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 L4  

UniProtKB / Swiss-Prot ID :  RL4_HUMAN

Gene Name (Synonyms) : 
RPL4, RPL1  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MACARPLISVYSEKGESSGKNVTLPAVFKAPIRPDIVNFVHTNLRKNNRQPYAVSELAGHQTSAESWGTG...
Predicted Secondary Structure CCCCCCCEEEECCCHHHHCCEECCHHHHCCCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCEEEEEECCCC...
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
2N-acetylalanine.---MACARP
---CCCCCC
8.83UniProtKB
Link-
14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VYSEKGESS
EECCCHHHH
63.14Phosphositeplus
Link
14N6-acetyllysineVYSEKGESS
EECCCHHHH
63.14HPRD
Link
14N6-acetyllysineVYSEKGESS
EECCCHHHH
63.14Phosphositeplus
Link
14N6-acetyllysine.VYSEKGESS
EECCCHHHH
63.14UniProtKB
Link
20Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ESSGKNVTL
HHHCCEECC
50.63Phosphositeplus
Link
96S-nitrosocysteineFGNMCRGGR
CCCCCCCCE
4.19dbSNO
Link
106Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FAPTKTWRR
ECCCCCCCC
45.06Phosphositeplus
Link
106N6-acetyllysineFAPTKTWRR
ECCCCCCCC
45.06HPRD
Link
106N6-acetyllysineFAPTKTWRR
ECCCCCCCC
45.06Phosphositeplus
Link
106N6-acetyllysine.FAPTKTWRR
ECCCCCCCC
45.06UniProtKB
Link
140Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LVMSKGHRI
HHHHCCCCC
40.41Phosphositeplus
Link
157Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VVEDKVEGY
EEECCHHCC
28.78Phosphositeplus
Link
162Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VEGYKKTKE
HHCCHHHHH
65.90Phosphositeplus
Link
165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YKKTKEAVL
CHHHHHHHH
53.18Phosphositeplus
Link
172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VLLLKKLKA
HHHHHHCCC
56.90Phosphositeplus
Link
175Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LKKLKAWND
HHHCCCCHH
61.30Phosphositeplus
Link
181Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)WNDIKKVYA
CHHHHHHHH
38.76Phosphositeplus
Link
208S-nitrosocysteineRRGPCIIYN
CCEEEEEEC
3.09dbSNO
Link
208S-nitrosocysteineRRGPCIIYN
CCEEEEEEC
3.09HPRD
Link
219Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NGIIKAFRN
CCEEEEECC
39.28Phosphositeplus
Link
234Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LNVSKLNIL
ECCCCCCHH
41.07Phosphositeplus
Link
239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LNILKLAPG
CCHHHHHHC
38.51Phosphositeplus
Link
250S-nitrosocysteineVGRFCIWTE
CCCEEEEEH
2.15dbSNO
Link
250S-nitrosocysteineVGRFCIWTE
CCCEEEEEH
2.15HPRD
Link
259Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SAFRKLDEL
HHHHHHHHH
54.56Phosphositeplus
Link
264PhosphotyrosineLDELYGTWR
HHHHHCCCC
15.51Phosphositeplus
Link
274Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AASLKSNYN
CCCCCCCCC
33.87Phosphositeplus
Link
283Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LPMHKMINT
CCCHHHHHH
34.91Phosphositeplus
Link
294Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SRILKSPEI
HHHHCCHHH
62.69Phosphositeplus
Link
295PhosphoserineRILKSPEIQ
HHHCCHHHH
25.07HPRD
Link
295PhosphoserineRILKSPEIQ
HHHCCHHHH
25.07PhosphoELM
Link
295PhosphoserineRILKSPEIQ
HHHCCHHHH
25.07Phosphositeplus
Link
295PhosphoserineRILKSPEIQ
HHHCCHHHH
25.07SysPTM
Link
295Phosphoserine.RILKSPEIQ
HHHCCHHHH
25.07UniProtKB
Link
320Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KNPLKNLRI
CCCHHHHHH
56.01Phosphositeplus
Link
327Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RIMLKLNPY
HHHHHHCCC
28.92Phosphositeplus
Link
333Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NPYAKTMRR
CCCHHHHHH
36.69Phosphositeplus
Link
333N6-acetyllysineNPYAKTMRR
CCCHHHHHH
36.69HPRD
Link
333N6-acetyllysineNPYAKTMRR
CCCHHHHHH
36.69Phosphositeplus
Link
333N6-acetyllysine.NPYAKTMRR
CCCHHHHHH
36.69UniProtKB
Link
334PhosphothreoninePYAKTMRRN
CCHHHHHHH
14.03HPRD
Link
353Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LRVDKAAAA
HHHHHHHHC
36.75Phosphositeplus
Link
364Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ALQAKSDEK
