GSH0_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GSH0_HUMAN
• UniProt AC: P48507
• Protein Name: Glutamate--cysteine ligase regulatory subunit
• Gene Name: GCLM
• Organism: Homo sapiens (Human).
• Sequence Length: 274
• Protein Sequence: MGTDSRAAKALLARARTLHLQTGNLLNWGRLRKKCPSTHSEELHDCIQKTLNEWSSQINPDLVREFPDVLECTVSHAVEKINPDEREEMKVSAKLFIVESNSSSSTRSAVDMACSVLGVAQLDSVIIASPPIEDGVNLSLEHLQPYWEELENLVQSKKIVAIGTSDLDKTQLEQLYQWAQVKPNSNQVNLASCCVMPPDLTAFAKQFDIQLLTHNDPKELLSEASFQEALQESIPDIQAHEWVPLWLLRYSVIVKSRGIIKSKGYILQAKRRGS

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
9	Malonylation	GTDSRAAKALLARAR CCHHHHHHHHHHHHH	38.28	26320211
9	Sumoylation	GTDSRAAKALLARAR CCHHHHHHHHHHHHH	38.28	-
9	Acetylation	GTDSRAAKALLARAR CCHHHHHHHHHHHHH	38.28	27452117
9	Sumoylation	GTDSRAAKALLARAR CCHHHHHHHHHHHHH	38.28	-
9	Ubiquitination	GTDSRAAKALLARAR CCHHHHHHHHHHHHH	38.28	24816145
17	Phosphorylation	ALLARARTLHLQTGN HHHHHHHHHHHCCCC	19.97	20873877
33	Ubiquitination	LNWGRLRKKCPSTHS CCHHHHHCCCCCCCH	64.42	-
34	Ubiquitination	NWGRLRKKCPSTHSE CHHHHHCCCCCCCHH	44.97	33845483
35	S-nitrosylation	WGRLRKKCPSTHSEE HHHHHCCCCCCCHHH	3.45	22178444
37	Phosphorylation	RLRKKCPSTHSEELH HHHCCCCCCCHHHHH	48.50	29449344
38	Phosphorylation	LRKKCPSTHSEELHD HHCCCCCCCHHHHHH	17.98	29449344
40	Phosphorylation	KKCPSTHSEELHDCI CCCCCCCHHHHHHHH	32.62	29449344
49	Ubiquitination	ELHDCIQKTLNEWSS HHHHHHHHHHHHHHH	34.76	29967540
56	Phosphorylation	KTLNEWSSQINPDLV HHHHHHHHHCCHHHH	35.83	28857561
58	Ubiquitination	LNEWSSQINPDLVRE HHHHHHHCCHHHHHH	9.74	32015554
68	Ubiquitination	DLVREFPDVLECTVS HHHHHCCCHHHHHHH	64.05	33845483
72	S-nitrosocysteine	EFPDVLECTVSHAVE HCCCHHHHHHHHHHH	3.88	-
72	S-nitrosylation	EFPDVLECTVSHAVE HCCCHHHHHHHHHHH	3.88	19483679
80	Ubiquitination	TVSHAVEKINPDERE HHHHHHHHCCCCHHH	40.98	32015554
90	Ubiquitination	PDEREEMKVSAKLFI CCHHHHHHEEEEEEE	36.00	33845483
90	Acetylation	PDEREEMKVSAKLFI CCHHHHHHEEEEEEE	36.00	25953088
103	Phosphorylation	FIVESNSSSSTRSAV EEEECCCCCCHHHHH	32.34	21712546
104	Phosphorylation	IVESNSSSSTRSAVD EEECCCCCCHHHHHH	35.23	23025827
136	Ubiquitination	SPPIEDGVNLSLEHL CCCCCCCCCCCHHHC	11.44	29967540
147	Ubiquitination	LEHLQPYWEELENLV HHHCHHHHHHHHHHH	10.16	29967540
158	Ubiquitination	ENLVQSKKIVAIGTS HHHHHHCCEEEECCC	47.89	29967540
158	Sumoylation	ENLVQSKKIVAIGTS HHHHHHCCEEEECCC	47.89	-
158	Sumoylation	ENLVQSKKIVAIGTS HHHHHHCCEEEECCC	47.89	-
164	Phosphorylation	KKIVAIGTSDLDKTQ CCEEEECCCCCCHHH	16.98	21406692
165	Phosphorylation	KIVAIGTSDLDKTQL CEEEECCCCCCHHHH	30.84	21406692
169	Ubiquitination	IGTSDLDKTQLEQLY ECCCCCCHHHHHHHH	45.53	29967540
205	Sumoylation	PDLTAFAKQFDIQLL CCHHHHHHHCCEEEE	45.07	-
241	Ubiquitination	IPDIQAHEWVPLWLL CCCCHHHCCHHHHHH	53.86	33845483
241	Acetylation	IPDIQAHEWVPLWLL CCCCHHHCCHHHHHH	53.86	19608861
248	Ubiquitination	EWVPLWLLRYSVIVK CCHHHHHHEEHHHHH	3.06	29967540
263	Malonylation	SRGIIKSKGYILQAK CCCCHHCCEEEEEEH	51.21	26320211
263	Ubiquitination	SRGIIKSKGYILQAK CCCCHHCCEEEEEEH	51.21	33845483
263	Acetylation	SRGIIKSKGYILQAK CCCCHHCCEEEEEEH	51.21	19608861
265	Phosphorylation	GIIKSKGYILQAKRR CCHHCCEEEEEEHHC	11.38	-
270	Ubiquitination	KGYILQAKRRGS--- CEEEEEEHHCCC---	29.66	29967540

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

Oops, there are no upstream regulatory protein records of GSH0_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GSH0_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GSH0_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STOX1_HUMAN	STOX1	physical	21988832
IRF7_HUMAN	IRF7	physical	21988832
GNAI2_HUMAN	GNAI2	physical	22863883
NAGK_HUMAN	NAGK	physical	22863883
CPNE3_HUMAN	CPNE3	physical	26344197
GSH1_HUMAN	GCLC	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00151: L-Cysteine

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-263, AND MASS SPECTROMETRY.
PubMed: 19608861