RT05_HUMAN - dbPTM
RT05_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RT05_HUMAN
UniProt AC P82675
Protein Name 28S ribosomal protein S5, mitochondrial
Gene Name MRPS5
Organism Homo sapiens (Human).
Sequence Length 430
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MATAVRAVGCLPVLCSGTAGHLLGRQCSLNTLPAASILAWKSVLGNGHLSSLGTRDTHPYASLSRALQTQCCISSPSHLMSQQYRPYSFFTKLTADELWKGALAETGAGAKKGRGKRTKKKKRKDLNRGQIIGEGRYGFLWPGLNVPLMKNGAVQTIAQRSKEEQEKVEADMIQQREEWDRKKKMKVKRERGWSGNSWGGISLGPPDPGPCGETYEDFDTRILEVRNVFTMTAKEGRKKSIRVLVAVGNGKGAAGFSIGKATDRMDAFRKAKNRAVHHLHYIERYEDHTIFHDISLRFKRTHIKMKKQPKGYGLRCHRAIITICRLIGIKDMYAKVSGSINMLSLTQGLFRGLSRQETHQQLADKKGLHVVEIREECGPLPIVVASPRGPLRKDPEPEDEVPDVKLDWEDVKTAQGMKRSVWSNLKRAAT
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
21UbiquitinationLCSGTAGHLLGRQCS
ECCCCHHHHHCCCCC		18.5429967540
28PhosphorylationHLLGRQCSLNTLPAA
HHHCCCCCCCCCCHH		19.1324719451
36PhosphorylationLNTLPAASILAWKSV
CCCCCHHHHHHHHHH		21.90-
42PhosphorylationASILAWKSVLGNGHL
HHHHHHHHHHCCCCH		16.33-
50PhosphorylationVLGNGHLSSLGTRDT
HHCCCCHHHCCCCCC		20.17-
62PhosphorylationRDTHPYASLSRALQT
CCCCCCHHHHHHHHH		22.4927174698
64PhosphorylationTHPYASLSRALQTQC
CCCCHHHHHHHHHHH		17.0127174698
68UbiquitinationASLSRALQTQCCISS
HHHHHHHHHHHHCCC		28.6523000965
72UbiquitinationRALQTQCCISSPSHL
HHHHHHHHCCCHHHH		2.1323000965
73UbiquitinationALQTQCCISSPSHLM
HHHHHHHCCCHHHHH		6.3323000965
88UbiquitinationSQQYRPYSFFTKLTA
CCCCCCCCHHHHCCH		19.3024816145
94UbiquitinationYSFFTKLTADELWKG
CCHHHHCCHHHHHHH		33.3529967540
100UbiquitinationLTADELWKGALAETG
CCHHHHHHHHHHHHC		47.1029967540
105UbiquitinationLWKGALAETGAGAKK
HHHHHHHHHCCCCCC		48.9324816145
106PhosphorylationWKGALAETGAGAKKG
HHHHHHHHCCCCCCC		27.0725599653
1112-HydroxyisobutyrylationAETGAGAKKGRGKRT
HHHCCCCCCCCCCCC		55.64-
155UbiquitinationLMKNGAVQTIAQRSK
CCCCCHHHHHHHCCH		27.0123000965
159UbiquitinationGAVQTIAQRSKEEQE
CHHHHHHHCCHHHHH		46.4523000965
160UbiquitinationAVQTIAQRSKEEQEK
HHHHHHHCCHHHHHH		40.4523000965
164UbiquitinationIAQRSKEEQEKVEAD
HHHCCHHHHHHHHHH		68.7123000965
167UbiquitinationRSKEEQEKVEADMIQ
CCHHHHHHHHHHHHH		45.1024816145
169UbiquitinationKEEQEKVEADMIQQR
HHHHHHHHHHHHHHH		50.4423000965
172SulfoxidationQEKVEADMIQQREEW
HHHHHHHHHHHHHHH		3.7221406390
181UbiquitinationQQREEWDRKKKMKVK
HHHHHHHHHHHHCCH		54.4929967540
184UbiquitinationEEWDRKKKMKVKRER
HHHHHHHHHCCHHHC		47.1724816145
200UbiquitinationWSGNSWGGISLGPPD
CCCCCCCCCCCCCCC		10.4724816145
230PhosphorylationLEVRNVFTMTAKEGR
HEEEEEEEEECCCCC		14.88-
232PhosphorylationVRNVFTMTAKEGRKK
EEEEEEEECCCCCCC		31.36-
234UbiquitinationNVFTMTAKEGRKKSI
EEEEEECCCCCCCEE		52.0823000965
238UbiquitinationMTAKEGRKKSIRVLV
EECCCCCCCEEEEEE		62.8223000965
239UbiquitinationTAKEGRKKSIRVLVA
ECCCCCCCEEEEEEE		50.1623000965
246UbiquitinationKSIRVLVAVGNGKGA
CEEEEEEEECCCCCC		10.1929967540
251UbiquitinationLVAVGNGKGAAGFSI
EEEECCCCCCCCCCC		49.7523000965
256UbiquitinationNGKGAAGFSIGKATD
CCCCCCCCCCCCCHH		4.0523000965
260UbiquitinationAAGFSIGKATDRMDA
CCCCCCCCCHHHHHH		46.5829967540
