dbPTM

PUR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PUR1_HUMAN
UniProt AC	Q06203
Protein Name	Amidophosphoribosyltransferase
Gene Name	PPAT
Organism	Homo sapiens (Human).
Sequence Length	517
Subcellular Localization
Protein Description
Protein Sequence	MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPTFKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFLSIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKEKKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MELEELGI -------CCHHHHCC	13.80	22814378
52	Phosphorylation	QESAGIVTSDGSSVP CCCCCEECCCCCCCC	21.12	-
62	Ubiquitination	GSSVPTFKSHKGMGL CCCCCCCCCCCCCCC	54.88	-
62	Methylation	GSSVPTFKSHKGMGL CCCCCCCCCCCCCCC	54.88	-
62	Acetylation	GSSVPTFKSHKGMGL CCCCCCCCCCCCCCC	54.88	23954790
62	Malonylation	GSSVPTFKSHKGMGL CCCCCCCCCCCCCCC	54.88	26320211
65	Ubiquitination	VPTFKSHKGMGLVNH CCCCCCCCCCCCCCE	58.65	-
67	Sulfoxidation	TFKSHKGMGLVNHVF CCCCCCCCCCCCEEE	4.47	21406390
80	Acetylation	VFTEDNLKKLYVSNL EECHHHHHHEEEECC	47.16	23236377
80	Ubiquitination	VFTEDNLKKLYVSNL EECHHHHHHEEEECC	47.16	21890473
80	2-Hydroxyisobutyrylation	VFTEDNLKKLYVSNL EECHHHHHHEEEECC	47.16	-
81	Malonylation	FTEDNLKKLYVSNLG ECHHHHHHEEEECCC	48.49	26320211
81	Ubiquitination	FTEDNLKKLYVSNLG ECHHHHHHEEEECCC	48.49	19608861
81	Acetylation	FTEDNLKKLYVSNLG ECHHHHHHEEEECCC	48.49	23954790
83	Phosphorylation	EDNLKKLYVSNLGIG HHHHHHEEEECCCCC	15.65	28152594
85	Phosphorylation	NLKKLYVSNLGIGHT HHHHEEEECCCCCCC	16.87	29449344
92	Phosphorylation	SNLGIGHTRYATTGK ECCCCCCCEEECCCC	21.84	29449344
94	Phosphorylation	LGIGHTRYATTGKCE CCCCCCEEECCCCEE	14.95	29083192
96	Phosphorylation	IGHTRYATTGKCELE CCCCEEECCCCEEEC	27.44	29083192
97	Phosphorylation	GHTRYATTGKCELEN CCCEEECCCCEEECC	26.86	29083192
99	Ubiquitination	TRYATTGKCELENCQ CEEECCCCEEECCCC	23.57	-
99	Acetylation	TRYATTGKCELENCQ CEEECCCCEEECCCC	23.57	23749302
116	Acetylation	VVETLHGKIAVAHNG EEEEECCEEEEEECC	19.42	25953088
130	Methylation	GELVNAARLRKKLLR CCHHCHHHHHHHHHH	32.39	-
166	Phosphorylation	PPQEQDDTPDWVARI CCCCCCCCCHHHHHH	31.28	-
178	Ubiquitination	ARIKNLMKEAPTAYS HHHHHHHHHCCCHHH	54.62	-
182	Phosphorylation	NLMKEAPTAYSLLIM HHHHHCCCHHHHHHH	45.32	29449344
184	Phosphorylation	MKEAPTAYSLLIMHR HHHCCCHHHHHHHCC	11.43	29449344
185	Phosphorylation	KEAPTAYSLLIMHRD HHCCCHHHHHHHCCC	17.78	29449344
201	Phosphorylation	IYAVRDPYGNRPLCI EEEECCCCCCCCCEE	31.18	28152594
220	2-Hydroxyisobutyrylation	PVSDINDKEKKTSET EHHHCCCCCCCCCCC	67.93	-
220	Ubiquitination	PVSDINDKEKKTSET EHHHCCCCCCCCCCC	67.93	-
222	Acetylation	SDINDKEKKTSETEG HHCCCCCCCCCCCCC	68.07	25953088
223	Ubiquitination	DINDKEKKTSETEGW HCCCCCCCCCCCCCE	59.37	-
306	Glutathionylation	VYTVRYRCGQQLAIE EEEEEEECCCEEEEE	4.23	22555962
339	S-nitrosocysteine	ALAYAGKCGLPYVEV HHHHCCCCCCCCEEH	7.09	-
339	S-nitrosylation	ALAYAGKCGLPYVEV HHHHCCCCCCCCEEH	7.09	19483679
348	S-nitrosocysteine	LPYVEVLCKNRYVGR CCCEEHHCCCCCCCC	4.42	-
348	S-nitrosylation	LPYVEVLCKNRYVGR CCCEEHHCCCCCCCC	4.42	19483679
349	Ubiquitination	PYVEVLCKNRYVGRT CCEEHHCCCCCCCCE	40.06	-
349	Acetylation	PYVEVLCKNRYVGRT CCEEHHCCCCCCCCE	40.06	25953088
356	Phosphorylation	KNRYVGRTFIQPNMR CCCCCCCEECCCCHH	21.11	20068231
371	Acetylation	LRQLGVAKKFGVLSD HHHHCHHHHHCCCCC	46.35	25953088
372	Malonylation	RQLGVAKKFGVLSDN HHHCHHHHHCCCCCC	37.30	26320211
372	Acetylation	RQLGVAKKFGVLSDN HHHCHHHHHCCCCCC	37.30	23749302
372	Ubiquitination	RQLGVAKKFGVLSDN HHHCHHHHHCCCCCC	37.30	21890473
377	Phosphorylation	AKKFGVLSDNFKGKR HHHHCCCCCCCCCCE	28.27	29083192
381	Ubiquitination	GVLSDNFKGKRIVLV CCCCCCCCCCEEEEE	70.54	21890473
383	Methylation	LSDNFKGKRIVLVDD CCCCCCCCEEEEECC	39.27	-
397	Phosphorylation	DSIVRGNTISPIIKL CCCCCCCCHHHHHHH	26.17	-
399	Phosphorylation	IVRGNTISPIIKLLK CCCCCCHHHHHHHHH	14.17	25159151
403	Ubiquitination	NTISPIIKLLKESGA CCHHHHHHHHHHCCC	48.78	21890473
406	Ubiquitination	SPIIKLLKESGAKEV HHHHHHHHHCCCCEE	61.34	-
408	Phosphorylation	IIKLLKESGAKEVHI HHHHHHHCCCCEEEE	42.33	-
411	Ubiquitination	LLKESGAKEVHIRVA HHHHCCCCEEEEEEE	64.89	21890473
419	Phosphorylation	EVHIRVASPPIKYPC EEEEEEECCCCCCCC	28.49	29396449
482	Acetylation	FKKQKEKKHDIMIQE CCCHHHCCCCEEEEE	47.83	24847243
499	Acetylation	NGLECFEKSGHCTAC CCEEEEEECCCCCEE	41.29	24847249
510	Acetylation	CTACLTGKYPVELEW CCEECCCCCCCEEEC	40.94	25953088
510	Ubiquitination	CTACLTGKYPVELEW CCEECCCCCCCEEEC	40.94	-

