ALDOA_RABIT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ALDOA_RABIT
• UniProt AC: P00883
• Protein Name: Fructose-bisphosphate aldolase A
• Gene Name: ALDOA
• Organism: Oryctolagus cuniculus (Rabbit).
• Sequence Length: 364
• Subcellular Localization: Cytoplasm, myofibril, sarcomere, I band . Cytoplasm, myofibril, sarcomere, M line . In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+).
• Protein Description: Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein..
• Protein Sequence: MPHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFISNHAY

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
9	Phosphorylation	PHSHPALTPEQKKEL CCCCCCCCHHHHHHH	27.21	-
36	Phosphorylation	GILAADESTGSIAKR CEEEEECCHHHHHHH	38.32	-
39	Phosphorylation	AADESTGSIAKRLQS EEECCHHHHHHHHHH	21.33	-
42	Acetylation	ESTGSIAKRLQSIGT CCHHHHHHHHHHHCC	52.55	-
46	Phosphorylation	SIAKRLQSIGTENTE HHHHHHHHHCCCCCH	27.81	-
73	Glutathionylation	ADDRVNPCIGGVILF CCCCCCHHHCCEEEE	3.68	22833525
99	Other	RPFPQVIKSKGGVVG CCCCCCHHCCCCEEE	47.46	-
108	Acetylation	KGGVVGIKVDKGVVP CCCEEEEEECCCCEE	38.15	-
111	Acetylation	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	-
111	Malonylation	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	-
111	N6-malonyllysine	VVGIKVDKGVVPLAG EEEEEECCCCEECCC	57.50	-
132	Phosphorylation	TQGLDGLSERCAQYK CCCCCHHHHHHHHHH	28.64	-
165	Sulfoxidation	TPSALAIMENANVLA CHHHHHHHHCHHHHH	2.43	28183972
204	Nitration	HDLKRCQYVTEKVLA CCHHHHHHHHHHHHH	16.99	-
223	Nitration	ALSDHHIYLEGTLLK HHCCCCEEEECEEEC	8.37	-
244	Nitration	GHACTQKYSHEEIAM CCCCCCCCCHHHHHH	12.87	-
272	Phosphorylation	VTGVTFLSGGQSEEE CCEEEEECCCCCHHH	36.36	-
312	Malonylation	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	-
312	N6-malonyllysine	ALQASALKAWGGKKE HHHHHHHHHCCCCHH	41.64	-
328	Nitration	LKAAQEEYVKRALAN HHHHHHHHHHHHHHH	15.54	-
330	Acetylation	AAQEEYVKRALANSL HHHHHHHHHHHHHHH	30.93	-
343	Nitration	SLACQGKYTPSGQAG HHHHCCCCCCCCCHH	30.61	-
361	Deamidation	SESLFISNHAY---- HHHEEECCCCC----	20.99	4857186
361	Deamidated asparagine	SESLFISNHAY---- HHHEEECCCCC----	20.99	-
362	Phosphorylation	ESLFISNHAY----- HHEEECCCCC-----	21.44	-
364	Nitration	LFISNHAY------- EEECCCCC-------	16.13	-

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of ALDOA_RABIT !!

Drug and Disease Associations

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