RT16_HUMAN - dbPTM
RT16_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RT16_HUMAN
UniProt AC Q9Y3D3
Protein Name 28S ribosomal protein S16, mitochondrial
Gene Name MRPS16
Organism Homo sapiens (Human).
Sequence Length 137
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MVHLTTLLCKAYRGGHLTIRLALGGCTNRPFYRIVAAHNKCPRDGRFVEQLGSYDPLPNSHGEKLVALNLDRIRHWIGCGAHLSKPMEKLLGLAGFFPLHPMMITNAERLRRKRAREVLLASQKTDAEATDTEATET
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
13MethylationTLLCKAYRGGHLTIR
HHHHHHHCCCCEEEE
49.86115483803
40UbiquitinationRIVAAHNKCPRDGRF
HHHHCCCCCCCCCCH
35.4324816145
64UbiquitinationLPNSHGEKLVALNLD
CCCCCCCCEEEECHH
53.5022817900
64UbiquitinationLPNSHGEKLVALNLD
CCCCCCCCEEEECHH
53.5021890473
64AcetylationLPNSHGEKLVALNLD
CCCCCCCCEEEECHH
53.5026051181
72MethylationLVALNLDRIRHWIGC
EEEECHHHHHHHHCC
30.89115483811
85MalonylationGCGAHLSKPMEKLLG
CCCHHHCHHHHHHHH
55.5326320211
85AcetylationGCGAHLSKPMEKLLG
CCCHHHCHHHHHHHH
55.5326051181
122PhosphorylationAREVLLASQKTDAEA
HHHHHHHHCCCCCCC
31.9822210691
125PhosphorylationVLLASQKTDAEATDT
HHHHHCCCCCCCCCC
32.5728176443
130PhosphorylationQKTDAEATDTEATET
CCCCCCCCCCCCCCC
34.6530278072
132PhosphorylationTDAEATDTEATET--
CCCCCCCCCCCCC--
24.1430278072
135PhosphorylationEATDTEATET-----
CCCCCCCCCC-----
33.6528176443
137PhosphorylationTDTEATET-------
CCCCCCCC-------
39.2924732914

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 RT16_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RT16_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 RT16_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT26_HUMANMRPS26physical
22939629
RT25_HUMANMRPS25physical
22939629
SSBP_HUMANSSBP1physical
22939629

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610498Combined oxidative phosphorylation deficiency 2 (COXPD2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RT16_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND MASSSPECTROMETRY.
"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-130, AND MASSSPECTROMETRY.

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