RM53_HUMAN - dbPTM
RM53_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RM53_HUMAN
UniProt AC Q96EL3
Protein Name 39S ribosomal protein L53, mitochondrial
Gene Name MRPL53
Organism Homo sapiens (Human).
Sequence Length 112
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MAAALARLGLRPVKQVRVQFCPFEKNVESTRTFLQTVSSEKVRSTNLNCSVIADVRHDGSEPCVDVLFGDGHRLIMRGAHLTALEMLTAFASHIRARDAAGSGDKPGADTGR
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------MAAALARLG
------CHHHHHHCC
11.05-
14MalonylationRLGLRPVKQVRVQFC
HCCCCCCCEEEEEEC
45.8432601280
21S-nitrosocysteineKQVRVQFCPFEKNVE
CEEEEEECCCCCCHH
1.79-
21S-nitrosylationKQVRVQFCPFEKNVE
CEEEEEECCCCCCHH
1.7919483679
25AcetylationVQFCPFEKNVESTRT
EEECCCCCCHHHHHH
67.6726051181
252-HydroxyisobutyrylationVQFCPFEKNVESTRT
EEECCCCCCHHHHHH
67.67-
29PhosphorylationPFEKNVESTRTFLQT
CCCCCHHHHHHHHHH
20.9326074081
30PhosphorylationFEKNVESTRTFLQTV
CCCCHHHHHHHHHHH
21.8826074081
32PhosphorylationKNVESTRTFLQTVSS
CCHHHHHHHHHHHCC
28.8726074081
36PhosphorylationSTRTFLQTVSSEKVR
HHHHHHHHHCCHHHH
25.2226074081
38PhosphorylationRTFLQTVSSEKVRST
HHHHHHHCCHHHHHC
35.8526074081
39PhosphorylationTFLQTVSSEKVRSTN
HHHHHHCCHHHHHCC
36.7826074081
41UbiquitinationLQTVSSEKVRSTNLN
HHHHCCHHHHHCCCC
44.9133845483
412-HydroxyisobutyrylationLQTVSSEKVRSTNLN
HHHHCCHHHHHCCCC
44.91-
44PhosphorylationVSSEKVRSTNLNCSV
HCCHHHHHCCCCCEE
25.3226074081
45PhosphorylationSSEKVRSTNLNCSVI
CCHHHHHCCCCCEEE
32.9126074081
49GlutathionylationVRSTNLNCSVIADVR
HHHCCCCCEEEEEEC
3.7622555962
50PhosphorylationRSTNLNCSVIADVRH
HHCCCCCEEEEEECC
18.5826074081
63GlutathionylationRHDGSEPCVDVLFGD
CCCCCCCEEEEEECC
3.4222555962
82PhosphorylationIMRGAHLTALEMLTA
HHHHHHHHHHHHHHH
21.2320068231
88PhosphorylationLTALEMLTAFASHIR
HHHHHHHHHHHHHHH
20.5820068231
92PhosphorylationEMLTAFASHIRARDA
HHHHHHHHHHHHHHC
17.0020068231
102PhosphorylationRARDAAGSGDKPGAD
HHHHCCCCCCCCCCC
38.8120068231
105UbiquitinationDAAGSGDKPGADTGR
HCCCCCCCCCCCCCC
49.2124816145
105AcetylationDAAGSGDKPGADTGR
HCCCCCCCCCCCCCC
49.2125953088
110PhosphorylationGDKPGADTGR-----
CCCCCCCCCC-----
34.0320068231

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 RM53_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RM53_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 RM53_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
RT28_HUMANMRPS28physical
22939629
RRFM_HUMANMRRFphysical
22939629
SPRE_HUMANSPRphysical
22939629
UBL4A_HUMANUBL4Aphysical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
SUGP1_HUMANSUGP1physical
22939629
SOSB1_HUMANNABP2physical
22939629
RS19_HUMANRPS19physical
22939629
SNX3_HUMANSNX3physical
22939629
MPLKI_HUMANMPLKIPphysical
22939629
RRBP1_HUMANRRBP1physical
22939629
RS28_HUMANRPS28physical
22939629
RU1C_HUMANSNRPCphysical
22939629
STX7_HUMANSTX7physical
22939629
TAGL_HUMANTAGLNphysical
22939629
TIM44_HUMANTIMM44physical
22939629
UBC9_HUMANUBE2Iphysical
22939629
THIK_HUMANACAA1physical
22939629
RIDA_HUMANHRSP12physical
22939629
TPX2_HUMANTPX2physical
22939629
UBE4B_HUMANUBE4Bphysical
22939629
SCO2_HUMANSCO2physical
22939629
UB2L3_HUMANUBE2L3physical
22939629
VDAC3_HUMANVDAC3physical
22939629
SBDS_HUMANSBDSphysical
22939629
TBL2_HUMANTBL2physical
22939629
TIAR_HUMANTIAL1physical
22939629
THY1_HUMANTHY1physical
22939629
ADIP_HUMANSSX2IPphysical
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 RM53_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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