RM46_HUMAN - dbPTM
RM46_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RM46_HUMAN
UniProt AC Q9H2W6
Protein Name 39S ribosomal protein L46, mitochondrial
Gene Name MRPL46
Organism Homo sapiens (Human).
Sequence Length 279
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MAAPVRRTLLGVAGGWRRFERLWAGSLSSRSLALAAAPSSNGSPWRLLGALCLQRPPVVSKPLTPLQEEMASLLQQIEIERSLYSDHELRALDENQRLAKKKADLHDEEDEQDILLAQDLEDMWEQKFLQFKLGARITEADEKNDRTSLNRKLDRNLVLLVREKFGDQDVWILPQAEWQPGETLRGTAERTLATLSENNMEAKFLGNAPCGHYTFKFPQAMRTESNLGAKVFFFKALLLTGDFSQAGNKGHHVWVTKDELGDYLKPKYLAQVRRFVSDL
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
8PhosphorylationMAAPVRRTLLGVAGG
CCCCHHHHHHHHHCC
18.77-
26PhosphorylationFERLWAGSLSSRSLA
HHHHHCCCCCCCHHH
19.8223025827
60PhosphorylationLQRPPVVSKPLTPLQ
CCCCCCCCCCCCHHH
28.8724719451
82PhosphorylationQQIEIERSLYSDHEL
HHHHHHHHCCCHHHH
20.9023186163
84PhosphorylationIEIERSLYSDHELRA
HHHHHHCCCHHHHHH
17.1925884760
85PhosphorylationEIERSLYSDHELRAL
HHHHHCCCHHHHHHH
37.4725003641
127UbiquitinationLEDMWEQKFLQFKLG
HHHHHHHHHHHHHHC
36.2122817900
132UbiquitinationEQKFLQFKLGARITE
HHHHHHHHHCCCCCC
32.8122817900
194PhosphorylationTAERTLATLSENNME
HHHHHHHHHCCCCCE
33.6522210691
200SulfoxidationATLSENNMEAKFLGN
HHHCCCCCEEEECCC
8.8121406390
203UbiquitinationSENNMEAKFLGNAPC
CCCCCEEEECCCCCC
28.0221890473
216AcetylationPCGHYTFKFPQAMRT
CCCCEEEECCCHHCC
48.6225953088
230UbiquitinationTESNLGAKVFFFKAL
CCCHHHCHHHHHHHH
37.4622817900
230AcetylationTESNLGAKVFFFKAL
CCCHHHCHHHHHHHH
37.4619608861
235UbiquitinationGAKVFFFKALLLTGD
HCHHHHHHHHHHHCC
32.7322817900
249MalonylationDFSQAGNKGHHVWVT
CHHHCCCCCCEEEEE
59.7226320211
263PhosphorylationTKDELGDYLKPKYLA
EHHHHHHHCCHHHHH
18.1520068231
265UbiquitinationDELGDYLKPKYLAQV
HHHHHHCCHHHHHHH
32.9819608861
265AcetylationDELGDYLKPKYLAQV
HHHHHHCCHHHHHHH
32.9823236377
267AcetylationLGDYLKPKYLAQVRR
HHHHCCHHHHHHHHH
51.8423236377
267MalonylationLGDYLKPKYLAQVRR
HHHHCCHHHHHHHHH
51.8426320211

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 RM46_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RM46_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 RM46_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPP1_HUMANATP6V0A1physical
22939629
RM48_HUMANMRPL48physical
26186194
RM40_HUMANMRPL40physical
26186194
ETFR1_HUMANLYRM5physical
26186194
RM55_HUMANMRPL55physical
26186194
MGME1_HUMANMGME1physical
26186194
ACPM_HUMANNDUFAB1physical
26186194
RM40_HUMANMRPL40physical
26344197
RM55_HUMANMRPL55physical
26344197
RM40_HUMANMRPL40physical
28514442
RM55_HUMANMRPL55physical
28514442
RM48_HUMANMRPL48physical
28514442
MGME1_HUMANMGME1physical
28514442
CGL_HUMANCTHphysical
28514442
ACPM_HUMANNDUFAB1physical
28514442

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 RM46_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-230 AND LYS-265, AND MASSSPECTROMETRY.

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