dbPTM

ARLY_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARLY_YEAST
UniProt AC	P04076
Protein Name	Argininosuccinate lyase
Gene Name	ARG4
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	463
Subcellular Localization
Protein Description
Protein Sequence	MSDGTQKLWGGRFTGETDPLMHLYNASLPYDYKMYKADLEGTKVYTAGLQKLGLLTETELAKIHEGLAEIKKEWDADKFVRHPNDEDIHTANERRLGELIGRDIAGKVHTGRSRNDQVVTDLRIYCRDIVNDTLFPALKGLVEVLIKRAEGEIDVLMPGYTHLQRAQPIRWSHWLSSYATYFTEDYKRLGQILHRLNQSPLGAGALAGHPYGIDREFLAEGLGFNSVIGNSLVAVSDRDFIVELMFWGTLFMNHISRFAEDLIIYCTAEFGFIQLSDAYSTGSSLMPQKKNADSLELLRGKSGRVFGDLTGFLMSLKGIPSTYDKDMQEDKEPLFDCLTTVEHSMLIATGVISTLTVNKEKMEAALTMDMLATDLADYLVRKGVPFRETHHISGECVATAERLGLSGIDKLTLEQYQKIDSRFGQDLFETFNFEQSVERRDATGGTAKSAVLKQLDNLKSQLN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Acetylation	-MSDGTQKLWGGRFT -CCCCCCEECCCCCC	46.15	24489116
27	Phosphorylation	LMHLYNASLPYDYKM HHHHHCCCCCCCCEE	26.66	28889911
33	Ubiquitination	ASLPYDYKMYKADLE CCCCCCCEEEECCCC	32.62	23749301
36	Ubiquitination	PYDYKMYKADLEGTK CCCCEEEECCCCCCE	31.74	23749301
43	Acetylation	KADLEGTKVYTAGLQ ECCCCCCEEEECHHH	44.06	24489116
43	Ubiquitination	KADLEGTKVYTAGLQ ECCCCCCEEEECHHH	44.06	23749301
51	Ubiquitination	VYTAGLQKLGLLTET EEECHHHHHCCCCHH	49.95	24961812
51	Acetylation	VYTAGLQKLGLLTET EEECHHHHHCCCCHH	49.95	24489116
78	Acetylation	KKEWDADKFVRHPND HHHHCHHHHCCCCCH	47.70	24489116
120	Phosphorylation	SRNDQVVTDLRIYCR CCCCCEEEEEEEHHH	30.38	28889911
290	Acetylation	SSLMPQKKNADSLEL CCCCCCCCCCCHHHH	52.71	24489116
410	Acetylation	LGLSGIDKLTLEQYQ HCCCCCCCCCHHHHH	41.26	24489116
410	Ubiquitination	LGLSGIDKLTLEQYQ HCCCCCCCCCHHHHH	41.26	17644757
418	Succinylation	LTLEQYQKIDSRFGQ CCHHHHHHHHHHHCH	43.47	23954790
418	Acetylation	LTLEQYQKIDSRFGQ CCHHHHHHHHHHHCH	43.47	24489116
418	Ubiquitination	LTLEQYQKIDSRFGQ CCHHHHHHHHHHHCH	43.47	24961812
443	Phosphorylation	SVERRDATGGTAKSA HHHHCCCCCHHHHHH	40.20	17563356
453	Acetylation	TAKSAVLKQLDNLKS HHHHHHHHHHHHHHH	42.06	24489116

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 ARLY_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARLY_YEAST !!

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 ARLY_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CAN1_YEAST	CAN1	genetic	16941010
GAP1_YEAST	GAP1	genetic	16941010

Drug and Disease Associations

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

Regulatory Network of ARLY_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASSSPECTROMETRY.	18407956 [Abstract]
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-443, AND MASSSPECTROMETRY.	17563356 [Abstract]