RM39_HUMAN - dbPTM
RM39_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RM39_HUMAN
UniProt AC Q9NYK5
Protein Name 39S ribosomal protein L39, mitochondrial
Gene Name MRPL39
Organism Homo sapiens (Human).
Sequence Length 338
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MEALAMGSRALRLWLVAPGGGIKWRFIATSSASQLSPTELTEMRNDLFNKEKARQLSLTPRTEKIEVKHVGKTDPGTVFVMNKNISTPYSCAMHLSEWYCRKSILALVDGQPWDMYKPLTKSCEIKFLTFKDCDPGEVNKAYWRSCAMMMGCVIERAFKDEYMVNLVRAPEVPVISGAFCYDVVLDSKLDEWMPTKENLRSFTKDAHALIYKDLPFETLEVEAKVALEIFQHSKYKVDFIEEKASQNPERIVKLHRIGDFIDVSEGPLIPRTSICFQYEVSAVHNLQPTQPSLIRRFQGVSLPVHLRAHFTIWDKLLERSRKMVTEDQSKATEECTST
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
8UbiquitinationMEALAMGSRALRLWL
CCHHHCCCCEEEEEE
10.9923503661
10UbiquitinationALAMGSRALRLWLVA
HHHCCCCEEEEEEEE
9.9524816145
50UbiquitinationMRNDLFNKEKARQLS
HHHHHCCHHHHHHHC
53.9423503661
50 (in isoform 2)Ubiquitination-53.94-
52UbiquitinationNDLFNKEKARQLSLT
HHHCCHHHHHHHCCC
50.9424816145
59PhosphorylationKARQLSLTPRTEKIE
HHHHHCCCCCCCEEE
13.83-
72AcetylationIEVKHVGKTDPGTVF
EEEEECCCCCCCCEE
48.9823236377
72UbiquitinationIEVKHVGKTDPGTVF
EEEEECCCCCCCCEE
48.9829967540
72SuccinylationIEVKHVGKTDPGTVF
EEEEECCCCCCCCEE
48.9827452117
72MalonylationIEVKHVGKTDPGTVF
EEEEECCCCCCCCEE
48.9826320211
75UbiquitinationKHVGKTDPGTVFVMN
EECCCCCCCCEEEEE
45.6623503661
79UbiquitinationKTDPGTVFVMNKNIS
CCCCCCEEEEECCCC
4.3023503661
89PhosphorylationNKNISTPYSCAMHLS
ECCCCCCCHHHHHHH
19.2318083107
96PhosphorylationYSCAMHLSEWYCRKS
CHHHHHHHHHHHCCH
16.05-
99PhosphorylationAMHLSEWYCRKSILA
HHHHHHHHHCCHHHH
4.3718083107
117 (in isoform 2)Ubiquitination-27.24-
117UbiquitinationGQPWDMYKPLTKSCE
CCCCCCCCCCCCCCE
27.2424816145
121UbiquitinationDMYKPLTKSCEIKFL
CCCCCCCCCCEEEEE
61.8723503661
126MalonylationLTKSCEIKFLTFKDC
CCCCCEEEEEEECCC
16.4226320211
126SuccinylationLTKSCEIKFLTFKDC
CCCCCEEEEEEECCC
16.4227452117
126AcetylationLTKSCEIKFLTFKDC
CCCCCEEEEEEECCC
16.4219608861
131UbiquitinationEIKFLTFKDCDPGEV
EEEEEEECCCCHHHC
52.8129967540
131AcetylationEIKFLTFKDCDPGEV
EEEEEEECCCCHHHC
52.8126051181
154UbiquitinationAMMMGCVIERAFKDE
HHHHHHHHHHHCCCC
3.2722817900
159AcetylationCVIERAFKDEYMVNL
HHHHHHCCCCHHEEE
48.9826822725
159UbiquitinationCVIERAFKDEYMVNL
HHHHHHCCCCHHEEE
48.9824816145
162UbiquitinationERAFKDEYMVNLVRA
HHHCCCCHHEEEEEC
19.2523503661
170UbiquitinationMVNLVRAPEVPVISG
HEEEEECCCCCEEEC
32.3323503661
192UbiquitinationLDSKLDEWMPTKENL
HCCCHHHCCCCHHHH
9.5623503661
194UbiquitinationSKLDEWMPTKENLRS
CCHHHCCCCHHHHHH
41.2023503661
195PhosphorylationKLDEWMPTKENLRSF
CHHHCCCCHHHHHHH
34.5822985185
196UbiquitinationLDEWMPTKENLRSFT
HHHCCCCHHHHHHHC
38.4421906983
196 (in isoform 2)Ubiquitination-38.4421890473
196 (in isoform 1)Ubiquitination-38.4421890473
