RS15A_HUMAN - dbPTM
RS15A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS15A_HUMAN
UniProt AC P62244
Protein Name 40S ribosomal protein S15a
Gene Name RPS15A
Organism Homo sapiens (Human).
Sequence Length 130
Subcellular Localization
Protein Description
Protein Sequence MVRMNVLADALKSINNAEKRGKRQVLIRPCSKVIVRFLTVMMKHGYIGEFEIIDDHRAGKIVVNLTGRLNKCGVISPRFDVQLKDLEKWQNNLLPSRQFGFIVLTTSAGIMDHEEARRKHTGGKILGFFF
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
4Sulfoxidation----MVRMNVLADAL
----CCCHHHHHHHH
2.5021406390
12AcetylationNVLADALKSINNAEK
HHHHHHHHHCCHHHH
51.5126051181
12UbiquitinationNVLADALKSINNAEK
HHHHHHHHHCCHHHH
51.5121890473
19AcetylationKSINNAEKRGKRQVL
HHCCHHHHHCCCCEE
65.1323749302
19UbiquitinationKSINNAEKRGKRQVL
HHCCHHHHHCCCCEE
65.1321890473
19SuccinylationKSINNAEKRGKRQVL
HHCCHHHHHCCCCEE
65.1323954790
192-HydroxyisobutyrylationKSINNAEKRGKRQVL
HHCCHHHHHCCCCEE
65.13-
32UbiquitinationVLIRPCSKVIVRFLT
EEEECCHHHHHHHHH
42.5721890473
32AcetylationVLIRPCSKVIVRFLT
EEEECCHHHHHHHHH
42.5725953088
46PhosphorylationTVMMKHGYIGEFEII
HHHHHCCCEEEEEEE
12.8928152594
60UbiquitinationIDDHRAGKIVVNLTG
ECCCCCCEEEEECCC
31.2021890473
602-HydroxyisobutyrylationIDDHRAGKIVVNLTG
ECCCCCCEEEEECCC
31.20-
66PhosphorylationGKIVVNLTGRLNKCG
CEEEEECCCCCCCCC
18.30-
71AcetylationNLTGRLNKCGVISPR
ECCCCCCCCCCCCCC
36.6425953088
71UbiquitinationNLTGRLNKCGVISPR
ECCCCCCCCCCCCCC
36.6421890473
712-HydroxyisobutyrylationNLTGRLNKCGVISPR
ECCCCCCCCCCCCCC
36.64-
72S-palmitoylationLTGRLNKCGVISPRF
CCCCCCCCCCCCCCC
5.2529575903
842-HydroxyisobutyrylationPRFDVQLKDLEKWQN
CCCCEEHHHHHHHHH
43.08-
84UbiquitinationPRFDVQLKDLEKWQN
CCCCEEHHHHHHHHH
43.0821890473
84AcetylationPRFDVQLKDLEKWQN
CCCCEEHHHHHHHHH
43.0826822725
882-HydroxyisobutyrylationVQLKDLEKWQNNLLP
EEHHHHHHHHHCCCC
62.47-
88AcetylationVQLKDLEKWQNNLLP
EEHHHHHHHHHCCCC
62.4725825284
88SuccinylationVQLKDLEKWQNNLLP
EEHHHHHHHHHCCCC
62.4721890473
88SuccinylationVQLKDLEKWQNNLLP
EEHHHHHHHHHCCCC
62.47-
88UbiquitinationVQLKDLEKWQNNLLP
EEHHHHHHHHHCCCC
62.4721890473
96PhosphorylationWQNNLLPSRQFGFIV
HHHCCCCHHHCCEEE
38.3925278378
121PhosphorylationEEARRKHTGGKILGF
HHHHHHHCCCCEEEE
51.14-
1242-HydroxyisobutyrylationRRKHTGGKILGFFF-
HHHHCCCCEEEEEC-
35.78-
124UbiquitinationRRKHTGGKILGFFF-
HHHHCCCCEEEEEC-
35.7821890473
124AcetylationRRKHTGGKILGFFF-
HHHHCCCCEEEEEC-
35.7819608861

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 RS15A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS15A_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 RS15A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS19_HUMANRPS19physical
22939629
RS26_HUMANRPS26physical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RS3_HUMANRPS3physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS5_HUMANRPS5physical
22939629
RS6_HUMANRPS6physical
22939629
RS7_HUMANRPS7physical
22939629
RS8_HUMANRPS8physical
