POP5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: POP5_HUMAN
• UniProt AC: Q969H6
• Protein Name: Ribonuclease P/MRP protein subunit POP5
• Gene Name: POP5
• Organism: Homo sapiens (Human).
• Sequence Length: 163
• Subcellular Localization: Nucleus, nucleolus.
• 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..
• Protein Sequence: MVRFKHRYLLCELVSDDPRCRLSLDDRVLSSLVRDTIARVHGTFGAAACSIGFAVRYLNAYTGIVLLRCRKEFYQLVWSALPFITYLENKGHRYPCFFNTLHVGGTIRTCQKFLIQYNRRQLLILLQNCTDEGEREAIQKSVTRSCLLEEEEESGEEAAEAME

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
31	Phosphorylation	LDDRVLSSLVRDTIA CCHHHHHHHHHHHHH	27.07	24719451
57	Phosphorylation	SIGFAVRYLNAYTGI HHHHHHHHHHHCCCC	9.56	-
61	Phosphorylation	AVRYLNAYTGIVLLR HHHHHHHCCCCCEEE	12.39	-
90	Ubiquitination	FITYLENKGHRYPCF HHHHHHCCCCCCCEE	46.87	33845483
104	Phosphorylation	FFNTLHVGGTIRTCQ ECEEECCCCHHHHHH	19.44	33259812
112	Acetylation	GTIRTCQKFLIQYNR CHHHHHHHHHHHCCH	44.26	26051181
117	Phosphorylation	CQKFLIQYNRRQLLI HHHHHHHCCHHHHHH	12.02	27642862
140	Ubiquitination	GEREAIQKSVTRSCL HHHHHHHHHHHHHHH	40.56	24816145
145	Phosphorylation	IQKSVTRSCLLEEEE HHHHHHHHHHHHHHH	10.35	30278072
154	Phosphorylation	LLEEEEESGEEAAEA HHHHHHHHHHHHHHH	55.58	30175587
158	Ubiquitination	EEESGEEAAEAME-- HHHHHHHHHHHHC--	13.29	24816145

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

Oops, there are no upstream regulatory protein records of POP5_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of POP5_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 POP5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPP25_HUMAN	RPP25	physical	15096576
RPP14_HUMAN	RPP14	physical	15096576
C102B_HUMAN	CCDC102B	physical	25416956
CEP44_HUMAN	CEP44	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956

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

Phosphorylation

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-154, AND MASSSPECTROMETRY.
PubMed: 18669648

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASSSPECTROMETRY.
PubMed: 18691976

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASSSPECTROMETRY.
PubMed: 17081983