200MethylationMPTKENLRSFTKDAH
CCCHHHHHHHCCCCC
41.11115483777
201UbiquitinationPTKENLRSFTKDAHA
CCHHHHHHHCCCCCE
40.2023503661
201PhosphorylationPTKENLRSFTKDAHA
CCHHHHHHHCCCCCE
40.2024719451
204AcetylationENLRSFTKDAHALIY
HHHHHHCCCCCEEEE
51.4019608861
204MalonylationENLRSFTKDAHALIY
HHHHHHCCCCCEEEE
51.4026320211
204 (in isoform 2)Ubiquitination-51.40-
204UbiquitinationENLRSFTKDAHALIY
HHHHHHCCCCCEEEE
51.4019608861
212 (in isoform 2)Ubiquitination-45.88-
212UbiquitinationDAHALIYKDLPFETL
CCCEEEECCCCCCEE
45.8823503661
234UbiquitinationLEIFQHSKYKVDFIE
HHHHHCCCCCCCHHH
47.1423503661
234AcetylationLEIFQHSKYKVDFIE
HHHHHCCCCCCCHHH
47.1423236377
236UbiquitinationIFQHSKYKVDFIEEK
HHHCCCCCCCHHHHH
38.7823503661
236 (in isoform 2)Ubiquitination-38.78-
243UbiquitinationKVDFIEEKASQNPER
CCCHHHHHHHCCHHH
40.3123503661
243 (in isoform 2)Ubiquitination-40.31-
253MethylationQNPERIVKLHRIGDF
CCHHHEEEEEEECCE
35.88-
253"N6,N6-dimethyllysine"QNPERIVKLHRIGDF
CCHHHEEEEEEECCE
35.88-
273UbiquitinationGPLIPRTSICFQYEV
CCCCCCEEEEEEEEE
20.7421890473
288UbiquitinationSAVHNLQPTQPSLIR
HHHCCCCCCCCHHHH
35.8524816145
315AcetylationAHFTIWDKLLERSRK
HHHHHHHHHHHHHHH
39.7226051181
315 (in isoform 1)Ubiquitination-39.7221890473
315UbiquitinationAHFTIWDKLLERSRK
HHHHHHHHHHHHHHH
39.7222817900
315UbiquitinationAHFTIWDKLLERSRK
HHHHHHHHHHHHHHH
39.7221890473
315 (in isoform 2)Ubiquitination-39.7221890473
325PhosphorylationERSRKMVTEDQSKAT
HHHHHHCCCCHHHHH
30.28-
329PhosphorylationKMVTEDQSKATEECT
HHCCCCHHHHHHHHC
36.26-
330UbiquitinationMVTEDQSKATEECTS
HCCCCHHHHHHHHCC
54.4124816145
332PhosphorylationTEDQSKATEECTST-
CCCHHHHHHHHCCC-
35.73-

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 RM39_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RM39_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 RM39_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RM44_HUMANMRPL44physical
22939629
RM40_HUMANMRPL40physical
22939629
RM49_HUMANMRPL49physical
22939629
RT09_HUMANMRPS9physical
22939629
RM55_HUMANMRPL55physical
22939629
RM52_HUMANMRPL52physical
22939629
TSR1_HUMANTSR1physical
22939629
PTCD1_HUMANPTCD1physical
26186194
NGRN_HUMANNGRNphysical
26186194
SYYM_HUMANYARS2physical
26186194
RM46_HUMANMRPL46physical
26186194
RM09_HUMANMRPL9physical
26186194
ARMC8_HUMANARMC8physical
26186194
MTEF3_HUMANMTERF3physical
26186194
RM32_HUMANMRPL32physical
26186194
RM11_HUMANMRPL11physical
26186194
RM48_HUMANMRPL48physical
26186194
RM40_HUMANMRPL40physical
26186194
RM03_HUMANMRPL3physical
26186194
RM01_HUMANMRPL1physical
26186194
RM41_HUMANMRPL41physical
26186194
RM22_HUMANMRPL22physical
26186194
RBP10_HUMANRANBP10physical
26186194
RM37_HUMANMRPL37physical
26186194
RM10_HUMANMRPL10physical
26186194
