6PGD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: 6PGD_HUMAN
• UniProt AC: P52209
• Protein Name: 6-phosphogluconate dehydrogenase, decarboxylating
• Gene Name: PGD
• Organism: Homo sapiens (Human).
• Sequence Length: 483
• Subcellular Localization: Cytoplasm.
• Protein Description: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH..
• Protein Sequence: MAQADIALIGLAVMGQNLILNMNDHGFVVCAFNRTVSKVDDFLANEAKGTKVVGAQSLKEMVSKLKKPRRIILLVKAGQAVDDFIEKLVPLLDTGDIIIDGGNSEYRDTTRRCRDLKAKGILFVGSGVSGGEEGARYGPSLMPGGNKEAWPHIKTIFQGIAAKVGTGEPCCDWVGDEGAGHFVKMVHNGIEYGDMQLICEAYHLMKDVLGMAQDEMAQAFEDWNKTELDSFLIEITANILKFQDTDGKHLLPKIRDSAGQKGTGKWTAISALEYGVPVTLIGEAVFARCLSSLKDERIQASKKLKGPQKFQFDGDKKSFLEDIRKALYASKIISYAQGFMLLRQAATEFGWTLNYGGIALMWRGGCIIRSVFLGKIKDAFDRNPELQNLLLDDFFKSAVENCQDSWRRAVSTGVQAGIPMPCFTTALSFYDGYRHEMLPASLIQAQRDYFGAHTYELLAKPGQFIHTNWTGHGGTVSSSSYNA

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
25	Acetylation	LILNMNDHGFVVCAF EEEECCCCCEEEEEE	26.96	-
25	Ubiquitination	LILNMNDHGFVVCAF EEEECCCCCEEEEEE	26.96	-
25	Acetylation	LILNMNDHGFVVCAF EEEECCCCCEEEEEE	26.96	19608861
25	Ubiquitination	LILNMNDHGFVVCAF EEEECCCCCEEEEEE	26.96	19608861
35	Ubiquitination	VVCAFNRTVSKVDDF EEEEEECCCCCHHHH	30.18	-
35	Phosphorylation	VVCAFNRTVSKVDDF EEEEEECCCCCHHHH	30.18	28450419
37	Phosphorylation	CAFNRTVSKVDDFLA EEEECCCCCHHHHHH	26.75	29978859
38	Ubiquitination	AFNRTVSKVDDFLAN EEECCCCCHHHHHHH	45.40	21890473
38	Ubiquitination	AFNRTVSKVDDFLAN EEECCCCCHHHHHHH	45.40	21890473
38	Acetylation	AFNRTVSKVDDFLAN EEECCCCCHHHHHHH	45.40	23954790
38	Malonylation	AFNRTVSKVDDFLAN EEECCCCCHHHHHHH	45.40	26320211
38	Ubiquitination	AFNRTVSKVDDFLAN EEECCCCCHHHHHHH	45.40	21890473
46	Acetylation	VDDFLANEAKGTKVV HHHHHHHCCCCCCEE	46.26	-
46	Ubiquitination	VDDFLANEAKGTKVV HHHHHHHCCCCCCEE	46.26	-
46	Acetylation	VDDFLANEAKGTKVV HHHHHHHCCCCCCEE	46.26	19608861
46	Ubiquitination	VDDFLANEAKGTKVV HHHHHHHCCCCCCEE	46.26	19608861
48	2-Hydroxyisobutyrylation	DFLANEAKGTKVVGA HHHHHCCCCCCEECC	62.02	-
48	Malonylation	DFLANEAKGTKVVGA HHHHHCCCCCCEECC	62.02	26320211
48	Ubiquitination	DFLANEAKGTKVVGA HHHHHCCCCCCEECC	62.02	21906983
50	Phosphorylation	LANEAKGTKVVGAQS HHHCCCCCCEECCHH	21.69	22210691
51	Malonylation	ANEAKGTKVVGAQSL HHCCCCCCEECCHHH	43.52	32601280
51	Ubiquitination	ANEAKGTKVVGAQSL HHCCCCCCEECCHHH	43.52	-
