Search Results

Overview

Uniprot ID	P15104
Protein Name	Glutamine synthetase
Gene Name	GLUL
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
103	LVLCEVFKYNRRPAE
11	SASSHLNKGIKQVYM
14	SHLNKGIKQVYMSLP
25	MSLPQGEKVQAMYIW
259	CHTNFSTKAMREENG
268	MREENGLKYIEEAIE
276	YIEEAIEKLSKRHQY
291	HIRAYDPKGGLDNAR
333	PRTVGQEKKGYFEDR
334	RTVGQEKKGYFEDRR
372	GDEPFQYKN******
95	PFRKDPNKLVLCEVF

Function

Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (PubMed:16267323, PubMed:30158707, PubMed:36289327). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia (By similarity). Plays a key role in ammonium detoxification during erythropoiesis: the glutamine synthetase activity is required to remove ammonium generated by porphobilinogen deaminase (HMBS) during heme biosynthesis to prevent ammonium accumulation and oxidative stress (By similarity). Essential for proliferation of fetal skin fibroblasts (PubMed:18662667). Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation (PubMed:30158707). May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (PubMed:30158707). Plays a role in ribosomal 40S subunit biogenesis (PubMed:26711351). Through the interaction with BEST2, inhibits BEST2 channel activity by affecting the gating at the aperture in the absence of intracellular L-glutamate, but sensitizes BEST2 to intracellular L-glutamate, which promotes the opening of BEST2 and thus relieves its inhibitory effect on BEST2 (PubMed:36289327)

Protein Sequence

10 MTTSASSHLN 20 KGIKQVYMSL 30 PQGEKVQAMY 40 IWIDGTGEGL 50 RCKTRTLDSE 60 PKCVEELPEW 70 NFDGSSTLQS 80 EGSNSDMYLV 90 PAAMFRDPFR 100 KDPNKLVLCE 110 VFKYNRRPAE 120 TNLRHTCKRI 130 MDMVSNQHPW 140 FGMEQEYTLM 150 GTDGHPFGWP 160 SNGFPGPQGP 170 YYCGVGADRA 180 YGRDIVEAHY 190 RACLYAGVKI 200 AGTNAEVMPA 210 QWEFQIGPCE 220 GISMGDHLWV 230 ARFILHRVCE 240 DFGVIATFDP 250 KPIPGNWNGA 260 GCHTNFSTKA 270 MREENGLKYI 280 EEAIEKLSKR 290 HQYHIRAYDP 300 KGGLDNARRL 310 TGFHETSNIN 320 DFSAGVANRS 330 ASIRIPRTVG 340 QEKKGYFEDR 350 RPSANCDPFS 360 VTEALIRTCL 370 LNETGDEPFQ YKN

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0044297	cell body
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0070062	extracellular exosome
Cellular Component	GO:0097386	glial cell projection
Cellular Component	GO:0005739	mitochondrion
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0005886	plasma membrane
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0004356	glutamine synthetase activity
Molecular Function	GO:0042802	identical protein binding
Molecular Function	GO:0046872	metal ion binding
Molecular Function	GO:0019706	protein-cysteine S-palmitoyltransferase activity
Biological Process	GO:0001525	angiogenesis
Biological Process	GO:0008283	cell population proliferation
Biological Process	GO:0006542	glutamine biosynthetic process
Biological Process	GO:0097275	intracellular ammonium homeostasis
Biological Process	GO:0006538	L-glutamate catabolic process
Biological Process	GO:0045648	positive regulation of erythrocyte differentiation
Biological Process	GO:0018345	protein palmitoylation
Biological Process	GO:0010594	regulation of endothelial cell migration
Biological Process	GO:1904749	regulation of protein localization to nucleolus
Biological Process	GO:1903670	regulation of sprouting angiogenesis
Biological Process	GO:0042254	ribosome biogenesis

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[4] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.