Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  60S ribosomal protein L30  

UniProtKB / Swiss-Prot ID :  RL30_HUMAN

Gene Name (Synonyms) : 
RPL30  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MVAAKKTKKSLESINSRLQLVMKSGKYVLGYKQTLKMIRQGKAKLVILANNCPALRKSEIEYYAMLAKTG...
Predicted Secondary Structure CCCCCHHHHHHHHHHHHHHHHHHCCCEEECHHHHHHHHHCCCCCEEEEECCCCHHHHHHHHHHHHHCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
9Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KKTKKSLES
CHHHHHHHH
66.56Phosphositeplus
Link
10PhosphoserineKTKKSLESI
HHHHHHHHH
38.64HPRD
Link
10PhosphoserineKTKKSLESI
HHHHHHHHH
38.64PhosphoELM
Link
10PhosphoserineKTKKSLESI
HHHHHHHHH
38.64Phosphositeplus
Link
10PhosphoserineKTKKSLESI
HHHHHHHHH
38.64SysPTM
Link
10Phosphoserine.KTKKSLESI
HHHHHHHHH
38.64UniProtKB
Link
13PhosphoserineKSLESINSR
HHHHHHHHH
32.15HPRD
Link
16PhosphoserineESINSRLQL
HHHHHHHHH
32.47HPRD
Link
16PhosphoserineESINSRLQL
HHHHHHHHH
32.47Phosphositeplus
Link
23Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QLVMKSGKY
HHHHHCCCE
48.88Phosphositeplus
Link
26Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MKSGKYVLG
HHCCCEEEC
39.00Phosphositeplus
Link
26N6-acetyllysineMKSGKYVLG
HHCCCEEEC
39.00HPRD
Link
26N6-acetyllysineMKSGKYVLG
HHCCCEEEC
39.00Phosphositeplus
Link
26N6-acetyllysine.MKSGKYVLG
HHCCCEEEC
39.00UniProtKB
Link
27PhosphotyrosineKSGKYVLGY
HCCCEEECH
12.39Phosphositeplus
Link
32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VLGYKQTLK
EECHHHHHH
34.70Phosphositeplus
Link
44Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QGKAKLVIL
CCCCCEEEE
46.93Phosphositeplus
Link
52S-nitrosocysteineLANNCPALR
EECCCCHHH
1.77dbSNO
Link
52S-nitrosocysteineLANNCPALR
EECCCCHHH
1.77HPRD
Link
57Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PALRKSEIE
CHHHHHHHH
53.98Phosphositeplus
Link
68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AMLAKTGVH
HHHCCCCEE
41.68Phosphositeplus
Link
74PhosphotyrosineGVHHYSGNN
CEEEEECCC
11.91Phosphositeplus
Link
74Phosphotyrosine.GVHHYSGNN
CEEEEECCC
11.91UniProtKB
Link
83PhosphothreonineIELGTACGK
CHHHHHCCC
31.25HPRD
Link
92S-nitrosocysteineYYRVCTLAI
CEEEEEEEE
1.59dbSNO
Link
92S-nitrosocysteineYYRVCTLAI
CEEEEEEEE
1.59HPRD
Link
102PhosphoserineDPGDSDIIR
CCCCHHHHH
36.30HPRD
Link
102PhosphoserineDPGDSDIIR
CCCCHHHHH
36.30Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NFKB2_HUMANphysical interactionMINT-48767MINT14743216
RELB_HUMANphysical interactionMINT-49033MINT14743216
M3K1_HUMANphysical interactionMINT-47981MINT14743216
NFKB2_HUMANphysical interactionDIP:44856EDIP14743216
M3K14_HUMANphysical interactionDIP:44920EDIP14743216
M3K14_HUMANin vitroHPRD:01595HPRD14743216
RS20_HUMANENSP00000287038STRING
RL18_HUMANENSP00000287038STRING
RS5_HUMANENSP00000287038STRING
RL6_HUMANENSP00000287038STRING
RS18_HUMANENSP00000287038STRING
RS19_HUMANENSP00000287038STRING
RL18A_HUMANENSP00000287038STRING
RL19_HUMANENSP00000287038STRING
RS13_HUMANENSP00000287038STRING
RS12_HUMANENSP00000287038STRING
RS15_HUMANENSP00000287038STRING
RS25_HUMANENSP00000287038STRING
RS4Y1_HUMANENSP00000287038STRING
RS16_HUMANENSP00000287038STRING
RL36_HUMANENSP00000287038STRING
RFX1_HUMANENSP00000287038STRING
RL35_HUMANENSP00000287038STRING
RL8_HUMANENSP00000287038STRING
RL31_HUMANENSP00000287038STRING
RL26L_HUMANENSP00000287038STRING
RL24_HUMANENSP00000287038STRING
RL3L_HUMANENSP00000287038STRING
RS11_HUMANENSP00000287038STRING
RL13A_HUMANENSP00000287038STRING
RS27A_HUMANENSP00000287038STRING
UBIQ_HUMANENSP00000287038STRING
RL37_HUMANENSP00000287038STRING
RS3_HUMANENSP00000287038STRING
UBIM_HUMANENSP00000287038STRING
RS30_HUMANENSP00000287038STRING
IF2P_HUMANENSP00000287038STRING
RL26_HUMANENSP00000287038STRING
RL29_HUMANENSP00000287038STRING
RS23_HUMANENSP00000287038STRING
RS9_HUMANENSP00000287038STRING
RL13_HUMANENSP00000287038STRING
EF2_HUMANENSP00000287038STRING
RL38_HUMANENSP00000287038STRING
RS14_HUMANENSP00000287038STRING
RL4_HUMANENSP00000287038STRING
RS15A_HUMANENSP00000287038STRING
RLA2_HUMANENSP00000287038STRING
RL35A_HUMANENSP00000287038STRING
RL35A_HUMANENSP00000287038STRING
RLA0_HUMANENSP00000287038STRING
RL32_HUMANENSP00000287038STRING
RS7_HUMANENSP00000287038STRING
RL7_HUMANENSP00000287038STRING
RL10_HUMANENSP00000287038STRING
RS2_HUMANENSP00000287038STRING
RL28_HUMANENSP00000287038STRING
RL3_HUMANENSP00000287038STRING
RL27A_HUMANENSP00000287038STRING
RLA1_HUMANENSP00000287038STRING
RL23_HUMANENSP00000287038STRING
RS17_HUMANENSP00000287038STRING
RS3A_HUMANENSP00000287038STRING
RSSA_HUMANENSP00000287038STRING
RL22_HUMANENSP00000287038STRING
RL15_HUMANENSP00000287038STRING
RL23A_HUMANENSP00000287038STRING
RS26_HUMANENSP00000287038STRING
RS28_HUMANENSP00000287038STRING
RL37A_HUMANENSP00000287038STRING
ERF1_HUMANENSP00000287038STRING
RL10A_HUMANENSP00000287038STRING
RL39_HUMANENSP00000287038STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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-26, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-74, AND MASSSPECTROMETRY.
"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-10, AND MASSSPECTROMETRY.
"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-10, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.
"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-10, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures