RL38_HUMAN - dbPTM
RL38_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL38_HUMAN
UniProt AC P63173
Protein Name 60S ribosomal protein L38
Gene Name RPL38
Organism Homo sapiens (Human).
Sequence Length 70
Subcellular Localization
Protein Description
Protein Sequence MPRKIEEIKDFLLTARRKDAKSVKIKKNKDNVKFKVRCSRYLYTLVITDKEKAEKLKQSLPPGLAVKELK
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
4Ubiquitination----MPRKIEEIKDF
----CCCCHHHHHHH
48.9121906983
4Sumoylation----MPRKIEEIKDF
----CCCCHHHHHHH
48.9128112733
42-Hydroxyisobutyrylation----MPRKIEEIKDF
----CCCCHHHHHHH
48.91-
9AcetylationPRKIEEIKDFLLTAR
CCCHHHHHHHHHHHH
45.7919608861
9UbiquitinationPRKIEEIKDFLLTAR
CCCHHHHHHHHHHHH
45.7921890473
92-HydroxyisobutyrylationPRKIEEIKDFLLTAR
CCCHHHHHHHHHHHH
45.79-
9SumoylationPRKIEEIKDFLLTAR
CCCHHHHHHHHHHHH
45.7928112733
9SumoylationPRKIEEIKDFLLTAR
CCCHHHHHHHHHHHH
45.79-
9UbiquitinationPRKIEEIKDFLLTAR
CCCHHHHHHHHHHHH
45.7921906983
14PhosphorylationEIKDFLLTARRKDAK
HHHHHHHHHHCCCCC
21.92-
16MethylationKDFLLTARRKDAKSV
HHHHHHHHCCCCCCC
40.73115492169
33UbiquitinationKKNKDNVKFKVRCSR
ECCCCCCEEEEEEEE
45.8021906983
39PhosphorylationVKFKVRCSRYLYTLV
CEEEEEEEEEEEEEE
17.2527422710
41PhosphorylationFKVRCSRYLYTLVIT
EEEEEEEEEEEEEEC
6.4328152594
43PhosphorylationVRCSRYLYTLVITDK
EEEEEEEEEEEECCH
6.7928152594
44PhosphorylationRCSRYLYTLVITDKE
EEEEEEEEEEECCHH
16.3828152594
48PhosphorylationYLYTLVITDKEKAEK
EEEEEEECCHHHHHH
33.2729978859
502-HydroxyisobutyrylationYTLVITDKEKAEKLK
EEEEECCHHHHHHHH
53.09-
50UbiquitinationYTLVITDKEKAEKLK
EEEEECCHHHHHHHH
53.0921890473
50AcetylationYTLVITDKEKAEKLK
EEEEECCHHHHHHHH
53.0925953088
50UbiquitinationYTLVITDKEKAEKLK
EEEEECCHHHHHHHH
53.0921906983
52AcetylationLVITDKEKAEKLKQS
EEECCHHHHHHHHHH
68.5323749302
52UbiquitinationLVITDKEKAEKLKQS
EEECCHHHHHHHHHH
68.53-
55UbiquitinationTDKEKAEKLKQSLPP
CCHHHHHHHHHHCCC
66.8821890473
55UbiquitinationTDKEKAEKLKQSLPP
CCHHHHHHHHHHCCC
66.8821906983
57UbiquitinationKEKAEKLKQSLPPGL
HHHHHHHHHHCCCCC
49.2421906983
57UbiquitinationKEKAEKLKQSLPPGL
HHHHHHHHHHCCCCC
49.2421890473
59PhosphorylationKAEKLKQSLPPGLAV
HHHHHHHHCCCCCCC
41.0521712546
67SumoylationLPPGLAVKELK----
CCCCCCCCCCC----
52.2819608861
67UbiquitinationLPPGLAVKELK----
CCCCCCCCCCC----
52.2821906983
67AcetylationLPPGLAVKELK----
CCCCCCCCCCC----
52.2819608861
67UbiquitinationLPPGLAVKELK----
CCCCCCCCCCC----
52.2821890473

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 RL38_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL38_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 RL38_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS6_HUMANRPS6physical
22939629
RS12_HUMANRPS12physical
22939629
RS28_HUMANRPS28physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RS19_HUMANRPS19physical
22939629
RS25_HUMANRPS25physical
22939629
RL5_HUMANRPL5physical
22939629
RL8_HUMANRPL8physical
22939629
RL3_HUMANRPL3physical
22939629
RL7_HUMANRPL7physical
22939629
RS13_HUMANRPS13physical
22939629
RS2_HUMANRPS2physical
22939629
RL7A_HUMANRPL7Aphysical
22939629
SRPRB_HUMANSRPRBphysical
22939629
SLIRP_HUMANSLIRPphysical
22939629
RM53_HUMANMRPL53physical
22939629
RRBP1_HUMANRRBP1physical
22939629
EHD4_HUMANEHD4physical
22863883
ROA1_HUMANHNRNPA1physical
22863883
SYIC_HUMANIARSphysical
22863883
IF2B3_HUMANIGF2BP3physical
22863883
NMT1_HUMANNMT1physical
22863883
PLCG1_HUMANPLCG1physical
22863883
RIC8A_HUMANRIC8Aphysical
22863883
NIPA_HUMANZC3HC1physical
22863883
EF1G_HUMANEEF1Gphysical
26344197
PESC_HUMANPES1physical
26344197
RL10_HUMANRPL10physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL13_HUMANRPL13physical
26344197
RL13A_HUMANRPL13Aphysical
26344197
RL15_HUMANRPL15physical
26344197
RL19_HUMANRPL19physical
26344197
RL22_HUMANRPL22physical
26344197
RL23A_HUMANRPL23Aphysical
26344197
RL26_HUMANRPL26physical
26344197
RL27_HUMANRPL27physical
26344197
RL27A_HUMANRPL27Aphysical
26344197
RL34_HUMANRPL34physical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL4_HUMANRPL4physical
26344197
RL7_HUMANRPL7physical
26344197
RL7A_HUMANRPL7Aphysical
26344197
RLA0_HUMANRPLP0physical
26344197
RLA1_HUMANRPLP1physical
26344197
RLA2_HUMANRPLP2physical
26344197
RS14_HUMANRPS14physical
26344197
RS18_HUMANRPS18physical
26344197
RS23_HUMANRPS23physical
26344197
RS26_HUMANRPS26physical
26344197
RS27_HUMANRPS27physical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS6_HUMANRPS6physical
26344197
RS7_HUMANRPS7physical
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 RL38_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-9 AND LYS-67, AND MASSSPECTROMETRY.

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