RM02_HUMAN - dbPTM
RM02_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RM02_HUMAN
UniProt AC Q5T653
Protein Name 39S ribosomal protein L2, mitochondrial
Gene Name MRPL2
Organism Homo sapiens (Human).
Sequence Length 305
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MALCALTRALRSLNLAPPTVAAPAPSLFPAAQMMNNGLLQQPSALMLLPCRPVLTSVALNANFVSWKSRTKYTITPVKMRKSGGRDHTGRIRVHGIGGGHKQRYRMIDFLRFRPEETKSGPFEEKVIQVRYDPCRSADIALVAGGSRKRWIIATENMQAGDTILNSNHIGRMAVAAREGDAHPLGALPVGTLINNVESEPGRGAQYIRAAGTCGVLLRKVNGTAIIQLPSKRQMQVLETCVATVGRVSNVDHNKRVIGKAGRNRWLGKRPNSGRWHRKGGWAGRKIRPLPPMKSYVKLPSASAQS
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
7Phosphorylation-MALCALTRALRSLN
-CHHHHHHHHHHHCC
8.7229759185
71UbiquitinationVSWKSRTKYTITPVK
CCCCCCCCEEEEEEE
39.01-
72PhosphorylationSWKSRTKYTITPVKM
CCCCCCCEEEEEEEE
11.63-
78AcetylationKYTITPVKMRKSGGR
CEEEEEEEEECCCCC
33.9020167786
78UbiquitinationKYTITPVKMRKSGGR
CEEEEEEEEECCCCC
33.90-
106SulfoxidationGHKQRYRMIDFLRFR
CCHHHEEEEEEEECC
2.2721406390
117PhosphorylationLRFRPEETKSGPFEE
EECCCCHHCCCCCCC
28.9321406692
118UbiquitinationRFRPEETKSGPFEEK
ECCCCHHCCCCCCCC
57.612190698
119PhosphorylationFRPEETKSGPFEEKV
CCCCHHCCCCCCCCE
60.1521406692
146PhosphorylationIALVAGGSRKRWIIA
EEEEECCCCCEEEEE
33.4430108239
223PhosphorylationLLRKVNGTAIIQLPS
EEEEECCEEEEECCC
14.96-
230PhosphorylationTAIIQLPSKRQMQVL
EEEEECCCHHHHHHH
49.4124719451
239PhosphorylationRQMQVLETCVATVGR
HHHHHHHHHHHHHCC
14.23-
248PhosphorylationVATVGRVSNVDHNKR
HHHHCCEECCCCCCC
29.7627251275
2542-HydroxyisobutyrylationVSNVDHNKRVIGKAG
EECCCCCCCEECCCC
44.62-
272PhosphorylationWLGKRPNSGRWHRKG
CCCCCCCCCCCCCCC
32.20-
293UbiquitinationIRPLPPMKSYVKLPS
CCCCCCCCCEEECCC
44.39-
297SumoylationPPMKSYVKLPSASAQ
CCCCCEEECCCCCCC
46.58-
297UbiquitinationPPMKSYVKLPSASAQ
CCCCCEEECCCCCCC
46.58-
297SumoylationPPMKSYVKLPSASAQ
CCCCCEEECCCCCCC
46.58-

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 RM02_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RM02_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 RM02_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RM11_HUMANMRPL11physical
22939629
RM09_HUMANMRPL9physical
22939629
RM37_HUMANMRPL37physical
22939629
RM04_HUMANMRPL4physical
22939629
RM23_HUMANMRPL23physical
22939629
RM14_HUMANMRPL14physical
22939629
RM24_HUMANMRPL24physical
22939629
RM40_HUMANMRPL40physical
22939629
RM13_HUMANMRPL13physical
22939629
RM16_HUMANMRPL16physical
22939629
RS18_HUMANRPS18physical
22939629
RS15_HUMANRPS15physical
22939629
RRF2M_HUMANGFM2physical
26344197
NOG1_HUMANGTPBP4physical
26344197
RM13_HUMANMRPL13physical
26344197
RM17_HUMANMRPL17physical
26344197
RM24_HUMANMRPL24physical
26344197
RM39_HUMANMRPL39physical
26344197
RM47_HUMANMRPL47physical
26344197
RM09_HUMANMRPL9physical
26344197
RT07_HUMANMRPS7physical
26344197
PHB2_HUMANPHB2physical
26344197
RPC1_HUMANPOLR3Aphysical
26344197
EFTU_HUMANTUFMphysical
26344197

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 RM02_HUMAN

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Related Literatures of Post-Translational Modification

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