RL27_HUMAN - dbPTM
RL27_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL27_HUMAN
UniProt AC P61353
Protein Name 60S ribosomal protein L27
Gene Name RPL27
Organism Homo sapiens (Human).
Sequence Length 136
Subcellular Localization Cytoplasm, cytosol . Cytoplasm . Rough endoplasmic reticulum . Detected on cytosolic polysomes (PubMed:25957688). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity).
Protein Description Component of the large ribosomal subunit. [PubMed: 12962325]
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
6Ubiquitination--MGKFMKPGKVVLV
--CCCCCCCCEEEEE		54.47-
92-HydroxyisobutyrylationGKFMKPGKVVLVLAG
CCCCCCCEEEEEEEE		37.38-
9UbiquitinationGKFMKPGKVVLVLAG
CCCCCCCEEEEEEEE		37.3821890473
272-HydroxyisobutyrylationGRKAVIVKNIDDGTS
CCEEEEEEECCCCCC		36.74-
27AcetylationGRKAVIVKNIDDGTS
CCEEEEEEECCCCCC		36.7419608861
27MalonylationGRKAVIVKNIDDGTS
CCEEEEEEECCCCCC		36.7426320211
27UbiquitinationGRKAVIVKNIDDGTS
CCEEEEEEECCCCCC		36.7421890473
33PhosphorylationVKNIDDGTSDRPYSH
EEECCCCCCCCCCCE		34.1523663014
34PhosphorylationKNIDDGTSDRPYSHA
EECCCCCCCCCCCEE		36.8323663014
36MethylationIDDGTSDRPYSHALV
CCCCCCCCCCCEEEE		31.65115491961
38PhosphorylationDGTSDRPYSHALVAG
CCCCCCCCCEEEECC		17.6223663014
39PhosphorylationGTSDRPYSHALVAGI
CCCCCCCCEEEECCH		12.6423663014
49PhosphorylationLVAGIDRYPRKVTAA
EECCHHCCCHHHHHH		12.0228152594
52UbiquitinationGIDRYPRKVTAAMGK
CHHCCCHHHHHHHCC		39.16-
54PhosphorylationDRYPRKVTAAMGKKK
HCCCHHHHHHHCCHH		16.2525367160
57SulfoxidationPRKVTAAMGKKKIAK
CHHHHHHHCCHHHHH		8.1930846556
59UbiquitinationKVTAAMGKKKIAKRS
HHHHHHCCHHHHHHH		37.50-
59AcetylationKVTAAMGKKKIAKRS
HHHHHHCCHHHHHHH		37.5025953088
73UbiquitinationSKIKSFVKVYNYNHL
HHCHHEEEECCCCCC		36.6721906983
73AcetylationSKIKSFVKVYNYNHL
HHCHHEEEECCCCCC		36.6726051181
732-HydroxyisobutyrylationSKIKSFVKVYNYNHL
HHCHHEEEECCCCCC		36.67-
75PhosphorylationIKSFVKVYNYNHLMP
CHHEEEECCCCCCCC		13.2529116813
77PhosphorylationSFVKVYNYNHLMPTR
HEEEECCCCCCCCCE		6.0529116813
83PhosphorylationNYNHLMPTRYSVDIP
CCCCCCCCEEEEECC		28.4229116813
84MethylationYNHLMPTRYSVDIPL
CCCCCCCEEEEECCC		18.83115491969
85PhosphorylationNHLMPTRYSVDIPLD
CCCCCCEEEEECCCC		18.6126657352
86PhosphorylationHLMPTRYSVDIPLDK
CCCCCEEEEECCCCC		15.2626657352
93MalonylationSVDIPLDKTVVNKDV
EEECCCCCCCCCCHH		51.4026320211
93UbiquitinationSVDIPLDKTVVNKDV
EEECCCCCCCCCCHH		51.4021890473
93AcetylationSVDIPLDKTVVNKDV
EEECCCCCCCCCCHH		51.4019608861
932-HydroxyisobutyrylationSVDIPLDKTVVNKDV
EEECCCCCCCCCCHH		51.40-
98SumoylationLDKTVVNKDVFRDPA
CCCCCCCCHHHCCHH		43.59-
98UbiquitinationLDKTVVNKDVFRDPA
CCCCCCCCHHHCCHH		43.5921890473
982-HydroxyisobutyrylationLDKTVVNKDVFRDPA
CCCCCCCCHHHCCHH		43.59-
98MalonylationLDKTVVNKDVFRDPA
CCCCCCCCHHHCCHH		43.5926320211
98AcetylationLDKTVVNKDVFRDPA
CCCCCCCCHHHCCHH		43.5923749302
107AcetylationVFRDPALKRKARREA
HHCCHHHHHHHHHHH		54.6926051181
1072-HydroxyisobutyrylationVFRDPALKRKARREA
HHCCHHHHHHHHHHH		54.69-
107UbiquitinationVFRDPALKRKARREA
HHCCHHHHHHHHHHH		54.69-
115UbiquitinationRKARREAKVKFEERY
HHHHHHHCCCHHHHH		41.00-
117SumoylationARREAKVKFEERYKT
HHHHHCCCHHHHHCC		46.4819608861
