RS21_HUMAN - dbPTM
RS21_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS21_HUMAN
UniProt AC P63220
Protein Name 40S ribosomal protein S21
Gene Name RPS21
Organism Homo sapiens (Human).
Sequence Length 83
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
Protein Sequence MQNDAGEFVDLYVPRKCSASNRIIGAKDHASIQMNVAEVDKVTGRFNGQFKTYAICGAIRRMGESDDSILRLAKADGIVSKNF
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
1Sulfoxidation-------MQNDAGEF
-------CCCCCCCE
8.2928183972
1Acetylation-------MQNDAGEF
-------CCCCCCCE
8.2919413330
12PhosphorylationAGEFVDLYVPRKCSA
CCCEEEEEECCCCCC
12.1626657352
12NitrationAGEFVDLYVPRKCSA
CCCEEEEEECCCCCC
12.16-
27AcetylationSNRIIGAKDHASIQM
CCCCCCCCCCEEEEE
44.8523954790
27UbiquitinationSNRIIGAKDHASIQM
CCCCCCCCCCEEEEE
44.8521890473
34SulfoxidationKDHASIQMNVAEVDK
CCCEEEEEEEEEHHE
4.0930846556
41SumoylationMNVAEVDKVTGRFNG
EEEEEHHEEEEEECC
47.0425114211
41MalonylationMNVAEVDKVTGRFNG
EEEEEHHEEEEEECC
47.0426320211
41UbiquitinationMNVAEVDKVTGRFNG
EEEEEHHEEEEEECC
47.04-
41AcetylationMNVAEVDKVTGRFNG
EEEEEHHEEEEEECC
47.0423954790
51UbiquitinationGRFNGQFKTYAICGA
EEECCCEEHHHHHHH
32.5121890473
51AcetylationGRFNGQFKTYAICGA
EEECCCEEHHHHHHH
32.5125953088
51MethylationGRFNGQFKTYAICGA
EEECCCEEHHHHHHH
32.5130592059
52PhosphorylationRFNGQFKTYAICGAI
EECCCEEHHHHHHHH
21.3423403867
53PhosphorylationFNGQFKTYAICGAIR
ECCCEEHHHHHHHHH
8.4425394399
56GlutathionylationQFKTYAICGAIRRMG
CEEHHHHHHHHHHHC
1.9922555962
56S-palmitoylationQFKTYAICGAIRRMG
CEEHHHHHHHHHHHC
1.9929575903
62SulfoxidationICGAIRRMGESDDSI
HHHHHHHHCCCCHHH
5.1221406390
65PhosphorylationAIRRMGESDDSILRL
HHHHHCCCCHHHHHH
40.7722617229
68PhosphorylationRMGESDDSILRLAKA
HHCCCCHHHHHHHHH
28.6320068231
71MethylationESDDSILRLAKADGI
CCCHHHHHHHHHCCC
30.81115492605
742-HydroxyisobutyrylationDSILRLAKADGIVSK
HHHHHHHHHCCCCCC
52.15-
74UbiquitinationDSILRLAKADGIVSK
HHHHHHHHHCCCCCC
52.152190698
74AcetylationDSILRLAKADGIVSK
HHHHHHHHHCCCCCC
52.1526051181
80PhosphorylationAKADGIVSKNF----
HHHCCCCCCCC----
21.6927251275
81UbiquitinationKADGIVSKNF-----
HHCCCCCCCC-----
52.0221890473
81AcetylationKADGIVSKNF-----
HHCCCCCCCC-----
52.0219608861

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 RS21_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS21_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 RS21_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSSA_HUMANRPSAphysical
16169070
A4_HUMANAPPphysical
21832049
RSSA_HUMANRPSAphysical
22939629
RS23_HUMANRPS23physical
22939629
RS28_HUMANRPS28physical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS6_HUMANRPS6physical
22939629
RS8_HUMANRPS8physical
22939629
RS26_HUMANRPS26physical
22939629
RS25_HUMANRPS25physical
22939629
RS24_HUMANRPS24physical
22939629
RS2_HUMANRPS2physical
22939629
RS5_HUMANRPS5physical
22939629
RS3_HUMANRPS3physical
22939629
RS29_HUMANRPS29physical
22939629
RS7_HUMANRPS7physical
22939629
RL40_HUMANUBA52physical
22939629
RS27L_HUMANRPS27Lphysical
22939629
RT21_HUMANMRPS21physical
22939629
UB2V2_HUMANUBE2V2physical
22939629
ADRM1_HUMANADRM1physical
22863883
DYL1_HUMANDYNLL1physical
22863883
RACK1_HUMANGNB2L1physical
22863883
RSSA_HUMANRPSAphysical
22863883
C1TC_HUMANMTHFD1physical
22863883
PRS4_HUMANPSMC1physical
22863883
PRS7_HUMANPSMC2physical
22863883
PRS10_HUMANPSMC6physical
22863883
PSD11_HUMANPSMD11physical
22863883
PSMD1_HUMANPSMD1physical
22863883
PSMD3_HUMANPSMD3physical
22863883
PSMD8_HUMANPSMD8physical
22863883
RS10_HUMANRPS10physical
22863883
RS13_HUMANRPS13physical
22863883
RS15A_HUMANRPS15Aphysical
22863883
RS16_HUMANRPS16physical
22863883
RS27L_HUMANRPS27Lphysical
22863883
RS28_HUMANRPS28physical
22863883
RS2_HUMANRPS2physical
22863883
RS3_HUMANRPS3physical
22863883
RS5_HUMANRPS5physical
22863883
RS8_HUMANRPS8physical
22863883
HNRPQ_HUMANSYNCRIPphysical
22863883
UCHL5_HUMANUCHL5physical
22863883
ZUFSP_HUMANZUFSPphysical
25416956

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 RS21_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
"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-81, AND MASS SPECTROMETRY.

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