylationNVVILAGTNRPDILD
CEEEEECCCCCCCCC		23.5824043423
481MalonylationFIGPPDIKGRASIFK
EECCCCCCCCCEEEE		50.1226320211
481UbiquitinationFIGPPDIKGRASIFK
EECCCCCCCCCEEEE		50.1221890473
485PhosphorylationPDIKGRASIFKVHLR
CCCCCCCEEEEEEEC		27.4824719451
488MalonylationKGRASIFKVHLRPLK
CCCCEEEEEEECCCC		27.3726320211
498PhosphorylationLRPLKLDSTLEKDKL
ECCCCCCCHHHHHHH		45.3824670416
502SuccinylationKLDSTLEKDKLARKL
CCCCHHHHHHHHHHH		64.3727452117
502AcetylationKLDSTLEKDKLARKL
CCCCHHHHHHHHHHH		64.3726051181
502MalonylationKLDSTLEKDKLARKL
CCCCHHHHHHHHHHH		64.3726320211
504MalonylationDSTLEKDKLARKLAS
CCHHHHHHHHHHHHH		55.9326320211
508UbiquitinationEKDKLARKLASLTPG
HHHHHHHHHHHCCCC		42.68-
543MalonylationLSDSINQKHFEQAIE
HCHHHCHHHHHHHHH		45.8626320211
543AcetylationLSDSINQKHFEQAIE
HCHHHCHHHHHHHHH		45.8623954790
543UbiquitinationLSDSINQKHFEQAIE
HCHHHCHHHHHHHHH		45.8621890473
558MalonylationRVIGGLEKKTQVLQP
HHHHHHHHHCEECCH		67.1926320211
558UbiquitinationRVIGGLEKKTQVLQP
HHHHHHHHHCEECCH		67.19-
5582-HydroxyisobutyrylationRVIGGLEKKTQVLQP
HHHHHHHHHCEECCH		67.19-
5592-HydroxyisobutyrylationVIGGLEKKTQVLQPE
HHHHHHHHCEECCHH		34.51-
559MalonylationVIGGLEKKTQVLQPE
HHHHHHHHCEECCHH		34.5126320211
559SuccinylationVIGGLEKKTQVLQPE
HHHHHHHHCEECCHH		34.5127452117
560PhosphorylationIGGLEKKTQVLQPEE
HHHHHHHCEECCHHH		34.6746160205
568AcetylationQVLQPEEKKTVAYHE
EECCHHHHCCEEEHH		52.6726051181
611AcetylationGYAQYLPKEQYLYTK
CCHHCCCHHHHCCCH		55.6526051181
611UbiquitinationGYAQYLPKEQYLYTK
CCHHCCCHHHHCCCH		55.6521890473
614PhosphorylationQYLPKEQYLYTKEQL
HCCCHHHHCCCHHHH		11.63110761165
618UbiquitinationKEQYLYTKEQLLDRM
HHHHCCCHHHHHHHH		29.88-
6182-HydroxyisobutyrylationKEQYLYTKEQLLDRM
HHHHCCCHHHHHHHH		29.88-
624MethylationTKEQLLDRMCMTLGG
CHHHHHHHHHHHHCC		21.85-
634PhosphorylationMTLGGRVSEEIFFGR
HHHCCCCCCHHCCCC		28.3120068231
689PhosphorylationDMVLEKPYSEATARL
CEEEECCCCHHHHHH		30.1520068231
690PhosphorylationMVLEKPYSEATARLI
EEEECCCCHHHHHHC		29.3120068231
693PhosphorylationEKPYSEATARLIDDE
ECCCCHHHHHHCCHH		14.3020068231
7102-HydroxyisobutyrylationILINDAYKRTVALLT
HHHCHHHHHHHHHHH		43.23-
710AcetylationILINDAYKRTVALLT
HHHCHHHHHHHHHHH		43.2325953088
710SuccinylationILINDAYKRTVALLT
HHHCHHHHHHHHHHH		43.2327452117
712PhosphorylationINDAYKRTVALLTEK
HCHHHHHHHHHHHCC		13.1320068231
7192-HydroxyisobutyrylationTVALLTEKKADVEKV
HHHHHHCCCCCHHHH		48.29-
7252-HydroxyisobutyrylationEKKADVEKVALLLLE
CCCCCHHHHHHHHHH		32.43-
738UbiquitinationLEKEVLDKNDMVELL
HHHHHCCCCCCHHHH		51.16-
763PhosphorylationYEEFVEGTGSLDEDT
HHHHHCCCCCCCCCC		15.3026471730
765PhosphorylationEFVEGTGSLDEDTSL
HHHCCCCCCCCCCCC		32.2728857561
770PhosphorylationTGSLDEDTSLPEGLK
CCCCCCCCCCCCHHH		30.0728857561
771PhosphorylationGSLDEDTSLPEGLKD
CCCCCCCCCCCHHHH		55.0028348404
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 AFG32_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AFG32_HUMAN !!
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 AFG32_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
AT1A1_HUMANATP1A1physical
26344197
ATPA_HUMANATP5A1physical
26344197
PHB_HUMANPHBphysical
26344197
PHB2_HUMANPHB2physical
26344197
RPN1_HUMANRPN1physical
26344197
TMCO1_HUMANTMCO1physical
26344197
QCR8_HUMANUQCRQphysical
26344197
Drug and Disease Associations
Kegg Disease
H00063 Spinocerebellar ataxia (SCA); Machado-Joseph disease (SCA3)
H00473 Mitochondrial respiratory chain deficiencies (MRCD), including: Mitochondrial complex I deficiency (
OMIM Disease
610246Spinocerebellar ataxia 28 (SCA28)
614487Spastic ataxia 5, autosomal recessive (SPAX5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00171Adenosine triphosphate
Regulatory Network of AFG32_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-306 AND LYS-543, AND MASSSPECTROMETRY.

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