117AcetylationARREAKVKFEERYKT
HHHHHCCCHHHHHCC		46.4819608861
117UbiquitinationARREAKVKFEERYKT
HHHHHCCCHHHHHCC		46.4819608861
117SumoylationARREAKVKFEERYKT
HHHHHCCCHHHHHCC		46.48-
128MalonylationRYKTGKNKWFFQKLR
HHCCCCCCCCEECCC		49.1926320211
128AcetylationRYKTGKNKWFFQKLR
HHCCCCCCCCEECCC		49.1925825284
128UbiquitinationRYKTGKNKWFFQKLR
HHCCCCCCCCEECCC		49.1919608861
133AcetylationKNKWFFQKLRF----
CCCCCEECCCC----		36.1525825284
133UbiquitinationKNKWFFQKLRF----
CCCCCEECCCC----		36.1521906983
1332-HydroxyisobutyrylationKNKWFFQKLRF----
CCCCCEECCCC----		36.15-
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

Oops, there are no upstream regulatory protein records of RL27_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL27_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL31_HUMANRPL31physical
22939629
RL9_HUMANRPL9physical
22939629
RS10_HUMANRPS10physical
22939629
RS13_HUMANRPS13physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RS16_HUMANRPS16physical
22939629
RS17_HUMANRPS17physical
22939629
RS23_HUMANRPS23physical
22939629
RSSA_HUMANRPSAphysical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS26_HUMANRPS26physical
22939629
RS24_HUMANRPS24physical
22939629
RL6_HUMANRPL6physical
22939629
RS2_HUMANRPS2physical
22939629
RS9_HUMANRPS9physical
22939629
RL30_HUMANRPL30physical
22939629
RL4_HUMANRPL4physical
22939629
RS8_HUMANRPS8physical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RS21_HUMANRPS21physical
22939629
RS29_HUMANRPS29physical
22939629
RL37_HUMANRPL37physical
22939629
HNRPM_HUMANHNRNPMphysical
22863883
MRE11_HUMANMRE11Aphysical
22863883
SYQ_HUMANQARSphysical
22863883
RL19_HUMANRPL19physical
22863883
RL26L_HUMANRPL26L1physical
22863883
DDX56_HUMANDDX56physical
26344197
NOC2L_HUMANNOC2Lphysical
26344197
RL10_HUMANRPL10physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL11_HUMANRPL11physical
26344197
RL12_HUMANRPL12physical
26344197
RL13A_HUMANRPL13Aphysical
26344197
RL14_HUMANRPL14physical
26344197
RL15_HUMANRPL15physical
26344197
RL23A_HUMANRPL23Aphysical
26344197
RL27A_HUMANRPL27Aphysical
26344197
RL3_HUMANRPL3physical
26344197
RL30_HUMANRPL30physical
26344197
RL32_HUMANRPL32physical
26344197
RL35_HUMANRPL35physical
26344197
RL35A_HUMANRPL35Aphysical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL3L_HUMANRPL3Lphysical
26344197
RL4_HUMANRPL4physical
26344197
RL7_HUMANRPL7physical
26344197
RL7A_HUMANRPL7Aphysical
26344197
RL8_HUMANRPL8physical
26344197
RL9_HUMANRPL9physical
26344197
RLA1_HUMANRPLP1physical
26344197
RLA2_HUMANRPLP2physical
26344197
RS11_HUMANRPS11physical
26344197
RS14_HUMANRPS14physical
26344197
RS15A_HUMANRPS15Aphysical
26344197
RS18_HUMANRPS18physical
26344197
RS2_HUMANRPS2physical
26344197
RS23_HUMANRPS23physical
26344197
RS26_HUMANRPS26physical
26344197
RS6_HUMANRPS6physical
26344197
RS7_HUMANRPS7physical
26344197
RS8_HUMANRPS8physical
26344197
RS9_HUMANRPS9physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL27_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-27; LYS-93; LYS-117 ANDLYS-128, AND MASS SPECTROMETRY.

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