dbPTM

PRPS3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRPS3_HUMAN
UniProt AC	P21108
Protein Name	Ribose-phosphate pyrophosphokinase 3
Gene Name	PRPS1L1
Organism	Homo sapiens (Human).
Sequence Length	318
Subcellular Localization
Protein Description	Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis..
Protein Sequence	MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIDESVRGEDVYIVQSGCGEINDSLMELLIMINACKIASASRVTAVIPCFPYARQDKKDKSRSPISAKLVANMLSIAGADHIITMDLHASQIQGFFDIPVDNLYAEPTVLKWIRENIPEWKNCIIVSPDAGGAKRVTSIADQLNVDFALIHKERKKANEVDCIVLVGDVNDRVAILVDDMADTCVTICLAADKLLSAGATRVYAILTHGIFSGPAISRINTACFEAVVVTNTIPQDEKMKHCSKIRVIDISMILAEAIRRTHNGESVSYLFSHVPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Ubiquitination	---MPNIKIFSGSSH ---CCCEEEECCCCC	44.32	21890473
16	Phosphorylation	GSSHQDLSQKIADRL CCCCHHHHHHHHHHH	37.40	27282143
18	Acetylation	SHQDLSQKIADRLGL CCHHHHHHHHHHHCH	36.16	23236377
18	Ubiquitination	SHQDLSQKIADRLGL CCHHHHHHHHHHHCH	36.16	21906983
22	Methylation	LSQKIADRLGLELGK HHHHHHHHHCHHHHC	22.95	-
29	Ubiquitination	RLGLELGKVVTKKFS HHCHHHHCHHHEECC	46.27	21906983
33	Ubiquitination	ELGKVVTKKFSNQET HHHCHHHEECCCCCE	39.96	22817900
34	Ubiquitination	LGKVVTKKFSNQETC HHCHHHEECCCCCEE	44.66	22817900
36	Phosphorylation	KVVTKKFSNQETCVE CHHHEECCCCCEEEE	46.62	24275569
94	Phosphorylation	AVIPCFPYARQDKKD EEEECCCHHCCCCCC	8.31	28152594
99	Ubiquitination	FPYARQDKKDKSRSP CCHHCCCCCCCCCCH	55.31	24816145
176	Acetylation	SPDAGGAKRVTSIAD CCCCCCCHHHHHHHH	51.15	133507
176	Ubiquitination	SPDAGGAKRVTSIAD CCCCCCCHHHHHHHH	51.15	27667366
194	Acetylation	VDFALIHKERKKANE CCEEHHCHHHHHCCC	52.82	23749302
194	Ubiquitination	VDFALIHKERKKANE CCEEHHCHHHHHCCC	52.82	21906983
197	Ubiquitination	ALIHKERKKANEVDC EHHCHHHHHCCCCCE	58.28	22817900
198	Ubiquitination	LIHKERKKANEVDCI HHCHHHHHCCCCCEE	63.77	22817900
238	Phosphorylation	LAADKLLSAGATRVY HHHHHHHHCCCCEEE	34.78	28857561
242	Phosphorylation	KLLSAGATRVYAILT HHHHCCCCEEEHHHH	21.54	-
245	Phosphorylation	SAGATRVYAILTHGI HCCCCEEEHHHHCCC	5.66	28152594
249	Phosphorylation	TRVYAILTHGIFSGP CEEEHHHHCCCCCCH	16.37	28152594
254	Phosphorylation	ILTHGIFSGPAISRI HHHCCCCCCHHHHHH	41.78	28348404
259	Phosphorylation	IFSGPAISRINTACF CCCCHHHHHHCHHHE	29.25	28348404
263	Phosphorylation	PAISRINTACFEAVV HHHHHHCHHHEEEEE	23.56	30301811
272	Phosphorylation	CFEAVVVTNTIPQDE HEEEEEECCCCCCCH	18.29	30301811
274	Phosphorylation	EAVVVTNTIPQDEKM EEEEECCCCCCCHHC	25.35	30301811
293	Phosphorylation	KIRVIDISMILAEAI CCEEEEHHHHHHHHH	8.95	28464451
303	Phosphorylation	LAEAIRRTHNGESVS HHHHHHHHCCCCEEE	15.16	20068231
308	Phosphorylation	RRTHNGESVSYLFSH HHHCCCCEEEEEEEC	20.12	18669648
310	Phosphorylation	THNGESVSYLFSHVP HCCCCEEEEEEECCC	25.95	20068231
311	Phosphorylation	HNGESVSYLFSHVPL CCCCEEEEEEECCCC	15.03	20068231
314	Phosphorylation	ESVSYLFSHVPL--- CEEEEEEECCCC---	22.45	20068231

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 PRPS3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PRPS3_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 PRPS3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PRPS3_HUMAN !!

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 PRPS3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-194, AND MASS SPECTROMETRY.	19608861 [Abstract]