dbPTM

GBRL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GBRL2_HUMAN
UniProt AC	P60520
Protein Name	Gamma-aminobutyric acid receptor-associated protein-like 2
Gene Name	GABARAPL2
Organism	Homo sapiens (Human).
Sequence Length	117
Subcellular Localization	Golgi apparatus. Cytoplasmic vesicle, autophagosome .
Protein Description	Ubiquitin-like modifier involved in intra-Golgi traffic. Modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation. It first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1 (By similarity). Involved in autophagy. Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation..
Protein Sequence	MKWMFKEDHSLEHRCVESAKIRAKYPDRVPVIVEKVSGSQIVDIDKRKYLVPSDITVAQFMWIIRKRIQLPSEKAIFLFVDKTVPQSSLTMGQLYEKEKDEDGFLYVAYSGENTFGF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	WMFKEDHSLEHRCVE CCCCCCCCCCHHHHH	48.01	22617229
15	S-nitrosocysteine	DHSLEHRCVESAKIR CCCCCHHHHHHHCHH	4.26	-
15	S-nitrosylation	DHSLEHRCVESAKIR CCCCCHHHHHHHCHH	4.26	19483679
20	Acetylation	HRCVESAKIRAKYPD HHHHHHHCHHHHCCC	41.84	25953088
20	Ubiquitination	HRCVESAKIRAKYPD HHHHHHHCHHHHCCC	41.84	29967540
24	Ubiquitination	ESAKIRAKYPDRVPV HHHCHHHHCCCCCCE	47.68	21890473
24	Acetylation	ESAKIRAKYPDRVPV HHHCHHHHCCCCCCE	47.68	19608861
24	Ubiquitination	ESAKIRAKYPDRVPV HHHCHHHHCCCCCCE	47.68	22817900
28	Methylation	IRAKYPDRVPVIVEK HHHHCCCCCCEEEEE	30.09	-
35	Acetylation	RVPVIVEKVSGSQIV CCCEEEEECCCCCEE	30.70	129671
37	Phosphorylation	PVIVEKVSGSQIVDI CEEEEECCCCCEEEC	43.74	23312004
39	Phosphorylation	IVEKVSGSQIVDIDK EEEECCCCCEEECCC	14.82	17525332
46	Acetylation	SQIVDIDKRKYLVPS CCEEECCCCCCCCCC	51.64	23749302
46	Malonylation	SQIVDIDKRKYLVPS CCEEECCCCCCCCCC	51.64	26320211
46	Ubiquitination	SQIVDIDKRKYLVPS CCEEECCCCCCCCCC	51.64	29967540
74	Ubiquitination	RIQLPSEKAIFLFVD HCCCCCCCEEEEEEE	51.63	33845483
74	Acetylation	RIQLPSEKAIFLFVD HCCCCCCCEEEEEEE	51.63	129667
83	Phosphorylation	IFLFVDKTVPQSSLT EEEEEECCCCHHHCC	32.71	26074081
87	Phosphorylation	VDKTVPQSSLTMGQL EECCCCHHHCCCCCE	22.65	26074081
88	Phosphorylation	DKTVPQSSLTMGQLY ECCCCHHHCCCCCEE	23.70	26074081
90	Phosphorylation	TVPQSSLTMGQLYEK CCCHHHCCCCCEEEE	22.62	26074081
97	Ubiquitination	TMGQLYEKEKDEDGF CCCCEEEEECCCCCC	57.41	32015554
116	Phosphatidylethanolamine amidation	YSGENTFGF------ ECCCCCCCC------	25.89	12507496

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
87	S	Phosphorylation	Kinase	TBK1	Q9UHD2	PSP
88	S	Phosphorylation	Kinase	TBK1	Q9UHD2	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GBRL2_HUMAN !!

