dbPTM

ARGI1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARGI1_MOUSE
UniProt AC	Q61176
Protein Name	Arginase-1
Gene Name	Arg1
Organism	Mus musculus (Mouse).
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. [PubMed: 27043409 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]
Protein Sequence	MSSKPKSLEIIGAPFSKGQPRGGVEKGPAALRKAGLLEKLKETEYDVRDHGDLAFVDVPNDSSFQIVKNPRSVGKANEELAGVVAEVQKNGRVSVVLGGDHSLAVGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVSFLLKELKGKFPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPAFTPATGTPVLGGLSYREGLYITEEIYKTGLLSGLDIMEVNPTLGKTAEEVKSTVNTAVALTLACFGTQREGNHKPGTDYLKPPK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSKPKSLE ------CCCCCCCEE	47.25	24719451
3	Phosphorylation	-----MSSKPKSLEI -----CCCCCCCEEE	52.24	17242355
6	Malonylation	--MSSKPKSLEIIGA --CCCCCCCEEECCC	71.99	26320211
6	Ubiquitination	--MSSKPKSLEIIGA --CCCCCCCEEECCC	71.99	-
6	Acetylation	--MSSKPKSLEIIGA --CCCCCCCEEECCC	71.99	23954790
7	Phosphorylation	-MSSKPKSLEIIGAP -CCCCCCCEEECCCC	39.50	25521595
16	Phosphorylation	EIIGAPFSKGQPRGG EECCCCCCCCCCCCC	34.51	29472430
17	Ubiquitination	IIGAPFSKGQPRGGV ECCCCCCCCCCCCCC	63.04	27667366
17	Acetylation	IIGAPFSKGQPRGGV ECCCCCCCCCCCCCC	63.04	23954790
17	Succinylation	IIGAPFSKGQPRGGV ECCCCCCCCCCCCCC	63.04	23806337
17	Malonylation	IIGAPFSKGQPRGGV ECCCCCCCCCCCCCC	63.04	26320211
17	Succinylation	IIGAPFSKGQPRGGV ECCCCCCCCCCCCCC	63.04	-
26	Malonylation	QPRGGVEKGPAALRK CCCCCCCCCHHHHHH	68.72	26320211
26	Acetylation	QPRGGVEKGPAALRK CCCCCCCCCHHHHHH	68.72	23864654
26	Ubiquitination	QPRGGVEKGPAALRK CCCCCCCCCHHHHHH	68.72	27667366
33	Malonylation	KGPAALRKAGLLEKL CCHHHHHHCCHHHHH	47.89	26320211
39	Malonylation	RKAGLLEKLKETEYD HHCCHHHHHHHCCCC	65.90	26320211
39	Ubiquitination	RKAGLLEKLKETEYD HHCCHHHHHHHCCCC	65.90	27667366
39	Acetylation	RKAGLLEKLKETEYD HHCCHHHHHHHCCCC	65.90	23864654
39	Succinylation	RKAGLLEKLKETEYD HHCCHHHHHHHCCCC	65.90	-
41	Ubiquitination	AGLLEKLKETEYDVR CCHHHHHHHCCCCCC	73.91	27667366
41	Malonylation	AGLLEKLKETEYDVR CCHHHHHHHCCCCCC	73.91	26073543
41	Acetylation	AGLLEKLKETEYDVR CCHHHHHHHCCCCCC	73.91	23954790
41	Glutarylation	AGLLEKLKETEYDVR CCHHHHHHHCCCCCC	73.91	24703693
41	Succinylation	AGLLEKLKETEYDVR CCHHHHHHHCCCCCC	73.91	-
62	Phosphorylation	FVDVPNDSSFQIVKN EEECCCCCCEEEECC	39.43	25521595
63	Phosphorylation	VDVPNDSSFQIVKNP EECCCCCCEEEECCC	24.84	25521595
68	Malonylation	DSSFQIVKNPRSVGK CCCEEEECCCCCCCC	63.96	26320211
68	Ubiquitination	DSSFQIVKNPRSVGK CCCEEEECCCCCCCC	63.96	-
68	Acetylation	DSSFQIVKNPRSVGK CCCEEEECCCCCCCC	63.96	23954790
72	Phosphorylation	QIVKNPRSVGKANEE EEECCCCCCCCCCHH	36.16	22324799
75	Acetylation	KNPRSVGKANEELAG CCCCCCCCCCHHHHH	45.97	23806337
75	Succinylation	KNPRSVGKANEELAG CCCCCCCCCCHHHHH	45.97	23806337
75	Malonylation	KNPRSVGKANEELAG CCCCCCCCCCHHHHH	45.97	26320211
75	Succinylation	KNPRSVGKANEELAG CCCCCCCCCCHHHHH	45.97	-
75	Ubiquitination	KNPRSVGKANEELAG CCCCCCCCCCHHHHH	45.97	27667366
89	Malonylation	GVVAEVQKNGRVSVV HHEEEEHHCCEEEEE	67.55	26320211
89	Acetylation	GVVAEVQKNGRVSVV HHEEEEHHCCEEEEE	67.55	23864654
89	Ubiquitination	GVVAEVQKNGRVSVV HHEEEEHHCCEEEEE	67.55	27667366
153	Ubiquitination	SFLLKELKGKFPDVP HHHHHHHCCCCCCCC	62.23	22790023