57	Phosphorylation	TKVVGAQSLKEMVSK CCEECCHHHHHHHHH	40.66	22210691
59	Ubiquitination	VVGAQSLKEMVSKLK EECCHHHHHHHHHCC	49.35	21890473
59	Ubiquitination	VVGAQSLKEMVSKLK EECCHHHHHHHHHCC	49.35	21890473
59	2-Hydroxyisobutyrylation	VVGAQSLKEMVSKLK EECCHHHHHHHHHCC	49.35	-
59	Acetylation	VVGAQSLKEMVSKLK EECCHHHHHHHHHCC	49.35	19608861
59	Malonylation	VVGAQSLKEMVSKLK EECCHHHHHHHHHCC	49.35	26320211
59	Ubiquitination	VVGAQSLKEMVSKLK EECCHHHHHHHHHCC	49.35	21890473
63	Acetylation	QSLKEMVSKLKKPRR HHHHHHHHHCCCCCE	30.84	19608861
74	Acetylation	KPRRIILLVKAGQAV CCCEEEEEEECCHHH	2.33	-
76	2-Hydroxyisobutyrylation	RRIILLVKAGQAVDD CEEEEEEECCHHHHH	46.93	-
76	Acetylation	RRIILLVKAGQAVDD CEEEEEEECCHHHHH	46.93	19608861
87	Acetylation	AVDDFIEKLVPLLDT HHHHHHHHHHHHHCC	50.39	21466224
94	Phosphorylation	KLVPLLDTGDIIIDG HHHHHHCCCCEEEEC	36.40	24076635
104	Phosphorylation	IIIDGGNSEYRDTTR EEEECCCHHHCCCCH	39.00	21712546
106	Ubiquitination	IDGGNSEYRDTTRRC EECCCHHHCCCCHHH	17.38	-
106	Phosphorylation	IDGGNSEYRDTTRRC EECCCHHHCCCCHHH	17.38	-
119	Ubiquitination	RCRDLKAKGILFVGS HHHHHCCCCEEEEEC	44.92	21890473
119	Ubiquitination	RCRDLKAKGILFVGS HHHHHCCCCEEEEEC	44.92	21890473
119	2-Hydroxyisobutyrylation	RCRDLKAKGILFVGS HHHHHCCCCEEEEEC	44.92	-
119	Ubiquitination	RCRDLKAKGILFVGS HHHHHCCCCEEEEEC	44.92	21906983
126	Phosphorylation	KGILFVGSGVSGGEE CCEEEEECCCCCCCC	30.62	23403867
129	Phosphorylation	LFVGSGVSGGEEGAR EEEECCCCCCCCCCC	44.60	25159151
134	Ubiquitination	GVSGGEEGARYGPSL CCCCCCCCCCCCCCC	15.85	-
141	Acetylation	GARYGPSLMPGGNKE CCCCCCCCCCCCCCC	5.59	-
141	Ubiquitination	GARYGPSLMPGGNKE CCCCCCCCCCCCCCC	5.59	-
141	Acetylation	GARYGPSLMPGGNKE CCCCCCCCCCCCCCC	5.59	19608861
141	Ubiquitination	GARYGPSLMPGGNKE CCCCCCCCCCCCCCC	5.59	19608861
142	Sulfoxidation	ARYGPSLMPGGNKEA CCCCCCCCCCCCCCC	3.21	30846556
147	Acetylation	SLMPGGNKEAWPHIK CCCCCCCCCCCHHHH	52.67	7430939
147	Ubiquitination	SLMPGGNKEAWPHIK CCCCCCCCCCCHHHH	52.67	-
150	Ubiquitination	PGGNKEAWPHIKTIF CCCCCCCCHHHHHHH	6.01	-
154	Ubiquitination	KEAWPHIKTIFQGIA CCCCHHHHHHHHHHH	32.31	21890473
154	Ubiquitination	KEAWPHIKTIFQGIA CCCCHHHHHHHHHHH	32.31	21890473
154	Acetylation	KEAWPHIKTIFQGIA CCCCHHHHHHHHHHH	32.31	23236377
154	Ubiquitination	KEAWPHIKTIFQGIA CCCCHHHHHHHHHHH	32.31	21890473
163	Acetylation	IFQGIAAKVGTGEPC HHHHHHHHHCCCCCC	31.98	25953088
163	Ubiquitination	IFQGIAAKVGTGEPC HHHHHHHHHCCCCCC	31.98	-