22939629
RSSA_HUMANRPSAphysical
22939629
RS23_HUMANRPS23physical
22939629
RS16_HUMANRPS16physical
22939629
RS17_HUMANRPS17physical
22939629
RS24_HUMANRPS24physical
22939629
RS2_HUMANRPS2physical
22939629
RS20_HUMANRPS20physical
22939629
RS15_HUMANRPS15physical
22939629
RS21_HUMANRPS21physical
22939629
RS27A_HUMANRPS27Aphysical
22939629
RT14_HUMANMRPS14physical
22939629
SAE2_HUMANUBA2physical
22939629
PRS4_HUMANPSMC1physical
22863883
PRS10_HUMANPSMC6physical
22863883
PSD11_HUMANPSMD11physical
22863883
PSMD3_HUMANPSMD3physical
22863883
RS26_HUMANRPS26physical
22863883
RS28_HUMANRPS28physical
22863883
RS3_HUMANRPS3physical
22863883
RS6_HUMANRPS6physical
22863883
RS8_HUMANRPS8physical
22863883
TSR1_HUMANTSR1physical
22863883
DIM1_HUMANDIMT1physical
26344197
IF6_HUMANEIF6physical
26344197
UBIM_HUMANFAUphysical
26344197
GNL1_HUMANGNL1physical
26344197
GNL3_HUMANGNL3physical
26344197
IMP3_HUMANIMP3physical
26344197
MPP10_HUMANMPHOSPH10physical
26344197
RM14_HUMANMRPL14physical
26344197
RM16_HUMANMRPL16physical
26344197
RM22_HUMANMRPL22physical
26344197
RT14_HUMANMRPS14physical
26344197
RT07_HUMANMRPS7physical
26344197
RL10_HUMANRPL10physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL11_HUMANRPL11physical
26344197
RL12_HUMANRPL12physical
26344197
RL13A_HUMANRPL13Aphysical
26344197
RL14_HUMANRPL14physical
26344197
RL15_HUMANRPL15physical
26344197
RL17_HUMANRPL17physical
26344197
RL18_HUMANRPL18physical
26344197
RL23A_HUMANRPL23Aphysical
26344197
RL27A_HUMANRPL27Aphysical
26344197
RL28_HUMANRPL28physical
26344197
RL30_HUMANRPL30physical
26344197
RL31_HUMANRPL31physical
26344197
RL32_HUMANRPL32physical
26344197
RL34_HUMANRPL34physical
26344197
RL35_HUMANRPL35physical
26344197
RL37_HUMANRPL37physical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL38_HUMANRPL38physical
26344197
RL6_HUMANRPL6physical
26344197
RL7_HUMANRPL7physical
26344197
RL7A_HUMANRPL7Aphysical
26344197
RL9_HUMANRPL9physical
26344197
RLA1_HUMANRPLP1physical
26344197
RS11_HUMANRPS11physical
26344197
RS13_HUMANRPS13physical
26344197
RS14_HUMANRPS14physical
26344197
RS15_HUMANRPS15physical
26344197
RS17_HUMANRPS17physical
26344197
RS18_HUMANRPS18physical
26344197
RS19_HUMANRPS19physical
26344197
RS23_HUMANRPS23physical
26344197
RS26_HUMANRPS26physical
26344197
RS3A_HUMANRPS3Aphysical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS5_HUMANRPS5physical
26344197
RS6_HUMANRPS6physical
26344197
RS7_HUMANRPS7physical
26344197
RS8_HUMANRPS8physical
26344197
RS9_HUMANRPS9physical
26344197
TBB5_HUMANTUBBphysical
26344197
TBB2B_HUMANTUBB2Bphysical
26344197
TBB4B_HUMANTUBB4Bphysical
26344197
RL40_HUMANUBA52physical
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 RS15A_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-124, AND MASS SPECTROMETRY.

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