RL7_MOUSE - dbPTM
RL7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL7_MOUSE
UniProt AC P14148
Protein Name 60S ribosomal protein L7
Gene Name Rpl7
Organism Mus musculus (Mouse).
Sequence Length 270
Subcellular Localization
Protein Description Component of the large ribosomal subunit (By similarity). Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs (By similarity)..
Protein Sequence MEAVPEKKKKVATVPGTLKKKVPAGPKTLKKKVPAVPETLKKKRRNFAELKVKRLRKKFALKTLRKARRKLIYEKAKHYHKEYRQMYRTEIRMARMARKAGNFYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASINMLRIVEPYIAWGYPNLKSVNELIYKRGYGKINKKRIALTDNSLIARSLGKFGIICMEDLIHEIYTVGKRFKEANNFLWPFKLSSPRGGMKKKTTHFVEGGDAGNREDQINRLIRRMN
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
1Acetylation-------MEAVPEKK
-------CCCCCCCC		7.23-
7Malonylation-MEAVPEKKKKVATV
-CCCCCCCCCCEEEC		64.9226320211
10UbiquitinationAVPEKKKKVATVPGT
CCCCCCCCEEECCCC		46.08-
10MalonylationAVPEKKKKVATVPGT
CCCCCCCCEEECCCC		46.0826320211
13PhosphorylationEKKKKVATVPGTLKK
CCCCCEEECCCCCCC		30.1622324799
17PhosphorylationKVATVPGTLKKKVPA
CEEECCCCCCCCCCC		29.3626824392
19MalonylationATVPGTLKKKVPAGP
EECCCCCCCCCCCCC		50.8426320211
19UbiquitinationATVPGTLKKKVPAGP
EECCCCCCCCCCCCC		50.84-
27MalonylationKKVPAGPKTLKKKVP
CCCCCCCCCHHHHCC		66.6226320211
32MalonylationGPKTLKKKVPAVPET
CCCCHHHHCCCCCHH		52.4426320211
39PhosphorylationKVPAVPETLKKKRRN
HCCCCCHHHHHHHCC		37.5029176673
42UbiquitinationAVPETLKKKRRNFAE
CCCHHHHHHHCCHHH		55.41-
62UbiquitinationLRKKFALKTLRKARR
HHHHHHHHHHHHHHH		41.9222790023
62AcetylationLRKKFALKTLRKARR
HHHHHHHHHHHHHHH		41.9222826441
79PhosphorylationIYEKAKHYHKEYRQM
HHHHHHHHHHHHHHH		17.5520139300
81UbiquitinationEKAKHYHKEYRQMYR
HHHHHHHHHHHHHHH		49.64-
81AcetylationEKAKHYHKEYRQMYR
HHHHHHHHHHHHHHH		49.6423864654
83PhosphorylationAKHYHKEYRQMYRTE
HHHHHHHHHHHHHHH		15.7929514104
87PhosphorylationHKEYRQMYRTEIRMA
HHHHHHHHHHHHHHH		13.1720139300
99UbiquitinationRMARMARKAGNFYVP
HHHHHHHHCCCEEEC		51.6222790023
104PhosphorylationARKAGNFYVPAEPKL
HHHCCCEEECCCCCE		14.9929514104
110UbiquitinationFYVPAEPKLAFVIRI
EEECCCCCEEEEEEE		43.9122790023
124PhosphorylationIRGINGVSPKVRKVL
ECCCCCCCHHHHHHH		22.0229514104
126UbiquitinationGINGVSPKVRKVLQL
CCCCCCHHHHHHHHH		47.36-
129AcetylationGVSPKVRKVLQLLRL
CCCHHHHHHHHHHHH		50.7323806337
129SuccinylationGVSPKVRKVLQLLRL
CCCHHHHHHHHHHHH		50.7323806337
146UbiquitinationIFNGTFVKLNKASIN
HHCCCEEECCHHHCC		42.0022790023
146AcetylationIFNGTFVKLNKASIN
HHCCCEEECCHHHCC		42.0022826441
149SuccinylationGTFVKLNKASINMLR
CCEEECCHHHCCCHH		54.6823806337
149AcetylationGTFVKLNKASINMLR
CCEEECCHHHCCCHH		54.6823806337
149SuccinylationGTFVKLNKASINMLR
CCEEECCHHHCCCHH		54.68-
161PhosphorylationMLRIVEPYIAWGYPN
CHHHCCCHHHCCCCC		6.9725367039
170UbiquitinationAWGYPNLKSVNELIY
HCCCCCHHHHHHHHH		60.02-
178AcetylationSVNELIYKRGYGKIN
HHHHHHHHCCCCCCC		32.1422826441
183SuccinylationIYKRGYGKINKKRIA
HHHCCCCCCCCCEEE		34.3223806337
183AcetylationIYKRGYGKINKKRIA
HHHCCCCCCCCCEEE		34.3223806337
192PhosphorylationNKKRIALTDNSLIAR
CCCEEEECCCHHHHH		24.9029472430
195PhosphorylationRIALTDNSLIARSLG
EEEECCCHHHHHHHH		24.7829233185
200PhosphorylationDNSLIARSLGKFGII
CCHHHHHHHHHCEEE		32.2429514104
203UbiquitinationLIARSLGKFGIICME
HHHHHHHHCEEEEHH		45.79-
203AcetylationLIARSLGKFGIICME
HHHHHHHHCEEEEHH		45.7922826441
208S-palmitoylationLGKFGIICMEDLIHE
HHHCEEEEHHHHHHH		2.0028526873
208GlutathionylationLGKFGIICMEDLIHE
HHHCEEEEHHHHHHH		2.0024333276
217PhosphorylationEDLIHEIYTVGKRFK
HHHHHHHHHHHHHHH		7.7422345495
218PhosphorylationDLIHEIYTVGKRFKE
HHHHHHHHHHHHHHH		28.5722345495
221UbiquitinationHEIYTVGKRFKEANN
HHHHHHHHHHHHHHC		50.77-
224AcetylationYTVGKRFKEANNFLW
HHHHHHHHHHHCCCC		61.0122826441
234AcetylationNNFLWPFKLSSPRGG
HCCCCCEECCCCCCC		43.3022826441
237PhosphorylationLWPFKLSSPRGGMKK
CCCEECCCCCCCCCC		29.1129514104
245UbiquitinationPRGGMKKKTTHFVEG
CCCCCCCCEEEEECC		53.81-
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 RL7_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL7_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 RL7_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NPM_MOUSENpm1physical
18809582
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL7_MOUSE

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Related Literatures of Post-Translational Modification

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