dbPTM

RPP30_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPP30_HUMAN
UniProt AC	P78346
Protein Name	Ribonuclease P protein subunit p30
Gene Name	RPP30
Organism	Homo sapiens (Human).
Sequence Length	268
Subcellular Localization	Nucleus, nucleolus .
Protein Description	Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends..
Protein Sequence	MAVFADLDLRAGSDLKALRGLVETAAHLGYSVVAINHIVDFKEKKQEIEKPVAVSELFTTLPIVQGKSRPIKILTRLTIIVSDPSHCNVLRATSSRARLYDVVAVFPKTEKLFHIACTHLDVDLVCITVTEKLPFYFKRPPINVAIDRGLAFELVYSPAIKDSTMRRYTISSALNLMQICKGKNVIISSAAERPLEIRGPYDVANLGLLFGLSESDAKAAVSTNCRAALLHGETRKTAFGIISTVKKPRPSEGDEDCLPASKKAKCEG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAVFADLDL ------CCEECCCCC	12.72	22223895
13	Phosphorylation	DLDLRAGSDLKALRG CCCCCCCCCHHHHHH	38.49	-
16	Ubiquitination	LRAGSDLKALRGLVE CCCCCCHHHHHHHHH	50.82	23000965
16	Acetylation	LRAGSDLKALRGLVE CCCCCCHHHHHHHHH	50.82	25953088
45	Acetylation	IVDFKEKKQEIEKPV EEEHHHHHHHCCCCC	55.01	26051181
45	Ubiquitination	IVDFKEKKQEIEKPV EEEHHHHHHHCCCCC	55.01	-
50	Ubiquitination	EKKQEIEKPVAVSEL HHHHHCCCCCHHHHH	50.91	29967540
78	Phosphorylation	IKILTRLTIIVSDPS CEEEEEEEEEECCHH	12.84	20068231
82	Phosphorylation	TRLTIIVSDPSHCNV EEEEEEECCHHHCCH	33.14	20068231
85	Phosphorylation	TIIVSDPSHCNVLRA EEEECCHHHCCHHHC	45.74	20068231
108	Acetylation	DVVAVFPKTEKLFHI EEEEEEECCCHHHHH	58.83	26051181
108	Ubiquitination	DVVAVFPKTEKLFHI EEEEEEECCCHHHHH	58.83	-
132	Ubiquitination	VCITVTEKLPFYFKR EEEEECCCCCCCCCC	52.69	23000965
138	Acetylation	EKLPFYFKRPPINVA CCCCCCCCCCCCEEE	53.25	25953088
138	Ubiquitination	EKLPFYFKRPPINVA CCCCCCCCCCCCEEE	53.25	23000965
161	Ubiquitination	LVYSPAIKDSTMRRY EEECCCCCCCCCHHH	47.97	2190698
168	Phosphorylation	KDSTMRRYTISSALN CCCCCHHHCHHHHHH	9.69	29496907
169	Phosphorylation	DSTMRRYTISSALNL CCCCHHHCHHHHHHH	16.75	-
171	Phosphorylation	TMRRYTISSALNLMQ CCHHHCHHHHHHHHH	11.19	-
172	Phosphorylation	MRRYTISSALNLMQI CHHHCHHHHHHHHHH	32.69	-
181	Ubiquitination	LNLMQICKGKNVIIS HHHHHHHCCCCEEEC	74.64	-
183	Ubiquitination	LMQICKGKNVIISSA HHHHHCCCCEEECCC	33.27	29967540
218	Ubiquitination	GLSESDAKAAVSTNC CCCHHHHHHHHHCCC	41.70	29967540
236	Ubiquitination	LLHGETRKTAFGIIS HHCCCCCCCEEEEEE	52.18	27667366
237	Phosphorylation	LHGETRKTAFGIIST HCCCCCCCEEEEEEE	24.75	28509920
243	Phosphorylation	KTAFGIISTVKKPRP CCEEEEEEECCCCCC	25.81	20068231
244	Phosphorylation	TAFGIISTVKKPRPS CEEEEEEECCCCCCC	26.40	20068231
246	Ubiquitination	FGIISTVKKPRPSEG EEEEEECCCCCCCCC	58.09	33845483
251	Phosphorylation	TVKKPRPSEGDEDCL ECCCCCCCCCCCCCC	56.33	29255136
261	Phosphorylation	DEDCLPASKKAKCEG CCCCCCHHHCCCCCC	32.52	20201521
262	Ubiquitination	EDCLPASKKAKCEG- CCCCCHHHCCCCCC-	59.88	29967540
262	Acetylation	EDCLPASKKAKCEG- CCCCCHHHCCCCCC-	59.88	25953088
263	Acetylation	DCLPASKKAKCEG-- CCCCHHHCCCCCC--	51.05	12431363

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 RPP30_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPP30_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 RPP30_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
E41L1_HUMAN	EPB41L1	physical	22863883
KIF15_HUMAN	KIF15	physical	22863883
POP1_HUMAN	POP1	physical	22863883
PSB1_HUMAN	PSMB1	physical	22863883
RPP25_HUMAN	RPP25	physical	28514442
RPP14_HUMAN	RPP14	physical	28514442
RPP40_HUMAN	RPP40	physical	28514442
RP25L_HUMAN	RPP25L	physical	28514442
RPP38_HUMAN	RPP38	physical	28514442
NEPRO_HUMAN	C3orf17	physical	28514442
POP5_HUMAN	POP5	physical	28514442
POP7_HUMAN	POP7	physical	28514442
POP1_HUMAN	POP1	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 RPP30_HUMAN

Related Literatures of Post-Translational Modification

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-251, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND MASSSPECTROMETRY.	18220336 [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-251, AND MASSSPECTROMETRY.	17287340 [Abstract]
"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-251, AND MASSSPECTROMETRY.	17081983 [Abstract]