RLA2_HUMAN - dbPTM
RLA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RLA2_HUMAN
UniProt AC P05387
Protein Name 60S acidic ribosomal protein P2
Gene Name RPLP2
Organism Homo sapiens (Human).
Sequence Length 115
Subcellular Localization
Protein Description Plays an important role in the elongation step of protein synthesis..
Protein Sequence MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD
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
1Acetylation-------MRYVASYL
-------CHHHHHHH		6.6920068231
3Phosphorylation-----MRYVASYLLA
-----CHHHHHHHHH		10.0821955146
6Phosphorylation--MRYVASYLLAALG
--CHHHHHHHHHHHC		13.2821955146
7Phosphorylation-MRYVASYLLAALGG
-CHHHHHHHHHHHCC		8.9421955146
16PhosphorylationLAALGGNSSPSAKDI
HHHHCCCCCCCHHHH		47.0722167270
17PhosphorylationAALGGNSSPSAKDIK
HHHCCCCCCCHHHHH		27.2022167270
19PhosphorylationLGGNSSPSAKDIKKI
HCCCCCCCHHHHHHH		50.3122167270
21UbiquitinationGNSSPSAKDIKKILD
CCCCCCHHHHHHHHH		65.4121890473
21UbiquitinationGNSSPSAKDIKKILD
CCCCCCHHHHHHHHH		65.4121890473
21SuccinylationGNSSPSAKDIKKILD
CCCCCCHHHHHHHHH		65.4123954790
21SuccinylationGNSSPSAKDIKKILD
CCCCCCHHHHHHHHH		65.41-
21AcetylationGNSSPSAKDIKKILD
CCCCCCHHHHHHHHH		65.4119608861
24UbiquitinationSPSAKDIKKILDSVG
CCCHHHHHHHHHHHC		43.8421906983
24AcetylationSPSAKDIKKILDSVG
CCCHHHHHHHHHHHC		43.8425953088
25AcetylationPSAKDIKKILDSVGI
CCHHHHHHHHHHHCC		49.1623749302
25UbiquitinationPSAKDIKKILDSVGI
CCHHHHHHHHHHHCC		49.1621906983
25UbiquitinationPSAKDIKKILDSVGI
CCHHHHHHHHHHHCC		49.1621890473
29PhosphorylationDIKKILDSVGIEADD
HHHHHHHHHCCCCCH		20.8521406692
41UbiquitinationADDDRLNKVISELNG
CCHHHHHHHHHHHCC		45.6021890473
41UbiquitinationADDDRLNKVISELNG
CCHHHHHHHHHHHCC		45.6021906983
41AcetylationADDDRLNKVISELNG
CCHHHHHHHHHHHCC		45.6026051181
41MethylationADDDRLNKVISELNG
CCHHHHHHHHHHHCC		45.6072602583
41SumoylationADDDRLNKVISELNG
CCHHHHHHHHHHHCC		45.60-
44PhosphorylationDRLNKVISELNGKNI
HHHHHHHHHHCCCCH		38.7324850871
49UbiquitinationVISELNGKNIEDVIA
HHHHHCCCCHHHHHH		54.3921890473
492-HydroxyisobutyrylationVISELNGKNIEDVIA
HHHHHCCCCHHHHHH		54.39-
49AcetylationVISELNGKNIEDVIA
HHHHHCCCCHHHHHH		54.3923954790
49UbiquitinationVISELNGKNIEDVIA
HHHHHCCCCHHHHHH		54.3921890473
61UbiquitinationVIAQGIGKLASVPAG
HHHHCCHHHHCCCCC		38.6721906983
61AcetylationVIAQGIGKLASVPAG
HHHHCCHHHHCCCCC		38.6726051181
64PhosphorylationQGIGKLASVPAGGAV
HCCHHHHCCCCCCEE		38.7829255136
74O-linked_GlycosylationAGGAVAVSAAPGSAA
CCCEEEEEECCCCCC		14.6930059200
74PhosphorylationAGGAVAVSAAPGSAA
CCCEEEEEECCCCCC		14.6930266825
79O-linked_GlycosylationAVSAAPGSAAPAAGS
EEEECCCCCCCCCCC		21.8730059200
79PhosphorylationAVSAAPGSAAPAAGS
EEEECCCCCCCCCCC		21.8729255136
86PhosphorylationSAAPAAGSAPAAAEE
CCCCCCCCCCHHHHH		26.7629255136
94UbiquitinationAPAAAEEKKDEKKEE
CCHHHHHHHHHHHHH		57.9621906983
94AcetylationAPAAAEEKKDEKKEE
CCHHHHHHHHHHHHH		57.9625953088
942-HydroxyisobutyrylationAPAAAEEKKDEKKEE
CCHHHHHHHHHHHHH		57.96-
95UbiquitinationPAAAEEKKDEKKEES
CHHHHHHHHHHHHHC		74.52-
98UbiquitinationAEEKKDEKKEESEES
HHHHHHHHHHHCCCC		75.51-
102PhosphorylationKDEKKEESEESDDDM
HHHHHHHCCCCCCCC		47.9919664994
105PhosphorylationKKEESEESDDDMGFG
HHHHCCCCCCCCCCC		42.1419664994
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
102SPhosphorylationKinaseADRBK1P25098
GPS
105SPhosphorylationKinaseADRBK1P25098
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RLA2_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 RLA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RLA2_HUMANRPLP2physical