166	Phosphorylation	GIAAKVGTGEPCCDW HHHHHHCCCCCCCCC	41.16	25159151
184	Ubiquitination	EGAGHFVKMVHNGIE CCCHHHHHCCCCCCC	33.97	-
235	Ubiquitination	LDSFLIEITANILKF HHHHHHHHHHHHHHE	3.32	-
248	2-Hydroxyisobutyrylation	KFQDTDGKHLLPKIR HEECCCCCCCCHHHH	33.61	-
248	Acetylation	KFQDTDGKHLLPKIR HEECCCCCCCCHHHH	33.61	25825284
248	Ubiquitination	KFQDTDGKHLLPKIR HEECCCCCCCCHHHH	33.61	-
252	Ubiquitination	TDGKHLLPKIRDSAG CCCCCCCHHHHCCCC	36.07	-
253	2-Hydroxyisobutyrylation	DGKHLLPKIRDSAGQ CCCCCCHHHHCCCCC	50.79	-
253	Ubiquitination	DGKHLLPKIRDSAGQ CCCCCCHHHHCCCCC	50.79	-
257	Phosphorylation	LLPKIRDSAGQKGTG CCHHHHCCCCCCCCC	25.17	24719451
261	Ubiquitination	IRDSAGQKGTGKWTA HHCCCCCCCCCCCHH	58.48	-
263	Phosphorylation	DSAGQKGTGKWTAIS CCCCCCCCCCCHHHH	42.49	18785766
265	Ubiquitination	AGQKGTGKWTAISAL CCCCCCCCCHHHHHH	41.01	-
281	Ubiquitination	YGVPVTLIGEAVFAR HCCCEEEEHHHHHHH	3.24	-
291	Phosphorylation	AVFARCLSSLKDERI HHHHHHHHCCCHHHH	36.93	24719451
292	Phosphorylation	VFARCLSSLKDERIQ HHHHHHHCCCHHHHH	26.87	24719451
294	Acetylation	ARCLSSLKDERIQAS HHHHHCCCHHHHHHH	60.53	25953088
294	Ubiquitination	ARCLSSLKDERIQAS HHHHHCCCHHHHHHH	60.53	-
296	Acetylation	CLSSLKDERIQASKK HHHCCCHHHHHHHHH	50.53	-
296	Acetylation	CLSSLKDERIQASKK HHHCCCHHHHHHHHH	50.53	19608861
303	Acetylation	ERIQASKKLKGPQKF HHHHHHHHCCCCCCC	53.59	-
303	Ubiquitination	ERIQASKKLKGPQKF HHHHHHHHCCCCCCC	53.59	-
304	Ubiquitination	RIQASKKLKGPQKFQ HHHHHHHCCCCCCCC	9.97	-
309	2-Hydroxyisobutyrylation	KKLKGPQKFQFDGDK HHCCCCCCCCCCCCH	44.24	-
309	Acetylation	KKLKGPQKFQFDGDK HHCCCCCCCCCCCCH	44.24	19608861
309	Ubiquitination	KKLKGPQKFQFDGDK HHCCCCCCCCCCCCH	44.24	19608861
316	2-Hydroxyisobutyrylation	KFQFDGDKKSFLEDI CCCCCCCHHHHHHHH	56.71	-
316	Acetylation	KFQFDGDKKSFLEDI CCCCCCCHHHHHHHH	56.71	23749302
316	Ubiquitination	KFQFDGDKKSFLEDI CCCCCCCHHHHHHHH	56.71	-
317	2-Hydroxyisobutyrylation	FQFDGDKKSFLEDIR CCCCCCHHHHHHHHH	51.70	-
317	Acetylation	FQFDGDKKSFLEDIR CCCCCCHHHHHHHHH	51.70	26822725
317	Ubiquitination	FQFDGDKKSFLEDIR CCCCCCHHHHHHHHH	51.70	-
318	Phosphorylation	QFDGDKKSFLEDIRK CCCCCHHHHHHHHHH	40.58	27050516
324	Methylation	KSFLEDIRKALYASK HHHHHHHHHHHHHHH	30.43	115487209
325	2-Hydroxyisobutyrylation	SFLEDIRKALYASKI HHHHHHHHHHHHHHH	42.98	-
334	Phosphorylation	LYASKIISYAQGFML HHHHHHHHHHHHHHH	20.21	23917254
335	Phosphorylation	YASKIISYAQGFMLL HHHHHHHHHHHHHHH	7.79	23917254
340	Sulfoxidation	ISYAQGFMLLRQAAT HHHHHHHHHHHHHHH	4.39	30846556
364	Ubiquitination	GIALMWRGGCIIRSV CEEEEEECCEEHHHH	21.58	-
375	Acetylation	IRSVFLGKIKDAFDR HHHHHHHHHHHHHHC	49.05	25953088
377	2-Hydroxyisobutyrylation	SVFLGKIKDAFDRNP HHHHHHHHHHHHCCH	46.63	-
377	Ubiquitination	SVFLGKIKDAFDRNP HHHHHHHHHHHHCCH	46.63	21906983
447	Ubiquitination	ASLIQAQRDYFGAHT HHHHHHHHHHHCCCH	43.54	-
449	Phosphorylation	LIQAQRDYFGAHTYE HHHHHHHHHCCCHHH	13.20	28152594
454	Phosphorylation	RDYFGAHTYELLAKP HHHHCCCHHHHHCCC	20.39	28796482
455	Phosphorylation	DYFGAHTYELLAKPG HHHCCCHHHHHCCCC	8.50	28796482
460	Ubiquitination	HTYELLAKPGQFIHT CHHHHHCCCCCEEEC	50.04	-
467	Phosphorylation	KPGQFIHTNWTGHGG CCCCEEECCCCCCCC	27.86	29514088
470	Phosphorylation	QFIHTNWTGHGGTVS CEEECCCCCCCCCCC	22.75	20068231
475	Phosphorylation	NWTGHGGTVSSSSYN CCCCCCCCCCCCCCC	23.08	28450419
477	Phosphorylation	TGHGGTVSSSSYNA- CCCCCCCCCCCCCC-	25.08	28796482
478	Phosphorylation	GHGGTVSSSSYNA-- CCCCCCCCCCCCC--	20.97	28796482
479	Phosphorylation	HGGTVSSSSYNA--- CCCCCCCCCCCC---	29.36	28796482
480	Phosphorylation	GGTVSSSSYNA---- CCCCCCCCCCC----	25.10	28464451
481	Phosphorylation	GTVSSSSYNA----- CCCCCCCCCC-----	19.63	28796482

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
481	Y	Phosphorylation	Kinase	FYN	P06241	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of 6PGD_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 6PGD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AL7A1_HUMAN	ALDH7A1	physical	22863883
AL9A1_HUMAN	ALDH9A1	physical	22863883
EF2_HUMAN	EEF2	physical	22863883
AGAL_HUMAN	GLA	physical	22863883
GNAI3_HUMAN	GNAI3	physical	22863883
HMGB2_HUMAN	HMGB2	physical	22863883
KS6A1_HUMAN	RPS6KA1	physical	22863883
TXND5_HUMAN	TXNDC5	physical	22863883
FABP5_HUMAN	FABP5	physical	26344197
GDIA_HUMAN	GDI1	physical	26344197
PDIA1_HUMAN	P4HB	physical	26344197
SUMO3_HUMAN	SUMO3	physical	26344197
TALDO_HUMAN	TALDO1	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
• DB00851: Dacarbazine
• DB00695: Furosemide
• DB00789: Gadopentetate dimeglumine
• DB00920: Ketotifen
• DB00814: Meloxicam
• DB00563: Methotrexate
• DB00867: Ritodrine

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-38; LYS-59; LYS-76; LYS-154AND LYS-309, AND MASS SPECTROMETRY.
PubMed: 19608861