GLNA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GLNA_MOUSE
• UniProt AC: P15105
• Protein Name: Glutamine synthetase
• Gene Name: Glul
• Organism: Mus musculus (Mouse).
• Sequence Length: 373
• Subcellular Localization: Cytoplasm. Mitochondrion.
• Protein Description: Essential for proliferation of fetal skin fibroblasts. This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity)..
• Protein Sequence: MATSASSHLNKGIKQMYMSLPQGEKVQAMYIWVDGTGEGLRCKTRTLDCEPKCVEELPEWNFDGSSTFQSEGSNSDMYLHPVAMFRDPFRKDPNKLVLCEVFKYNRKPAETNLRHICKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSNGFPGPQGPYYCGVGADKAYGRDIVEAHYRACLYAGVKITGTNAEVMPAQWEFQIGPCEGIRMGDHLWIARFILHRVCEDFGVIATFDPKPIPGNWNGAGCHTNFSTKAMREENGLKCIEEAIDKLSKRHQYHIRAYDPKGGLDNARRLTGFHETSNINDFSAGVANRGASIRIPRTVGQEKKGYFEDRRPSANCDPYAVTEAIVRTCLLNETGDEPFQYKN

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	Acetylation	------MATSASSHL ------CCCCHHHHH	15.40	-
3	Phosphorylation	-----MATSASSHLN -----CCCCHHHHHH	24.43	29472430
4	Phosphorylation	----MATSASSHLNK ----CCCCHHHHHHH	19.33	30352176
6	Phosphorylation	--MATSASSHLNKGI --CCCCHHHHHHHHH	20.32	30352176
7	Phosphorylation	-MATSASSHLNKGIK -CCCCHHHHHHHHHH	31.54	30352176
11	Ubiquitination	SASSHLNKGIKQMYM CHHHHHHHHHHHHHH	69.26	22790023
14	Acetylation	SHLNKGIKQMYMSLP HHHHHHHHHHHHHCC	37.37	22826441
14	Ubiquitination	SHLNKGIKQMYMSLP HHHHHHHHHHHHHCC	37.37	22790023
17	Phosphorylation	NKGIKQMYMSLPQGE HHHHHHHHHHCCCCC	4.89	29899451
19	Phosphorylation	GIKQMYMSLPQGEKV HHHHHHHHCCCCCEE	21.29	25521595
25	Acetylation	MSLPQGEKVQAMYIW HHCCCCCEEEEEEEE	46.61	23954790
44	Phosphorylation	GEGLRCKTRTLDCEP CCCEEEEEEEECCCC	32.29	25521595
46	Phosphorylation	GLRCKTRTLDCEPKC CEEEEEEEECCCCCH	31.98	29899451
49	S-nitrosylation	CKTRTLDCEPKCVEE EEEEEECCCCCHHHC	12.41	24895380
52	Malonylation	RTLDCEPKCVEELPE EEECCCCCHHHCCCC	28.72	26073543
91	Malonylation	MFRDPFRKDPNKLVL ECCCCCCCCCCCEEE	77.30	26320211
91	Ubiquitination	MFRDPFRKDPNKLVL ECCCCCCCCCCCEEE	77.30	-
91	Acetylation	MFRDPFRKDPNKLVL ECCCCCCCCCCCEEE	77.30	23201123
95	Ubiquitination	PFRKDPNKLVLCEVF CCCCCCCCEEEEEEE	45.41	22790023
99	S-nitrosylation	DPNKLVLCEVFKYNR CCCCEEEEEEECCCC	3.06	24895380
99	S-palmitoylation	DPNKLVLCEVFKYNR CCCCEEEEEEECCCC	3.06	28526873
103	Malonylation	LVLCEVFKYNRKPAE EEEEEEECCCCCCCH	46.95	26320211
103	Ubiquitination	LVLCEVFKYNRKPAE EEEEEEECCCCCCCH	46.95	-
104	Phosphorylation	VLCEVFKYNRKPAET EEEEEECCCCCCCHH	14.56	26032504
107	Malonylation	EVFKYNRKPAETNLR EEECCCCCCCHHHHH	44.96	26320211
107	Acetylation	EVFKYNRKPAETNLR EEECCCCCCCHHHHH	44.96	19844885
107	Ubiquitination	EVFKYNRKPAETNLR EEECCCCCCCHHHHH	44.96	27667366
118	Acetylation	TNLRHICKRIMDMVS HHHHHHHHHHHHHHH	44.34	23201123
180	Phosphorylation	RDIVEAHYRACLYAG CCHHHHHHHHHHHHC	13.62	22817900
183	S-palmitoylation	VEAHYRACLYAGVKI HHHHHHHHHHHCCEE	1.90	28526873
183	S-nitrosocysteine	VEAHYRACLYAGVKI HHHHHHHHHHHCCEE	1.90	-