10856704
RLA1_HUMANRPLP1physical
10856704
RS11_HUMANRPS11physical
22939629
RS17_HUMANRPS17physical
22939629
RS25_HUMANRPS25physical
22939629
RS26_HUMANRPS26physical
22939629
RS8_HUMANRPS8physical
22939629
RS7_HUMANRPS7physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RS23_HUMANRPS23physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS24_HUMANRPS24physical
22939629
RS13_HUMANRPS13physical
22939629
RS16_HUMANRPS16physical
22939629
RS5_HUMANRPS5physical
22939629
RS6_HUMANRPS6physical
22939629
RS15_HUMANRPS15physical
22939629
RS2_HUMANRPS2physical
22939629
RS3_HUMANRPS3physical
22939629
RSSA_HUMANRPSAphysical
22939629
RS28_HUMANRPS28physical
22939629
RS14_HUMANRPS14physical
22939629
RS20_HUMANRPS20physical
22939629
RS21_HUMANRPS21physical
22939629
RL40_HUMANUBA52physical
22939629
ROA1_HUMANHNRNPA1physical
22939629
ROA3_HUMANHNRNPA3physical
22939629
RM12_HUMANMRPL12physical
22939629
RS27L_HUMANRPS27Lphysical
22939629
CNDP2_HUMANCNDP2physical
22863883
SIAS_HUMANNANSphysical
22863883
PSA_HUMANNPEPPSphysical
22863883
RL23_HUMANRPL23physical
22863883
DDX24_HUMANDDX24physical
26344197
HNRPU_HUMANHNRNPUphysical
26344197
RT21_HUMANMRPS21physical
26344197
RL10_HUMANRPL10physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL11_HUMANRPL11physical
26344197
RL12_HUMANRPL12physical
26344197
RL14_HUMANRPL14physical
26344197
RL15_HUMANRPL15physical
26344197
RL18A_HUMANRPL18Aphysical
26344197
RL23A_HUMANRPL23Aphysical
26344197
RL27A_HUMANRPL27Aphysical
26344197
RL31_HUMANRPL31physical
26344197
RL35A_HUMANRPL35Aphysical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL5_HUMANRPL5physical
26344197
RL7_HUMANRPL7physical
26344197
RL9_HUMANRPL9physical
26344197
RLA0_HUMANRPLP0physical
26344197
RLA1_HUMANRPLP1physical
26344197
RS15A_HUMANRPS15Aphysical
26344197
RS18_HUMANRPS18physical
26344197
RS19_HUMANRPS19physical
26344197
RS23_HUMANRPS23physical
26344197
RS26_HUMANRPS26physical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS5_HUMANRPS5physical
26344197
RS7_HUMANRPS7physical
26344197
RS8_HUMANRPS8physical
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 RLA2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-49, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-17; SER-79; SER-102 ANDSER-105, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-17; SER-79;SER-102 AND SER-105, AND MASS SPECTROMETRY.
"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-17; SER-79 AND SER-86,AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, ANDMASS 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-17; SER-79; SER-86;SER-102 AND SER-105, AND MASS SPECTROMETRY.
"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-79; SER-102 AND SER-105,AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-17; SER-102 ANDSER-105, AND MASS 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-102 AND SER-105, ANDMASS 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-102 AND SER-105, 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-102, AND MASSSPECTROMETRY.
"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-102 AND SER-105, 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-17, 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-17, AND MASSSPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, 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-102.

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