RL13_HUMAN - dbPTM
RL13_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL13_HUMAN
UniProt AC P26373
Protein Name 60S ribosomal protein L13
Gene Name RPL13
Organism Homo sapiens (Human).
Sequence Length 211
Subcellular Localization
Protein Description
Protein Sequence MAPSRNGMVLKPHFHKDWQRRVATWFNQPARKIRRRKARQAKARRIAPRPASGPIRPIVRCPTVRYHTKVRAGRGFSLEELRVAGIHKKVARTIGISVDPRRRNKSTESLQANVQRLKEYRSKLILFPRKPSAPKKGDSSAEELKLATQLTGPVMPVRNVYKKEKARVITEEEKNFKAFASLRMARANARLFGIRAKRAKEAAEQDVEKKK
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
11AcetylationSRNGMVLKPHFHKDW
CCCCEEECCCCCHHH
25.6525953088
11UbiquitinationSRNGMVLKPHFHKDW
CCCCEEECCCCCHHH
25.65-
16UbiquitinationVLKPHFHKDWQRRVA
EECCCCCHHHHHHHH
60.7719608861
16AcetylationVLKPHFHKDWQRRVA
EECCCCCHHHHHHHH
60.7719608861
52PhosphorylationRIAPRPASGPIRPIV
HHCCCCCCCCCCCCE
48.0223403867
74MethylationHTKVRAGRGFSLEEL
ECCCCCCCCCCHHHH
41.8354558869
77PhosphorylationVRAGRGFSLEELRVA
CCCCCCCCHHHHHHC
37.3823927012
82MethylationGFSLEELRVAGIHKK
CCCHHHHHHCCHHHH
21.37115491663
882-HydroxyisobutyrylationLRVAGIHKKVARTIG
HHHCCHHHHHHHHHC
47.20-
88UbiquitinationLRVAGIHKKVARTIG
HHHCCHHHHHHHHHC
47.20-
93PhosphorylationIHKKVARTIGISVDP
HHHHHHHHHCCCCCC
17.5120068231
93 (in isoform 2)Phosphorylation-17.5129743597
97PhosphorylationVARTIGISVDPRRRN
HHHHHCCCCCCCCCC
18.4324670416
101MethylationIGISVDPRRRNKSTE
HCCCCCCCCCCCCHH
45.81115491671
1052-HydroxyisobutyrylationVDPRRRNKSTESLQA
CCCCCCCCCHHHHHH
57.87-
105UbiquitinationVDPRRRNKSTESLQA
CCCCCCCCCHHHHHH
57.8721890473
105UbiquitinationVDPRRRNKSTESLQA
CCCCCCCCCHHHHHH
57.8721890473
105AcetylationVDPRRRNKSTESLQA
CCCCCCCCCHHHHHH
57.8726051181
106PhosphorylationDPRRRNKSTESLQAN
CCCCCCCCHHHHHHH
40.7422167270
107PhosphorylationPRRRNKSTESLQANV
CCCCCCCHHHHHHHH
31.0730266825
109PhosphorylationRRNKSTESLQANVQR
CCCCCHHHHHHHHHH
26.3530266825
122PhosphorylationQRLKEYRSKLILFPR
HHHHHHHHHEEEECC
30.80-
123UbiquitinationRLKEYRSKLILFPRK
HHHHHHHHEEEECCC
30.4621890473
1232-HydroxyisobutyrylationRLKEYRSKLILFPRK
HHHHHHHHEEEECCC
30.46-
123SumoylationRLKEYRSKLILFPRK
HHHHHHHHEEEECCC
30.4628112733
123SumoylationRLKEYRSKLILFPRK
HHHHHHHHEEEECCC
30.46-
123UbiquitinationRLKEYRSKLILFPRK
HHHHHHHHEEEECCC
30.4621890473
123AcetylationRLKEYRSKLILFPRK
HHHHHHHHEEEECCC
30.4625953088
130AcetylationKLILFPRKPSAPKKG
HEEEECCCCCCCCCC
43.4919608861
130UbiquitinationKLILFPRKPSAPKKG
HEEEECCCCCCCCCC
43.4919608861
132PhosphorylationILFPRKPSAPKKGDS
EEECCCCCCCCCCCC
61.3120860994
136AcetylationRKPSAPKKGDSSAEE
CCCCCCCCCCCCHHH
67.8825953088
136UbiquitinationRKPSAPKKGDSSAEE
CCCCCCCCCCCCHHH
67.8821890473
139PhosphorylationSAPKKGDSSAEELKL
CCCCCCCCCHHHHHH
39.8729255136
140PhosphorylationAPKKGDSSAEELKLA
CCCCCCCCHHHHHHH
44.4329255136
145SumoylationDSSAEELKLATQLTG
CCCHHHHHHHHHCCC
39.0828112733
145AcetylationDSSAEELKLATQLTG
CCCHHHHHHHHHCCC
39.0825953088
145UbiquitinationDSSAEELKLATQLTG
CCCHHHHHHHHHCCC
39.0821890473
148PhosphorylationAEELKLATQLTGPVM
HHHHHHHHHCCCCCC
34.2530108239
151PhosphorylationLKLATQLTGPVMPVR
HHHHHHCCCCCCCCC
29.6230108239
155SulfoxidationTQLTGPVMPVRNVYK
HHCCCCCCCCCCCCH
2.6028465586
158AcetylationTGPVMPVRNVYKKEK
CCCCCCCCCCCHHHH
22.4919608861
158UbiquitinationTGPVMPVRNVYKKEK
CCCCCCCCCCCHHHH
22.4919608861
162SumoylationMPVRNVYKKEKARVI
CCCCCCCHHHHCEEE
50.61-
170PhosphorylationKEKARVITEEEKNFK
HHHCEEECHHHHHHH
34.19-
174UbiquitinationRVITEEEKNFKAFAS
EEECHHHHHHHHHHH
71.6021890473
174SumoylationRVITEEEKNFKAFAS
