RL29_MOUSE - dbPTM
RL29_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL29_MOUSE
UniProt AC P47915
Protein Name 60S ribosomal protein L29
Gene Name Rpl29
Organism Mus musculus (Mouse).
Sequence Length 160
Subcellular Localization
Protein Description Component of the large ribosomal subunit..
Protein Sequence MAKSKNHTTHNQSRKWHRNGIKKPRSQRYESLKGVDPKFLRNMRFAKKHNKKGLKKMQANNAKAVSARAEAIKALVKPQAIKPKMPKGPKLKRLAFIAHPKLGKRIRSYMAKGQRLCQPKPKVQTKAGAKAPAKAQASAPAQAPKGAQAPKGAQAPVKAP
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
5Methylation---MAKSKNHTTHNQ
---CCCCCCCCCCHH
52.63-
26PhosphorylationNGIKKPRSQRYESLK
CCCCCCHHHHHHHHC
27.7729176673
29PhosphorylationKKPRSQRYESLKGVD
CCCHHHHHHHHCCCC
11.3928066266
31PhosphorylationPRSQRYESLKGVDPK
CHHHHHHHHCCCCHH
26.8426824392
33AcetylationSQRYESLKGVDPKFL
HHHHHHHCCCCHHHH
67.19-
33UbiquitinationSQRYESLKGVDPKFL
HHHHHHHCCCCHHHH
67.19-
38UbiquitinationSLKGVDPKFLRNMRF
HHCCCCHHHHHHHHH
53.2022790023
63MalonylationKMQANNAKAVSARAE
HHHHCCHHHHHHHHH
51.9826320211
63UbiquitinationKMQANNAKAVSARAE
HHHHCCHHHHHHHHH
51.98-
66PhosphorylationANNAKAVSARAEAIK
HCCHHHHHHHHHHHH
19.5222817900
73MalonylationSARAEAIKALVKPQA
HHHHHHHHHHHCHHH
42.5932601280
73UbiquitinationSARAEAIKALVKPQA
HHHHHHHHHHHCHHH
42.5922790023
77UbiquitinationEAIKALVKPQAIKPK
HHHHHHHCHHHCCCC
32.06-
77AcetylationEAIKALVKPQAIKPK
HHHHHHHCHHHCCCC
32.0623201123
82UbiquitinationLVKPQAIKPKMPKGP
HHCHHHCCCCCCCCH
41.42-
82AcetylationLVKPQAIKPKMPKGP
HHCHHHCCCCCCCCH
41.4223864654
84AcetylationKPQAIKPKMPKGPKL
CHHHCCCCCCCCHHH
63.9323864654
101AcetylationLAFIAHPKLGKRIRS
HEEECCHHHHHHHHH
61.0623806337
101UbiquitinationLAFIAHPKLGKRIRS
HEEECCHHHHHHHHH
61.0622790023
108PhosphorylationKLGKRIRSYMAKGQR
HHHHHHHHHHHHCCC
19.5229176673
112SuccinylationRIRSYMAKGQRLCQP
HHHHHHHHCCCCCCC
38.7623806337
112AcetylationRIRSYMAKGQRLCQP
HHHHHHHHCCCCCCC
38.7623806337
117GlutathionylationMAKGQRLCQPKPKVQ
HHHCCCCCCCCCCCC
7.6824333276
117S-nitrosylationMAKGQRLCQPKPKVQ
HHHCCCCCCCCCCCC
7.6821278135
117S-nitrosocysteineMAKGQRLCQPKPKVQ
HHHCCCCCCCCCCCC
7.68-
125PhosphorylationQPKPKVQTKAGAKAP
CCCCCCCCCCCCCCC
26.3323649490
134MalonylationAGAKAPAKAQASAPA
CCCCCCCHHHCCCCC
39.7226320211
134UbiquitinationAGAKAPAKAQASAPA
CCCCCCCHHHCCCCC
39.72-
134AcetylationAGAKAPAKAQASAPA
CCCCCCCHHHCCCCC
39.7223806337
138PhosphorylationAPAKAQASAPAQAPK
CCCHHHCCCCCCCCC
23.7826824392
145MalonylationSAPAQAPKGAQAPKG
CCCCCCCCCCCCCCC
70.6526320211
145AcetylationSAPAQAPKGAQAPKG
CCCCCCCCCCCCCCC
70.6523806337
145UbiquitinationSAPAQAPKGAQAPKG
CCCCCCCCCCCCCCC
70.65-
151MalonylationPKGAQAPKGAQAPVK
CCCCCCCCCCCCCCC
70.6526320211
151AcetylationPKGAQAPKGAQAPVK
CCCCCCCCCCCCCCC
70.6523806337
151UbiquitinationPKGAQAPKGAQAPVK
CCCCCCCCCCCCCCC
70.65-
158MalonylationKGAQAPVKAP-----
CCCCCCCCCC-----
54.6126320211
158UbiquitinationKGAQAPVKAP-----
CCCCCCCCCC-----
54.61-

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

Oops, there are no upstream regulatory protein records of RL29_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL29_MOUSE !!

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 RL29_MOUSE !!

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

Oops, there are no PPI records of RL29_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL29_MOUSE

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Related Literatures of Post-Translational Modification

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