dbPTM

GMPR2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GMPR2_HUMAN
UniProt AC	Q9P2T1
Protein Name	GMP reductase 2 {ECO:0000255\|HAMAP-Rule:MF_03195}
Gene Name	GMPR2 {ECO:0000255\|HAMAP-Rule:MF_03195}
Organism	Homo sapiens (Human).
Sequence Length	348
Subcellular Localization
Protein Description	Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. [PubMed: 12009299]
Protein Sequence	MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGTFEMAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIFSEAC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Ubiquitination	PHIDNDVKLDFKDVL CCCCCCCCCCHHHHH	45.24	-
13	Acetylation	NDVKLDFKDVLLRPK CCCCCCHHHHHCCCC	46.74	19608861
13	Ubiquitination	NDVKLDFKDVLLRPK CCCCCCHHHHHCCCC	46.74	19608861
20	Ubiquitination	KDVLLRPKRSTLKSR HHHHCCCCCCCCCCC	53.17	-
26	Phosphorylation	PKRSTLKSRSEVDLT CCCCCCCCCCCCCCC	44.12	28857561
28	Phosphorylation	RSTLKSRSEVDLTRS CCCCCCCCCCCCCEE	49.41	23401153
31	Acetylation	LKSRSEVDLTRSFSF CCCCCCCCCCEEEEE	37.97	19608861
33	Phosphorylation	SRSEVDLTRSFSFRN CCCCCCCCEEEEECC	21.58	23403867
35	Phosphorylation	SEVDLTRSFSFRNSK CCCCCCEEEEECCCC	21.73	24719451
37	Phosphorylation	VDLTRSFSFRNSKQT CCCCEEEEECCCCCE	25.25	23927012
44	Phosphorylation	SFRNSKQTYSGVPII EECCCCCEECCCCEE	24.32	27251275
46	Phosphorylation	RNSKQTYSGVPIIAA CCCCCEECCCCEEEE	36.38	24719451
53	Phosphorylation	SGVPIIAANMDTVGT CCCCEEEECCCCCCH	11.06	24719451
55	Phosphorylation	VPIIAANMDTVGTFE CCEEEECCCCCCHHH	3.81	24719451
184	Phosphorylation	KVGIGPGSVCTTRKK EECCCCCCCCCCCCC	19.70	28857561
187	Phosphorylation	IGPGSVCTTRKKTGV CCCCCCCCCCCCCCC	27.72	27050516
188	Phosphorylation	GPGSVCTTRKKTGVG CCCCCCCCCCCCCCC	35.05	28857561
202	Phosphorylation	GYPQLSAVMECADAA CCCHHHHHHHHHHHH	2.74	27251275
223	Phosphorylation	IISDGGCSCPGDVAK EEECCCCCCCHHHHH	26.99	-
263	Phosphorylation	IERDGKKYKLFYGMS EEECCCEEEEEEECC	19.19	22817901
263	Acetylation	IERDGKKYKLFYGMS EEECCCEEEEEEECC	19.19	19608861
267	Phosphorylation	GKKYKLFYGMSSEMA CCEEEEEEECCHHHH	23.50	22817901
270	Phosphorylation	YKLFYGMSSEMAMKK EEEEEECCHHHHHHH	20.84	22817901
277	Ubiquitination	SSEMAMKKYAGGVAE CHHHHHHHHCCCCEE	27.52	-
278	Phosphorylation	SEMAMKKYAGGVAEY HHHHHHHHCCCCEEE	12.64	29496907
285	Phosphorylation	YAGGVAEYRASEGKT HCCCCEEEECCCCCE	11.18	25884760
291	Ubiquitination	EYRASEGKTVEVPFK EEECCCCCEEEECCC	45.40	19608861
291	Malonylation	EYRASEGKTVEVPFK EEECCCCCEEEECCC	45.40	26320211
291	Acetylation	EYRASEGKTVEVPFK EEECCCCCEEEECCC	45.40	19608861
298	Ubiquitination	KTVEVPFKGDVEHTI CEEEECCCCCHHHHH	48.40	-
298	Acetylation	KTVEVPFKGDVEHTI CEEEECCCCCHHHHH	48.40	23749302
309	Acetylation	EHTIRDILGGIRSTC HHHHHHHHHHHHHHC	6.35	19608861
314	Phosphorylation	DILGGIRSTCTYVGA HHHHHHHHHCCHHCH	26.39	21406692
315	Phosphorylation	ILGGIRSTCTYVGAA HHHHHHHHCCHHCHH	10.06	21406692
317	Phosphorylation	GGIRSTCTYVGAAKL HHHHHHCCHHCHHHH	22.72	21406692
318	Phosphorylation	GIRSTCTYVGAAKLK HHHHHCCHHCHHHHH	10.07	28152594
332	Phosphorylation	KELSRRTTFIRVTQQ HHHHCCCCEEEHHHC	18.43	27282143

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 GMPR2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GMPR2_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 GMPR2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SC24C_HUMAN	SEC24C	physical	22863883
GMPR1_HUMAN	GMPR	physical	26186194
SNX17_HUMAN	SNX17	physical	26186194
SNX17_HUMAN	SNX17	physical	28514442
GMPR1_HUMAN	GMPR	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
There are no disease associations of PTM sites.

Regulatory Network of GMPR2_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-13 AND LYS-291, AND MASSSPECTROMETRY.	19608861 [Abstract]