ARGI1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ARGI1_RAT
• UniProt AC: P07824
• Protein Name: Arginase-1
• Gene Name: Arg1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 323
• Subcellular Localization: Cytoplasm . Cytoplasmic granule .
• Protein Description: Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.; Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion (By similarity). In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival. Plays a role in the immune response of alternatively activated or M2 macrophages in processes such as wound healing and tissue regeneration, immune defense against multicellular pathogens and parasites, and immune suppression and allergic inflammation; the regulatory outcome seems to be organ specific. In tumor-infiltrating dendritic cells (DCs) and myeloid-derived suppressor cells (MDSCs) plays a role in suppression of T cell-mediated antitumor immunity..
• Protein Sequence: MSSKPKPIEIIGAPFSKGQPRGGVEKGPAALRKAGLVEKLKETEYNVRDHGDLAFVDVPNDSPFQIVKNPRSVGKANEQLAAVVAETQKNGTISVVLGGDHSMAIGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVAFLLKELKGKFPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPVFTPATGTPVVGGLSYREGLYITEEIYKTGLLSGLDIMEVNPTLGKTPEEVTRTVNTAVALTLSCFGTKREGNHKPETDYLKPPK

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
2	Phosphorylation	------MSSKPKPIE ------CCCCCCCCE	47.25	25575281
3	Phosphorylation	-----MSSKPKPIEI -----CCCCCCCCEE	52.24	25575281
6	Acetylation	--MSSKPKPIEIIGA --CCCCCCCCEEEEC	63.46	22902405
6	Succinylation	--MSSKPKPIEIIGA --CCCCCCCCEEEEC	63.46	26843850
17	Succinylation	IIGAPFSKGQPRGGV EEECCCCCCCCCCCC	63.04	-
17	Succinylation	IIGAPFSKGQPRGGV EEECCCCCCCCCCCC	63.04	-
26	Acetylation	QPRGGVEKGPAALRK CCCCCCCCCHHHHHH	68.72	22902405
39	Acetylation	RKAGLVEKLKETEYN HHCCHHHHHHHCCCC	58.33	22902405
41	Succinylation	AGLVEKLKETEYNVR CCHHHHHHHCCCCCC	73.91	26843850
41	Acetylation	AGLVEKLKETEYNVR CCHHHHHHHCCCCCC	73.91	22902405
62	Phosphorylation	FVDVPNDSPFQIVKN EEECCCCCCCEEECC	33.96	29779826
68	Acetylation	DSPFQIVKNPRSVGK CCCCEEECCHHCCCC	63.96	22902405
72	Phosphorylation	QIVKNPRSVGKANEQ EEECCHHCCCCHHHH	36.16	25575281
75	Acetylation	KNPRSVGKANEQLAA CCHHCCCCHHHHHHH	45.97	22902405
75	Succinylation	KNPRSVGKANEQLAA CCHHCCCCHHHHHHH	45.97	-
75	Succinylation	KNPRSVGKANEQLAA CCHHCCCCHHHHHHH	45.97	-
163	Phosphorylation	FPDVPGFSWVTPCIS CCCCCCCCCCCCCCC	26.93	29779826
166	Phosphorylation	VPGFSWVTPCISAKD CCCCCCCCCCCCHHH	13.24	23984901
170	Phosphorylation	SWVTPCISAKDIVYI CCCCCCCCHHHEEEE	35.66	23984901
188	Phosphorylation	DVDPGEHYIIKTLGI CCCCCCCEEEEECCC	10.47	25575281
191	Acetylation	PGEHYIIKTLGIKYF CCCCEEEEECCCEEE	28.30	22902405
196	Acetylation	IIKTLGIKYFSMTEV EEEECCCEEEECCCH	38.14	22902405
197	Phosphorylation	IKTLGIKYFSMTEVD EEECCCEEEECCCHH	10.04	30181290
199	Phosphorylation	TLGIKYFSMTEVDKL ECCCEEEECCCHHHH	23.00	30181290
205	Acetylation	FSMTEVDKLGIGKVM EECCCHHHHCHHHHH	54.51	22902405
215	Phosphorylation	IGKVMEETFSYLLGR HHHHHHHHHHHHHCC	12.46	22673903
217	Phosphorylation	KVMEETFSYLLGRKK HHHHHHHHHHHCCCC	23.45	22673903
218	Phosphorylation	VMEETFSYLLGRKKR HHHHHHHHHHCCCCC	11.18	25575281
265	Phosphorylation	LYITEEIYKTGLLSG EEECHHHHHCCCCCC	13.04	28689409
281	Phosphorylation	DIMEVNPTLGKTPEE CEEECCCCCCCCHHH	42.83	29779826
284	Acetylation	EVNPTLGKTPEEVTR ECCCCCCCCHHHHHH	65.11	22902405
285	Phosphorylation	VNPTLGKTPEEVTRT CCCCCCCCHHHHHHH	33.85	23984901
290	Phosphorylation	GKTPEEVTRTVNTAV CCCHHHHHHHHHHHH	24.73	23984901
320	Succinylation	KPETDYLKPPK---- CCCCCCCCCCC----	53.71	26843850

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

Oops, there are no upstream regulatory protein records of ARGI1_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ARGI1_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ARGI1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of ARGI1_RAT !!

Drug and Disease Associations

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