dbPTM

GUAA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GUAA_HUMAN
UniProt AC	P49915
Protein Name	GMP synthase [glutamine-hydrolyzing]
Gene Name	GMPS
Organism	Homo sapiens (Human).
Sequence Length	693
Subcellular Localization	Cytoplasm.
Protein Description	Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division..
Protein Sequence	MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILRESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MALCNGDSK ------CCCCCCCCC	22.33	19413330
8	Phosphorylation	MALCNGDSKLENAGG CCCCCCCCCCCCCCC	40.30	28450419
9	Acetylation	ALCNGDSKLENAGGD CCCCCCCCCCCCCCC	65.64	19608861
9	Ubiquitination	ALCNGDSKLENAGGD CCCCCCCCCCCCCCC	65.64	21906983
46	Ubiquitination	KVIDRRVRELFVQSE HHHHHHHHHHHHCCE	32.84	-
59	Phosphorylation	SEIFPLETPAFAIKE CEEECCCCCCEEEHH	27.83	-
65	Ubiquitination	ETPAFAIKEQGFRAI CCCCEEEHHCCCEEE	40.32	21906983
66	Ubiquitination	TPAFAIKEQGFRAII CCCEEEHHCCCEEEE	50.23	-
66	Ubiquitination	TPAFAIKEQGFRAII CCCEEEHHCCCEEEE	50.23	-
83	Ubiquitination	GGPNSVYAEDAPWFD CCCCCCCCCCCCCCC	13.16	-
84	Ubiquitination	GPNSVYAEDAPWFDP CCCCCCCCCCCCCCC	36.70	21890473
84	Ubiquitination	GPNSVYAEDAPWFDP CCCCCCCCCCCCCCC	36.70	-
101	Ubiquitination	FTIGKPVLGICYGMQ EECCCCHHHHHHHHH	5.33	-
105	Ubiquitination	KPVLGICYGMQMMNK CCHHHHHHHHHHHHH	17.45	-
120	2-Hydroxyisobutyrylation	VFGGTVHKKSVREDG HHCCCCCCCCCCCCC	42.27	-
120	Acetylation	VFGGTVHKKSVREDG HHCCCCCCCCCCCCC	42.27	25953088
120	Ubiquitination	VFGGTVHKKSVREDG HHCCCCCCCCCCCCC	42.27	-
122	Phosphorylation	GGTVHKKSVREDGVF CCCCCCCCCCCCCEE	31.07	29457462
145	Acetylation	SLFRGLQKEEVVLLT HHHCCCCCCCEEEEE	61.97	26051181
145	Malonylation	SLFRGLQKEEVVLLT HHHCCCCCCCEEEEE	61.97	26320211
145	Ubiquitination	SLFRGLQKEEVVLLT HHHCCCCCCCEEEEE	61.97	-
159	2-Hydroxyisobutyrylation	THGDSVDKVADGFKV ECCCCHHHHCCCEEE	36.85	-
159	Acetylation	THGDSVDKVADGFKV ECCCCHHHHCCCEEE	36.85	25953088
159	Ubiquitination	THGDSVDKVADGFKV ECCCCHHHHCCCEEE	36.85	-
165	2-Hydroxyisobutyrylation	DKVADGFKVVARSGN HHHCCCEEEEEECCC	41.13	-
165	Acetylation	DKVADGFKVVARSGN HHHCCCEEEEEECCC	41.13	25953088
165	Ubiquitination	DKVADGFKVVARSGN HHHCCCEEEEEECCC	41.13	21906983
182	2-Hydroxyisobutyrylation	AGIANESKKLYGAQF EEEECCCCCCCCCCC	40.39	-
182	Acetylation	AGIANESKKLYGAQF EEEECCCCCCCCCCC	40.39	25953088
182	Ubiquitination	AGIANESKKLYGAQF EEEECCCCCCCCCCC	40.39	21906983
183	Ubiquitination	GIANESKKLYGAQFH EEECCCCCCCCCCCC	57.11	21890473
183	Ubiquitination	GIANESKKLYGAQFH EEECCCCCCCCCCCC	57.11	21906983
185	Phosphorylation	ANESKKLYGAQFHPE ECCCCCCCCCCCCCC	21.21	29496907
190	Ubiquitination	KLYGAQFHPEVGLTE CCCCCCCCCCCCCCC	12.91	-
200	Ubiquitination	VGLTENGKVILKNFL CCCCCCCEEEEEECC	37.37	-
204	Ubiquitination	ENGKVILKNFLYDIA CCCEEEEEECCCHHC	34.23	-
208	Phosphorylation	VILKNFLYDIAGCSG EEEEECCCHHCCCCC	10.93	20068231
