RT23_HUMAN - dbPTM
RT23_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RT23_HUMAN
UniProt AC Q9Y3D9
Protein Name 28S ribosomal protein S23, mitochondrial
Gene Name MRPS23
Organism Homo sapiens (Human).
Sequence Length 190
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MAGSRLETVGSIFSRTRDLVRAGVLKEKPLWFDVYDAFPPLREPVFQRPRVRYGKAKAPIQDIWYHEDRIRAKFYSVYGSGQRAFDLFNPNFKSTCQRFVEKYTELQKLGETDEEKLFVETGKALLAEGVILRRVGEARTQHGGSHVSRKSEHLSVRPQTALEENETQKEVPQDQHLEAPADQSKGLLPP
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
2Acetylation------MAGSRLETV
------CCCCCCCCH
25.3525944712
8PhosphorylationMAGSRLETVGSIFSR
CCCCCCCCHHHHHHH
34.4623403867
11PhosphorylationSRLETVGSIFSRTRD
CCCCCHHHHHHHHHH
19.0024043423
14PhosphorylationETVGSIFSRTRDLVR
CCHHHHHHHHHHHHH
30.9523403867
16PhosphorylationVGSIFSRTRDLVRAG
HHHHHHHHHHHHHCC
27.6024043423
21MethylationSRTRDLVRAGVLKEK
HHHHHHHHCCCCCCC
32.6816187653
55UbiquitinationRPRVRYGKAKAPIQD
CCCCHHCCCCCCHHH
37.4722817900
57UbiquitinationRVRYGKAKAPIQDIW
CCHHCCCCCCHHHCE
59.1721890473
57MalonylationRVRYGKAKAPIQDIW
CCHHCCCCCCHHHCE
59.1733225896
65PhosphorylationAPIQDIWYHEDRIRA
CCHHHCEECHHHHHH
8.82-
73UbiquitinationHEDRIRAKFYSVYGS
CHHHHHHEEEEECCC
34.68-
73AcetylationHEDRIRAKFYSVYGS
CHHHHHHEEEEECCC
34.6823954790
73MalonylationHEDRIRAKFYSVYGS
CHHHHHHEEEEECCC
34.6826320211
78PhosphorylationRAKFYSVYGSGQRAF
HHEEEEECCCCCHHH
10.3028152594
80PhosphorylationKFYSVYGSGQRAFDL
EEEEECCCCCHHHHC
17.6728152594
93SuccinylationDLFNPNFKSTCQRFV
HCCCCCHHHHHHHHH
52.0423954790
93UbiquitinationDLFNPNFKSTCQRFV
HCCCCCHHHHHHHHH
52.04-
93AcetylationDLFNPNFKSTCQRFV
HCCCCCHHHHHHHHH
52.0425953088
102AcetylationTCQRFVEKYTELQKL
HHHHHHHHHHHHHHC
52.7719608861
1022-HydroxyisobutyrylationTCQRFVEKYTELQKL
HHHHHHHHHHHHHHC
52.77-
108AcetylationEKYTELQKLGETDEE
HHHHHHHHCCCCCHH
71.7023236377
108UbiquitinationEKYTELQKLGETDEE
HHHHHHHHCCCCCHH
71.7022817900
112PhosphorylationELQKLGETDEEKLFV
HHHHCCCCCHHHHHH
47.0829396449
116AcetylationLGETDEEKLFVETGK
CCCCCHHHHHHHHHH
45.2225953088
145PhosphorylationARTQHGGSHVSRKSE
HHHCCCCCCCCCCCC
25.8820860994

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 RT23_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RT23_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 RT23_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RT27_HUMANMRPS27physical
22939629
SYQ_HUMANQARSphysical
22939629
USBP1_HUMANUSHBP1physical
25416956

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 RT23_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-102, AND MASS SPECTROMETRY.

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