260AcetylationAAGFSIGKATDRMDA
CCCCCCCCCHHHHHH		46.5826051181
260SuccinylationAAGFSIGKATDRMDA
CCCCCCCCCHHHHHH		46.5823954790
262PhosphorylationGFSIGKATDRMDAFR
CCCCCCCHHHHHHHH		27.8523532336
287UbiquitinationHYIERYEDHTIFHDI
HHHHHCCCCCEEECE		34.9824816145
295PhosphorylationHTIFHDISLRFKRTH
CCEEECEEEEEECCE		21.3930108239
301PhosphorylationISLRFKRTHIKMKKQ
EEEEEECCEEECCCC		28.6624719451
312PhosphorylationMKKQPKGYGLRCHRA
CCCCCCCCCCHHHHH		21.0717924679
326UbiquitinationAIITICRLIGIKDMY
HHHHHHHHHCCHHHH		3.4929967540
330UbiquitinationICRLIGIKDMYAKVS
HHHHHCCHHHHHHHC		31.0923000965
3302-HydroxyisobutyrylationICRLIGIKDMYAKVS
HHHHHCCHHHHHHHC		31.09-
333PhosphorylationLIGIKDMYAKVSGSI
HHCCHHHHHHHCCCC		17.2620860994
333UbiquitinationLIGIKDMYAKVSGSI
HHCCHHHHHHHCCCC		17.2629967540
335UbiquitinationGIKDMYAKVSGSINM
CCHHHHHHHCCCCCH		21.3223000965
337PhosphorylationKDMYAKVSGSINMLS
HHHHHHHCCCCCHHH		26.5622210691
339PhosphorylationMYAKVSGSINMLSLT
HHHHHCCCCCHHHHH		11.8622210691
344PhosphorylationSGSINMLSLTQGLFR
CCCCCHHHHHHHHHH		20.71-
346PhosphorylationSINMLSLTQGLFRGL
CCCHHHHHHHHHHCC		19.74-
3652-HydroxyisobutyrylationTHQQLADKKGLHVVE
HHHHHHHHCCCEEEE		43.03-
366UbiquitinationHQQLADKKGLHVVEI
HHHHHHHCCCEEEEE		68.2224816145
386PhosphorylationPLPIVVASPRGPLRK
CCCEEEECCCCCCCC		11.9721815630
393MalonylationSPRGPLRKDPEPEDE
CCCCCCCCCCCCCCC		82.4326320211
393SuccinylationSPRGPLRKDPEPEDE
CCCCCCCCCCCCCCC		82.4323954790
405UbiquitinationEDEVPDVKLDWEDVK
CCCCCCCCCCHHHHH		48.3829967540
412UbiquitinationKLDWEDVKTAQGMKR
CCCHHHHHHHHHHHH		50.9229967540
4182-HydroxyisobutyrylationVKTAQGMKRSVWSNL
HHHHHHHHHHHHHHH		48.63-
426MethylationRSVWSNLKRAAT---
HHHHHHHHHHCC---		44.21115973277
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 RT05_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RT05_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 RT05_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT35_HUMANMRPS35physical
22939629
RT10_HUMANMRPS10physical
22939629
TMM43_HUMANTMEM43physical
22939629
RT09_HUMANMRPS9physical
26186194
RT26_HUMANMRPS26physical
26186194
PTCD3_HUMANPTCD3physical
26186194
RT23_HUMANMRPS23physical
26186194
RT27_HUMANMRPS27physical
26186194
RT29_HUMANDAP3physical
26186194
RT18C_HUMANMRPS18Cphysical
26186194
RT07_HUMANMRPS7physical
26186194
RT22_HUMANMRPS22physical
26186194
RT15_HUMANMRPS15physical
26186194
RT25_HUMANMRPS25physical
26186194
RT33_HUMANMRPS33physical
26186194
RT11_HUMANMRPS11physical
26186194
RT24_HUMANMRPS24physical
26186194
RL17_HUMANRPL17physical
26344197
RT27_HUMANMRPS27physical
28514442
RT33_HUMANMRPS33physical
28514442
RT18C_HUMANMRPS18Cphysical
28514442
RT26_HUMANMRPS26physical
28514442
PTCD3_HUMANPTCD3physical
28514442
RT29_HUMANDAP3physical
28514442
RT23_HUMANMRPS23physical
28514442
RT09_HUMANMRPS9physical
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 RT05_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-312, AND MASSSPECTROMETRY.

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