213	Glutathionylation	FLYDIAGCSGTFTVQ CCCHHCCCCCEEEEC	2.21	22555962
214	Phosphorylation	LYDIAGCSGTFTVQN CCHHCCCCCEEEECC	39.69	20068231
218	Phosphorylation	AGCSGTFTVQNRELE CCCCCEEEECCHHHH	22.48	20068231
226	Ubiquitination	VQNRELECIREIKER ECCHHHHHHHHHHHH	5.78	-
237	Ubiquitination	IKERVGTSKVLVLLS HHHHHCCCCEEEEEC	18.16	-
239	Ubiquitination	ERVGTSKVLVLLSGG HHHCCCCEEEEECCC	4.47	-
253	Phosphorylation	GVDSTVCTALLNRAL CCCHHHHHHHHHHHC	18.92	-
280	Phosphorylation	GFMRKRESQSVEEAL CCCCHHCCCCHHHHH	31.61	25627689
282	Phosphorylation	MRKRESQSVEEALKK CCHHCCCCHHHHHHH	40.55	25159151
288	Acetylation	QSVEEALKKLGIQVK CCHHHHHHHCCCCEE	53.66	25953088
289	2-Hydroxyisobutyrylation	SVEEALKKLGIQVKV CHHHHHHHCCCCEEE	53.44	-
289	Ubiquitination	SVEEALKKLGIQVKV CHHHHHHHCCCCEEE	53.44	-
290	Ubiquitination	VEEALKKLGIQVKVI HHHHHHHCCCCEEEE	7.55	21890473
290	Acetylation	VEEALKKLGIQVKVI HHHHHHHCCCCEEEE	7.55	-
290	Ubiquitination	VEEALKKLGIQVKVI HHHHHHHCCCCEEEE	7.55	-
302	Phosphorylation	KVINAAHSFYNGTTT EEEECCCCCCCCCCC	25.38	23927012
304	Phosphorylation	INAAHSFYNGTTTLP EECCCCCCCCCCCCC	18.72	23927012
307	Phosphorylation	AHSFYNGTTTLPISD CCCCCCCCCCCCCCC	16.99	30266825
308	Phosphorylation	HSFYNGTTTLPISDE CCCCCCCCCCCCCCC	27.95	30266825
309	Phosphorylation	SFYNGTTTLPISDED CCCCCCCCCCCCCCC	30.30	30266825
313	Ubiquitination	GTTTLPISDEDRTPR CCCCCCCCCCCCCCC	32.76	21890473
313	Ubiquitination	GTTTLPISDEDRTPR CCCCCCCCCCCCCCC	32.76	-
313	Phosphorylation	GTTTLPISDEDRTPR CCCCCCCCCCCCCCC	32.76	30266825
317	Acetylation	LPISDEDRTPRKRIS CCCCCCCCCCCHHHH	44.58	-
317	Ubiquitination	LPISDEDRTPRKRIS CCCCCCCCCCCHHHH	44.58	-
318	Phosphorylation	PISDEDRTPRKRISK CCCCCCCCCCHHHHH	39.50	29255136
325	Ubiquitination	TPRKRISKTLNMTTS CCCHHHHHHCCCCCC	55.44	-
326	Phosphorylation	PRKRISKTLNMTTSP CCHHHHHHCCCCCCH	19.30	30266825
329	Sulfoxidation	RISKTLNMTTSPEEK HHHHHCCCCCCHHHH	4.94	21406390
330	Phosphorylation	ISKTLNMTTSPEEKR HHHHCCCCCCHHHHH	24.05	25463755
331	Phosphorylation	SKTLNMTTSPEEKRK HHHCCCCCCHHHHHH	31.36	23927012
332	Phosphorylation	KTLNMTTSPEEKRKI HHCCCCCCHHHHHHH	22.58	29255136
336	Ubiquitination	MTTSPEEKRKIIGDT CCCCHHHHHHHHHHH	58.28	-
338	2-Hydroxyisobutyrylation	TSPEEKRKIIGDTFV CCHHHHHHHHHHHHH	50.14	-
338	Ubiquitination	TSPEEKRKIIGDTFV CCHHHHHHHHHHHHH	50.14	-
343	Phosphorylation	KRKIIGDTFVKIANE HHHHHHHHHHHHHHH	25.72	20068231
358	Ubiquitination	VIGEMNLKPEEVFLA HHHHCCCCHHHEEEE	45.43	21890473
358	Ubiquitination	VIGEMNLKPEEVFLA HHHHCCCCHHHEEEE	45.43	-
358	Ubiquitination	VIGEMNLKPEEVFLA HHHHCCCCHHHEEEE	45.43	-
368	Phosphorylation	EVFLAQGTLRPDLIE HEEEECCCCCHHHHH	13.91	29523821
376	Phosphorylation	LRPDLIESASLVASG CCHHHHHHHHHHHHC	19.03	29523821
378	Ubiquitination	PDLIESASLVASGKA HHHHHHHHHHHHCCC	32.43	-
378	Phosphorylation	PDLIESASLVASGKA HHHHHHHHHHHHCCC	32.43	29523821
