dbPTM

RPP25_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPP25_HUMAN
UniProt AC	Q9BUL9
Protein Name	Ribonuclease P protein subunit p25
Gene Name	RPP25
Organism	Homo sapiens (Human).
Sequence Length	199
Subcellular Localization	Nucleus .
Protein Description	Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. This subunit binds to RNA..
Protein Sequence	MENFRKVRSEEAPAGCGAEGGGPGSGPFADLAPGAVHMRVKEGSKIRNLMAFATASMAQPATRAIVFSGCGRATTKTVTCAEILKRRLAGLHQVTRLRYRSVREVWQSLPPGPTQGQTPGEPAASLSVLKNVPGLAILLSKDALDPRQPGYQPPNPHPGPSSPPAAPASKRSLGEPAAGEGSAKRSQPEPGVADEDQTA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	Phosphorylation	HMRVKEGSKIRNLMA EEEECCCHHHHHHHH	26.46	20068231
54	Phosphorylation	RNLMAFATASMAQPA HHHHHHHHHHHCCCC	16.89	20068231
56	Phosphorylation	LMAFATASMAQPATR HHHHHHHHHCCCCCE	15.42	20068231
62	Phosphorylation	ASMAQPATRAIVFSG HHHCCCCCEEEEECC	27.58	22210691
68	Phosphorylation	ATRAIVFSGCGRATT CCEEEEECCCCCCCC	23.45	22210691
74	Phosphorylation	FSGCGRATTKTVTCA ECCCCCCCCCCCHHH	27.71	22210691
75	Phosphorylation	SGCGRATTKTVTCAE CCCCCCCCCCCHHHH	24.59	22210691
85	2-Hydroxyisobutyrylation	VTCAEILKRRLAGLH CHHHHHHHHHHCCHH	40.93	-
151	Phosphorylation	LDPRQPGYQPPNPHP CCCCCCCCCCCCCCC	25.24	24732914
161	Phosphorylation	PNPHPGPSSPPAAPA CCCCCCCCCCCCCCC	62.48	23401153
162	Phosphorylation	NPHPGPSSPPAAPAS CCCCCCCCCCCCCCH	37.73	30278072
169	Phosphorylation	SPPAAPASKRSLGEP CCCCCCCHHCCCCCC	27.78	28176443
170	Acetylation	PPAAPASKRSLGEPA CCCCCCHHCCCCCCC	48.38	26051181
172	Phosphorylation	AAPASKRSLGEPAAG CCCCHHCCCCCCCCC	44.45	29255136
182	Phosphorylation	EPAAGEGSAKRSQPE CCCCCCCCCCCCCCC	26.72	25159151
184	Acetylation	AAGEGSAKRSQPEPG CCCCCCCCCCCCCCC	55.04	26051181
186	Phosphorylation	GEGSAKRSQPEPGVA CCCCCCCCCCCCCCC	49.75	25849741
198	Phosphorylation	GVADEDQTA------ CCCCCCCCC------	46.81	28450419

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 RPP25_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPP25_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 RPP25_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
POP1_HUMAN	POP1	physical	15096576
RPP29_HUMAN	POP4	physical	15096576
POP7_HUMAN	POP7	physical	15096576
LARP7_HUMAN	LARP7	physical	22863883
MTA2_HUMAN	MTA2	physical	22863883
RPP40_HUMAN	RPP40	physical	22863883
POP1_HUMAN	POP1	physical	26186194
NEPRO_HUMAN	C3orf17	physical	26186194
RPP40_HUMAN	RPP40	physical	26186194
POP5_HUMAN	POP5	physical	26186194
RBL2A_HUMAN	RABL2A	physical	26186194
RPP38_HUMAN	RPP38	physical	26186194
RPP30_HUMAN	RPP30	physical	26186194
UBP13_HUMAN	USP13	physical	26186194
RPP14_HUMAN	RPP14	physical	26186194
CR021_HUMAN	C18orf21	physical	26186194
POP7_HUMAN	POP7	physical	26186194
UBP13_HUMAN	USP13	physical	28514442
RPP40_HUMAN	RPP40	physical	28514442
POP7_HUMAN	POP7	physical	28514442
RPP38_HUMAN	RPP38	physical	28514442
RBL2A_HUMAN	RABL2A	physical	28514442
RPP14_HUMAN	RPP14	physical	28514442
POP5_HUMAN	POP5	physical	28514442
POP1_HUMAN	POP1	physical	28514442
NEPRO_HUMAN	C3orf17	physical	28514442
RBM4_HUMAN	RBM4	physical	28514442
AKAP1_HUMAN	AKAP1	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.

Regulatory Network of RPP25_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-172, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASSSPECTROMETRY.	17287340 [Abstract]