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 GBRL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
B2L13_HUMAN	BCL2L13	physical	16189514
UBA5_HUMAN	UBA5	physical	16189514
IRGQ_HUMAN	IRGQ	physical	17353931
ATG4B_HUMAN	ATG4B	physical	17353931
ATG3_HUMAN	ATG3	physical	17353931
LPPRC_HUMAN	LRPPRC	physical	17353931
IF4G1_HUMAN	EIF4G1	physical	17353931
EZRI_HUMAN	EZR	physical	17353931
NEK9_HUMAN	NEK9	physical	17353931
VDAC1_HUMAN	VDAC1	physical	17353931
HBG1_HUMAN	HBG1	physical	17353931
RAP2A_HUMAN	RAP2A	physical	12581858
RAP1A_HUMAN	RAP1A	physical	12581858
ATG4B_HUMAN	ATG4B	physical	16169070
ULK1_HUMAN	ULK1	physical	11146101
WDR62_HUMAN	WDR62	physical	20562859
NEDD4_HUMAN	NEDD4	physical	20562859
NEK9_HUMAN	NEK9	physical	20562859
UBA5_HUMAN	UBA5	physical	20562859
SQSTM_HUMAN	SQSTM1	physical	20562859
NIPS2_HUMAN	GBAS	physical	20562859
ATG7_HUMAN	ATG7	physical	20562859
NIPS1_HUMAN	NIPSNAP1	physical	20562859
ECHB_HUMAN	HADHB	physical	20562859
NBR1_HUMAN	NBR1	physical	20562859
TM160_HUMAN	TMEM160	physical	20562859
ECHA_HUMAN	HADHA	physical	20562859
KPCI_HUMAN	PRKCI	physical	20562859
ATG4B_HUMAN	ATG4B	physical	20562859
IPO5_HUMAN	IPO5	physical	20562859
KEAP1_HUMAN	KEAP1	physical	20562859
ATG3_HUMAN	ATG3	physical	20562859
RCN2_HUMAN	RCN2	physical	20562859
CUL3_HUMAN	CUL3	physical	20562859
HACD3_HUMAN	PTPLAD1	physical	20562859
STBD1_HUMAN	STBD1	physical	20562859
ATG7_HUMAN	ATG7	physical	11096062
RS2_HUMAN	RPS2	physical	21900206
KLHL5_HUMAN	KLHL5	physical	21900206
SQSTM_HUMAN	SQSTM1	physical	21900206
PTPRA_HUMAN	PTPRA	physical	21900206
UBA5_HUMAN	UBA5	physical	21900206
AAMP_HUMAN	AAMP	physical	21900206
KBTB7_HUMAN	KBTBD7	physical	21900206
1433Z_HUMAN	YWHAZ	physical	21900206
ATG13_HUMAN	ATG13	physical	21900206
ATG4B_HUMAN	ATG4B	physical	21900206
RCN2_HUMAN	RCN2	physical	21900206
TBC25_HUMAN	TBC1D25	physical	21383079
SQSTM_HUMAN	SQSTM1	physical	21460636
TBCD9_HUMAN	TBC1D9	physical	22354992
TBC9B_HUMAN	TBC1D9B	physical	22354992
ULK1_HUMAN	ULK1	physical	23043107
ATG13_HUMAN	ATG13	physical	23043107
ULK2_HUMAN	ULK2	physical	23043107
A4_HUMAN	APP	physical	21832049
VAPA_HUMAN	VAPA	physical	23142642
BNI3L_HUMAN	BNIP3L	physical	20010802
SGTA_HUMAN	SGTA	physical	21988832
TBC9B_HUMAN	TBC1D9B	physical	25416956
SIK2_HUMAN	SIK2	physical	25416956
B2L13_HUMAN	BCL2L13	physical	25416956
ARFG1_HUMAN	ARFGAP1	physical	25416956
ATRAP_HUMAN	AGTRAP	physical	25416956
CACO1_HUMAN	CALCOCO1	physical	25416956
UBA5_HUMAN	UBA5	physical	25416956
TSR2_HUMAN	TSR2	physical	25416956
AHNK2_HUMAN	AHNAK2	physical	25416956
FUND1_HUMAN	FUNDC1	physical	25416956
KASH5_HUMAN	CCDC155	physical	25416956
K1958_HUMAN	KIAA1958	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
GIMA6_HUMAN	GIMAP6	physical	25416956
WDFY3_HUMAN	WDFY3	physical	24668264
KBTB7_HUMAN	KBTBD7	physical	25684205
KBTB6_HUMAN	KBTBD6	physical	25684205
CUL3_HUMAN	CUL3	physical	25684205
SQSTM_HUMAN	SQSTM1	physical	21516116
RO52_HUMAN	TRIM21	physical	26347139
CACO2_HUMAN	CALCOCO2	physical	25771791
TBC25_HUMAN	TBC1D25	physical	26902585

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
There are no disease associations of PTM sites.

Regulatory Network of GBRL2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-24, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.	17287340 [Abstract]