379	Ubiquitination	DLIESASLVASGKAE HHHHHHHHHHHCCCE	3.59	-
382	Phosphorylation	ESASLVASGKAELIK HHHHHHHHCCCEEHH	33.09	29523821
389	Ubiquitination	SGKAELIKTHHNDTE HCCCEEHHHCCCCHH	55.20	21890473
389	2-Hydroxyisobutyrylation	SGKAELIKTHHNDTE HCCCEEHHHCCCCHH	55.20	-
389	Acetylation	SGKAELIKTHHNDTE HCCCEEHHHCCCCHH	55.20	23749302
389	Ubiquitination	SGKAELIKTHHNDTE HCCCEEHHHCCCCHH	55.20	21906983
390	Phosphorylation	GKAELIKTHHNDTEL CCCEEHHHCCCCHHH	22.75	21406692
395	Phosphorylation	IKTHHNDTELIRKLR HHHCCCCHHHHHHHH	37.70	21406692
399	Methylation	HNDTELIRKLREEGK CCCHHHHHHHHHCCC	44.58	-
400	Ubiquitination	NDTELIRKLREEGKV CCHHHHHHHHHCCCC	44.92	-
406	Ubiquitination	RKLREEGKVIEPLKD HHHHHCCCCCCCCCC	43.23	-
412	Ubiquitination	GKVIEPLKDFHKDEV CCCCCCCCCCCHHHH	69.89	21890473
412	2-Hydroxyisobutyrylation	GKVIEPLKDFHKDEV CCCCCCCCCCCHHHH	69.89	-
412	Acetylation	GKVIEPLKDFHKDEV CCCCCCCCCCCHHHH	69.89	27452117
412	Ubiquitination	GKVIEPLKDFHKDEV CCCCCCCCCCCHHHH	69.89	21906983
416	Sumoylation	EPLKDFHKDEVRILG CCCCCCCHHHHHHHC	56.42	-
416	Acetylation	EPLKDFHKDEVRILG CCCCCCCHHHHHHHC	56.42	23749302
416	Malonylation	EPLKDFHKDEVRILG CCCCCCCHHHHHHHC	56.42	26320211
416	Sumoylation	EPLKDFHKDEVRILG CCCCCCCHHHHHHHC	56.42	19608861
416	Ubiquitination	EPLKDFHKDEVRILG CCCCCCCHHHHHHHC	56.42	-
436	Ubiquitination	PEELVSRHPFPGPGL CHHHHHHCCCCCCCE	22.35	-
449	S-nitrosocysteine	GLAIRVICAEEPYIC CEEEEEEECCCCEEC	3.40	-
449	S-nitrosylation	GLAIRVICAEEPYIC CEEEEEEECCCCEEC	3.40	19483679
454	Phosphorylation	VICAEEPYICKDFPE EEECCCCEECCCCCC	23.41	28152594
456	S-nitrosocysteine	CAEEPYICKDFPETN ECCCCEECCCCCCCC	2.60	-
456	S-nitrosylation	CAEEPYICKDFPETN ECCCCEECCCCCCCC	2.60	19483679
457	Ubiquitination	AEEPYICKDFPETNN CCCCEECCCCCCCCC	53.50	21890473
457	Acetylation	AEEPYICKDFPETNN CCCCEECCCCCCCCC	53.50	26051181
457	Ubiquitination	AEEPYICKDFPETNN CCCCEECCCCCCCCC	53.50	21906983
470	Ubiquitination	NNILKIVADFSASVK CCCHHHHHHHHHCCC	18.66	-
477	Ubiquitination	ADFSASVKKPHTLLQ HHHHHCCCCHHHHHH	59.08	-
478	Ubiquitination	DFSASVKKPHTLLQR HHHHCCCCHHHHHHH	39.62	-
487	Sumoylation	HTLLQRVKACTTEED HHHHHHHHCCCCHHH	39.68	-
487	Sumoylation	HTLLQRVKACTTEED HHHHHHHHCCCCHHH	39.68	-
487	Ubiquitination	HTLLQRVKACTTEED HHHHHHHHCCCCHHH	39.68	-
503	O-linked_Glycosylation	EKLMQITSLHSLNAF HHHHHHHHHHHCCEE	26.22	23301498
508	Ubiquitination	ITSLHSLNAFLLPIK HHHHHHCCEEEEEEC	31.49	-
523	Glutathionylation	TVGVQGDCRSYSYVC EEECCCCCCCEEEEC	3.88	22555962
525	Phosphorylation	GVQGDCRSYSYVCGI ECCCCCCCEEEECCC	25.43	28442448
526	Phosphorylation	VQGDCRSYSYVCGIS CCCCCCCEEEECCCC	5.67	21406692
527	Phosphorylation	QGDCRSYSYVCGISS CCCCCCEEEECCCCC	16.61	28442448
528	Ubiquitination	GDCRSYSYVCGISSK CCCCCEEEECCCCCC	7.48	-
528	Phosphorylation	GDCRSYSYVCGISSK CCCCCEEEECCCCCC	7.48	28442448
533	Phosphorylation	YSYVCGISSKDEPDW EEEECCCCCCCCCCH	19.33	21406692
534	Phosphorylation	SYVCGISSKDEPDWE EEECCCCCCCCCCHH	42.05	21406692
535	Ubiquitination	YVCGISSKDEPDWES EECCCCCCCCCCHHH	60.36	-
542	Phosphorylation	KDEPDWESLIFLARL CCCCCHHHHHHHHHH	23.63	27732954
562	Phosphorylation	HNVNRVVYIFGPPVK CCCCCEEEEECCCCC	6.41	28152594
569	Ubiquitination	YIFGPPVKEPPTDVT EEECCCCCCCCCCCC	70.99	-
582	Phosphorylation	VTPTFLTTGVLSTLR CCCCCCCCCHHHHHH	27.69	27050516
586	Ubiquitination	FLTTGVLSTLRQADF CCCCCHHHHHHHHHH	24.00	-
586	Phosphorylation	FLTTGVLSTLRQADF CCCCCHHHHHHHHHH	24.00	27050516
587	Phosphorylation	LTTGVLSTLRQADFE CCCCHHHHHHHHHHH	23.07	27050516
607	Acetylation	RESGYAGKISQMPVI HHCCCCCCCCCCCEE	30.89	26051181
607	Ubiquitination	RESGYAGKISQMPVI HHCCCCCCCCCCCEE	30.89	-
616	Phosphorylation	SQMPVILTPLHFDRD CCCCEEEEECCCCCC	16.81	-
622	Methylation	LTPLHFDRDPLQKQP EEECCCCCCHHHCCC	46.64	-
627	Acetylation	FDRDPLQKQPSCQRS CCCCHHHCCCCCCCE	72.38	25953088
627	Ubiquitination	FDRDPLQKQPSCQRS CCCCHHHCCCCCCCE	72.38	-
643	Phosphorylation	VIRTFITSDFMTGIP EEEEEECCCCCCCCC	24.84	28787133
652	Phosphorylation	FMTGIPATPGNEIPV CCCCCCCCCCCCCCH	26.78	28787133
676	Phosphorylation	IKKIPGISRIMYDLT HHCCCCCCEEEEECC	22.97	26074081
680	Phosphorylation	PGISRIMYDLTSKPP CCCCEEEEECCCCCC	12.87	26074081
683	Phosphorylation	SRIMYDLTSKPPGTT CEEEEECCCCCCCCC	31.63	26074081
684	Phosphorylation	RIMYDLTSKPPGTTE EEEEECCCCCCCCCC	50.92	26074081
685	Acetylation	IMYDLTSKPPGTTEW EEEECCCCCCCCCCC	50.42	25953088
685	Ubiquitination	IMYDLTSKPPGTTEW EEEECCCCCCCCCCC	50.42	-
689	Phosphorylation	LTSKPPGTTEWE--- CCCCCCCCCCCC---	27.58	28270605
690	Phosphorylation	TSKPPGTTEWE---- CCCCCCCCCCC----	45.04	28270605

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
318	T	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBP7_HUMAN	USP7	physical	15749019
SAHH_HUMAN	AHCY	physical	22939629
MTAP_HUMAN	MTAP	physical	22863883
PSMD5_HUMAN	PSMD5	physical	22863883
RAB1A_HUMAN	RAB1A	physical	22863883
FCL_HUMAN	TSTA3	physical	22863883
PYRG1_HUMAN	CTPS1	physical	26344197
LGUL_HUMAN	GLO1	physical	26344197
IMDH1_HUMAN	IMPDH1	physical	26344197
IMDH2_HUMAN	IMPDH2	physical	26344197
UBP7_HUMAN	USP7	physical	26344197
UBP7_HUMAN	USP7	physical	26046769
UBP7_HUMAN	USP7	physical	24462112
RO52_HUMAN	TRIM21	physical	24462112
P53_HUMAN	TP53	physical	24462112

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
DB00130	L-Glutamine

Regulatory Network of GUAA_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-332, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-9 AND LYS-416, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-332, AND MASS SPECTROMETRY.	19413330 [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-332, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, AND MASSSPECTROMETRY.	17924679 [Abstract]