dbPTM

APT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	APT_HUMAN
UniProt AC	P07741
Protein Name	Adenine phosphoribosyltransferase
Gene Name	APRT
Organism	Homo sapiens (Human).
Sequence Length	180
Subcellular Localization	Cytoplasm.
Protein Description	Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis..
Protein Sequence	MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADSELQLV ------CCHHHHHHH	29.09	19413330
4	Phosphorylation	----MADSELQLVEQ ----CCHHHHHHHHH	30.57	28857561
15	Phosphorylation	LVEQRIRSFPDFPTP HHHHHHHCCCCCCCC	38.47	29255136
21	Phosphorylation	RSFPDFPTPGVVFRD HCCCCCCCCCEEEEC	32.44	28464451
30	Phosphorylation	GVVFRDISPVLKDPA CEEEECCHHHHCCHH	17.16	29255136
34	Ubiquitination	RDISPVLKDPASFRA ECCHHHHCCHHHHHH	63.00	23000965
34	Acetylation	RDISPVLKDPASFRA ECCHHHHCCHHHHHH	63.00	26051181
38	Phosphorylation	PVLKDPASFRAAIGL HHHCCHHHHHHHHHH	22.21	23927012
51	2-Hydroxyisobutyrylation	GLLARHLKATHGGRI HHHHHHHHHHCCCCC	45.15	-
51	Ubiquitination	GLLARHLKATHGGRI HHHHHHHHHHCCCCC	45.15	21890473
57	Methylation	LKATHGGRIDYIAGL HHHHCCCCCCEEEEE	24.17	-
60	Phosphorylation	THGGRIDYIAGLDSR HCCCCCCEEEEECCC	7.12	28152594
66	Phosphorylation	DYIAGLDSRGFLFGP CEEEEECCCCCCCCH	39.07	23401153
83	S-palmitoylation	AQELGLGCVLIRKRG HHHHCCCEEEEEECC	2.43	29575903
96	Phosphorylation	RGKLPGPTLWASYSL CCCCCCCEEEEEEEE	40.63	20068231
100	Phosphorylation	PGPTLWASYSLEYGK CCCEEEEEEEECCCC	12.04	19060867
102	Phosphorylation	PTLWASYSLEYGKAE CEEEEEEEECCCCEE	16.54	28348404
105	Phosphorylation	WASYSLEYGKAELEI EEEEEECCCCEEEEE	29.26	20071362
114	Ubiquitination	KAELEIQKDALEPGQ CEEEEEEHHHCCCCC	51.10	21906983
114	Acetylation	KAELEIQKDALEPGQ CEEEEEEHHHCCCCC	51.10	19608861
114	2-Hydroxyisobutyrylation	KAELEIQKDALEPGQ CEEEEEEHHHCCCCC	51.10	-
114	Malonylation	KAELEIQKDALEPGQ CEEEEEEHHHCCCCC	51.10	26320211
132	Phosphorylation	VVDDLLATGGTMNAA EEECHHCCCCHHHHH	35.79	21406692
135	Phosphorylation	DLLATGGTMNAACEL CHHCCCCHHHHHHHH	14.48	21635362
140	Glutathionylation	GGTMNAACELLGRLQ CCHHHHHHHHHHHHH	3.35	22555962
163	Ubiquitination	LVELTSLKGREKLAP HHHHHCCCCCHHCCC	56.54	22817900
167	Ubiquitination	TSLKGREKLAPVPFF HCCCCCHHCCCCCCH	48.89	21906983
167	Sumoylation	TSLKGREKLAPVPFF HCCCCCHHCCCCCCH	48.89	-

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 APT_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
HPRT_HUMAN	HPRT1	physical	22939629
PNCB_HUMAN	NAPRT	physical	22939629
UMPS_HUMAN	UMPS	physical	22939629
GUAA_HUMAN	GMPS	physical	22939629
HECW2_HUMAN	HECW2	physical	22939629
RAB7A_HUMAN	RAB7A	physical	26344197
SNX12_HUMAN	SNX12	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614723	Adenine phosphoribosyltransferase deficiency (APRTD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00173	Adenine
DB00131	Adenosine monophosphate

Regulatory Network of APT_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]
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2.	12665801 [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-114, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-66, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-15; SER-30;TYR-60; SER-66; SER-100 AND THR-135, AND MASS SPECTROMETRY.	19369195 [Abstract]