PURA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PURA1_HUMAN
• UniProt AC: Q8N142
• Protein Name: Adenylosuccinate synthetase isozyme 1 {ECO:0000255|HAMAP-Rule:MF_03126}
• Gene Name: ADSSL1 {ECO:0000255|HAMAP-Rule:MF_03126}
• Organism: Homo sapiens (Human).
• Sequence Length: 457
• Subcellular Localization: Cytoplasm .
• Protein Description: Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP..
• Protein Sequence: MSGTRASNDRPPGAGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADIISRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKGLKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGLRICDLLSDFDEFSSRFKNLAHQHQSMFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWEDLPPQAQNYIRFVENHVGVAVKWVGVGKSRESMIQLF

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
7	Phosphorylation	-MSGTRASNDRPPGA -CCCCCCCCCCCCCC	35.65	28674419
18	Acetylation	PPGAGGVKRGRLQQE CCCCCCCCCCCHHHH	53.03	7609191
55	Phosphorylation	KVVDLLATDADIISR CEEEEEECCHHHHHH	31.52	63771625
57 (in isoform 2)	Phosphorylation	-	12.92	-
61	Phosphorylation	ATDADIISRCQGGNN ECCHHHHHHCCCCCC	27.60	68731321
62 (in isoform 2)	Phosphorylation	-	13.33	-
68 (in isoform 2)	Phosphorylation	-	51.04	-
71 (in isoform 2)	Phosphorylation	-	17.06	22210691
80 (in isoform 2)	Phosphorylation	-	27.65	22210691
83 (in isoform 2)	Phosphorylation	-	24.45	22210691
89 (in isoform 2)	Phosphorylation	-	2.29	22210691
131	Phosphorylation	WEKRLIISDRAHLVF HHHHEEEECCCEEEE	17.66	25106551
172	Phosphorylation	KGIGPTYSSKAARTG CCCCCCCCHHHHHHC	28.04	28857561
173	Phosphorylation	GIGPTYSSKAARTGL CCCCCCCHHHHHHCH	18.85	28857561
174	Acetylation	IGPTYSSKAARTGLR CCCCCCHHHHHHCHH	39.87	30585569
248	Acetylation	EALHGPPKKILVEGA HHHHCCCCEEEEECC	56.43	30585563
332	Phosphorylation	RGHEWGVTTGRKRRC CCCCCCCCCCCCCCC	21.42	26437602
388	Phosphorylation	LNGKRIPYFPANQEM ECCEECCCCCCCHHH	21.59	25884760
403	Phosphorylation	LQKVEVEYETLPGWK HHHCEEEEECCCCCC	21.27	25884760
410	Ubiquitination	YETLPGWKADTTGAR EECCCCCCCCCCCCC	42.15	-
449	Phosphorylation	KWVGVGKSRESMIQL EEEECCCCHHHHHHC	35.04	23403867
452	Phosphorylation	GVGKSRESMIQLF-- ECCCCHHHHHHCC--	21.78	22617229

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

Oops, there are no upstream regulatory protein records of PURA1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PURA1_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 PURA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LYAR_HUMAN	LYAR	physical	21988832
AZIN1_HUMAN	AZIN1	physical	21988832

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
• DB00128: L-Aspartic Acid

Related Literatures of Post-Translational Modification

Phosphorylation

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-388, AND MASSSPECTROMETRY.
PubMed: 18083107