ASGL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ASGL1_HUMAN
• UniProt AC: Q7L266
• Protein Name: Isoaspartyl peptidase/L-asparaginase
• Gene Name: ASRGL1
• Organism: Homo sapiens (Human).
• Sequence Length: 308
• Subcellular Localization: Cytoplasm . Midpiece of sperm tail.
• Protein Description: Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine..
• Protein Sequence: MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP

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
1	Acetylation	-------MNPIVVVH -------CCCEEEEE	14.02	19413330
16	Phosphorylation	GGGAGPISKDRKERV CCCCCCCCCCHHHHH	31.47	28355574
32	Phosphorylation	QGMVRAATVGYGILR HHHCHHHHHHHHHHC	17.30	23312004
32	O-linked_Glycosylation	QGMVRAATVGYGILR HHHCHHHHHHHHHHC	17.30	OGP
35	Phosphorylation	VRAATVGYGILREGG CHHHHHHHHHHCCCC	9.17	27642862
103	Ubiquitination	QCIANPIKLARLVME HHHHCHHHHHHHHHH	37.03	-
150	Acetylation	RNKKRLEKEKHEKGA HHHHHHHHHHHHHHC	76.33	24431373
164	Acetylation	AQKTDCQKNLGTVGA CCCCHHHHHCCCCCE	61.54	25953088
168	Phosphorylation	DCQKNLGTVGAVALD HHHHHCCCCCEEEEE	20.94	25332170
177	Ubiquitination	GAVALDCKGNVAYAT CEEEEECCCCEEEEE	53.86	-
192	Ubiquitination	STGGIVNKMVGRVGD CCCCCCHHHCCCCCC	24.86	-
224	Phosphorylation	STTGHGESILKVNLA ECCCCCHHHEEHHHH	37.50	24719451
243	Phosphorylation	FHIEQGKTVEEAADL EEECCCCCHHHHHHH	39.72	30177828
251	Phosphorylation	VEEAADLSLGYMKSR HHHHHHHCHHHHHHH	21.94	27135362
254	Phosphorylation	AADLSLGYMKSRVKG HHHHCHHHHHHHHCC	13.48	30177828
256	Ubiquitination	DLSLGYMKSRVKGLG HHCHHHHHHHHCCCC	26.99	-
269	Phosphorylation	LGGLIVVSKTGDWVA CCEEEEEECCCCCEE	17.38	-
282	Phosphorylation	VAKWTSTSMPWAAAK EEEEEECCCCCEECC	23.71	22210691
289	Ubiquitination	SMPWAAAKDGKLHFG CCCCEECCCCCEEEE	63.39	-
292	Ubiquitination	WAAAKDGKLHFGIDP CEECCCCCEEEEECC	49.26	-
305	Phosphorylation	DPDDTTITDLP---- CCCCCCCCCCC----	29.41	22210691

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

Oops, there are no upstream regulatory protein records of ASGL1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ASGL1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ASGL1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ASGL1_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00174: L-Asparagine
• DB00128: L-Aspartic Acid

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330