RS28_HUMAN - dbPTM
RS28_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS28_HUMAN
UniProt AC P62857
Protein Name 40S ribosomal protein S28
Gene Name RPS28
Organism Homo sapiens (Human).
Sequence Length 69
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 MDTSRVQPIKLARVTKVLGRTGSQGQCTQVRVEFMDDTSRSIIRNVKGPVREGDVLTLLESEREARRLR
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
1Acetylation-------MDTSRVQP
-------CCCCCCCC
13.15-
3Phosphorylation-----MDTSRVQPIK
-----CCCCCCCCHH
19.6825849741
4Phosphorylation----MDTSRVQPIKL
----CCCCCCCCHHH
26.6220068231
10AcetylationTSRVQPIKLARVTKV
CCCCCCHHHHHHEEE
42.6625953088
102-HydroxyisobutyrylationTSRVQPIKLARVTKV
CCCCCCHHHHHHEEE
42.66-
10UbiquitinationTSRVQPIKLARVTKV
CCCCCCHHHHHHEEE
42.6621890473
16AcetylationIKLARVTKVLGRTGS
HHHHHHEEECCCCCC
32.3826051181
16MalonylationIKLARVTKVLGRTGS
HHHHHHEEECCCCCC
32.3826320211
162-HydroxyisobutyrylationIKLARVTKVLGRTGS
HHHHHHEEECCCCCC
32.38-
16UbiquitinationIKLARVTKVLGRTGS
HHHHHHEEECCCCCC
32.38-
21PhosphorylationVTKVLGRTGSQGQCT
HEEECCCCCCCCCEE
39.1122617229
23PhosphorylationKVLGRTGSQGQCTQV
EECCCCCCCCCEEEE
30.4423401153
27S-nitrosocysteineRTGSQGQCTQVRVEF
CCCCCCCEEEEEEEE
3.53-
27S-nitrosylationRTGSQGQCTQVRVEF
CCCCCCCEEEEEEEE
3.5319483679
28PhosphorylationTGSQGQCTQVRVEFM
CCCCCCEEEEEEEEC
23.3929396449
35SulfoxidationTQVRVEFMDDTSRSI
EEEEEEECCCCCCHH
2.6321406390
38PhosphorylationRVEFMDDTSRSIIRN
EEEECCCCCCHHHHH
23.0623312004
39PhosphorylationVEFMDDTSRSIIRNV
EEECCCCCCHHHHHC
30.9021712546
41PhosphorylationFMDDTSRSIIRNVKG
ECCCCCCHHHHHCCC
23.3323186163
472-HydroxyisobutyrylationRSIIRNVKGPVREGD
CHHHHHCCCCCCCCC
62.13-
47UbiquitinationRSIIRNVKGPVREGD
CHHHHHCCCCCCCCC
62.13-
47SuccinylationRSIIRNVKGPVREGD
CHHHHHCCCCCCCCC
62.1327452117
57PhosphorylationVREGDVLTLLESERE
CCCCCHHHHHHHHHH
29.1921712546
61PhosphorylationDVLTLLESEREARRL
CHHHHHHHHHHHHHC
41.7630624053
63MethylationLTLLESEREARRLR-
HHHHHHHHHHHHCC-
52.75115492667

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 RS28_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS28_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 RS28_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR412_HUMANKRTAP4-12physical
16189514
EF1G_HUMANEEF1Gphysical
16169070
RS3_HUMANRPS3physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS6_HUMANRPS6physical
22939629
RS8_HUMANRPS8physical
22939629
RSSA_HUMANRPSAphysical
22939629
RS2_HUMANRPS2physical
22939629
RS9_HUMANRPS9physical
22939629
RT28_HUMANMRPS28physical
22939629
UBL4A_HUMANUBL4Aphysical
22939629
ROA2_HUMANHNRNPA2B1physical
22863883
RSSA_HUMANRPSAphysical
22863883
PSMD3_HUMANPSMD3physical
22863883
RS10_HUMANRPS10physical
22863883
RS12_HUMANRPS12physical
22863883
RS13_HUMANRPS13physical
22863883
RS14_HUMANRPS14physical
22863883
RS16_HUMANRPS16physical
22863883
RS19_HUMANRPS19physical
22863883
RS20_HUMANRPS20physical
22863883
RS23_HUMANRPS23physical
22863883
RS24_HUMANRPS24physical
22863883
RS25_HUMANRPS25physical
22863883
RS27L_HUMANRPS27Lphysical
22863883
RS27_HUMANRPS27physical
22863883
RS2_HUMANRPS2physical
22863883
RS3_HUMANRPS3physical
22863883
RS6_HUMANRPS6physical
22863883
TSR1_HUMANTSR1physical
22863883
PYM1_HUMANWIBGphysical
22863883
CCDB1_HUMANCCNDBP1physical
25416956
KRA23_HUMANKRTAP2-4physical
25416956
KRA24_HUMANKRTAP2-4physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
NHRF2_HUMANSLC9A3R2physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
606164Diamond-Blackfan anemia 15, with mandibulofacial dysostosis (DBA15)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS28_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-23, AND MASS SPECTROMETRY.
Phosphorylation
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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-23, AND MASS SPECTROMETRY.

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