EEECHHHHHHHHHHH
71.6025114211
174AcetylationRVITEEEKNFKAFAS
EEECHHHHHHHHHHH
71.6023749302
174UbiquitinationRVITEEEKNFKAFAS
EEECHHHHHHHHHHH
71.6021890473
177UbiquitinationTEEEKNFKAFASLRM
CHHHHHHHHHHHHHH
52.5721890473
177UbiquitinationTEEEKNFKAFASLRM
CHHHHHHHHHHHHHH
52.5721890473
177MethylationTEEEKNFKAFASLRM
CHHHHHHHHHHHHHH
52.5719608861
177AcetylationTEEEKNFKAFASLRM
CHHHHHHHHHHHHHH
52.5719608861
177SumoylationTEEEKNFKAFASLRM
CHHHHHHHHHHHHHH
52.57-
177SumoylationTEEEKNFKAFASLRM
CHHHHHHHHHHHHHH
52.5728112733
181PhosphorylationKNFKAFASLRMARAN
HHHHHHHHHHHHHHH
15.2822199227
200AcetylationGIRAKRAKEAAEQDV
CHHHHHHHHHHHHHH
52.5026051181
200UbiquitinationGIRAKRAKEAAEQDV
CHHHHHHHHHHHHHH
52.5021890473
200MethylationGIRAKRAKEAAEQDV
CHHHHHHHHHHHHHH
52.5021679131
210AcetylationAEQDVEKKK------
HHHHHHHCC------
50.6523749302
211AcetylationEQDVEKKK-------
HHHHHHCC-------
76.3212435169

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
106SPhosphorylationKinaseAKT1P31749
PSP
170TPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL13_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 RL13_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS16_HUMANRPS16physical
22939629
RS25_HUMANRPS25physical
22939629
RL14_HUMANRPL14physical
22939629
RL15_HUMANRPL15physical
22939629
RL18_HUMANRPL18physical
22939629
RL19_HUMANRPL19physical
22939629
RL21_HUMANRPL21physical
22939629
RL23_HUMANRPL23physical
22939629
RL24_HUMANRPL24physical
22939629
RL27A_HUMANRPL27Aphysical
22939629
RL37A_HUMANRPL37Aphysical
22939629
RL4_HUMANRPL4physical
22939629
RL5_HUMANRPL5physical
22939629
RL6_HUMANRPL6physical
22939629
RL7A_HUMANRPL7Aphysical
22939629
RS23_HUMANRPS23physical
22939629
RS2_HUMANRPS2physical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RS3_HUMANRPS3physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS6_HUMANRPS6physical
22939629
RS8_HUMANRPS8physical
22939629
RSSA_HUMANRPSAphysical
22939629
RL23A_HUMANRPL23Aphysical
22939629
RS28_HUMANRPS28physical
22939629
RL7_HUMANRPL7physical
22939629
RL22_HUMANRPL22physical
22939629
RS20_HUMANRPS20physical
22939629
RL30_HUMANRPL30physical
22939629
RLA0_HUMANRPLP0physical
22939629
RS7_HUMANRPS7physical
22939629
RS13_HUMANRPS13physical
22939629
RL36_HUMANRPL36physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RL17_HUMANRPL17physical
22939629
RS21_HUMANRPS21physical
22939629
UBIM_HUMANFAUphysical
22939629
RS27L_HUMANRPS27Lphysical
22939629
AIMP1_HUMANAIMP1physical
22863883
SYDC_HUMANDARSphysical
22863883
SYMC_HUMANMARSphysical
22863883
SYQ_HUMANQARSphysical
22863883
RL19_HUMANRPL19physical
22863883
RL21_HUMANRPL21physical
22863883
RL23A_HUMANRPL23Aphysical
22863883
RL24_HUMANRPL24physical
22863883
RL26_HUMANRPL26physical
22863883
RL36_HUMANRPL36physical
22863883
CEP70_HUMANCEP70physical
25416956
TF3C2_HUMANGTF3C2physical
26186194
RT09_HUMANMRPS9physical
26186194
PTCD3_HUMANPTCD3physical
26186194
TF3C3_HUMANGTF3C3physical
26186194
RNBP6_HUMANRANBP6physical
26186194
IPO5_HUMANIPO5physical
26186194
RT27_HUMANMRPS27physical
26186194
RM09_HUMANMRPL9physical
26186194
RL26L_HUMANRPL26L1physical
26186194
TROP_HUMANTROphysical
26186194
RM32_HUMANMRPL32physical
26186194
RM48_HUMANMRPL48physical
26186194
RM40_HUMANMRPL40physical
26186194
RM01_HUMANMRPL1physical
26186194
TF3C1_HUMANGTF3C1physical
26186194
RT05_HUMANMRPS5physical
26186194
RM28_HUMANMRPL28physical
26186194
SENP3_HUMANSENP3physical
