dbPTM

PYRG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PYRG2_HUMAN
UniProt AC	Q9NRF8
Protein Name	CTP synthase 2
Gene Name	CTPS2
Organism	Homo sapiens (Human).
Sequence Length	586
Subcellular Localization
Protein Description	Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides..
Protein Sequence	MKYILVTGGVISGIGKGIIASSIGTILKSCGLRVTAIKIDPYINIDAGTFSPYEHGEVFVLNDGGEVDLDLGNYERFLDINLYKDNNITTGKIYQHVINKERRGDYLGKTVQVVPHITDAVQEWVMNQAKVPVDGNKEEPQICVIELGGTIGDIEGMPFVEAFRQFQFKAKRENFCNIHVSLVPQLSATGEQKTKPTQNSVRALRGLGLSPDLIVCRSSTPIEMAVKEKISMFCHVNPEQVICIHDVSSTYRVPVLLEEQSIVKYFKERLHLPIGDSASNLLFKWRNMADRYERLQKICSIALVGKYTKLRDCYASVFKALEHSALAINHKLNLMYIDSIDLEKITETEDPVKFHEAWQKLCKADGILVPGGFGIRGTLGKLQAISWARTKKIPFLGVCLGMQLAVIEFARNCLNLKDADSTEFRPNAPVPLVIDMPEHNPGNLGGTMRLGIRRTVFKTENSILRKLYGDVPFIEERHRHRFEVNPNLIKQFEQNDLSFVGQDVDGDRMEIIELANHPYFVGVQFHPEFSSRPMKPSPPYLGLLLAATGNLNAYLQQGCKLSSSDRYSDASDDSFSEPRIAELEIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	LVTGGVISGIGKGII EEECCCCCCCCCHHH	23.19	21712546
51	Phosphorylation	NIDAGTFSPYEHGEV CCCCCCCCCCCCCCE	26.81	26074081
53	Phosphorylation	DAGTFSPYEHGEVFV CCCCCCCCCCCCEEE	21.25	26074081
83	Phosphorylation	RFLDINLYKDNNITT EEEEEEEECCCCCCC	16.29	22210691
90	Phosphorylation	YKDNNITTGKIYQHV ECCCCCCCCCEEEHH	32.45	22210691
92	Ubiquitination	DNNITTGKIYQHVIN CCCCCCCCEEEHHHC	35.83	-
94	Phosphorylation	NITTGKIYQHVINKE CCCCCCEEEHHHCHH	8.96	22210691
100	Ubiquitination	IYQHVINKERRGDYL EEEHHHCHHHCCCCC	41.28	-
169	Methylation	AFRQFQFKAKRENFC HHHHHCHHHCCCCCC	42.06	-
189	Phosphorylation	LVPQLSATGEQKTKP ECCCCCCCCCCCCCC	37.56	24719451
195	Ubiquitination	ATGEQKTKPTQNSVR CCCCCCCCCCHHHHH	53.77	-
200	Phosphorylation	KTKPTQNSVRALRGL CCCCCHHHHHHHHHC	11.80	24114839
205	Methylation	QNSVRALRGLGLSPD HHHHHHHHHCCCCCC	36.99	-
216	Glutathionylation	LSPDLIVCRSSTPIE CCCCEEEEECCCCHH	2.50	22555962
218	Phosphorylation	PDLIVCRSSTPIEMA CCEEEEECCCCHHHH	33.18	24719451
219	Phosphorylation	DLIVCRSSTPIEMAV CEEEEECCCCHHHHH	20.89	28348404
220	Phosphorylation	LIVCRSSTPIEMAVK EEEEECCCCHHHHHH	29.54	28348404
261	Phosphorylation	PVLLEEQSIVKYFKE EEEECCHHHHHHHHH	32.40	21406692
264	Ubiquitination	LEEQSIVKYFKERLH ECCHHHHHHHHHHCC	43.21	21890473
264	Ubiquitination	LEEQSIVKYFKERLH ECCHHHHHHHHHHCC	43.21	21890473
277	Phosphorylation	LHLPIGDSASNLLFK CCCCCCCHHHHHHHH	28.52	22210691
279	Phosphorylation	LPIGDSASNLLFKWR CCCCCHHHHHHHHHH	31.78	22210691
336	Phosphorylation	NHKLNLMYIDSIDLE HCCCCEEEEEECCHH	12.54	-
346	Phosphorylation	SIDLEKITETEDPVK ECCHHHHCCCCCCHH	48.17	21406692
348	Phosphorylation	DLEKITETEDPVKFH CHHHHCCCCCCHHHH	36.72	21406692
353	Ubiquitination	TETEDPVKFHEAWQK CCCCCCHHHHHHHHH	46.52	-
360	Ubiquitination	KFHEAWQKLCKADGI HHHHHHHHHHHCCCC	45.19	-
378	Phosphorylation	GGFGIRGTLGKLQAI CCCCCCCHHHHHHHH	23.61	-
386	Phosphorylation	LGKLQAISWARTKKI HHHHHHHHHHHCCCC	20.07	29496963
389	Methylation	LQAISWARTKKIPFL HHHHHHHHCCCCCCH	40.60	-
466	Ubiquitination	TENSILRKLYGDVPF CCHHHHHHHHCCCCC	42.49	-
548	Phosphorylation	LGLLLAATGNLNAYL HHHHHHHHCCHHHHH	22.46	30576142
562	Phosphorylation	LQQGCKLSSSDRYSD HHCCCCCCCCCCCCC	17.19	22167270
563	Phosphorylation	QQGCKLSSSDRYSDA HCCCCCCCCCCCCCC	46.85	22167270
564	Phosphorylation	QGCKLSSSDRYSDAS CCCCCCCCCCCCCCC	23.80	23401153
566	Methylation	CKLSSSDRYSDASDD CCCCCCCCCCCCCCC	34.50	-
567	Phosphorylation	KLSSSDRYSDASDDS CCCCCCCCCCCCCCC	18.85	22167270
568	Phosphorylation	LSSSDRYSDASDDSF CCCCCCCCCCCCCCC	27.82	22167270
571	Phosphorylation	SDRYSDASDDSFSEP CCCCCCCCCCCCCCC	47.11	29255136
574	Phosphorylation	YSDASDDSFSEPRIA CCCCCCCCCCCCCEE	35.35	29255136
576	Phosphorylation	DASDDSFSEPRIAEL CCCCCCCCCCCEEEE	51.12	22167270

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
568	S	Phosphorylation	Kinase	CSNK1A1	P48729	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PYRG2_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 PYRG2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PYRG2_HUMAN	CTPS2	physical	16189514
FGFR1_HUMAN	FGFR1	physical	21988832
RL23A_HUMAN	RPL23A	physical	21988832
RL37A_HUMAN	RPL37A	physical	21988832
HSF1_HUMAN	HSF1	physical	22863883
LRSM1_HUMAN	LRSAM1	physical	22863883
MTMR2_HUMAN	MTMR2	physical	22863883
PLIN3_HUMAN	PLIN3	physical	22863883
PYRG2_HUMAN	CTPS2	physical	25416956
PYRG1_HUMAN	CTPS1	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 PYRG2_HUMAN

Related Literatures of Post-Translational Modification

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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-567; SER-568; SER-571AND SER-574, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; SER-571 ANDSER-574, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568 AND SER-571, ANDMASS SPECTROMETRY.	17081983 [Abstract]