NT5D1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NT5D1_HUMAN
• UniProt AC: Q5TFE4
• Protein Name: 5'-nucleotidase domain-containing protein 1
• Gene Name: NT5DC1
• Organism: Homo sapiens (Human).
• Sequence Length: 455
• Protein Sequence: MAQHFSLAACDVVGFDLDHTLCRYNLPESAPLIYNSFAQFLVKEKGYDKELLNVTPEDWDFCCKGLALDLEDGNFLKLANNGTVLRASHGTKMMTPEVLAEAYGKKEWKHFLSDTGMACRSGKYYFYDNYFDLPGALLCARVVDYLTKLNNGQKTFDFWKDIVAAIQHNYKMSAFKENCGIYFPEIKRDPGRYLHSCPESVKKWLRQLKNAGKILLLITSSHSDYCRLLCEYILGNDFTDLFDIVITNALKPGFFSHLPSQRPFRTLENDEEQEALPSLDKPGWYSQGNAVHLYELLKKMTGKPEPKVVYFGDSMHSDIFPARHYSNWETVLILEELRGDEGTRSQRPEESEPLEKKGKYEGPKAKPLNTSSKKWGSFFIDSVLGLENTEDSLVYTWSCKRISTYSTIAIPSIEAIAELPLDYKFTRFSSSNSKTAGYYPNPPLVLSSDETLISK

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
6	Phosphorylation	--MAQHFSLAACDVV --CCCCCCCCCCCEE	18.25	-
43	Ubiquitination	SFAQFLVKEKGYDKE HHHHHHHHHCCCCHH	56.72	-
45	Ubiquitination	AQFLVKEKGYDKELL HHHHHHHCCCCHHHH	57.99	-
49	Ubiquitination	VKEKGYDKELLNVTP HHHCCCCHHHHCCCH	41.60	-
55	Phosphorylation	DKELLNVTPEDWDFC CHHHHCCCHHHHHCC	21.64	28348404
77	Ubiquitination	LEDGNFLKLANNGTV CCCCCEEEECCCCCE	41.22	21906983
103	Phosphorylation	PEVLAEAYGKKEWKH HHHHHHHHCCHHHHH	22.45	27762562
104	Ubiquitination	EVLAEAYGKKEWKHF HHHHHHHCCHHHHHH	41.42	21890473
113	Phosphorylation	KEWKHFLSDTGMACR HHHHHHHHHCCCCCC	31.98	27251275
115	Phosphorylation	WKHFLSDTGMACRSG HHHHHHHCCCCCCCC	26.02	28555341
119	Glutathionylation	LSDTGMACRSGKYYF HHHCCCCCCCCCEEE	2.36	22555962
145	Phosphorylation	LCARVVDYLTKLNNG HHHHHHHHHHHHCCC	12.50	19835603
154	Ubiquitination	TKLNNGQKTFDFWKD HHHCCCCCCCHHHHH	53.19	21890473
160	Ubiquitination	QKTFDFWKDIVAAIQ CCCCHHHHHHHHHHH	37.26	-
171	Acetylation	AAIQHNYKMSAFKEN HHHHHHHHHHHHHHH	31.53	19608861
171	Malonylation	AAIQHNYKMSAFKEN HHHHHHHHHHHHHHH	31.53	26320211
173	Phosphorylation	IQHNYKMSAFKENCG HHHHHHHHHHHHHCC	26.80	23663014
182	Phosphorylation	FKENCGIYFPEIKRD HHHHCCEECCCCCCC	9.81	23663014
187	Ubiquitination	GIYFPEIKRDPGRYL CEECCCCCCCCCCCC	49.43	-
260	Phosphorylation	GFFSHLPSQRPFRTL CHHHCCCCCCCCCCC	45.22	24719451
301	Phosphorylation	YELLKKMTGKPEPKV HHHHHHHHCCCCCEE	51.43	-
306	Ubiquitination	KMTGKPEPKVVYFGD HHHCCCCCEEEEECC	43.18	21890473
356	Ubiquitination	EESEPLEKKGKYEGP CCCCCCHHCCCCCCC	74.61	21890473
357	Acetylation	ESEPLEKKGKYEGPK CCCCCHHCCCCCCCC	51.78	21339330
357	Ubiquitination	ESEPLEKKGKYEGPK CCCCCHHCCCCCCCC	51.78	-
359	Acetylation	EPLEKKGKYEGPKAK CCCHHCCCCCCCCCC	49.35	23749302
360	Phosphorylation	PLEKKGKYEGPKAKP CCHHCCCCCCCCCCC	34.48	-
384	Ubiquitination	SFFIDSVLGLENTED HEEHHHHHCCCCCCC	8.20	21890473
403	Phosphorylation	TWSCKRISTYSTIAI EEECCEEECCCEEEE	25.89	28348404
404	Phosphorylation	WSCKRISTYSTIAIP EECCEEECCCEEEEC	21.08	28348404
405	Phosphorylation	SCKRISTYSTIAIPS ECCEEECCCEEEECC	9.31	28122231
406	Phosphorylation	CKRISTYSTIAIPSI CCEEECCCEEEECCH	17.27	28122231
407	Phosphorylation	KRISTYSTIAIPSIE CEEECCCEEEECCHH	12.19	24719451
412	Phosphorylation	YSTIAIPSIEAIAEL CCEEEECCHHHHHCC	27.26	28122231
431	Phosphorylation	KFTRFSSSNSKTAGY ECEEECCCCCCCCCC	43.88	25627689
434	Ubiquitination	RFSSSNSKTAGYYPN EECCCCCCCCCCCCC	46.79	2190698
447	Phosphorylation	PNPPLVLSSDETLIS CCCCEEECCCCCCCC	28.41	25627689
448	Phosphorylation	NPPLVLSSDETLISK CCCEEECCCCCCCCC	34.99	25627689
455	Acetylation	SDETLISK------- CCCCCCCC-------	58.32	90529

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

Oops, there are no upstream regulatory protein records of NT5D1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NT5D1_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 NT5D1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SPEE_HUMAN	SRM	physical	22939629
UBA3_HUMAN	UBA3	physical	22939629
UCHL3_HUMAN	UCHL3	physical	22939629
GFAP_HUMAN	GFAP	physical	26186194
KPYR_HUMAN	PKLR	physical	26186194
HBD_HUMAN	HBD	physical	26186194
KPYR_HUMAN	PKLR	physical	28514442
GFAP_HUMAN	GFAP	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.

Related Literatures of Post-Translational Modification

Acetylation

"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-171, AND MASS SPECTROMETRY.
PubMed: 19608861