RLA1_HUMAN - dbPTM
RLA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RLA1_HUMAN
UniProt AC P05386
Protein Name 60S acidic ribosomal protein P1
Gene Name RPLP1
Organism Homo sapiens (Human).
Sequence Length 114
Subcellular Localization
Protein Description Plays an important role in the elongation step of protein synthesis..
Protein Sequence MASVSELACIYSALILHDDEVTVTEDKINALIKAAGVNVEPFWPGLFAKALANVNIGSLICNVGAGGPAPAAGAAPAGGPAPSTAAAPAEEKKVEAKKEESEESDDDMGFGLFD
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------MASVSELAC
------CCCHHHHHH		20.7422223895
3Phosphorylation-----MASVSELACI
-----CCCHHHHHHH		25.5225159151
5Phosphorylation---MASVSELACIYS
---CCCHHHHHHHHH		25.1326657352
11PhosphorylationVSELACIYSALILHD
HHHHHHHHHHHHCCC		6.4317924679
12PhosphorylationSELACIYSALILHDD
HHHHHHHHHHHCCCC		9.1830140170
22PhosphorylationILHDDEVTVTEDKIN
HCCCCCCCCCHHHHH		21.4728348404
33UbiquitinationDKINALIKAAGVNVE
HHHHHHHHHHCCCCC		32.79-
49MethylationFWPGLFAKALANVNI
CCHHHHHHHHHCCCC		36.2830793797
49UbiquitinationFWPGLFAKALANVNI
CCHHHHHHHHHCCCC		36.282063986
58PhosphorylationLANVNIGSLICNVGA
HHCCCCCCEEECCCC		15.68-
61GlutathionylationVNIGSLICNVGAGGP
CCCCCEEECCCCCCC		4.0222555962
83PhosphorylationPAGGPAPSTAAAPAE
CCCCCCCCCCCCCHH		32.5529514088
84PhosphorylationAGGPAPSTAAAPAEE
CCCCCCCCCCCCHHH		21.1829514088
92AcetylationAAAPAEEKKVEAKKE
CCCCHHHHHHHHHHH		54.3323236377
92UbiquitinationAAAPAEEKKVEAKKE
CCCCHHHHHHHHHHH		54.33-
93AcetylationAAPAEEKKVEAKKEE
CCCHHHHHHHHHHHH		48.8926051181
93UbiquitinationAAPAEEKKVEAKKEE
CCCHHHHHHHHHHHH		48.89-
101PhosphorylationVEAKKEESEESDDDM
HHHHHHHCCCCCCCC		47.9919664994
104PhosphorylationKKEESEESDDDMGFG
HHHHCCCCCCCCCCC		42.1419664994
108SulfoxidationSEESDDDMGFGLFD-
CCCCCCCCCCCCCC-		6.5321406390
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 RLA1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RLA1_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 RLA1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RLA2_HUMANRPLP2physical
10856704
XRCC6_HUMANXRCC6physical
16169070
PTN_HUMANPTNphysical
16169070
LRIF1_HUMANLRIF1physical
16169070
BRD7_HUMANBRD7physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
TBB2A_HUMANTUBB2Aphysical
16169070
RLA1_HUMANRPLP1physical
10856704
RLA2_HUMANRPLP2physical
22939629
RS15_HUMANRPS15physical
22939629
RS16_HUMANRPS16physical
22939629
RS13_HUMANRPS13physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RS2_HUMANRPS2physical
22939629
RSSA_HUMANRPSAphysical
22939629
RS7_HUMANRPS7physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS11_HUMANRPS11physical
22939629
RS6_HUMANRPS6physical
22939629
RS8_HUMANRPS8physical
22939629
RS5_HUMANRPS5physical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RS26_HUMANRPS26physical
22939629
RS23_HUMANRPS23physical
22939629
RS3_HUMANRPS3physical
22939629
RS17_HUMANRPS17physical
22939629
RS24_HUMANRPS24physical
22939629
RS19_HUMANRPS19physical
22939629
RS10_HUMANRPS10physical
22939629
RS25_HUMANRPS25physical
22939629
RS21_HUMANRPS21physical
22939629
RS27A_HUMANRPS27Aphysical
22939629
TM165_HUMANTMEM165physical
22939629
RT35_HUMANMRPS35physical
22939629
RL19_HUMANRPL19physical
22863883
RLA0_HUMANRPLP0physical
22863883
RL10A_HUMANRPL10Aphysical
26344197
RL12_HUMANRPL12physical
26344197
RL14_HUMANRPL14physical
26344197
RL18_HUMANRPL18physical
26344197
RL27A_HUMANRPL27Aphysical
26344197
RL29_HUMANRPL29physical
26344197
RL30_HUMANRPL30physical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL4_HUMANRPL4physical
26344197
RL7A_HUMANRPL7Aphysical
26344197
RS14_HUMANRPS14physical
26344197
RS16_HUMANRPS16physical
26344197
RS18_HUMANRPS18physical
26344197
RS19_HUMANRPS19physical
26344197
RS25_HUMANRPS25physical
26344197
RS26_HUMANRPS26physical
26344197
RS3_HUMANRPS3physical
26344197
RS3A_HUMANRPS3Aphysical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS7_HUMANRPS7physical
26344197
RSSA_HUMANRPSAphysical
26344197
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 RLA1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-101 AND SER-104, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-101 AND SER-104, AND MASS SPECTROMETRY.
"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-101 AND SER-104, ANDMASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, ANDMASS SPECTROMETRY.
"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-101 AND SER-104, ANDMASS SPECTROMETRY.
"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-5; TYR-11 AND SER-12,AND MASS SPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, ANDMASS SPECTROMETRY.
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.
"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-101 AND SER-104, ANDMASS SPECTROMETRY.
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, ANDMASS SPECTROMETRY.
"Identification and characterization of phosphorylated proteins in thehuman pituitary.";
Giorgianni F., Beranova-Giorgianni S., Desiderio D.M.;
Proteomics 4:587-598(2004).
Cited for: PHOSPHORYLATION AT SER-101.

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