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 L13a  

UniProtKB / Swiss-Prot ID :  RL13A_HUMAN

Gene Name (Synonyms) : 
RPL13A  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MAEVQVLVLDGRGHLLGRLAAIVAKQVLLGRKVVVVRCEGINISGNFYRNKLKYLAFLRKRMNTNPSRGP...
Predicted Secondary Structure CCCCCEEEEECCCCEEHHHHHHHHHHHHCCCEEEEEEECEEEEECCHHHHHHHHHHCCCCCCCCCCCHHH...
Protein Variant -
- top -

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
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine; partial.---MAEVQV
---CCCCCE
26.18UniProtKB
Link
25Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AIVAKQVLL
HHHHHHHHC
30.00Phosphositeplus
Link
51Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FYRNKLKYL
HHHHHHHHH
37.04Phosphositeplus
Link
53Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RNKLKYLAF
HHHHHHHHC
39.57Phosphositeplus
Link
77PhosphoserineFRAPSRIFW
CCCHHHHHH
36.70Phosphositeplus
Link
77Phosphoserine (DAPK3)FRAPSRIFW
CCCHHHHHH
36.70PhosphoELM
Link
103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LDRLKVFDG
HHCCEEECC
41.57Phosphositeplus
Link
114Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PPYDKKKRM
CCHHCCCCE
55.11Phosphositeplus
Link
125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PAALKVVRL
CCHHHHHHC
33.68Phosphositeplus
Link
134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KPTRKFAYL
CCCCCEEEE
36.50Phosphositeplus
Link
148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EVGWKYQAV
HHCCHHHHH
22.89Phosphositeplus
Link
159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TLEEKRKEK
HHHHHHHHH
60.44Phosphositeplus
Link
191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KKIDKYTEV
HHHHHHHHH
58.51Phosphositeplus
Link
191N6-acetyllysineKKIDKYTEV
HHHHHHHHH
58.51HPRD
Link
191N6-acetyllysineKKIDKYTEV
HHHHHHHHH
58.51Phosphositeplus
Link
191N6-acetyllysine.KKIDKYTEV
HHHHHHHHH
58.51UniProtKB
Link
193PhosphothreonineIDKYTEVLK
HHHHHHHHH
25.92HPRD
Link
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
Q5JVB6_HUMANphysical interactionMINT-64407MINT16169070
FBX18_HUMANyeast 2-hybridHPRD:11775HPRD16169070
GOLM1_HUMANyeast 2-hybridHPRD:11775HPRD16169070
RS20_HUMANENSP00000270634STRING
RL18_HUMANENSP00000270634STRING
RS5_HUMANENSP00000270634STRING
RL6_HUMANENSP00000270634STRING
RS18_HUMANENSP00000270634STRING
EIF3D_HUMANENSP00000270634STRING
EIF3E_HUMANENSP00000270634STRING
RS19_HUMANENSP00000270634STRING
RL18A_HUMANENSP00000270634STRING
RL19_HUMANENSP00000270634STRING
RS13_HUMANENSP00000270634STRING
RS12_HUMANENSP00000270634STRING
RS15_HUMANENSP00000270634STRING
RS25_HUMANENSP00000270634STRING
EIF3K_HUMANENSP00000270634STRING
RS4Y1_HUMANENSP00000270634STRING
RS16_HUMANENSP00000270634STRING
RL36_HUMANENSP00000270634STRING
IF2G_HUMANENSP00000270634STRING
EIF3G_HUMANENSP00000270634STRING
IF2A_HUMANENSP00000270634STRING
RL35_HUMANENSP00000270634STRING
EIF3J_HUMANENSP00000270634STRING
IF4B_HUMANENSP00000270634STRING
RL8_HUMANENSP00000270634STRING
RL31_HUMANENSP00000270634STRING
RL26L_HUMANENSP00000270634STRING
RL24_HUMANENSP00000270634STRING
IF4H_HUMANENSP00000270634STRING
RL3L_HUMANENSP00000270634STRING
RS11_HUMANENSP00000270634STRING
RS27A_HUMANENSP00000270634STRING
UBIQ_HUMANENSP00000270634STRING
RL37_HUMANENSP00000270634STRING
EIF3H_HUMANENSP00000270634STRING
RS3_HUMANENSP00000270634STRING
UBIM_HUMANENSP00000270634STRING
RS30_HUMANENSP00000270634STRING
IF4E_HUMANENSP00000270634STRING
RL30_HUMANENSP00000270634STRING
IF2P_HUMANENSP00000270634STRING
RL26_HUMANENSP00000270634STRING
RL29_HUMANENSP00000270634STRING
RS23_HUMANENSP00000270634STRING
RS9_HUMANENSP00000270634STRING
RL13_HUMANENSP00000270634STRING
EF2_HUMANENSP00000270634STRING
RL38_HUMANENSP00000270634STRING
EIF3F_HUMANENSP00000270634STRING
EIF3F_HUMANENSP00000270634STRING
RS14_HUMANENSP00000270634STRING
RL4_HUMANENSP00000270634STRING
PABP1_HUMANENSP00000270634STRING
RS15A_HUMANENSP00000270634STRING
RLA2_HUMANENSP00000270634STRING
IF4G1_HUMANENSP00000270634STRING
IF4A2_HUMANENSP00000270634STRING
RL35A_HUMANENSP00000270634STRING
RL35A_HUMANENSP00000270634STRING
EIF3C_HUMANENSP00000270634STRING
RLA0_HUMANENSP00000270634STRING
RL32_HUMANENSP00000270634STRING
RS7_HUMANENSP00000270634STRING
RL7_HUMANENSP00000270634STRING
RL10_HUMANENSP00000270634STRING
RS2_HUMANENSP00000270634STRING
RL28_HUMANENSP00000270634STRING
RL3_HUMANENSP00000270634STRING
RL27A_HUMANENSP00000270634STRING
RLA1_HUMANENSP00000270634STRING
RL23_HUMANENSP00000270634STRING
RS17_HUMANENSP00000270634STRING
RS3A_HUMANENSP00000270634STRING
RSSA_HUMANENSP00000270634STRING
RL22_HUMANENSP00000270634STRING
RL15_HUMANENSP00000270634STRING
RL23A_HUMANENSP00000270634STRING
RS26_HUMANENSP00000270634STRING
RS28_HUMANENSP00000270634STRING
RL37A_HUMANENSP00000270634STRING
ERF1_HUMANENSP00000270634STRING
RL10A_HUMANENSP00000270634STRING
RL39_HUMANENSP00000270634STRING
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Characterization and analysis of posttranslational modifications ofthe human large cytoplasmic ribosomal subunit proteins by massspectrometry and Edman sequencing.";
Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,Karpova G.G.;
J. Protein Chem. 22:249-258(2003).
Cited for: MASS SPECTROMETRY, AND PROBABLE ACETYLATION AT ALA-2.
"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-191, AND MASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures