RS4X_HUMAN - dbPTM
RS4X_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS4X_HUMAN
UniProt AC P62701
Protein Name 40S ribosomal protein S4, X isoform
Gene Name RPS4X
Organism Homo sapiens (Human).
Sequence Length 263
Subcellular Localization Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Protein Description
Protein Sequence MARGPKKHLKRVAAPKHWMLDKLTGVFAPRPSTGPHKLRECLPLIIFLRNRLKYALTGDEVKKICMQRFIKIDGKVRTDITYPAGFMDVISIDKTGENFRLIYDTKGRFAVHRITPEEAKYKLCKVRKIFVGTKGIPHLVTHDARTIRYPDPLIKVNDTIQIDLETGKITDFIKFDTGNLCMVTGGANLGRIGVITNRERHPGSFDVVHVKDANGNSFATRLSNIFVIGKGNKPWISLPRGKGIRLTIAEERDKRLAAKQSSG
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
7Methylation-MARGPKKHLKRVAA
-CCCCCHHHHHHHHC		58.2554413981
16AcetylationLKRVAAPKHWMLDKL
HHHHHCCCCHHHHHC		45.2124791509
162-HydroxyisobutyrylationLKRVAAPKHWMLDKL
HHHHHCCCCHHHHHC		45.21-
16UbiquitinationLKRVAAPKHWMLDKL
HHHHHCCCCHHHHHC		45.2121890473
22AcetylationPKHWMLDKLTGVFAP
CCCHHHHHCCCCCCC		43.9422635365
222-HydroxyisobutyrylationPKHWMLDKLTGVFAP
CCCHHHHHCCCCCCC		43.94-
22UbiquitinationPKHWMLDKLTGVFAP
CCCHHHHHCCCCCCC		43.9421906983
24PhosphorylationHWMLDKLTGVFAPRP
CHHHHHCCCCCCCCC		36.7220363803
32PhosphorylationGVFAPRPSTGPHKLR
CCCCCCCCCCCCHHH		47.4728450419
33PhosphorylationVFAPRPSTGPHKLRE
CCCCCCCCCCCHHHH		58.3728450419
37UbiquitinationRPSTGPHKLRECLPL
CCCCCCCHHHHHHHH		52.9921890473
372-HydroxyisobutyrylationRPSTGPHKLRECLPL
CCCCCCCHHHHHHHH		52.99-
41GlutathionylationGPHKLRECLPLIIFL
CCCHHHHHHHHHHHH		3.7122555962
41S-palmitoylationGPHKLRECLPLIIFL
CCCHHHHHHHHHHHH		3.7129575903
41S-nitrosylationGPHKLRECLPLIIFL
CCCHHHHHHHHHHHH		3.7121278135
41S-nitrosocysteineGPHKLRECLPLIIFL
CCCHHHHHHHHHHHH		3.71-
53UbiquitinationIFLRNRLKYALTGDE
HHHHHCHHHHHHHHH		25.8221906983
53MethylationIFLRNRLKYALTGDE
HHHHHCHHHHHHHHH		25.82164141
532-HydroxyisobutyrylationIFLRNRLKYALTGDE
HHHHHCHHHHHHHHH		25.82-
53AcetylationIFLRNRLKYALTGDE
HHHHHCHHHHHHHHH		25.82164141
54PhosphorylationFLRNRLKYALTGDEV
HHHHCHHHHHHHHHH		16.0728152594
57PhosphorylationNRLKYALTGDEVKKI
HCHHHHHHHHHHHHH		34.1228152594
62AcetylationALTGDEVKKICMQRF
HHHHHHHHHHHHHHE		34.0824470465
622-HydroxyisobutyrylationALTGDEVKKICMQRF
HHHHHHHHHHHHHHE		34.08-
62UbiquitinationALTGDEVKKICMQRF
HHHHHHHHHHHHHHE		34.0821906983
63UbiquitinationLTGDEVKKICMQRFI
HHHHHHHHHHHHHEE		46.4421906983
712-HydroxyisobutyrylationICMQRFIKIDGKVRT
HHHHHEEEECCEEEC		31.84-
71UbiquitinationICMQRFIKIDGKVRT
HHHHHEEEECCEEEC		31.84-
75UbiquitinationRFIKIDGKVRTDITY
HEEEECCEEECCCCC		25.46-
78PhosphorylationKIDGKVRTDITYPAG
EECCEEECCCCCCCC		34.4421712546
82NitrationKVRTDITYPAGFMDV
EEECCCCCCCCEEEE		7.45-
87SulfoxidationITYPAGFMDVISIDK
CCCCCCEEEEEEEEC		3.8328183972
91PhosphorylationAGFMDVISIDKTGEN
CCEEEEEEEECCCCC		25.2821712546
942-HydroxyisobutyrylationMDVISIDKTGENFRL
EEEEEEECCCCCEEE		57.68-
94UbiquitinationMDVISIDKTGENFRL
EEEEEEECCCCCEEE		57.6821906983
94AcetylationMDVISIDKTGENFRL
EEEEEEECCCCCEEE		57.6826051181
95PhosphorylationDVISIDKTGENFRLI
EEEEEECCCCCEEEE		46.0821406692
103PhosphorylationGENFRLIYDTKGRFA
CCCEEEEEECCCCEE		23.3521406692
105PhosphorylationNFRLIYDTKGRFAVH
