dbPTM

RPP38_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPP38_HUMAN
UniProt AC	P78345
Protein Name	Ribonuclease P protein subunit p38
Gene Name	RPP38
Organism	Homo sapiens (Human).
Sequence Length	283
Subcellular Localization	Nucleus, nucleolus .
Protein Description	Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. RPP38 may associate transiently with RNase P RNA as a factor involved in the transport of H1 RNA to the putative site of its assembly in the cell, the nucleolus..
Protein Sequence	MAAAPQAPGRGSLRKTRPLVVKTSLNNPYIIRWSALESEDMHFILQTLEDRLKAIGLQKIEDKKKKNKTPFLKKESREKCSIAVDISENLKEKKTDAKQQVSGWTPAHVRKQLAIGVNEVTRALERRELLLVLVCKSVKPAMITSHLIQLSLSRSVPACQVPRLSERIAPVIGLKCVLALAFKKNTTDFVDEVRAIIPRVPSLSVPWLQDRIEDSGENLETEPLESQDRELLDTSFEDLSKPKRKLADGRQASVTLQPLKIKKLIPNPNKIRKPPKSKKATPK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAPQAPG ------CCCCCCCCC	16.60	19413330
10	Methylation	AAPQAPGRGSLRKTR CCCCCCCCCCCCCCC	30.39	115386055
12	Phosphorylation	PQAPGRGSLRKTRPL CCCCCCCCCCCCCCE	24.52	23401153
14	Methylation	APGRGSLRKTRPLVV CCCCCCCCCCCCEEE	39.74	115386061
23	Phosphorylation	TRPLVVKTSLNNPYI CCCEEEEECCCCCEE	27.17	28450419
24	Phosphorylation	RPLVVKTSLNNPYII CCEEEEECCCCCEEE	24.31	23186163
53	Ubiquitination	QTLEDRLKAIGLQKI HHHHHHHHHHCCHHH	38.56	-
59	Ubiquitination	LKAIGLQKIEDKKKK HHHHCCHHHHHHHHC	53.78	-
69	Phosphorylation	DKKKKNKTPFLKKES HHHHCCCCCCCCHHH	28.77	28555341
102	Phosphorylation	TDAKQQVSGWTPAHV CCHHHHHCCCCHHHH	25.03	-
111	Ubiquitination	WTPAHVRKQLAIGVN CCHHHHHHHHHHCHH	48.88	-
151	Phosphorylation	TSHLIQLSLSRSVPA HHHHHHHHHCCCCCH	14.13	24719451
153	Phosphorylation	HLIQLSLSRSVPACQ HHHHHHHCCCCCHHH	21.09	17081983
184	Ubiquitination	VLALAFKKNTTDFVD HHHHHHHCCCCCHHH	53.74	29967540
215	Phosphorylation	LQDRIEDSGENLETE HHHHHHCCCCCCCCC	34.91	21815630
221	Phosphorylation	DSGENLETEPLESQD CCCCCCCCCCCCHHC	46.17	22115753
226	Phosphorylation	LETEPLESQDRELLD CCCCCCCHHCHHHHH	45.09	29255136
234	Phosphorylation	QDRELLDTSFEDLSK HCHHHHHCCHHHHCC	34.97	30266825
235	Phosphorylation	DRELLDTSFEDLSKP CHHHHHCCHHHHCCC	26.72	19664994
240	Phosphorylation	DTSFEDLSKPKRKLA HCCHHHHCCCCHHHC	60.27	29255136
241	Ubiquitination	TSFEDLSKPKRKLAD CCHHHHCCCCHHHCC	62.95	29967540
241	Acetylation	TSFEDLSKPKRKLAD CCHHHHCCCCHHHCC	62.95	23236377
253	Phosphorylation	LADGRQASVTLQPLK HCCCCCCEEEECCCE	13.80	28355574
255	Phosphorylation	DGRQASVTLQPLKIK CCCCCEEEECCCEEH	19.72	29978859
283	Ubiquitination	KSKKATPK------- CCCCCCCC-------	69.49	24816145

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 RPP38_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPP38_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 RPP38_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPP29_HUMAN	POP4	physical	15096576
ICAL_HUMAN	CAST	physical	22863883
PSA1_HUMAN	PSMA1	physical	22863883
PSA4_HUMAN	PSMA4	physical	22863883
PSA5_HUMAN	PSMA5	physical	22863883
PSB1_HUMAN	PSMB1	physical	22863883
PSB4_HUMAN	PSMB4	physical	22863883
PSB5_HUMAN	PSMB5	physical	22863883
PSB8_HUMAN	PSMB8	physical	22863883
VASP_HUMAN	VASP	physical	22863883

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 RPP38_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-235, AND MASSSPECTROMETRY.	18669648 [Abstract]