RPP29_HUMAN - dbPTM
RPP29_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPP29_HUMAN
UniProt AC O95707
Protein Name Ribonuclease P protein subunit p29
Gene Name POP4
Organism Homo sapiens (Human).
Sequence Length 220
Subcellular Localization Nucleus, nucleolus .
Protein Description Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. May function with RPP38 to coordinate the nucleolar targeting and/or assembly of RNase P..
Protein Sequence MKSVIYHALSQKEANDSDVQPSGAQRAEAFVRAFLKRSTPRMSPQAREDQLQRKAVVLEYFTRHKRKEKKKKAKGLSARQRRELRLFDIKPEQQRYSLFLPLHELWKQYIRDLCSGLKPDTQPQMIQAKLLKADLHGAIISVTKSKCPSYVGITGILLQETKHIFKIITKEDRLKVIPKLNCVFTVETDGFISYIYGSKFQLRSSERSAKKFKAKGTIDL
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 Orthologous
Protein Cluster
2Acetylation------MKSVIYHAL
------CCHHHHHHH		54.1325953088
2Methylation------MKSVIYHAL
------CCHHHHHHH		54.13115975399
3Phosphorylation-----MKSVIYHALS
-----CCHHHHHHHC		16.6728555341
6Phosphorylation--MKSVIYHALSQKE
--CCHHHHHHHCHHH		4.4721945579
10PhosphorylationSVIYHALSQKEANDS
HHHHHHHCHHHCCCC		39.7321945579
12AcetylationIYHALSQKEANDSDV
HHHHHCHHHCCCCCC		56.2526051181
12UbiquitinationIYHALSQKEANDSDV
HHHHHCHHHCCCCCC		56.2522817900
17PhosphorylationSQKEANDSDVQPSGA
CHHHCCCCCCCCCHH		39.2225850435
22PhosphorylationNDSDVQPSGAQRAEA
CCCCCCCCHHHHHHH		29.6629396449
36"N6,N6-dimethyllysine"AFVRAFLKRSTPRMS
HHHHHHHHHCCCCCC		37.54-
36MethylationAFVRAFLKRSTPRMS
HHHHHHHHHCCCCCC		37.5423644510
38PhosphorylationVRAFLKRSTPRMSPQ
HHHHHHHCCCCCCHH		40.9726074081
39PhosphorylationRAFLKRSTPRMSPQA
HHHHHHCCCCCCHHH		20.9626074081
43PhosphorylationKRSTPRMSPQAREDQ
HHCCCCCCHHHCHHH		18.3630576142
54UbiquitinationREDQLQRKAVVLEYF
CHHHHHHHHHHHHHH		32.3533845483
60PhosphorylationRKAVVLEYFTRHKRK
HHHHHHHHHHHHHHH		13.1921214269
62PhosphorylationAVVLEYFTRHKRKEK
HHHHHHHHHHHHHHH		30.84-
70UbiquitinationRHKRKEKKKKAKGLS
HHHHHHHHHHHCCCC		61.6724816145
90UbiquitinationELRLFDIKPEQQRYS
HHHCCCCCHHHHHHH		44.3321906983
118AcetylationRDLCSGLKPDTQPQM
HHHHCCCCCCCCCHH		44.3526051181
118UbiquitinationRDLCSGLKPDTQPQM
HHHHCCCCCCCCCHH		44.35-
129UbiquitinationQPQMIQAKLLKADLH
CCHHHHHHHHHCCCC		37.6729967540
144UbiquitinationGAIISVTKSKCPSYV
CCEEEEECCCCCCCC		45.8433845483
145PhosphorylationAIISVTKSKCPSYVG
CEEEEECCCCCCCCC		30.0817924679
150PhosphorylationTKSKCPSYVGITGIL
ECCCCCCCCCCCEEH		6.4517924679
161PhosphorylationTGILLQETKHIFKII
CEEHHHCHHHHHEEC		18.2417924679
166UbiquitinationQETKHIFKIITKEDR
HCHHHHHEECCHHHH		32.3729967540
215UbiquitinationSAKKFKAKGTIDL--
HHHHHHCCCCCCC--		58.12-
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
10SPhosphorylationKinaseCHEK1O14757
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPP29_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 RPP29_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
POP1_HUMANPOP1physical
15096576
RPP29_HUMANPOP4physical
15096576
POP5_HUMANPOP5physical
15096576
RPP38_HUMANRPP38physical
15096576
POP1_HUMANPOP1physical
26186194
RP25L_HUMANRPP25Lphysical
26186194
NEPRO_HUMANC3orf17physical
26186194
GLU2B_HUMANPRKCSHphysical
26186194
NPM_HUMANNPM1physical
26186194
RPP40_HUMANRPP40physical
26186194
POP5_HUMANPOP5physical
26186194
CR021_HUMANC18orf21physical
26186194
RPP38_HUMANRPP38physical
26186194
POP7_HUMANPOP7physical
26186194
RPP14_HUMANRPP14physical
26186194
RPP30_HUMANRPP30physical
26186194
RPP25_HUMANRPP25physical
26186194
CR021_HUMANC18orf21physical
28514442
RPP25_HUMANRPP25physical
28514442
RPP30_HUMANRPP30physical
28514442
RPP40_HUMANRPP40physical
28514442
RPP14_HUMANRPP14physical
28514442
POP7_HUMANPOP7physical
28514442
RP25L_HUMANRPP25Lphysical
28514442
NEPRO_HUMANC3orf17physical
28514442
RPP38_HUMANRPP38physical
28514442
POP5_HUMANPOP5physical
28514442
POP1_HUMANPOP1physical
28514442
OSTF1_HUMANOSTF1physical
28514442
NPM_HUMANNPM1physical
28514442
DCAM_HUMANAMD1physical
28514442
RBM4B_HUMANRBM4Bphysical
28514442
NEB2_HUMANPPP1R9Bphysical
28514442
GLU2B_HUMANPRKCSHphysical
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 RPP29_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; TYR-150 ANDTHR-161, AND MASS SPECTROMETRY.

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