CEEEEEECCCCEEEE		20.5821406692
106AcetylationFRLIYDTKGRFAVHR
EEEEEECCCCEEEEE		45.2326051181
106UbiquitinationFRLIYDTKGRFAVHR
EEEEEECCCCEEEEE		45.2321906983
1062-HydroxyisobutyrylationFRLIYDTKGRFAVHR
EEEEEECCCCEEEEE		45.23-
115O-linked_GlycosylationRFAVHRITPEEAKYK
CEEEEECCHHHHHHH		25.3030379171
120SuccinylationRITPEEAKYKLCKVR
ECCHHHHHHHEEEEE		46.3123954790
120AcetylationRITPEEAKYKLCKVR
ECCHHHHHHHEEEEE		46.3125825284
1202-HydroxyisobutyrylationRITPEEAKYKLCKVR
ECCHHHHHHHEEEEE		46.31-
120UbiquitinationRITPEEAKYKLCKVR
ECCHHHHHHHEEEEE		46.3119608861
121PhosphorylationITPEEAKYKLCKVRK
CCHHHHHHHEEEEEE		19.0825839225
122UbiquitinationTPEEAKYKLCKVRKI
CHHHHHHHEEEEEEE		46.86-
125UbiquitinationEAKYKLCKVRKIFVG
HHHHHEEEEEEEEEC		56.35-
1282-HydroxyisobutyrylationYKLCKVRKIFVGTKG
HHEEEEEEEEECCCC		43.41-
128UbiquitinationYKLCKVRKIFVGTKG
HHEEEEEEEEECCCC		43.4121906983
133PhosphorylationVRKIFVGTKGIPHLV
EEEEEECCCCCCCEE		22.3123312004
1342-HydroxyisobutyrylationRKIFVGTKGIPHLVT
EEEEECCCCCCCEEC		49.25-
134UbiquitinationRKIFVGTKGIPHLVT
EEEEECCCCCCCEEC		49.2521906983
134AcetylationRKIFVGTKGIPHLVT
EEEEECCCCCCCEEC		49.2523954790
145MethylationHLVTHDARTIRYPDP
CEECCCCCCCCCCCC		36.42-
146PhosphorylationLVTHDARTIRYPDPL
EECCCCCCCCCCCCE		16.1328152594
148MethylationTHDARTIRYPDPLIK
CCCCCCCCCCCCEEE		36.00-
149PhosphorylationHDARTIRYPDPLIKV
CCCCCCCCCCCEEEE		14.2428152594
155UbiquitinationRYPDPLIKVNDTIQI
CCCCCEEEECCEEEE		42.54-
168UbiquitinationQIDLETGKITDFIKF
EEECCCCCEEEEEEE		50.2621906983
168AcetylationQIDLETGKITDFIKF
EEECCCCCEEEEEEE		50.2626051181
174SumoylationGKITDFIKFDTGNLC
CCEEEEEEECCCCEE		36.86-
177PhosphorylationTDFIKFDTGNLCMVT
EEEEEECCCCEEEEE		30.9720068231
181S-nitrosocysteineKFDTGNLCMVTGGAN
EECCCCEEEEECCCC		2.09-
181S-nitrosylationKFDTGNLCMVTGGAN
EECCCCEEEEECCCC		2.0921278135
181GlutathionylationKFDTGNLCMVTGGAN
EECCCCEEEEECCCC		2.0922555962
182SulfoxidationFDTGNLCMVTGGANL
ECCCCEEEEECCCCC		3.2221406390
184PhosphorylationTGNLCMVTGGANLGR
CCCEEEEECCCCCCE		11.7420068231
196PhosphorylationLGRIGVITNRERHPG
CCEEEEEECCCCCCC		26.3023911959
198MethylationRIGVITNRERHPGSF
EEEEEECCCCCCCCE		33.41115492707
200MethylationGVITNRERHPGSFDV
EEEECCCCCCCCEEE		37.76-
204PhosphorylationNRERHPGSFDVVHVK
CCCCCCCCEEEEEEE		23.7920068231
211UbiquitinationSFDVVHVKDANGNSF
CEEEEEEECCCCCCE		35.9221890473
217PhosphorylationVKDANGNSFATRLSN
EECCCCCCEEEEEEE		20.0430266825
220PhosphorylationANGNSFATRLSNIFV
CCCCCEEEEEEEEEE		30.0830266825
223PhosphorylationNSFATRLSNIFVIGK
CCEEEEEEEEEEECC		25.2930266825
2302-HydroxyisobutyrylationSNIFVIGKGNKPWIS
EEEEEECCCCCCEEE		48.46-
230AcetylationSNIFVIGKGNKPWIS
EEEEEECCCCCCEEE		48.4626051181
230UbiquitinationSNIFVIGKGNKPWIS
EEEEEECCCCCCEEE		48.4621890473
230SumoylationSNIFVIGKGNKPWIS
EEEEEECCCCCCEEE		48.4628112733
233AcetylationFVIGKGNKPWISLPR
EEECCCCCCEEECCC		50.8526051181
2332-HydroxyisobutyrylationFVIGKGNKPWISLPR
EEECCCCCCEEECCC		50.85-
233UbiquitinationFVIGKGNKPWISLPR
EEECCCCCCEEECCC		50.8521906983
233MalonylationFVIGKGNKPWISLPR
EEECCCCCCEEECCC		50.8526320211
237PhosphorylationKGNKPWISLPRGKGI
CCCCCEEECCCCCCE		28.5828450419
