RL13A_MOUSE - dbPTM
RL13A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL13A_MOUSE
UniProt AC P19253
Protein Name 60S ribosomal protein L13a
Gene Name Rpl13a
Organism Mus musculus (Mouse).
Sequence Length 203
Subcellular Localization
Protein Description Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex..
Protein Sequence MAEGQVLVLDGRGHLLGRLAAIVAKQVLLGRKVVVVRCEGINISGNFYRNKLKYLAFLRKRMNTNPSRGPYHFRAPSRIFWRTVRGMLPHKTKRGQAALERLKVLDGIPPPYDKKKRMVVPAALKVVRLKPTRKFAYLGRLAHEVGWKYQAVTATLEEKRKEKAKMHYRKKKQILRLRKQAEKNVEKKICKFTEVLKTNGLLV
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------MAEGQVLVL
------CCCCCEEEE
29.62-
25UbiquitinationRLAAIVAKQVLLGRK
HHHHHHHHHHHCCCC
30.00-
25AcetylationRLAAIVAKQVLLGRK
HHHHHHHHHHHCCCC
30.0022826441
38S-palmitoylationRKVVVVRCEGINISG
CCEEEEECEEECCCC
3.6728526873
38S-nitrosylationRKVVVVRCEGINISG
CCEEEEECEEECCCC
3.6721278135
38S-nitrosocysteineRKVVVVRCEGINISG
CCEEEEECEEECCCC
3.67-
53AcetylationNFYRNKLKYLAFLRK
CCHHHHHHHHHHHHH
39.5722826441
53UbiquitinationNFYRNKLKYLAFLRK
CCHHHHHHHHHHHHH
39.57-
54PhosphorylationFYRNKLKYLAFLRKR
CHHHHHHHHHHHHHH
17.4429514104
59CitrullinationLKYLAFLRKRMNTNP
HHHHHHHHHHCCCCC
20.34-
59CitrullinationLKYLAFLRKRMNTNP
HHHHHHHHHHCCCCC
20.3424463520
71PhosphorylationTNPSRGPYHFRAPSR
CCCCCCCCCCCCCCH
19.2029514104
77PhosphorylationPYHFRAPSRIFWRTV
CCCCCCCCHHHHHHH
36.7023071094
103UbiquitinationQAALERLKVLDGIPP
HHHHHHHHHHCCCCC
47.15-
114UbiquitinationGIPPPYDKKKRMVVP
CCCCCCCHHHCCHHH
55.11-
115UbiquitinationIPPPYDKKKRMVVPA
CCCCCCHHHCCHHHH
42.59-
125AcetylationMVVPAALKVVRLKPT
CHHHHHHEEEECCCC
33.6822826441
125UbiquitinationMVVPAALKVVRLKPT
CHHHHHHEEEECCCC
33.68-
134AcetylationVRLKPTRKFAYLGRL
EECCCCCCHHHHHHH
36.5022826441
134UbiquitinationVRLKPTRKFAYLGRL
EECCCCCCHHHHHHH
36.50-
140CitrullinationRKFAYLGRLAHEVGW
CCHHHHHHHHHHHHH
26.5524463520
140CitrullinationRKFAYLGRLAHEVGW
CCHHHHHHHHHHHHH
26.55-
148AcetylationLAHEVGWKYQAVTAT
HHHHHHHHHHHHHHC
22.8922826441
149PhosphorylationAHEVGWKYQAVTATL
HHHHHHHHHHHHHCH
8.6629514104
155PhosphorylationKYQAVTATLEEKRKE
HHHHHHHCHHHHHHH
25.9025338131
159UbiquitinationVTATLEEKRKEKAKM
HHHCHHHHHHHHHHH
60.44-
183AcetylationRLRKQAEKNVEKKIC
HHHHHHHHHHHHHHH
70.1223201123
188AcetylationAEKNVEKKICKFTEV
HHHHHHHHHHHHHHH
39.5723201123
188UbiquitinationAEKNVEKKICKFTEV
HHHHHHHHHHHHHHH
39.57-
190GlutathionylationKNVEKKICKFTEVLK
HHHHHHHHHHHHHHH
3.9924333276
191UbiquitinationNVEKKICKFTEVLKT
HHHHHHHHHHHHHHH
59.81-
191AcetylationNVEKKICKFTEVLKT
HHHHHHHHHHHHHHH
59.8123806337
191MalonylationNVEKKICKFTEVLKT
HHHHHHHHHHHHHHH
59.8126320211
191SuccinylationNVEKKICKFTEVLKT
HHHHHHHHHHHHHHH
59.8123806337
197UbiquitinationCKFTEVLKTNGLLV-
HHHHHHHHHCCCCC-
45.15-

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
77SPhosphorylationKinaseDAPK3O54784
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
77SPhosphorylation

23071094

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 RL13A_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RL13A_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL13A_MOUSE

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Related Literatures of Post-Translational Modification

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