dbPTM

ADAS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ADAS_HUMAN
UniProt AC	O00116
Protein Name	Alkyldihydroxyacetonephosphate synthase, peroxisomal
Gene Name	AGPS
Organism	Homo sapiens (Human).
Sequence Length	658
Subcellular Localization	Peroxisome membrane. Localized to the inner aspect of the peroxisomal membrane.
Protein Description	Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids..
Protein Sequence	MAEAAAAAGGTGLGAGASYGSAADRDRDPDPDRAGRRLRVLSGHLLGRPREALSTNECKARRAASAATAAPTATPAAQESGTIPKKRQEVMKWNGWGYNDSKFIFNKKGQIELTGKRYPLSGMGLPTFKEWIQNTLGVNVEHKTTSKASLNPSDTPPSVVNEDFLHDLKETNISYSQEADDRVFRAHGHCLHEIFLLREGMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPQVSSIFTSFLDGLKKFYITKFKGFDPNQLSVATLLFEGDREKVLQHEKQVYDIAAKFGGLAAGEDNGQRGYLLTYVIAYIRDLALEYYVLGESFETSAPWDRVVDLCRNVKERITRECKEKGVQFAPFSTCRVTQTYDAGACIYFYFAFNYRGISDPLTVFEQTEAAAREEILANGGSLSHHHGVGKLRKQWLKESISDVGFGMLKSVKEYVDPNNIFGNRNLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	AAAAAGGTGLGAGAS HHHHCCCCCCCCCCC	28.46	20068231
18	Phosphorylation	TGLGAGASYGSAADR CCCCCCCCCCCCCCC	29.16	20068231
19	Phosphorylation	GLGAGASYGSAADRD CCCCCCCCCCCCCCC	17.99	20068231
21	Phosphorylation	GAGASYGSAADRDRD CCCCCCCCCCCCCCC	16.43	20068231
42	Phosphorylation	GRRLRVLSGHLLGRP HHHHHHHHHHHCCCC	22.70	22617229
65	Phosphorylation	CKARRAASAATAAPT HHHHHHHHHHHHCCC	19.90	29255136
68	Phosphorylation	RRAASAATAAPTATP HHHHHHHHHCCCCCH	24.06	30266825
72	Phosphorylation	SAATAAPTATPAAQE HHHHHCCCCCHHHHH	38.14	30266825
74	Phosphorylation	ATAAPTATPAAQESG HHHCCCCCHHHHHHC	18.88	30266825
80	Phosphorylation	ATPAAQESGTIPKKR CCHHHHHHCCCCHHH	29.20	30266825
82	Phosphorylation	PAAQESGTIPKKRQE HHHHHHCCCCHHHHH	43.30	30266825
85	Ubiquitination	QESGTIPKKRQEVMK HHHCCCCHHHHHHHH	57.65	21890473
92	Ubiquitination	KKRQEVMKWNGWGYN HHHHHHHHHCCCCCC	42.56	21890473
101	Phosphorylation	NGWGYNDSKFIFNKK CCCCCCCCCEEEECC	26.31	21601212
102	Acetylation	GWGYNDSKFIFNKKG CCCCCCCCEEEECCC	45.39	19608861
102	Ubiquitination	GWGYNDSKFIFNKKG CCCCCCCCEEEECCC	45.39	21890473
107	Acetylation	DSKFIFNKKGQIELT CCCEEEECCCEEEEC	47.75	26051181
108	Ubiquitination	SKFIFNKKGQIELTG CCEEEECCCEEEECC	58.09	-
108	Acetylation	SKFIFNKKGQIELTG CCEEEECCCEEEECC	58.09	25953088
108	Malonylation	SKFIFNKKGQIELTG CCEEEECCCEEEECC	58.09	26320211
116	2-Hydroxyisobutyrylation	GQIELTGKRYPLSGM CEEEECCCEECCCCC	43.45	-
116	Ubiquitination	GQIELTGKRYPLSGM CEEEECCCEECCCCC	43.45	-
116	Acetylation	GQIELTGKRYPLSGM CEEEECCCEECCCCC	43.45	25953088
118	Phosphorylation	IELTGKRYPLSGMGL EEECCCEECCCCCCC	16.41	21406692
121	Phosphorylation	TGKRYPLSGMGLPTF CCCEECCCCCCCHHH	23.41	21406692
127	Phosphorylation	LSGMGLPTFKEWIQN CCCCCCHHHHHHHHH	53.00	21406692
143	Acetylation	LGVNVEHKTTSKASL HCCCCEECCCCCCCC	39.74	25953088
143	Ubiquitination	LGVNVEHKTTSKASL HCCCCEECCCCCCCC	39.74	-
147	Ubiquitination	VEHKTTSKASLNPSD CEECCCCCCCCCCCC	39.64	-
149	Phosphorylation	HKTTSKASLNPSDTP ECCCCCCCCCCCCCC	32.20	29255136
153	Phosphorylation	SKASLNPSDTPPSVV CCCCCCCCCCCCCCC	53.71	29255136
155	Phosphorylation	ASLNPSDTPPSVVNE CCCCCCCCCCCCCCH	41.24	29255136
158	Phosphorylation	NPSDTPPSVVNEDFL CCCCCCCCCCCHHHH	39.64	29255136
169	Acetylation	EDFLHDLKETNISYS HHHHHHHHHCCCCCC	69.42	23954790
169	Ubiquitination	EDFLHDLKETNISYS HHHHHHHHHCCCCCC	69.42	19608861
174	Phosphorylation	DLKETNISYSQEADD HHHHCCCCCCHHHHH	22.32	28674419
220	Acetylation	TCHDDVVKIVNLACK CCCCHHHHHHHHHHC	40.56	26051181
257	Phosphorylation	DETRTIISLDTSQMN CCCCEEEEECHHHCC	19.15	21712546
261	Phosphorylation	TIISLDTSQMNRILW EEEEECHHHCCEEEE	27.39	21712546
263	Sulfoxidation	ISLDTSQMNRILWVD EEECHHHCCEEEEEE	3.49	21406390
292	Acetylation	QELERQLKESGYCTG HHHHHHHHHHCCCCC	41.31	26051181
323	Ubiquitination	TRASGMKKNIYGNIE HCCCCCCCCCCCCHH	39.42	-
326	Phosphorylation	SGMKKNIYGNIEDLV CCCCCCCCCCHHHHE	17.32	20068231
347	Acetylation	TPRGIIEKSCQGPRM CCCCHHHHHCCCCCC	46.23	19608861
347	Ubiquitination	TPRGIIEKSCQGPRM CCCCHHHHHCCCCCC	46.23	19608861
375	Phosphorylation	EGTLGVITEATIKIR CCCEEEEEEEEEEEE	19.70	30387612
378	Phosphorylation	LGVITEATIKIRPVP EEEEEEEEEEEEECC	19.30	30387612
387	Phosphorylation	KIRPVPEYQKYGSVA EEEECCCHHCCCCCC	12.30	28152594
389	Ubiquitination	RPVPEYQKYGSVAFP EECCCHHCCCCCCCC	51.15	-
390	Phosphorylation	PVPEYQKYGSVAFPN ECCCHHCCCCCCCCC	10.10	28152594
392	Phosphorylation	PEYQKYGSVAFPNFE CCHHCCCCCCCCCHH	13.74	28152594
417	Phosphorylation	KQRCAPASIRLMDNK HHHCCCCEEEECCCC	13.74	23532336
456	Ubiquitination	KFYITKFKGFDPNQL HEEEEECCCCCHHHC	61.29	21890473
476	Ubiquitination	LFEGDREKVLQHEKQ EECCCHHHHHHHHHH	49.49	-
482	Ubiquitination	EKVLQHEKQVYDIAA HHHHHHHHHHHHHHH	42.83	-
482	2-Hydroxyisobutyrylation	EKVLQHEKQVYDIAA HHHHHHHHHHHHHHH	42.83	-
482	Acetylation	EKVLQHEKQVYDIAA HHHHHHHHHHHHHHH	42.83	25953088
490	Ubiquitination	QVYDIAAKFGGLAAG HHHHHHHHHCCEECC	35.20	21890473
555	Acetylation	ITRECKEKGVQFAPF HHHHHHHCCCCCCCC	50.29	25953088
589	Phosphorylation	AFNYRGISDPLTVFE ECCCCCCCCCCHHHH	35.68	23663014
593	Phosphorylation	RGISDPLTVFEQTEA CCCCCCCHHHHHHHH	28.65	23403867
628	Methylation	KLRKQWLKESISDVG HHHHHHHHHHHHHHC	46.59	-
630	Phosphorylation	RKQWLKESISDVGFG HHHHHHHHHHHHCCH	26.29	30377224
632	Phosphorylation	QWLKESISDVGFGML HHHHHHHHHHCCHHH	35.21	63773457
640	Ubiquitination	DVGFGMLKSVKEYVD HHCCHHHHHHHHHCC	44.29	-
640	Acetylation	DVGFGMLKSVKEYVD HHCCHHHHHHHHHCC	44.29	26051181
641	Phosphorylation	VGFGMLKSVKEYVDP HCCHHHHHHHHHCCC	34.16	28152594
643	Ubiquitination	FGMLKSVKEYVDPNN CHHHHHHHHHCCCCC	50.87	-
645	Phosphorylation	MLKSVKEYVDPNNIF HHHHHHHHCCCCCCC	12.39	65571

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

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GNPAT_HUMAN	GNPAT	physical	10215861
IDH3G_HUMAN	IDH3G	physical	22939629
LEG3_HUMAN	LGALS3	physical	22939629
NLTP_HUMAN	SCP2	physical	22939629
CSRP2_HUMAN	CSRP2	physical	22939629
GORS1_HUMAN	GORASP1	physical	25416956
LMAN1_HUMAN	LMAN1	physical	26344197

Drug and Disease Associations

Kegg Disease
H00207	Rhizomelic chondrodysplasia punctata, including: Rhizomelic chondrodysplasia punctata, type I (RCDP1
OMIM Disease
600121	Rhizomelic chondrodysplasia punctata 3 (RCDP3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ADAS_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-102; LYS-169 AND LYS-347,AND MASS SPECTROMETRY.	19608861 [Abstract]