RT09_HUMAN - dbPTM
RT09_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RT09_HUMAN
UniProt AC P82933
Protein Name 28S ribosomal protein S9, mitochondrial
Gene Name MRPS9
Organism Homo sapiens (Human).
Sequence Length 396
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MAAPCVSYGGAVSYRLLLWGRGSLARKQGLWKTAAPELQTNVRSQILRLRHTAFVIPKKNVPTSKRETYTEDFIKKQIEEFNIGKRHLANMMGEDPETFTQEDIDRAIAYLFPSGLFEKRARPVMKHPEQIFPRQRAIQWGEDGRPFHYLFYTGKQSYYSLMHDVYGMLLNLEKHQSHLQAKSLLPEKTVTRDVIGSRWLIKEELEEMLVEKLSDLDYMQFIRLLEKLLTSQCGAAEEEFVQRFRRSVTLESKKQLIEPVQYDEQGMAFSKSEGKRKTAKAEAIVYKHGSGRIKVNGIDYQLYFPITQDREQLMFPFHFVDRLGKHDVTCTVSGGGRSAQAGAIRLAMAKALCSFVTEDEVEWMRQAGLLTTDPRVRERKKPGQEGARRKFTWKKR
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
7Phosphorylation-MAAPCVSYGGAVSY
-CCCCCCCCCCHHHH		25.4424719451
8PhosphorylationMAAPCVSYGGAVSYR
CCCCCCCCCCHHHHH		10.1224719451
13PhosphorylationVSYGGAVSYRLLLWG
CCCCCHHHHHHHHCC		12.1924719451
33PhosphorylationRKQGLWKTAAPELQT
HHCCCHHHCCHHHHH		19.2322210691
52PhosphorylationQILRLRHTAFVIPKK
HHHHHHHEEEEEECC		18.50-
64UbiquitinationPKKNVPTSKRETYTE
ECCCCCCCCCCCCCH		24.5227667366
68PhosphorylationVPTSKRETYTEDFIK
CCCCCCCCCCHHHHH		39.5129083192
69PhosphorylationPTSKRETYTEDFIKK
CCCCCCCCCHHHHHH		11.9029083192
70PhosphorylationTSKRETYTEDFIKKQ
CCCCCCCCHHHHHHH		36.1829083192
75UbiquitinationTYTEDFIKKQIEEFN
CCCHHHHHHHHHHCC		38.3229967540
76UbiquitinationYTEDFIKKQIEEFNI
CCHHHHHHHHHHCCC		52.2529967540
85AcetylationIEEFNIGKRHLANMM
HHHCCCCHHHHHHHC		32.6125953088
85SuccinylationIEEFNIGKRHLANMM
HHHCCCCHHHHHHHC		32.6123954790
85UbiquitinationIEEFNIGKRHLANMM
HHHCCCCHHHHHHHC		32.6122817900
98PhosphorylationMMGEDPETFTQEDID
HCCCCCCCCCHHHHH		37.0521406692
100PhosphorylationGEDPETFTQEDIDRA
CCCCCCCCHHHHHHH		38.1721406692
110PhosphorylationDIDRAIAYLFPSGLF
HHHHHHHHHCCCCHH		11.6321406692
114PhosphorylationAIAYLFPSGLFEKRA
HHHHHCCCCHHHHCC		40.5721406692
1192-HydroxyisobutyrylationFPSGLFEKRARPVMK
CCCCHHHHCCCCCCC		43.98-
119UbiquitinationFPSGLFEKRARPVMK
CCCCHHHHCCCCCCC		43.9823000965
126UbiquitinationKRARPVMKHPEQIFP
HCCCCCCCCHHHHCC		57.1323503661
129UbiquitinationRPVMKHPEQIFPRQR
CCCCCCHHHHCCHHH		56.9022817900
130UbiquitinationPVMKHPEQIFPRQRA
CCCCCHHHHCCHHHH		47.2622817900
147UbiquitinationWGEDGRPFHYLFYTG
CCCCCCEEEEEEECC		5.9522817900
151UbiquitinationGRPFHYLFYTGKQSY
CCEEEEEEECCCHHH		3.9622817900
153UbiquitinationPFHYLFYTGKQSYYS
EEEEEEECCCHHHHH		30.4823503661
157PhosphorylationLFYTGKQSYYSLMHD
EEECCCHHHHHHHHH		29.5328122231
158PhosphorylationFYTGKQSYYSLMHDV
EECCCHHHHHHHHHH		8.4528122231
159PhosphorylationYTGKQSYYSLMHDVY
ECCCHHHHHHHHHHH		10.6928122231
160PhosphorylationTGKQSYYSLMHDVYG
CCCHHHHHHHHHHHH		15.8128122231
166PhosphorylationYSLMHDVYGMLLNLE
HHHHHHHHHHHHCHH		11.6828122231
1822-HydroxyisobutyrylationHQSHLQAKSLLPEKT
HHHHHHHHHCCCCCC		28.77-
182UbiquitinationHQSHLQAKSLLPEKT
HHHHHHHHHCCCCCC		28.7729967540
183PhosphorylationQSHLQAKSLLPEKTV
HHHHHHHHCCCCCCC		37.8520860994