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
397	T	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PUR1_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 PUR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPT1_HUMAN	EPT1	physical	21988832
SYCC_HUMAN	CARS	physical	22863883
NXP20_HUMAN	FAM114A1	physical	22863883
PUR2_HUMAN	GART	physical	22863883
HSP74_HUMAN	HSPA4	physical	22863883
ILK_HUMAN	ILK	physical	22863883
MEA1_HUMAN	MEA1	physical	22863883
PARVA_HUMAN	PARVA	physical	22863883
RSU1_HUMAN	RSU1	physical	22863883
RO60_HUMAN	TROVE2	physical	22863883
G6PD_HUMAN	G6PD	physical	26186194
CCZ1B_HUMAN	CCZ1	physical	26186194
CCZ1_HUMAN	CCZ1	physical	26186194
HDAC3_HUMAN	HDAC3	physical	26186194
RHG01_HUMAN	ARHGAP1	physical	26344197
PUR2_HUMAN	GART	physical	26344197
IMDH2_HUMAN	IMPDH2	physical	26344197
PEPL1_HUMAN	NPEPL1	physical	26344197
PAK1_HUMAN	PAK1	physical	26344197
PRPS1_HUMAN	PRPS1	physical	26344197
PRPS2_HUMAN	PRPS2	physical	26344197
GLYC_HUMAN	SHMT1	physical	26344197
TYSY_HUMAN	TYMS	physical	26344197
NUDT5_HUMAN	NUDT5	physical	28514442

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
DB00544	Fluorouracil
DB00130	L-Glutamine
DB01033	Mercaptopurine

Regulatory Network of PUR1_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-81, AND MASS SPECTROMETRY.	19608861 [Abstract]