RM24_HUMANMRPL24physical
26186194
RM49_HUMANMRPL49physical
26186194
RM44_HUMANMRPL44physical
26186194
RM50_HUMANMRPL50physical
26186194
RM38_HUMANMRPL38physical
26186194
RM20_HUMANMRPL20physical
26186194
RM27_HUMANMRPL27physical
26186194
RM55_HUMANMRPL55physical
26186194
MASU1_HUMANMALSU1physical
26186194
GID4_HUMANGID4physical
26186194
RM47_HUMANMRPL47physical
26186194
RM16_HUMANMRPL16physical
26186194
RM19_HUMANMRPL19physical
26186194
ICT1_HUMANICT1physical
26186194
RM02_HUMANMRPL2physical
26186194
RM21_HUMANMRPL21physical
26186194
RM13_HUMANMRPL13physical
26186194
RUSD3_HUMANRPUSD3physical
26186194
RM17_HUMANMRPL17physical
26186194
FABD_HUMANMCATphysical
26186194
RM35_HUMANMRPL35physical
26186194
RM15_HUMANMRPL15physical
26186194
RM30_HUMANMRPL30physical
26186194
RT30_HUMANMRPS30physical
26186194
RM14_HUMANMRPL14physical
26186194
RM42_HUMANMRPL42physical
26186194
MRM3_HUMANRNMTL1physical
26186194
RM18_HUMANMRPL18physical
26186194
RM51_HUMANMRPL51physical
26186194
RT63_HUMANMRPL57physical
26186194
RM23_HUMANMRPL23physical
26186194
RM34_HUMANMRPL34physical
26186194
RM37_HUMANMRPL37physical
26344197
RM46_HUMANMRPL46physical
26344197
RT30_HUMANMRPS30physical
28514442
RM47_HUMANMRPL47physical
28514442
RM40_HUMANMRPL40physical
28514442
RM13_HUMANMRPL13physical
28514442
NGRN_HUMANNGRNphysical
28514442
RM24_HUMANMRPL24physical
28514442
RM38_HUMANMRPL38physical
28514442
RM30_HUMANMRPL30physical
28514442
ICT1_HUMANICT1physical
28514442
RUSD4_HUMANRPUSD4physical
28514442
RM55_HUMANMRPL55physical
28514442
RM17_HUMANMRPL17physical
28514442
RM32_HUMANMRPL32physical
28514442
RM02_HUMANMRPL2physical
28514442
RM22_HUMANMRPL22physical
28514442
RM41_HUMANMRPL41physical
28514442
RM49_HUMANMRPL49physical
28514442
RM51_HUMANMRPL51physical
28514442
RM27_HUMANMRPL27physical
28514442
RM20_HUMANMRPL20physical
28514442
RM03_HUMANMRPL3physical
28514442
RT63_HUMANMRPL57physical
28514442
RM15_HUMANMRPL15physical
28514442
RM16_HUMANMRPL16physical
28514442
RM48_HUMANMRPL48physical
28514442
MRM3_HUMANRNMTL1physical
28514442
MTEF3_HUMANMTERF3physical
28514442
RM19_HUMANMRPL19physical
28514442
RM44_HUMANMRPL44physical
28514442
MASU1_HUMANMALSU1physical
28514442
RM01_HUMANMRPL1physical
28514442
RM46_HUMANMRPL46physical
28514442
RM11_HUMANMRPL11physical
28514442
RM18_HUMANMRPL18physical
28514442
ARMC8_HUMANARMC8physical
28514442
SYYM_HUMANYARS2physical
28514442
PTCD1_HUMANPTCD1physical
28514442
RM14_HUMANMRPL14physical
28514442
TEKT2_HUMANTEKT2physical
27173435

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 RM39_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-126 AND LYS-204, AND MASSSPECTROMETRY.

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