RL27_MOUSE - dbPTM
RL27_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL27_MOUSE
UniProt AC P61358
Protein Name 60S ribosomal protein L27
Gene Name Rpl27
Organism Mus musculus (Mouse).
Sequence Length 136
Subcellular Localization Cytoplasm, cytosol . Cytoplasm . Rough endoplasmic reticulum . Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity).
Protein Description Component of the large ribosomal subunit (By similarity). Required for proper rRNA processing and maturation of 28S and 5.8S rRNAs (By similarity)..
Protein Sequence MGKFMKPGKVVLVLAGRYSGRKAVIVKNIDDGTSDRPYSHALVAGIDRYPRKVTAAMGKKKIAKRSKIKSFVKVYNYNHLMPTRYSVDIPLDKTVVNKDVFRDPALKRKARREAKVKFEERYKTGKNKWFFQKLRF
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
3Acetylation-----MGKFMKPGKV
-----CCCCCCCCEE
40.7723864654
6Acetylation--MGKFMKPGKVVLV
--CCCCCCCCEEEEE
54.472373155
9MalonylationGKFMKPGKVVLVLAG
CCCCCCCEEEEEEEE
37.3826073543
9AcetylationGKFMKPGKVVLVLAG
CCCCCCCEEEEEEEE
37.3823201123
27AcetylationGRKAVIVKNIDDGTS
CCEEEEEEECCCCCC
36.7423576753
27UbiquitinationGRKAVIVKNIDDGTS
CCEEEEEEECCCCCC
36.74-
27MalonylationGRKAVIVKNIDDGTS
CCEEEEEEECCCCCC
36.7426320211
33PhosphorylationVKNIDDGTSDRPYSH
EEECCCCCCCCCCCE
34.1525521595
34PhosphorylationKNIDDGTSDRPYSHA
EECCCCCCCCCCCEE
36.8325367039
38PhosphorylationDGTSDRPYSHALVAG
CCCCCCCCCEEEECC
17.6225367039
39PhosphorylationGTSDRPYSHALVAGI
CCCCCCCCEEEECCH
12.6425367039
49PhosphorylationLVAGIDRYPRKVTAA
EECCHHCCCHHHHHH
12.0225367039
59AcetylationKVTAAMGKKKIAKRS
HHHHHHCCHHHHHHH
37.5023201123
73UbiquitinationSKIKSFVKVYNYNHL
HHCHHEEEECCCCCC
36.6722790023
73AcetylationSKIKSFVKVYNYNHL
HHCHHEEEECCCCCC
36.6722826441
77PhosphorylationSFVKVYNYNHLMPTR
HEEEECCCCCCCCCE
6.0526643407
83PhosphorylationNYNHLMPTRYSVDIP
CCCCCCCCEEEEECC
28.4226643407
85PhosphorylationNHLMPTRYSVDIPLD
CCCCCCEEEEECCCC
18.6126643407
86PhosphorylationHLMPTRYSVDIPLDK
CCCCCEEEEECCCCC
15.2627180971
93UbiquitinationSVDIPLDKTVVNKDV
EEECCCCCCCCCCHH
51.40-
93MalonylationSVDIPLDKTVVNKDV
EEECCCCCCCCCCHH
51.4026320211
93AcetylationSVDIPLDKTVVNKDV
EEECCCCCCCCCCHH
51.4023864654
98AcetylationLDKTVVNKDVFRDPA
CCCCCCCCHHHCCHH
43.5923864654
98MalonylationLDKTVVNKDVFRDPA
CCCCCCCCHHHCCHH
43.5926320211
98UbiquitinationLDKTVVNKDVFRDPA
CCCCCCCCHHHCCHH
43.59-
107UbiquitinationVFRDPALKRKARREA
HHCCHHHHHHHHHHH
54.6922790023
107AcetylationVFRDPALKRKARREA
HHCCHHHHHHHHHHH
54.6923864654
117AcetylationARREAKVKFEERYKT
HHHHHCCCHHHHHCC
46.4823864654
128AcetylationRYKTGKNKWFFQKLR
HHCCCCCCCCEECCC
49.1923201123
128MalonylationRYKTGKNKWFFQKLR
HHCCCCCCCCEECCC
49.1926320211
128UbiquitinationRYKTGKNKWFFQKLR
HHCCCCCCCCEECCC
49.19-
133UbiquitinationKNKWFFQKLRF----
CCCCCEECCCC----
36.1522790023
133AcetylationKNKWFFQKLRF----
CCCCCEECCCC----
36.1522826441

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 RL27_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL27_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 RL27_MOUSE !!

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

Oops, there are no PPI records of RL27_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL27_MOUSE

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Related Literatures of Post-Translational Modification

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