MRM3_HUMAN - dbPTM
MRM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MRM3_HUMAN
UniProt AC Q9HC36
Protein Name rRNA methyltransferase 3, mitochondrial {ECO:0000303|PubMed:25009282}
Gene Name MRM3 {ECO:0000303|PubMed:25009282, ECO:0000312|HGNC:HGNC:18485}
Organism Homo sapiens (Human).
Sequence Length 420
Subcellular Localization Mitochondrion .
Protein Description S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1370 (Gm1370) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a conserved modification in the peptidyl transferase domain of the mtLSU rRNA..
Protein Sequence MAALVRPARFVVRPLLQVVQAWDLDARRWVRALRRSPVKVVFPSGEVVEQKRAPGKQPRKAPSEASAQEQREKQPLEESASRAPSTWEESGLRYDKAYPGDRRLSSVMTIVKSRPFREKQGKILLEGRRLISDALKAGAVPKMFFFSRLEYLKELPVDKLKGVSLIKVKFEDIKDWSDLVTPQGIMGIFAKPDHVKMTYPKTQLQHSLPLLLICDNLRDPGNLGTILRSAAGAGCSKVLLTKGCVDAWEPKVLRAGMGAHFRMPIINNLEWETVPNYLPPDTRVYVADNCGLYAQAEMSNKASDHGWVCDQRVMKFHKYEEEEDVETGASQDWLPHVEVQSYDSDWTEAPAAVVIGGETYGVSLESLQLAESTGGKRLLIPVVPGVDSLNSAMAASILLFEGKRQLRGRAEDLSRDRSYH
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
56UbiquitinationEQKRAPGKQPRKAPS
EECCCCCCCCCCCCC
27667366
60UbiquitinationAPGKQPRKAPSEASA
CCCCCCCCCCCHHHH
24816145
66PhosphorylationRKAPSEASAQEQREK
CCCCCHHHHHHHHHH
24719451
79PhosphorylationEKQPLEESASRAPST
HHCCHHHHHHCCCCC
24719451
81PhosphorylationQPLEESASRAPSTWE
CCHHHHHHCCCCCHH
28634298
86PhosphorylationSASRAPSTWEESGLR
HHHCCCCCHHHHCCC
28152594
90PhosphorylationAPSTWEESGLRYDKA
CCCCHHHHCCCCCCC
28152594
94PhosphorylationWEESGLRYDKAYPGD
HHHHCCCCCCCCCCC
28152594
96UbiquitinationESGLRYDKAYPGDRR
HHCCCCCCCCCCCCC
24816145
98PhosphorylationGLRYDKAYPGDRRLS
CCCCCCCCCCCCCHH
28152594
105PhosphorylationYPGDRRLSSVMTIVK
CCCCCCHHHHHHHEE
21406692
106PhosphorylationPGDRRLSSVMTIVKS
CCCCCHHHHHHHEEC
21406692
109PhosphorylationRRLSSVMTIVKSRPF
CCHHHHHHHEECCCC
21406692
113PhosphorylationSVMTIVKSRPFREKQ
HHHHHEECCCCHHHC
21406692
119UbiquitinationKSRPFREKQGKILLE
ECCCCHHHCCCEEEE
24816145
1532-HydroxyisobutyrylationFSRLEYLKELPVDKL
HHHHHHHHHCCCCCC
-
153AcetylationFSRLEYLKELPVDKL
HHHHHHHHHCCCCCC
23236377
153SuccinylationFSRLEYLKELPVDKL
HHHHHHHHHCCCCCC
27452117
1592-HydroxyisobutyrylationLKELPVDKLKGVSLI
HHHCCCCCCCCCEEE
-
161UbiquitinationELPVDKLKGVSLIKV
HCCCCCCCCCEEEEE
27667366
164PhosphorylationVDKLKGVSLIKVKFE
CCCCCCCEEEEEEHH
24719451
167MalonylationLKGVSLIKVKFEDIK
CCCCEEEEEEHHHCC
26320211
181O-linked_GlycosylationKDWSDLVTPQGIMGI
CCHHHCCCCCCEEEE
30379171
237AcetylationAAGAGCSKVLLTKGC
HCCCCCCEEEEECCC
26051181
237SuccinylationAAGAGCSKVLLTKGC
HCCCCCCEEEEECCC
27452117
237UbiquitinationAAGAGCSKVLLTKGC
HCCCCCCEEEEECCC
29967540
2372-HydroxyisobutyrylationAAGAGCSKVLLTKGC
HCCCCCCEEEEECCC
-
242UbiquitinationCSKVLLTKGCVDAWE
CCEEEEECCCHHCCC
29967540
251AcetylationCVDAWEPKVLRAGMG
CHHCCCHHHHHCCCC
26051181
414PhosphorylationRGRAEDLSRDRSYH-
CCCHHHHHCCCCCC-
27966365

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 MRM3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MRM3_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 MRM3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
RT30_HUMANMRPS30physical
22939629
RUSD4_HUMANRPUSD4physical
22939629
RT07_HUMANMRPS7physical
22939629
MPPB_HUMANPMPCBphysical
26186194
SPT2_HUMANSPTY2D1physical
26186194
ZN131_HUMANZNF131physical
28514442
UHRF1_HUMANUHRF1physical
28514442
ATPF2_HUMANATPAF2physical
28514442
MPPA_HUMANPMPCAphysical
28514442
NDUS6_HUMANNDUFS6physical
28514442
MPPB_HUMANPMPCBphysical
28514442
SC24B_HUMANSEC24Bphysical
28514442
CPT2_HUMANCPT2physical
28514442
PTER_HUMANPTERphysical
28514442
IF2M_HUMANMTIF2physical
28514442
NDUF7_HUMANNDUFAF7physical
28514442
KLH42_HUMANKLHL42physical
28514442
RLA0_HUMANRPLP0physical
28514442
MASU1_HUMANMALSU1physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MRM3_HUMAN

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Related Literatures of Post-Translational Modification

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