HHHCCCCCC
45.54Phosphositeplus
Link
365PhosphoserineLQAKSDEKA
HHCCCCCCC
54.76HPRD
Link
365PhosphoserineLQAKSDEKA
HHCCCCCCC
54.76PhosphoELM
Link
365PhosphoserineLQAKSDEKA
HHCCCCCCC
54.76Phosphositeplus
Link
365PhosphoserineLQAKSDEKA
HHCCCCCCC
54.76SysPTM
Link
365Phosphoserine.LQAKSDEKA
HHCCCCCCC
54.76UniProtKB
Link
368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KSDEKAAVA
CCCCCCCCC
46.79Phosphositeplus
Link
420PhosphothreonineKKPTTEEKK
CCCCCCCCC
51.15HPRD
Link-
420PhosphothreonineKKPTTEEKK
CCCCCCCCC
51.15Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PBX2_HUMANphysical interactionMINT-62673MINT14667819
PBX2_HUMANphysical interactionMINT-62749MINT14667819
M3K1_HUMANphysical interactionMINT-47982MINT14743216
M3K1_HUMANphysical interactionMINT-48278MINT14743216
M3K14_HUMANphysical interactionMINT-48003MINT14743216
M3K14_HUMANphysical interactionDIP:44921EDIP14743216
EF1G_HUMANphysical interactionEBI-729027
intact16169070
TRIM9_HUMANphysical interactionEBI-734956
intact16169070
M3K14_HUMANin vitroHPRD:01607HPRD14743216
RS20_HUMANENSP00000311430STRING
RL18_HUMANENSP00000311430STRING
RS5_HUMANENSP00000311430STRING
RL6_HUMANENSP00000311430STRING
RS18_HUMANENSP00000311430STRING
RS19_HUMANENSP00000311430STRING
RL18A_HUMANENSP00000311430STRING
RL19_HUMANENSP00000311430STRING
RS13_HUMANENSP00000311430STRING
RS12_HUMANENSP00000311430STRING
RS15_HUMANENSP00000311430STRING
RS25_HUMANENSP00000311430STRING
RS4Y1_HUMANENSP00000311430STRING
RS16_HUMANENSP00000311430STRING
RL36_HUMANENSP00000311430STRING
RL35_HUMANENSP00000311430STRING
RL8_HUMANENSP00000311430STRING
RL31_HUMANENSP00000311430STRING
RL26L_HUMANENSP00000311430STRING
RL24_HUMANENSP00000311430STRING
RL3L_HUMANENSP00000311430STRING
RS11_HUMANENSP00000311430STRING
RL13A_HUMANENSP00000311430STRING
RS27A_HUMANENSP00000311430STRING
UBIQ_HUMANENSP00000311430STRING
RL37_HUMANENSP00000311430STRING
RS3_HUMANENSP00000311430STRING
UBIM_HUMANENSP00000311430STRING
RS30_HUMANENSP00000311430STRING
RL30_HUMANENSP00000311430STRING
IF2P_HUMANENSP00000311430STRING
RL26_HUMANENSP00000311430STRING
RL29_HUMANENSP00000311430STRING
RS23_HUMANENSP00000311430STRING
RS9_HUMANENSP00000311430STRING
RL13_HUMANENSP00000311430STRING
EF2_HUMANENSP00000311430STRING
RL38_HUMANENSP00000311430STRING
RS14_HUMANENSP00000311430STRING
RS15A_HUMANENSP00000311430STRING
RLA2_HUMANENSP00000311430STRING
RL35A_HUMANENSP00000311430STRING
RL35A_HUMANENSP00000311430STRING
RLA0_HUMANENSP00000311430STRING
RL32_HUMANENSP00000311430STRING
RS7_HUMANENSP00000311430STRING
RL7_HUMANENSP00000311430STRING
RL10_HUMANENSP00000311430STRING
RS2_HUMANENSP00000311430STRING
RL28_HUMANENSP00000311430STRING
RL3_HUMANENSP00000311430STRING
RL27A_HUMANENSP00000311430STRING
RLA1_HUMANENSP00000311430STRING
RL23_HUMANENSP00000311430STRING
RS17_HUMANENSP00000311430STRING
RS3A_HUMANENSP00000311430STRING
RSSA_HUMANENSP00000311430STRING
RL22_HUMANENSP00000311430STRING
RL15_HUMANENSP00000311430STRING
RL23A_HUMANENSP00000311430STRING
RS26_HUMANENSP00000311430STRING
RS28_HUMANENSP00000311430STRING
RL37A_HUMANENSP00000311430STRING
ERF1_HUMANENSP00000311430STRING
RL10A_HUMANENSP00000311430STRING
RL39_HUMANENSP00000311430STRING
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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
"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, AND MASS SPECTROMETRY.
"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-14; LYS-106 AND LYS-333, ANDMASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-295, 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-295 AND SER-365, ANDMASS 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-295, AND MASSSPECTROMETRY.
"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-295 AND SER-365, 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-295 AND SER-365, ANDMASS 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-295, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures