dbPTM

NTPCR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NTPCR_HUMAN
UniProt AC	Q9BSD7
Protein Name	Cancer-related nucleoside-triphosphatase
Gene Name	NTPCR
Organism	Homo sapiens (Human).
Sequence Length	190
Subcellular Localization
Protein Description	Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency..
Protein Sequence	MARHVFLTGPPGVGKTTLIHKASEVLKSSGVPVDGFYTEEVRQGGRRIGFDVVTLSGTRGPLSRVGLEPPPGKRECRVGQYVVDLTSFEQLALPVLRNADCSSGPGQRVCVIDEIGKMELFSQLFIQAVRQTLSTPGTIILGTIPVPKGKPLALVEEIRNRKDVKVFNVTKENRNHLLPDIVTCVQSSRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MARHVFLTG ------CCCEEEECC	15.41	19413330
8	Phosphorylation	MARHVFLTGPPGVGK CCCEEEECCCCCCCH	35.86	23532336
15	Acetylation	TGPPGVGKTTLIHKA CCCCCCCHHHHHHHH	35.61	25953088
15	Ubiquitination	TGPPGVGKTTLIHKA CCCCCCCHHHHHHHH	35.61	-
21	Acetylation	GKTTLIHKASEVLKS CHHHHHHHHHHHHHH	46.76	19608861
21	Ubiquitination	GKTTLIHKASEVLKS CHHHHHHHHHHHHHH	46.76	21890473
27	Ubiquitination	HKASEVLKSSGVPVD HHHHHHHHHCCCCCC	47.99	-
37	Phosphorylation	GVPVDGFYTEEVRQG CCCCCCEEHHHHHCC	20.83	28796482
38	Phosphorylation	VPVDGFYTEEVRQGG CCCCCEEHHHHHCCC	24.33	28796482
54	Phosphorylation	RIGFDVVTLSGTRGP EEEEEEEEECCCCCC	18.30	20068231
56	Phosphorylation	GFDVVTLSGTRGPLS EEEEEEECCCCCCHH	28.84	20068231
58	Phosphorylation	DVVTLSGTRGPLSRV EEEEECCCCCCHHHC	29.13	20068231
73	Acetylation	GLEPPPGKRECRVGQ CCCCCCCCCCCCCCC	51.28	25953088
73	Ubiquitination	GLEPPPGKRECRVGQ CCCCCCCCCCCCCCC	51.28	-
102	Phosphorylation	VLRNADCSSGPGQRV HHHCCCCCCCCCCEE	38.59	21406692
103	Phosphorylation	LRNADCSSGPGQRVC HHCCCCCCCCCCEEE	56.17	21406692
135	Phosphorylation	AVRQTLSTPGTIILG HHHHHCCCCCEEEEE	28.93	24719451
148	Ubiquitination	LGTIPVPKGKPLALV EEEEECCCCCCCHHH	78.70	21890473
150	Ubiquitination	TIPVPKGKPLALVEE EEECCCCCCCHHHHH	42.88	-
150	Malonylation	TIPVPKGKPLALVEE EEECCCCCCCHHHHH	42.88	26320211
165	Ubiquitination	IRNRKDVKVFNVTKE HHCCCCCEEEEECCC	51.77	21890473
165	Acetylation	IRNRKDVKVFNVTKE HHCCCCCEEEEECCC	51.77	19608861
165	Malonylation	IRNRKDVKVFNVTKE HHCCCCCEEEEECCC	51.77	26320211
170	Phosphorylation	DVKVFNVTKENRNHL CCEEEEECCCCCCCC	33.47	-
171	Acetylation	VKVFNVTKENRNHLL CEEEEECCCCCCCCC	49.02	25953088
171	Ubiquitination	VKVFNVTKENRNHLL CEEEEECCCCCCCCC	49.02	21890473
171	Malonylation	VKVFNVTKENRNHLL CEEEEECCCCCCCCC	49.02	26320211
184	Glutathionylation	LLPDIVTCVQSSRK- CCHHHHHHHHHCCC-	1.49	22555962

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 NTPCR_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STABP_HUMAN	STAMBP	physical	21988832
WDR19_HUMAN	WDR19	physical	27173435
WDR35_HUMAN	WDR35	physical	27173435

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 NTPCR_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, 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-21 AND LYS-165, AND MASSSPECTROMETRY.	19608861 [Abstract]