26186194
TEX10_HUMANTEX10physical
26186194
RBM34_HUMANRBM34physical
26186194
DCAF1_HUMANVPRBPphysical
26186194
RM50_HUMANMRPL50physical
26186194
RM27_HUMANMRPL27physical
26186194
RM55_HUMANMRPL55physical
26186194
RL15_HUMANRPL15physical
26186194
RM47_HUMANMRPL47physical
26186194
RM16_HUMANMRPL16physical
26186194
RT24_HUMANMRPS24physical
26186194
RM38_HUMANMRPL38physical
26186194
NSUN4_HUMANNSUN4physical
26186194
ICT1_HUMANICT1physical
26186194
RM13_HUMANMRPL13physical
26186194
PELP1_HUMANPELP1physical
26186194
RM17_HUMANMRPL17physical
26186194
RT33_HUMANMRPS33physical
26186194
G45IP_HUMANGADD45GIP1physical
26186194
RM30_HUMANMRPL30physical
26186194
NSA2_HUMANNSA2physical
26186194
RM20_HUMANMRPL20physical
26186194
RT18A_HUMANMRPS18Aphysical
26186194
RM42_HUMANMRPL42physical
26186194
RM18_HUMANMRPL18physical
26186194
RT30_HUMANMRPS30physical
26186194
RM34_HUMANMRPL34physical
26186194
NSA2_HUMANNSA2physical
26344197
RL10_HUMANRPL10physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL12_HUMANRPL12physical
26344197
RL13A_HUMANRPL13Aphysical
26344197
RL14_HUMANRPL14physical
26344197
RL15_HUMANRPL15physical
26344197
RL23A_HUMANRPL23Aphysical
26344197
RL24_HUMANRPL24physical
26344197
RL26_HUMANRPL26physical
26344197
RL26L_HUMANRPL26L1physical
26344197
RL27_HUMANRPL27physical
26344197
RL27A_HUMANRPL27Aphysical
26344197
RL28_HUMANRPL28physical
26344197
RL34_HUMANRPL34physical
26344197
RL35A_HUMANRPL35Aphysical
26344197
RL36_HUMANRPL36physical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL4_HUMANRPL4physical
26344197
RL6_HUMANRPL6physical
26344197
RL7_HUMANRPL7physical
26344197
RL7A_HUMANRPL7Aphysical
26344197
RL9_HUMANRPL9physical
26344197
RLA1_HUMANRPLP1physical
26344197
RS14_HUMANRPS14physical
26344197
RS15_HUMANRPS15physical
26344197
RS15A_HUMANRPS15Aphysical
26344197
RS18_HUMANRPS18physical
26344197
RS2_HUMANRPS2physical
26344197
RS23_HUMANRPS23physical
26344197
RS26_HUMANRPS26physical
26344197
RS27_HUMANRPS27physical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS5_HUMANRPS5physical
26344197
RS6_HUMANRPS6physical
26344197
RS7_HUMANRPS7physical
26344197
RS9_HUMANRPS9physical
26344197
NSUN4_HUMANNSUN4physical
28514442
RM30_HUMANMRPL30physical
28514442
RM28_HUMANMRPL28physical
28514442
RM38_HUMANMRPL38physical
28514442
RM27_HUMANMRPL27physical
28514442
RM13_HUMANMRPL13physical
28514442
TEX10_HUMANTEX10physical
28514442
RM47_HUMANMRPL47physical
28514442
RM55_HUMANMRPL55physical
28514442
RM48_HUMANMRPL48physical
28514442
RBM34_HUMANRBM34physical
28514442
RL30_HUMANRPL30physical
28514442
IPO5_HUMANIPO5physical
28514442
PUM3_HUMANKIAA0020physical
28514442
RM32_HUMANMRPL32physical
28514442
ZCCHV_HUMANZC3HAV1physical
28514442
RNBP6_HUMANRANBP6physical
28514442
RL18A_HUMANRPL18Aphysical
28514442
ZN512_HUMANZNF512physical
28514442
G45IP_HUMANGADD45GIP1physical
28514442
RM40_HUMANMRPL40physical
28514442
RM01_HUMANMRPL1physical
28514442
NUFP1_HUMANNUFIP1physical
28514442
RM17_HUMANMRPL17physical
28514442
RL26L_HUMANRPL26L1physical
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 RL13_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-16 AND LYS-177, AND MASSSPECTROMETRY.
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-106, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-106, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.

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