155	Malonylation	LLKELKGKFPDVPGF HHHHHCCCCCCCCCC	52.73	26320211
155	Acetylation	LLKELKGKFPDVPGF HHHHHCCCCCCCCCC	52.73	22733758
155	Ubiquitination	LLKELKGKFPDVPGF HHHHHCCCCCCCCCC	52.73	-
163	Phosphorylation	FPDVPGFSWVTPCIS CCCCCCCCCCCCCCC	26.93	22324799
166	Phosphorylation	VPGFSWVTPCISAKD CCCCCCCCCCCCHHH	13.24	23140645
168	S-palmitoylation	GFSWVTPCISAKDIV CCCCCCCCCCHHHEE	2.54	28526873
170	Phosphorylation	SWVTPCISAKDIVYI CCCCCCCCHHHEEEE	35.66	23140645
172	Malonylation	VTPCISAKDIVYIGL CCCCCCHHHEEEEEE	40.99	26073543
176	Phosphorylation	ISAKDIVYIGLRDVD CCHHHEEEEEECCCC	6.93	20531401
191	Acetylation	PGEHYIIKTLGIKYF CCCCEEEEECCCEEE	28.30	22733758
191	Ubiquitination	PGEHYIIKTLGIKYF CCCCEEEEECCCEEE	28.30	-
191	Malonylation	PGEHYIIKTLGIKYF CCCCEEEEECCCEEE	28.30	26320211
196	Acetylation	IIKTLGIKYFSMTEV EEEECCCEEEECCCH	38.14	23954790
196	Ubiquitination	IIKTLGIKYFSMTEV EEEECCCEEEECCCH	38.14	22790023
197	Phosphorylation	IKTLGIKYFSMTEVD EEECCCEEEECCCHH	10.04	29472430
199	Phosphorylation	TLGIKYFSMTEVDKL ECCCEEEECCCHHHH	23.00	25521595
201	Phosphorylation	GIKYFSMTEVDKLGI CCEEEECCCHHHHCH	31.49	25521595
205	Acetylation	FSMTEVDKLGIGKVM EECCCHHHHCHHHHH	54.51	23954790
205	Ubiquitination	FSMTEVDKLGIGKVM EECCCHHHHCHHHHH	54.51	27667366
205	Malonylation	FSMTEVDKLGIGKVM EECCCHHHHCHHHHH	54.51	26320211
215	Phosphorylation	IGKVMEETFSYLLGR HHHHHHHHHHHHHCC	12.46	23984901
217	Phosphorylation	KVMEETFSYLLGRKK HHHHHHHHHHHCCCC	23.45	22817900
218	Phosphorylation	VMEETFSYLLGRKKR HHHHHHHHHHCCCCC	11.18	23984901
224	Malonylation	SYLLGRKKRPIHLSF HHHHCCCCCCEEEEE	63.14	26320211
230	Phosphorylation	KKRPIHLSFDVDGLD CCCCEEEEEECCCCC	12.77	17203969
241	Phosphorylation	DGLDPAFTPATGTPV CCCCCCCCCCCCCCC	17.70	-
244	Phosphorylation	DPAFTPATGTPVLGG CCCCCCCCCCCCCCC	42.67	17203969
246	Phosphorylation	AFTPATGTPVLGGLS CCCCCCCCCCCCCCC	13.08	17203969
265	Phosphorylation	LYITEEIYKTGLLSG EEECHHHHHCCCCCC	13.04	17242355
281	Phosphorylation	DIMEVNPTLGKTAEE CEEECCCCCCCCHHH	42.83	25521595
284	Acetylation	EVNPTLGKTAEEVKS ECCCCCCCCHHHHHH	47.91	22733758
284	Malonylation	EVNPTLGKTAEEVKS ECCCCCCCCHHHHHH	47.91	26320211
284	Ubiquitination	EVNPTLGKTAEEVKS ECCCCCCCCHHHHHH	47.91	-
285	Phosphorylation	VNPTLGKTAEEVKST CCCCCCCCHHHHHHH	37.19	21082442
290	Malonylation	GKTAEEVKSTVNTAV CCCHHHHHHHHHHHH	43.63	26320211
303	S-palmitoylation	AVALTLACFGTQREG HHHHHHHHHCCCCCC	3.48	28526873
313	Malonylation	TQREGNHKPGTDYLK CCCCCCCCCCCCCCC	49.49	26073543
313	Acetylation	TQREGNHKPGTDYLK CCCCCCCCCCCCCCC	49.49	23201123
313	Ubiquitination	TQREGNHKPGTDYLK CCCCCCCCCCCCCCC	49.49	27667366
320	Malonylation	KPGTDYLKPPK---- CCCCCCCCCCC----	53.71	26320211
320	Ubiquitination	KPGTDYLKPPK---- CCCCCCCCCCC----	53.71	27667366
320	Acetylation	KPGTDYLKPPK---- CCCCCCCCCCC----	53.71	23864654

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 ARGI1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ARGI1_MOUSE !!

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 ARGI1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ARGI1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of ARGI1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASSSPECTROMETRY.	17203969 [Abstract]