RS24_HUMAN - dbPTM
RS24_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS24_HUMAN
UniProt AC P62847
Protein Name 40S ribosomal protein S24
Gene Name RPS24
Organism Homo sapiens (Human).
Sequence Length 133
Subcellular Localization
Protein Description Required for processing of pre-rRNA and maturation of 40S ribosomal subunits..
Protein Sequence MNDTVTIRTRKFMTNRLLQRKQMVIDVLHPGKATVPKTEIREKLAKMYKTTPDVIFVFGFRTHFGGGKTTGFGMIYDSLDYAKKNEPKHRLARHGLYEKKKTSRKQRKERKNRMKKVRGTAKANVGAGKKPKE
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-------MNDTVTIR
-------CCCCEEEH
10.3822223895
4Phosphorylation----MNDTVTIRTRK
----CCCCEEEHHHH
17.9719691289
6Phosphorylation--MNDTVTIRTRKFM
--CCCCEEEHHHHHH
13.5624719451
9PhosphorylationNDTVTIRTRKFMTNR
CCCEEEHHHHHHHHH
34.0728112733
14PhosphorylationIRTRKFMTNRLLQRK
EHHHHHHHHHHHHHC
21.9621406692
21AcetylationTNRLLQRKQMVIDVL
HHHHHHHCCHHHEEE
29.7726051181
21UbiquitinationTNRLLQRKQMVIDVL
HHHHHHHCCHHHEEE
29.7721890473
21 (in isoform 1)Ubiquitination-29.7721890473
21 (in isoform 2)Ubiquitination-29.7721890473
21UbiquitinationTNRLLQRKQMVIDVL
HHHHHHHCCHHHEEE
29.7721890473
21UbiquitinationTNRLLQRKQMVIDVL
HHHHHHHCCHHHEEE
29.7721890473
21UbiquitinationTNRLLQRKQMVIDVL
HHHHHHHCCHHHEEE
29.7721890473
23SulfoxidationRLLQRKQMVIDVLHP
HHHHHCCHHHEEECC
2.9830846556
32 (in isoform 2)Ubiquitination-45.3921890473
32AcetylationIDVLHPGKATVPKTE
HEEECCCCCCCCHHH
45.3926051181
32UbiquitinationIDVLHPGKATVPKTE
HEEECCCCCCCCHHH
45.3921890473
32 (in isoform 1)Ubiquitination-45.3921890473
32UbiquitinationIDVLHPGKATVPKTE
HEEECCCCCCCCHHH
45.3921890473
32UbiquitinationIDVLHPGKATVPKTE
HEEECCCCCCCCHHH
45.3921890473
32UbiquitinationIDVLHPGKATVPKTE
HEEECCCCCCCCHHH
45.3921890473
37SumoylationPGKATVPKTEIREKL
CCCCCCCHHHHHHHH
55.2228112733
37SumoylationPGKATVPKTEIREKL
CCCCCCCHHHHHHHH
55.22-
37UbiquitinationPGKATVPKTEIREKL
CCCCCCCHHHHHHHH
55.2221890473
37AcetylationPGKATVPKTEIREKL
CCCCCCCHHHHHHHH
55.2223749302
37UbiquitinationPGKATVPKTEIREKL
CCCCCCCHHHHHHHH
55.2221890473
37 (in isoform 1)Ubiquitination-55.2221890473
37 (in isoform 2)Ubiquitination-55.2221890473
37UbiquitinationPGKATVPKTEIREKL
CCCCCCCHHHHHHHH
55.2221890473
37UbiquitinationPGKATVPKTEIREKL
CCCCCCCHHHHHHHH
55.2221890473
38PhosphorylationGKATVPKTEIREKLA
CCCCCCHHHHHHHHH
30.4923312004
46UbiquitinationEIREKLAKMYKTTPD
HHHHHHHHHHCCCCC
53.88-
46AcetylationEIREKLAKMYKTTPD
HHHHHHHHHHCCCCC
53.8826051181
49UbiquitinationEKLAKMYKTTPDVIF
HHHHHHHCCCCCEEE
42.28-
50PhosphorylationKLAKMYKTTPDVIFV
HHHHHHCCCCCEEEE
26.5220068231
62PhosphorylationIFVFGFRTHFGGGKT
EEEEEEECCCCCCCC
21.2120068231
68UbiquitinationRTHFGGGKTTGFGMI
ECCCCCCCCCCEEEH
46.3021890473
68UbiquitinationRTHFGGGKTTGFGMI
ECCCCCCCCCCEEEH
46.3021890473
68 (in isoform 2)Ubiquitination-46.3021890473
68AcetylationRTHFGGGKTTGFGMI
ECCCCCCCCCCEEEH
46.3023954790
68UbiquitinationRTHFGGGKTTGFGMI
ECCCCCCCCCCEEEH
46.3021890473
68 (in isoform 1)Ubiquitination-46.3021890473
68UbiquitinationRTHFGGGKTTGFGMI
ECCCCCCCCCCEEEH
46.3021890473
69PhosphorylationTHFGGGKTTGFGMIY
CCCCCCCCCCEEEHH
35.1121406692
70PhosphorylationHFGGGKTTGFGMIYD
CCCCCCCCCEEEHHH
33.7221406692
74SulfoxidationGKTTGFGMIYDSLDY
CCCCCEEEHHHCHHH
2.1030846556
76PhosphorylationTTGFGMIYDSLDYAK
CCCEEEHHHCHHHHH
7.2128152594
76 (in isoform 4)Phosphorylation-7.2127642862
78PhosphorylationGFGMIYDSLDYAKKN
CEEEHHHCHHHHHHC
13.2328152594
81PhosphorylationMIYDSLDYAKKNEPK
EHHHCHHHHHHCCCC
26.1328152594
81 (in isoform 4)Phosphorylation-26.1327642862
83 (in isoform 2)Ubiquitination-50.3221890473
83UbiquitinationYDSLDYAKKNEPKHR
HHCHHHHHHCCCCHH
50.3221890473
83UbiquitinationYDSLDYAKKNEPKHR
HHCHHHHHHCCCCHH
50.3221890473
83UbiquitinationYDSLDYAKKNEPKHR
HHCHHHHHHCCCCHH
50.3221890473
83UbiquitinationYDSLDYAKKNEPKHR
HHCHHHHHHCCCCHH
50.3221890473
83AcetylationYDSLDYAKKNEPKHR
HHCHHHHHHCCCCHH
50.3223236377
83SuccinylationYDSLDYAKKNEPKHR
HHCHHHHHHCCCCHH
50.3223954790
83 (in isoform 1)Ubiquitination-50.3221890473
84UbiquitinationDSLDYAKKNEPKHRL
HCHHHHHHCCCCHHH
59.37-
88UbiquitinationYAKKNEPKHRLARHG
HHHHCCCCHHHHHCC
34.87-
99UbiquitinationARHGLYEKKKTSRKQ
HHCCHHHHHHHCHHH
46.11-
99AcetylationARHGLYEKKKTSRKQ
HHCCHHHHHHHCHHH
46.1123749302
100UbiquitinationRHGLYEKKKTSRKQR
HCCHHHHHHHCHHHH
49.71-
115AcetylationKERKNRMKKVRGTAK
HHHHHHHHHHHHHHH
44.9019608861
120PhosphorylationRMKKVRGTAKANVGA
HHHHHHHHHHCCCCC
17.89-
122SumoylationKKVRGTAKANVGAGK
HHHHHHHHCCCCCCC
40.09-
122AcetylationKKVRGTAKANVGAGK
HHHHHHHHCCCCCCC
40.0925953088
122SumoylationKKVRGTAKANVGAGK
HHHHHHHHCCCCCCC
40.09-
122UbiquitinationKKVRGTAKANVGAGK
HHHHHHHHCCCCCCC
40.09-
129UbiquitinationKANVGAGKKPKE---
HCCCCCCCCCCC---
66.42-
130AcetylationANVGAGKKPKE----
CCCCCCCCCCC----
61.4813467605
132AcetylationVGAGKKPKE------
CCCCCCCCC------
82.1913467609