183	S-nitrosylation	VEAHYRACLYAGVKI HHHHHHHHHHHCCEE	1.90	21278135
185	Phosphorylation	AHYRACLYAGVKITG HHHHHHHHHCCEEEE	10.95	26032504
209	S-nitrosylation	WEFQIGPCEGIRMGD EEEEECCCCCCCCCC	6.70	21278135
209	S-palmitoylation	WEFQIGPCEGIRMGD EEEEECCCCCCCCCC	6.70	28526873
209	S-nitrosocysteine	WEFQIGPCEGIRMGD EEEEECCCCCCCCCC	6.70	-
259	Ubiquitination	CHTNFSTKAMREENG CCCCCCHHHHHHHHH	38.70	-
259	Malonylation	CHTNFSTKAMREENG CCCCCCHHHHHHHHH	38.70	26320211
268	Malonylation	MREENGLKCIEEAID HHHHHHHHHHHHHHH	34.27	26073543
268	Ubiquitination	MREENGLKCIEEAID HHHHHHHHHHHHHHH	34.27	-
268	Acetylation	MREENGLKCIEEAID HHHHHHHHHHHHHHH	34.27	22733758
269	S-palmitoylation	REENGLKCIEEAIDK HHHHHHHHHHHHHHH	5.94	28526873
269	S-nitrosylation	REENGLKCIEEAIDK HHHHHHHHHHHHHHH	5.94	24895380
276	Ubiquitination	CIEEAIDKLSKRHQY HHHHHHHHHHHHHCE	48.85	22790023
291	Malonylation	HIRAYDPKGGLDNAR EEEEECCCCCCCCHH	63.81	26320211
291	Acetylation	HIRAYDPKGGLDNAR EEEEECCCCCCCCHH	63.81	23954790
291	Ubiquitination	HIRAYDPKGGLDNAR EEEEECCCCCCCCHH	63.81	27667366
301	Phosphorylation	LDNARRLTGFHETSN CCCHHHHCCCCCCCC	35.67	27180971
306	Phosphorylation	RLTGFHETSNINDFS HHCCCCCCCCCCCCC	20.64	29899451
307	Phosphorylation	LTGFHETSNINDFSA HCCCCCCCCCCCCCH	32.50	27180971
322	Phosphorylation	GVANRGASIRIPRTV HHHCCCCEEEECCCC	18.41	23684622
328	Phosphorylation	ASIRIPRTVGQEKKG CEEEECCCCCCCCCC	24.51	25521595
333	Ubiquitination	PRTVGQEKKGYFEDR CCCCCCCCCCCCCCC	43.54	27667366
333	Acetylation	PRTVGQEKKGYFEDR CCCCCCCCCCCCCCC	43.54	23864654
334	Ubiquitination	RTVGQEKKGYFEDRR CCCCCCCCCCCCCCC	59.08	27667366
334	Malonylation	RTVGQEKKGYFEDRR CCCCCCCCCCCCCCC	59.08	26320211
336	Phosphorylation	VGQEKKGYFEDRRPS CCCCCCCCCCCCCCC	16.81	21183079
336	Nitration	VGQEKKGYFEDRRPS CCCCCCCCCCCCCCC	16.81	-
343	Phosphorylation	YFEDRRPSANCDPYA CCCCCCCCCCCCHHH	30.24	25521595
346	S-nitrosylation	DRRPSANCDPYAVTE CCCCCCCCCHHHHHH	5.80	24895380
346	S-palmitoylation	DRRPSANCDPYAVTE CCCCCCCCCHHHHHH	5.80	28526873
349	Nitration	PSANCDPYAVTEAIV CCCCCCHHHHHHHHH	10.64	-
349	Phosphorylation	PSANCDPYAVTEAIV CCCCCCHHHHHHHHH	10.64	19060867
352	Phosphorylation	NCDPYAVTEAIVRTC CCCHHHHHHHHHHHH	16.13	22871156
359	S-palmitoylation	TEAIVRTCLLNETGD HHHHHHHHHCCCCCC	2.59	28526873
359	S-nitrosocysteine	TEAIVRTCLLNETGD HHHHHHHHHCCCCCC	2.59	-
359	S-nitrosylation	TEAIVRTCLLNETGD HHHHHHHHHCCCCCC	2.59	24895380
371	Nitration	TGDEPFQYKN----- CCCCCCCCCC-----	16.93	-
372	Malonylation	GDEPFQYKN------ CCCCCCCCC------	45.45	26320211
372	Acetylation	GDEPFQYKN------ CCCCCCCCC------	45.45	88341
372	Ubiquitination	GDEPFQYKN------ CCCCCCCCC------	45.45	-

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
301	T	Phosphorylation	Kinase	PKACA	P05132	PSP
343	S	Phosphorylation	Kinase	PKACA	P05132	PSP

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of GLNA_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-104 AND TYR-180, ANDMASS SPECTROMETRY.
PubMed: 18034455