AFG32_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AFG32_MOUSE
• UniProt AC: Q8JZQ2
• Protein Name: AFG3-like protein 2
• Gene Name: Afg3l2
• Organism: Mus musculus (Mouse).
• Sequence Length: 802
• Subcellular Localization: Mitochondrion inner membrane ; Multi-pass membrane protein .
• Protein Description: ATP-dependent protease which is essential for axonal and neuron development. [PubMed: 18337413]
• Protein Sequence: MAHRCLLLWSRGGCRRGLPPLLVPRGCLGPDRRPCLRTLYQYATVQTASSRRSLLRDVIAAYQRFCSRPPKGFEKYFPNGKNGKKASEPKEAVGEKKEPQPSGPQPSGGAGGGGGKRRGKKEDSHWWSRFQKGDFPWDDKDFRMYFLWTALFWGGVMIYFVFKSSGREITWKDFVNNYLSKGVVDRLEVVNKRFVRVTFTPGKTPVDGQYVWFNIGSVDTFERNLETLQQELGIEGENRVPVVYIAESDGSFLLSMLPTVLIIAFLLYTIRRGPAGIGRTGRGMGGLFSVGETTAKVLKDEIDVKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQGDMVLEKPYSEATARMIDDEVRILISDAYRRTVALLTEKKADVEKVALLLLEKEVLDKNDMVQLLGPRPFTEKSTYEEFVEGTGSLDEDTSLPEGLQDWNKEREKEEKKEKEKEEPLNEKVVS

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
87	Phosphorylation	GKNGKKASEPKEAVG CCCCCCCCCCHHHCC	64.41	51458647
96	Acetylation	PKEAVGEKKEPQPSG CHHHCCCCCCCCCCC	57.41	23201123
97	Acetylation	KEAVGEKKEPQPSGP HHHCCCCCCCCCCCC	71.03	23576753
102	Phosphorylation	EKKEPQPSGPQPSGG CCCCCCCCCCCCCCC	58.83	21454597
107	Phosphorylation	QPSGPQPSGGAGGGG CCCCCCCCCCCCCCC	44.61	21454597
116	Acetylation	GAGGGGGKRRGKKED CCCCCCCCCCCCCCC	42.04	23806337
116	Succinylation	GAGGGGGKRRGKKED CCCCCCCCCCCCCCC	42.04	23806337
116	Succinylation	GAGGGGGKRRGKKED CCCCCCCCCCCCCCC	42.04	-
145	Phosphorylation	DDKDFRMYFLWTALF CCHHHHHHHHHHHHH	7.40	28059163
149	Phosphorylation	FRMYFLWTALFWGGV HHHHHHHHHHHHCCE	18.68	28059163
159	Phosphorylation	FWGGVMIYFVFKSSG HHCCEEEEEEECCCC	3.90	29895711
172	Ubiquitination	SGREITWKDFVNNYL CCCEEEHHHHHHHHH	32.41	-
299	Acetylation	ETTAKVLKDEIDVKF HHHHHHHHHHCCCCC	57.19	23201123
305	Acetylation	LKDEIDVKFKDVAGC HHHHCCCCCCCCCCC	42.84	23201123
307	Succinylation	DEIDVKFKDVAGCEE HHCCCCCCCCCCCHH	45.64	26388266
307	Acetylation	DEIDVKFKDVAGCEE HHCCCCCCCCCCCHH	45.64	23864654
330	Acetylation	VNFLKNPKQYQDLGA HHHHHCHHHHHCCCC	71.66	23806337
330	Succinylation	VNFLKNPKQYQDLGA HHHHHCHHHHHCCCC	71.66	23806337
401	S-palmitoylation	LARKNAPCILFIDEI HHHCCCCEEEEEEEC	3.81	28526873
480	Succinylation	FIGPPDIKGRASIFK EECCCCCCCCCEEEE	50.12	26388266
487	Acetylation	KGRASIFKVHLRPLK CCCCEEEEEEECCCC	27.37	23864654
501	Acetylation	KLDSALEKDKLARKL CCCHHHHHHHHHHHH	62.10	23864654
501	Succinylation	KLDSALEKDKLARKL CCCHHHHHHHHHHHH	62.10	23954790
503	Acetylation	DSALEKDKLARKLAS CHHHHHHHHHHHHHH	55.93	24062335
524	S-palmitoylation	GADVANVCNEAALIA HHHHHHHCHHHHHHH	3.70	28680068
542	Acetylation	LSDAINEKHFEQAIE HHHHHCHHHHHHHHH	49.45	23864654
557	Succinylation	RVIGGLEKKTQVLQP HHHHHHHHHCEECCH	67.19	23954790
557	Acetylation	RVIGGLEKKTQVLQP HHHHHHHHHCEECCH	67.19	23864654
567	Acetylation	QVLQPEEKKTVAYHE EECCHHHHCCEEEHH	52.67	23201123
600	Succinylation	VSIIPRGKGLGYAQY EEEEECCCCCCCHHC	52.85	23806337
600	Acetylation	VSIIPRGKGLGYAQY EEEEECCCCCCCHHC	52.85	23806337
610	Acetylation	GYAQYLPKEQYLYTK CCHHCCCHHHHCCCH	55.65	23954790
610	Ubiquitination	GYAQYLPKEQYLYTK CCHHCCCHHHHCCCH	55.65	-
617	Succinylation	KEQYLYTKEQLLDRM HHHHCCCHHHHHHHH	29.88	23954790
625	S-nitrosylation	EQLLDRMCMTLGGRV HHHHHHHHHHHCCCC	1.64	21278135
625	S-nitrosocysteine	EQLLDRMCMTLGGRV HHHHHHHHHHHCCCC	1.64	-
686	Acetylation	QGDMVLEKPYSEATA CCCEEEECCCCHHHH	45.13	23864654
737	Acetylation	LEKEVLDKNDMVQLL HHHHHCCCCCCHHHH	51.16	23201123
764	Phosphorylation	EFVEGTGSLDEDTSL HHHCCCCCCCCCCCC	32.27	25195567
790	Acetylation	EKEEKKEKEKEEPLN HHHHHHHHHCCCCCC	80.91	23201123
792	Acetylation	EEKKEKEKEEPLNEK HHHHHHHCCCCCCCC	77.70	23201123

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of AFG32_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AFG32_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of AFG32_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of AFG32_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"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-307 AND LYS-542, AND MASSSPECTROMETRY.
PubMed: 16916647