dbPTM

ATG4B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATG4B_HUMAN
UniProt AC	Q9Y4P1
Protein Name	Cysteine protease ATG4B
Gene Name	ATG4B
Organism	Homo sapiens (Human).
Sequence Length	393
Subcellular Localization	Cytoplasm.
Protein Description	Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Cleaves the C-terminal amino acid of ATG8 family proteins MAP1LC3, GABARAPL1, GABARAPL2 and GABARAP, to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Has also an activity of delipidating enzyme for the PE-conjugated forms..
Protein Sequence	MDAATLTYDTLRFAEFEDFPETSEPVWILGRKYSIFTEKDEILSDVASRLWFTYRKNFPAIGGTGPTSDTGWGCMLRCGQMIFAQALVCRHLGRDWRWTQRKRQPDSYFSVLNAFIDRKDSYYSIHQIAQMGVGEGKSIGQWYGPNTVAQVLKKLAVFDTWSSLAVHIAMDNTVVMEEIRRLCRTSVPCAGATAFPADSDRHCNGFPAGAEVTNRPSPWRPLVLLIPLRLGLTDINEAYVETLKHCFMMPQSLGVIGGKPNSAHYFIGYVGEELIYLDPHTTQPAVEPTDGCFIPDESFHCQHPPCRMSIAELDPSIAVGFFCKTEDDFNDWCQQVKKLSLLGGALPMFELVELQPSHLACPDVLNLSLDSSDVERLERFFDSEDEDFEILSL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDAATLTY -------CCCCCCCC	7.74	22223895
5	Phosphorylation	---MDAATLTYDTLR ---CCCCCCCCCHHH	22.73	28111955
7	Phosphorylation	-MDAATLTYDTLRFA -CCCCCCCCCHHHHH	18.26	28442448
8	Phosphorylation	MDAATLTYDTLRFAE CCCCCCCCCHHHHHC	15.28	25106551
10	Phosphorylation	AATLTYDTLRFAEFE CCCCCCCHHHHHCCC	14.93	28442448
33	Phosphorylation	VWILGRKYSIFTEKD EEECCCCEEECCCHH	12.97	26434776
34	Phosphorylation	WILGRKYSIFTEKDE EECCCCEEECCCHHH	17.79	25849741
37	Phosphorylation	GRKYSIFTEKDEILS CCCEEECCCHHHHHH	40.22	26434776
39	Ubiquitination	KYSIFTEKDEILSDV CEEECCCHHHHHHHH	58.57	-
44	Phosphorylation	TEKDEILSDVASRLW CCHHHHHHHHHHHHH	35.38	26434776
69 (in isoform 2)	Phosphorylation	-	52.28	-
79 (in isoform 3)	Ubiquitination	-	17.41	21906983
96 (in isoform 2)	Phosphorylation	-	9.06	28064214
102	Ubiquitination	DWRWTQRKRQPDSYF CCCCCCCCCCCCCCH	45.63	-
119	Ubiquitination	LNAFIDRKDSYYSIH HHHHHCCCCCCEEHH	47.48	-
122	Phosphorylation	FIDRKDSYYSIHQIA HHCCCCCCEEHHHHH	16.03	-
123	Phosphorylation	IDRKDSYYSIHQIAQ HCCCCCCEEHHHHHH	12.71	-
153 (in isoform 1)	Ubiquitination	-	47.05	21906983
153 (in isoform 6)	Ubiquitination	-	47.05	21906983
153	Ubiquitination	NTVAQVLKKLAVFDT HHHHHHHHHHHCHHC	47.05	2190698
207 (in isoform 2)	Ubiquitination	-	31.05	-
241 (in isoform 2)	Ubiquitination	-	35.43	21906983
242 (in isoform 2)	Ubiquitination	-	30.94	-
270 (in isoform 4)	Ubiquitination	-	7.02	21906983
316	Phosphorylation	SIAELDPSIAVGFFC EHHHCCCCEEEEEEE	23.89	18187866
321 (in isoform 4)	Phosphorylation	-	5.37	29507054
337	Ubiquitination	NDWCQQVKKLSLLGG HHHHHHHHHHHHHCC	43.59	-
337	Acetylation	NDWCQQVKKLSLLGG HHHHHHHHHHHHHCC	43.59	25953088
368	Phosphorylation	CPDVLNLSLDSSDVE CCCCCCCCCCHHHHH	29.11	28464451
383	Phosphorylation	RLERFFDSEDEDFEI HHHHHHCCCCCCCEE	41.62	19664994
392	Phosphorylation	DEDFEILSL------ CCCCEEECC------	37.38	25159151
425 (in isoform 2)	Ubiquitination	-		-

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
34	S	Phosphorylation	Kinase	AKT1	P31749	PSP
316	S	Phosphorylation	Kinase	ULK1	O75385	PSP
383	S	Phosphorylation	Kinase	MST4	Q9P289	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ATG4B_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 ATG4B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GBRL1_HUMAN	GABARAPL1	physical	20562859
GBRAP_HUMAN	GABARAP	physical	20562859
GBRL2_HUMAN	GABARAPL2	physical	20562859
ANXA1_HUMAN	ANXA1	physical	20562859
GBRL1_HUMAN	GABARAPL1	physical	16704426
MLP3B_HUMAN	MAP1LC3B	physical	15355958
MLP3A_HUMAN	MAP1LC3A	physical	19322194
MLP3A_HUMAN	MAP1LC3A	physical	19549685
GBRL2_HUMAN	GABARAPL2	physical	19549685
GBRL1_HUMAN	GABARAPL1	physical	19549685

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 ATG4B_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND SER-392, ANDMASS SPECTROMETRY.	17081983 [Abstract]