RT17_HUMAN - dbPTM
RT17_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RT17_HUMAN
UniProt AC Q9Y2R5
Protein Name 28S ribosomal protein S17, mitochondrial
Gene Name MRPS17
Organism Homo sapiens (Human).
Sequence Length 130
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MSVVRSSVHARWIVGKVIGTKMQKTAKVRVTRLVLDPYLLKYFNKRKTYFAHDALQQCTVGDIVLLRALPVPRAKHVKHELAEIVFKVGKVIDPVTGKPCAGTTYLESPLSSETTQLSKNLEELNISSAQ
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
6Phosphorylation--MSVVRSSVHARWI
--CCCCCCHHHHHHH
25.7122617229
21AcetylationVGKVIGTKMQKTAKV
HHHHHCCCCHHCCCE
33.8325953088
21UbiquitinationVGKVIGTKMQKTAKV
HHHHHCCCCHHCCCE
33.8329967540
38PhosphorylationTRLVLDPYLLKYFNK
HHHHHCHHHHHHHCC
25.0821406692
41UbiquitinationVLDPYLLKYFNKRKT
HHCHHHHHHHCCCCC
45.2423000965
42PhosphorylationLDPYLLKYFNKRKTY
HCHHHHHHHCCCCCC
16.6229083192
45UbiquitinationYLLKYFNKRKTYFAH
HHHHHHCCCCCCCHH
45.4323000965
47UbiquitinationLKYFNKRKTYFAHDA
HHHHCCCCCCCHHHH
49.5423000965
48PhosphorylationKYFNKRKTYFAHDAL
HHHCCCCCCCHHHHH
28.0929496907
782-HydroxyisobutyrylationVPRAKHVKHELAEIV
CCCCHHHHHHHHHHH
30.95-
90UbiquitinationEIVFKVGKVIDPVTG
HHHHHHCCEECCCCC
38.7229967540
90AcetylationEIVFKVGKVIDPVTG
HHHHHHCCEECCCCC
38.7226051181
98UbiquitinationVIDPVTGKPCAGTTY
EECCCCCCCCCCCCE
27.7929967540
100GlutathionylationDPVTGKPCAGTTYLE
CCCCCCCCCCCCEEC
6.5922555962
108PhosphorylationAGTTYLESPLSSETT
CCCCEECCCCCCHHH
28.66-
111PhosphorylationTYLESPLSSETTQLS
CEECCCCCCHHHHHH
29.52-
127PhosphorylationNLEELNISSAQ----
HHHHHCCCCCC----
20.6730266825
128PhosphorylationLEELNISSAQ-----
HHHHCCCCCC-----
27.2230266825

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 RT17_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RT17_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 RT17_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIFA3_HUMANKIFAP3physical
27173435

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 RT17_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND MASSSPECTROMETRY.

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