RM09_HUMAN - dbPTM
RM09_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RM09_HUMAN
UniProt AC Q9BYD2
Protein Name 39S ribosomal protein L9, mitochondrial
Gene Name MRPL9
Organism Homo sapiens (Human).
Sequence Length 267
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MAAPVVTAPGRALLRAGAGRLLRGGVQELLRPRHEGNAPDLACNFSLSQNRGTVIVERWWKVPLAGEGRKPRLHRRHRVYKLVEDTKHRPKENLELILTQSVENVGVRGDLVSVKKSLGRNRLLPQGLAVYASPENKKLFEEEKLLRQEGKLEKIQTKAGEATVKFLKSCRLEVGMKNNVKWELNPEIVARHFFKNLGVVVAPHTLKLPEEPITRWGEYWCEVTVNGLDTVRVPMSVVNFEKPKTKRYKYWLAQQAAKAMAPTSPQI
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
80PhosphorylationLHRRHRVYKLVEDTK
HHHHHHHHHHHHCCC
9.88-
81AcetylationHRRHRVYKLVEDTKH
HHHHHHHHHHHCCCC
43.1027452117
99PhosphorylationENLELILTQSVENVG
HHHEEEEEECCCCCC
16.2920068231
101PhosphorylationLELILTQSVENVGVR
HEEEEEECCCCCCCC
26.6020068231
131PhosphorylationLPQGLAVYASPENKK
CCCCEEEEECHHHHH
8.8526852163
133PhosphorylationQGLAVYASPENKKLF
CCEEEEECHHHHHHH
18.3028674419
144UbiquitinationKKLFEEEKLLRQEGK
HHHHHHHHHHHHHCC
56.98-
154UbiquitinationRQEGKLEKIQTKAGE
HHHCCHHHHHHHHHH
51.02-
154AcetylationRQEGKLEKIQTKAGE
HHHCCHHHHHHHHHH
51.0228640981
157PhosphorylationGKLEKIQTKAGEATV
CCHHHHHHHHHHHHH
26.7429396449
158AcetylationKLEKIQTKAGEATVK
CHHHHHHHHHHHHHH
37.7120167786
163PhosphorylationQTKAGEATVKFLKSC
HHHHHHHHHHHHHHC
21.6729396449
165AcetylationKAGEATVKFLKSCRL
HHHHHHHHHHHHCCC
40.3925953088
177AcetylationCRLEVGMKNNVKWEL
CCCEECCCCCCCEEC
39.1720167786
205PhosphorylationGVVVAPHTLKLPEEP
CEEECCCCCCCCCCC
25.2421406692
263PhosphorylationAAKAMAPTSPQI---
HHHHHCCCCCCC---
43.4330266825
264PhosphorylationAKAMAPTSPQI----
HHHHCCCCCCC----
17.4730266825

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 RM09_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RM09_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 RM09_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RM15_HUMANMRPL15physical
22939629
RM37_HUMANMRPL37physical
22939629
RM44_HUMANMRPL44physical
22939629
RM39_HUMANMRPL39physical
22939629
RM38_HUMANMRPL38physical
22939629
RM19_HUMANMRPL19physical
22939629
RM40_HUMANMRPL40physical
22939629
RM55_HUMANMRPL55physical
22939629
RM11_HUMANMRPL11physical
22939629
RM13_HUMANMRPL13physical
22939629
RM32_HUMANMRPL32physical
22939629
RM23_HUMANMRPL23physical
22939629
RM12_HUMANMRPL12physical
22939629
RM28_HUMANMRPL28physical
22939629
TM177_HUMANTMEM177physical
22939629
SAT1_HUMANSAT1physical
19060904
FAM9B_HUMANFAM9Bphysical
25416956
LYAG_HUMANGAAphysical
26344197
RM17_HUMANMRPL17physical
26344197
RM18_HUMANMRPL18physical
26344197
RM28_HUMANMRPL28physical
26344197
RM38_HUMANMRPL38physical
26344197
RM39_HUMANMRPL39physical
26344197
RM46_HUMANMRPL46physical
26344197
RM47_HUMANMRPL47physical
26344197
RM48_HUMANMRPL48physical
26344197
PLBL2_HUMANPLBD2physical
26344197
RM49_HUMANMRPL49physical
26496610
DIC_HUMANSLC25A10physical
26496610
IF4G1_HUMANEIF4G1physical
26496610
ICT1_HUMANICT1physical
26496610
PLAK_HUMANJUPphysical
26496610
RM23_HUMANMRPL23physical
26496610
RM12_HUMANMRPL12physical
26496610
KITM_HUMANTK2physical
26496610
RM33_HUMANMRPL33physical
26496610
RM19_HUMANMRPL19physical
26496610
RM28_HUMANMRPL28physical
26496610
RT30_HUMANMRPS30physical
26496610
RM03_HUMANMRPL3physical
26496610
RM46_HUMANMRPL46physical
26496610
RM42_HUMANMRPL42physical
26496610
RM13_HUMANMRPL13physical
26496610
RM18_HUMANMRPL18physical
26496610
RM15_HUMANMRPL15physical
26496610
RM22_HUMANMRPL22physical
26496610
ITSN2_HUMANITSN2physical
26496610
RM02_HUMANMRPL2physical
26496610
RM04_HUMANMRPL4physical
26496610
RM37_HUMANMRPL37physical
26496610
RM51_HUMANMRPL51physical
26496610
RM30_HUMANMRPL30physical
26496610
RM27_HUMANMRPL27physical
26496610
RM35_HUMANMRPL35physical
26496610
RM48_HUMANMRPL48physical
26496610
RM39_HUMANMRPL39physical
26496610
RM50_HUMANMRPL50physical
26496610
RM16_HUMANMRPL16physical
26496610
RM20_HUMANMRPL20physical
26496610
RT18A_HUMANMRPS18Aphysical
26496610
RM47_HUMANMRPL47physical
26496610
NEUL_HUMANNLNphysical
26496610
RM17_HUMANMRPL17physical
26496610
RM14_HUMANMRPL14physical
26496610
RM41_HUMANMRPL41physical
26496610
RM40_HUMANMRPL40physical
26496610
RM38_HUMANMRPL38physical
26496610
RM34_HUMANMRPL34physical
26496610
RM32_HUMANMRPL32physical
26496610
RM01_HUMANMRPL1physical
26496610
RM44_HUMANMRPL44physical
26496610
RM24_HUMANMRPL24physical
26496610
THAP9_HUMANTHAP9physical
26496610
RM43_HUMANMRPL43physical
26496610
MILK1_HUMANMICALL1physical
26496610
G45IP_HUMANGADD45GIP1physical
26496610
RM53_HUMANMRPL53physical
26496610
RM54_HUMANMRPL54physical
26496610
RM52_HUMANMRPL52physical
26496610
RM10_HUMANMRPL10physical
26496610
TMM92_HUMANTMEM92physical
26496610
RM21_HUMANMRPL21physical
26496610

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 RM09_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND MASSSPECTROMETRY.

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