188UbiquitinationAKSLLPEKTVTRDVI
HHHCCCCCCCCHHHH		46.4827667366
201UbiquitinationVIGSRWLIKEELEEM
HHCCCHHHHHHHHHH		4.1327667366
214PhosphorylationEMLVEKLSDLDYMQF
HHHHHHHCCCCHHHH		47.3920068231
218PhosphorylationEKLSDLDYMQFIRLL
HHHCCCCHHHHHHHH		10.50-
227AcetylationQFIRLLEKLLTSQCG
HHHHHHHHHHHCCCC		49.0926051181
2272-HydroxyisobutyrylationQFIRLLEKLLTSQCG
HHHHHHHHHHHCCCC		49.09-
247PhosphorylationFVQRFRRSVTLESKK
HHHHHHHHCCHHHHH		18.3928348404
249O-linked_GlycosylationQRFRRSVTLESKKQL
HHHHHHCCHHHHHHH		26.5030379171
249PhosphorylationQRFRRSVTLESKKQL
HHHHHHCCHHHHHHH		26.5028509920
252PhosphorylationRRSVTLESKKQLIEP
HHHCCHHHHHHHCCC		48.5428509920
2532-HydroxyisobutyrylationRSVTLESKKQLIEPV
HHCCHHHHHHHCCCE		34.85-
253UbiquitinationRSVTLESKKQLIEPV
HHCCHHHHHHHCCCE		34.8522817900
254UbiquitinationSVTLESKKQLIEPVQ
HCCHHHHHHHCCCEE		60.6621906983
262PhosphorylationQLIEPVQYDEQGMAF
HHCCCEEECCCCCCC		22.9822817900
271UbiquitinationEQGMAFSKSEGKRKT
CCCCCCCCCCCCCCC		46.1821906983
275UbiquitinationAFSKSEGKRKTAKAE
CCCCCCCCCCCCCEE		46.8222817900
277UbiquitinationSKSEGKRKTAKAEAI
CCCCCCCCCCCEEEE		57.2123503661
280MalonylationEGKRKTAKAEAIVYK
CCCCCCCCEEEEEEE		52.5732601280
280UbiquitinationEGKRKTAKAEAIVYK
CCCCCCCCEEEEEEE		52.5729967540
287UbiquitinationKAEAIVYKHGSGRIK
CEEEEEEECCCCEEE		30.5119608861
287SuccinylationKAEAIVYKHGSGRIK
CEEEEEEECCCCEEE		30.5127452117
287AcetylationKAEAIVYKHGSGRIK
CEEEEEEECCCCEEE		30.5119608861
325AcetylationHFVDRLGKHDVTCTV
HHHHCCCCCCEEEEE		41.0225825284
325MalonylationHFVDRLGKHDVTCTV
HHHHCCCCCCEEEEE		41.0226320211
325UbiquitinationHFVDRLGKHDVTCTV
HHHHCCCCCCEEEEE		41.0227667366
330S-nitrosocysteineLGKHDVTCTVSGGGR
CCCCCEEEEEECCCH		3.39-
330S-nitrosylationLGKHDVTCTVSGGGR
CCCCCEEEEEECCCH		3.3919483679
353GlutathionylationLAMAKALCSFVTEDE
HHHHHHHHCCCCHHH		3.3822555962
380AcetylationDPRVRERKKPGQEGA
CHHHHHCCCCCCCCC		59.5730590479
392PhosphorylationEGARRKFTWKKR---
CCCCCCCCCCCC---		39.13-
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 RT09_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RT09_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 RT09_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAP1_HUMANHAP1physical
16169070
RT25_HUMANMRPS25physical
22939629
RT16_HUMANMRPS16physical
22939629
RT28_HUMANMRPS28physical
22939629
RT18B_HUMANMRPS18Bphysical
22939629
RT26_HUMANMRPS26physical
22939629
RT21_HUMANMRPS21physical
22939629
RT16_HUMANMRPS16physical
26344197
RT18B_HUMANMRPS18Bphysical
26344197
RT22_HUMANMRPS22physical
26344197
RT23_HUMANMRPS23physical
26344197
PSA4_HUMANPSMA4physical
26344197
PSA5_HUMANPSMA5physical
26344197
PSB2_HUMANPSMB2physical
26344197
PSB8_HUMANPSMB8physical
26344197
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 RT09_HUMAN

loading...

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-287, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-262, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory