KPRA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KPRA_HUMAN
• UniProt AC: Q14558
• Protein Name: Phosphoribosyl pyrophosphate synthase-associated protein 1
• Gene Name: PRPSAP1
• Organism: Homo sapiens (Human).
• Sequence Length: 356
• Protein Description: Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis..
• Protein Sequence: MNAARTGYRVFSANSTAACTELAKRITERLGAELGKSVVYQETNGETRVEIKESVRGQDIFIIQTIPRDVNTAVMELLIMAYALKTACARNIIGVIPYFPYSKQSKMRKRGSIVCKLLASMLAKAGLTHIITMDLHQKEIQGFFSFPVDNLRASPFLLQYIQEEIPNYRNAVIVAKSPDAAKRAQSYAERLRLGLAVIHGEAQCTELDMDDGRHSPPMVKNATVHPGLELPLMMAKEKPPITVVGDVGGRIAIIVDDIIDDVESFVAAAEILKERGAYKIYVMATHGILSAEAPRLIEESSVDEVVVTNTVPHEVQKLQCPKIKTVDISLILSEAIRRIHNGESMAYLFRNITVDD

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
1	Acetylation	-------MNAARTGY -------CCCCCCCE	7.50	19413330
24	Ubiquitination	AACTELAKRITERLG HHHHHHHHHHHHHHC	57.89	-
24	Acetylation	AACTELAKRITERLG HHHHHHHHHHHHHHC	57.89	26051181
36	Ubiquitination	RLGAELGKSVVYQET HHCHHHCCEEEEECC	53.34	21890473
40	Phosphorylation	ELGKSVVYQETNGET HHCCEEEEECCCCCE	9.85	25839225
52	Ubiquitination	GETRVEIKESVRGQD CCEEEEEEHHHCCCE	30.36	-
53 (in isoform 2)	Ubiquitination	-	61.19	-
65 (in isoform 2)	Ubiquitination	-	23.65	-
101	Phosphorylation	GVIPYFPYSKQSKMR EEECCCCCCCCHHHH	20.71	21712546
102	Phosphorylation	VIPYFPYSKQSKMRK EECCCCCCCCHHHHH	25.18	21712546
120	Phosphorylation	IVCKLLASMLAKAGL HHHHHHHHHHHHCCC	17.82	22210691
128	Phosphorylation	MLAKAGLTHIITMDL HHHHCCCCEEEEEEC	15.31	22210691
132	Phosphorylation	AGLTHIITMDLHQKE CCCCEEEEEECCCCH	12.20	18491316
132 (in isoform 2)	Ubiquitination	-	12.20	-
160	Phosphorylation	ASPFLLQYIQEEIPN CCHHHHHHHHHHCCC	12.44	-
168	Phosphorylation	IQEEIPNYRNAVIVA HHHHCCCCCCEEEEE	10.41	-
176	Ubiquitination	RNAVIVAKSPDAAKR CCEEEEECCHHHHHH	52.18	21890473
177	Phosphorylation	NAVIVAKSPDAAKRA CEEEEECCHHHHHHH	20.48	29214152
186	Phosphorylation	DAAKRAQSYAERLRL HHHHHHHHHHHHHHH	25.89	23312004
187	Phosphorylation	AAKRAQSYAERLRLG HHHHHHHHHHHHHHC	10.62	24275569
205	Phosphorylation	IHGEAQCTELDMDDG ECCCCEEEECCCCCC	27.74	30266825
215	Phosphorylation	DMDDGRHSPPMVKNA CCCCCCCCCCCCCCC	29.36	29255136
223	Phosphorylation	PPMVKNATVHPGLEL CCCCCCCEECCCCCH	28.83	26074081
234	Phosphorylation	GLELPLMMAKEKPPI CCCHHHEECCCCCCE	6.76	24719451
238	Ubiquitination	PLMMAKEKPPITVVG HHEECCCCCCEEEEE	56.22	21890473
238	Acetylation	PLMMAKEKPPITVVG HHEECCCCCCEEEEE	56.22	42364885
238	2-Hydroxyisobutyrylation	PLMMAKEKPPITVVG HHEECCCCCCEEEEE	56.22	-
238	Ubiquitination	PLMMAKEKPPITVVG HHEECCCCCCEEEEE	56.22	21890473
242	Phosphorylation	AKEKPPITVVGDVGG CCCCCCEEEEECCCC	18.21	26074081
244	Phosphorylation	EKPPITVVGDVGGRI CCCCEEEEECCCCEE	3.97	24719451
267 (in isoform 2)	Ubiquitination	-	10.03	-
278	Phosphorylation	ILKERGAYKIYVMAT HHHHCCCEEEEEEEE	10.76	-
281	Phosphorylation	ERGAYKIYVMATHGI HCCCEEEEEEEECCC	4.68	-
317	Acetylation	TVPHEVQKLQCPKIK CCCHHHHHCCCCCCC	45.78	26051181
344	Phosphorylation	RRIHNGESMAYLFRN HHHHCCCCCEEEEEC	15.31	25693802
347	Phosphorylation	HNGESMAYLFRNITV HCCCCCEEEEECCCC	9.57	25693802

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KPRA_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 KPRA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KPRA_HUMAN	PRPSAP1	physical	16189514
PKHF2_HUMAN	PLEKHF2	physical	16189514
PRPS1_HUMAN	PRPS1	physical	9366267
PRPS2_HUMAN	PRPS2	physical	9366267
UBCP1_HUMAN	UBLCP1	physical	22939629
KPRA_HUMAN	PRPSAP1	physical	19447967
NS1BP_HUMAN	IVNS1ABP	physical	26186194
KPRB_HUMAN	PRPSAP2	physical	26186194
KPRB_HUMAN	PRPSAP2	physical	28514442
NS1BP_HUMAN	IVNS1ABP	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

"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 MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

Phosphorylation

"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-215, AND MASSSPECTROMETRY.
PubMed: 18669648