NT5C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NT5C_HUMAN
• UniProt AC: Q8TCD5
• Protein Name: 5'(3')-deoxyribonucleotidase, cytosolic type
• Gene Name: NT5C
• Organism: Homo sapiens (Human).
• Sequence Length: 201
• Subcellular Localization: Cytoplasm.
• Protein Description: Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP..
• Protein Sequence: MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADKVASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRLLSWSDNWREILDSKRGAAQRE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
63	Phosphorylation	DLADKVASVYEAPGF HHHHHHHHHHCCCCE	28.37	-
65	Phosphorylation	ADKVASVYEAPGFFL HHHHHHHHCCCCEEE	12.13	-
93	Phosphorylation	EMNDLPDTQVFICTS HHCCCCCCEEEEECC	25.37	25693802
99	Phosphorylation	DTQVFICTSPLLKYH CCEEEEECCHHHHHC	28.67	26657352
100	Phosphorylation	TQVFICTSPLLKYHH CEEEEECCHHHHHCC	14.78	27050516
104	Acetylation	ICTSPLLKYHHCVGE EECCHHHHHCCCCCH	50.66	25038526
112	Ubiquitination	YHHCVGEKYRWVEQH HCCCCCHHHHHHHHH	33.90	-
112	Acetylation	YHHCVGEKYRWVEQH HCCCCCHHHHHHHHH	33.90	26051181
112	2-Hydroxyisobutyrylation	YHHCVGEKYRWVEQH HCCCCCHHHHHHHHH	33.90	-
134	Ubiquitination	RIILTRDKTVVLGDL EEEECCCCEEEECCE	39.67	-
146	Ubiquitination	GDLLIDDKDTVRGQE CCEEECCCCCCCCCC	52.10	-
146	Acetylation	GDLLIDDKDTVRGQE CCEEECCCCCCCCCC	52.10	26822725
146	Succinylation	GDLLIDDKDTVRGQE CCEEECCCCCCCCCC	52.10	27452117
146 (in isoform 1)	Ubiquitination	-	52.10	21906983
182	Phosphorylation	PTRRRLLSWSDNWRE CCHHHHHHCCHHHHH	29.17	23927012
184	Phosphorylation	RRRLLSWSDNWREIL HHHHHHCCHHHHHHH	20.07	23927012
194	Ubiquitination	WREILDSKRGAAQRE HHHHHHHHCCHHHCC	55.29	2190698
194 (in isoform 1)	Ubiquitination	-	55.29	21906983

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of NT5C_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NT5C_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of NT5C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FLNC_HUMAN	FLNC	physical	28514442
GDS1_HUMAN	RAP1GDS1	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
• DB00709: Lamivudine

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-182, AND MASSSPECTROMETRY.
PubMed: 18669648