247PhosphorylationRGKGIRLTIAEERDK
CCCCEEEEEEHHHHH		14.3219060867
259UbiquitinationRDKRLAAKQSSG---
HHHHHHHHHCCC---		45.14-
261PhosphorylationKRLAAKQSSG-----
HHHHHHHCCC-----		36.0024719451
262PhosphorylationRLAAKQSSG------
HHHHHHCCC------		46.1329514088
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 RS4X_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS4X_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 RS4X_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS7_HUMANRPS7physical
6188845
RS8_HUMANRPS8physical
6188845
RS15_HUMANRPS15physical
6188845
RS16_HUMANRPS16physical
6188845
RS17_HUMANRPS17physical
6188845
RS19_HUMANRPS19physical
6188845
RS20_HUMANRPS20physical
6188845
RS5_HUMANRPS5physical
6188845
RS6_HUMANRPS6physical
6188845
RS9_HUMANRPS9physical
6188845
RS11_HUMANRPS11physical
6188845
RS12_HUMANRPS12physical
6188845
RS13_HUMANRPS13physical
6188845
RS18_HUMANRPS18physical
6188845
RS2_HUMANRPS2physical
6188845
RS3_HUMANRPS3physical
6188845
RS10_HUMANRPS10physical
6188845
RS21_HUMANRPS21physical
6188845
RS14_HUMANRPS14physical
6188845
RS6_HUMANRPS6physical
22939629
RSSA_HUMANRPSAphysical
22939629
RS5_HUMANRPS5physical
22939629
RS7_HUMANRPS7physical
22939629
RS8_HUMANRPS8physical
22939629
SRP14_HUMANSRP14physical
22939629
U2AF1_HUMANU2AF1physical
22939629
TSR1_HUMANTSR1physical
22939629
EIFCL_HUMANEIF3CLphysical
22863883
RSSA_HUMANRPSAphysical
22863883
LARP1_HUMANLARP1physical
22863883
RS13_HUMANRPS13physical
22863883
RS14_HUMANRPS14physical
22863883
RS15A_HUMANRPS15Aphysical
22863883
RS16_HUMANRPS16physical
22863883
RS19_HUMANRPS19physical
22863883
RS20_HUMANRPS20physical
22863883
RS21_HUMANRPS21physical
22863883
RS24_HUMANRPS24physical
22863883
RS25_HUMANRPS25physical
22863883
RS26_HUMANRPS26physical
22863883
RS27_HUMANRPS27physical
22863883
RS28_HUMANRPS28physical
22863883
RS29_HUMANRPS29physical
22863883
RS2_HUMANRPS2physical
22863883
RS3_HUMANRPS3physical
22863883
RS5_HUMANRPS5physical
22863883
RS6_HUMANRPS6physical
22863883
RS7_HUMANRPS7physical
22863883
RS8_HUMANRPS8physical
22863883
RS9_HUMANRPS9physical
22863883
TSR1_HUMANTSR1physical
22863883
PYM1_HUMANWIBGphysical
22863883
ZZEF1_HUMANZZEF1physical
26186194
HECD3_HUMANHECTD3physical
26186194
IF6_HUMANEIF6physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL17_HUMANRPL17physical
26344197
RL18_HUMANRPL18physical
26344197
RL27_HUMANRPL27physical
26344197
RL29_HUMANRPL29physical
26344197
RL35_HUMANRPL35physical
26344197
RL35A_HUMANRPL35Aphysical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL8_HUMANRPL8physical
26344197
RS10_HUMANRPS10physical
26344197
RS18_HUMANRPS18physical
26344197
RS6_HUMANRPS6physical
26344197
RS7_HUMANRPS7physical
26344197
RS8_HUMANRPS8physical
26344197
ZZEF1_HUMANZZEF1physical
28514442
GGPPS_HUMANGGPS1physical
28514442
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 RS4X_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-120 AND LYS-134, AND MASSSPECTROMETRY.
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 THR-247, AND MASSSPECTROMETRY.

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