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 RS24_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS24_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 RS24_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS3A_HUMANRPS3Aphysical
22939629
RS3_HUMANRPS3physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS5_HUMANRPS5physical
22939629
RS6_HUMANRPS6physical
22939629
RS8_HUMANRPS8physical
22939629
RSSA_HUMANRPSAphysical
22939629
RS7_HUMANRPS7physical
22939629
RS26_HUMANRPS26physical
22939629
RS2_HUMANRPS2physical
22939629
RS9_HUMANRPS9physical
22939629
RS25_HUMANRPS25physical
22939629
RS27A_HUMANRPS27Aphysical
22939629
U2AF1_HUMANU2AF1physical
22939629
U2AF2_HUMANU2AF2physical
22939629
RS27L_HUMANRPS27Lphysical
22939629
PNISR_HUMANPNISRphysical
21988832
ST17B_HUMANSTK17Bphysical
21988832
NU188_HUMANNUP188physical
22863883
PNO1_HUMANPNO1physical
22863883
RS12_HUMANRPS12physical
22863883
RS13_HUMANRPS13physical
22863883
RS14_HUMANRPS14physical
22863883
RS15A_HUMANRPS15Aphysical
22863883
RS16_HUMANRPS16physical
22863883
RS18_HUMANRPS18physical
22863883
RS20_HUMANRPS20physical
22863883
RS27_HUMANRPS27physical
22863883
RS6_HUMANRPS6physical
22863883
RS7_HUMANRPS7physical
22863883
RS8_HUMANRPS8physical
22863883
TSR1_HUMANTSR1physical
22863883
PYM1_HUMANWIBGphysical
22863883

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610629Diamond-Blackfan anemia 3 (DBA3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS24_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-37, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-4, AND MASSSPECTROMETRY.

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