RL19_HUMAN - dbPTM
RL19_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL19_HUMAN
UniProt AC P84098
Protein Name 60S ribosomal protein L19
Gene Name RPL19
Organism Homo sapiens (Human).
Sequence Length 196
Subcellular Localization
Protein Description
Protein Sequence MSMLRLQKRLASSVLRCGKKKVWLDPNETNEIANANSRQQIRKLIKDGLIIRKPVTVHSRARCRKNTLARRKGRHMGIGKRKGTANARMPEKVTWMRRMRILRRLLRRYRESKKIDRHMYHSLYLKVKGNVFKNKRILMEHIHKLKADKARKKLLADQAEARRSKTKEARKRREERLQAKKEEIIKTLSKEEETKK
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
2Phosphorylation------MSMLRLQKR
------CCHHHHHHH
26.9029514088
5Citrullination---MSMLRLQKRLAS
---CCHHHHHHHHHH
26.82-
5Citrullination---MSMLRLQKRLAS
---CCHHHHHHHHHH
26.82-
5Methylation---MSMLRLQKRLAS
---CCHHHHHHHHHH
26.82115491861
9MethylationSMLRLQKRLASSVLR
CHHHHHHHHHHHHHH
23.64115491851
12PhosphorylationRLQKRLASSVLRCGK
HHHHHHHHHHHHCCC
26.1030266825
13PhosphorylationLQKRLASSVLRCGKK
HHHHHHHHHHHCCCC
21.4030266825
16CitrullinationRLASSVLRCGKKKVW
HHHHHHHHCCCCEEE
25.61-
16CitrullinationRLASSVLRCGKKKVW
HHHHHHHHCCCCEEE
25.61-
20UbiquitinationSVLRCGKKKVWLDPN
HHHHCCCCEEECCCC
37.53-
21AcetylationVLRCGKKKVWLDPNE
HHHCCCCEEECCCCC
41.9726822725
21UbiquitinationVLRCGKKKVWLDPNE
HHHCCCCEEECCCCC
41.9721906983
29PhosphorylationVWLDPNETNEIANAN
EECCCCCCCHHCCCC
44.8023663014
37PhosphorylationNEIANANSRQQIRKL
CHHCCCCHHHHHHHH
29.1119664994
38CitrullinationEIANANSRQQIRKLI
HHCCCCHHHHHHHHH
32.03-
38CitrullinationEIANANSRQQIRKLI
HHCCCCHHHHHHHHH
32.03-
43UbiquitinationNSRQQIRKLIKDGLI
CHHHHHHHHHHCCCE
57.0821906983
46AcetylationQQIRKLIKDGLIIRK
HHHHHHHHCCCEECC
57.0626051181
46UbiquitinationQQIRKLIKDGLIIRK
HHHHHHHHCCCEECC
57.0621890473
53UbiquitinationKDGLIIRKPVTVHSR
HCCCEECCCCCCCCC
33.17-
53AcetylationKDGLIIRKPVTVHSR
HCCCEECCCCCCCCC
33.1726051181
56PhosphorylationLIIRKPVTVHSRARC
CEECCCCCCCCCHHH
22.49-
59PhosphorylationRKPVTVHSRARCRKN
CCCCCCCCCHHHCCC
24.2524719451
67PhosphorylationRARCRKNTLARRKGR
CHHHCCCHHHHHCCC
25.48-
80UbiquitinationGRHMGIGKRKGTANA
CCCCCCCCCCCCCCC
49.36-
80AcetylationGRHMGIGKRKGTANA
CCCCCCCCCCCCCCC
49.3623954790
82AcetylationHMGIGKRKGTANARM
CCCCCCCCCCCCCCC
65.197668529
84PhosphorylationGIGKRKGTANARMPE
CCCCCCCCCCCCCCH
21.55-
922-HydroxyisobutyrylationANARMPEKVTWMRRM
CCCCCCHHHHHHHHH
38.81-
92UbiquitinationANARMPEKVTWMRRM
CCCCCCHHHHHHHHH
38.8121906983
94PhosphorylationARMPEKVTWMRRMRI
CCCCHHHHHHHHHHH
25.31-
117MethylationRESKKIDRHMYHSLY
HHHCCCCHHHHHHHH
21.68115491831
119SulfoxidationSKKIDRHMYHSLYLK
HCCCCHHHHHHHHHH
3.1630846556
120PhosphorylationKKIDRHMYHSLYLKV
CCCCHHHHHHHHHHE
5.1127642862
122PhosphorylationIDRHMYHSLYLKVKG
CCHHHHHHHHHHEEC
10.9628450419
124PhosphorylationRHMYHSLYLKVKGNV
HHHHHHHHHHEECCH
13.9027642862
126UbiquitinationMYHSLYLKVKGNVFK
HHHHHHHHEECCHHC
28.48-
126AcetylationMYHSLYLKVKGNVFK
HHHHHHHHEECCHHC
28.4826051181
128UbiquitinationHSLYLKVKGNVFKNK
HHHHHHEECCHHCCH
43.0821906983
128AcetylationHSLYLKVKGNVFKNK
HHHHHHEECCHHCCH
43.0826210075
133UbiquitinationKVKGNVFKNKRILME
HEECCHHCCHHHHHH
58.2221906983
135UbiquitinationKGNVFKNKRILMEHI
ECCHHCCHHHHHHHH
41.21-
139SulfoxidationFKNKRILMEHIHKLK
HCCHHHHHHHHHHHH
3.0730846556
144MethylationILMEHIHKLKADKAR
HHHHHHHHHHHHHHH
51.5972631043
144UbiquitinationILMEHIHKLKADKAR
HHHHHHHHHHHHHHH
51.5921890473
1442-HydroxyisobutyrylationILMEHIHKLKADKAR
HHHHHHHHHHHHHHH
51.59-
144MalonylationILMEHIHKLKADKAR
HHHHHHHHHHHHHHH
51.5926320211
144AcetylationILMEHIHKLKADKAR
HHHHHHHHHHHHHHH
51.5925953088
146UbiquitinationMEHIHKLKADKARKK
HHHHHHHHHHHHHHH
60.38-
152UbiquitinationLKADKARKKLLADQA
HHHHHHHHHHHHHHH
53.2721890473
152AcetylationLKADKARKKLLADQA
HHHHHHHHHHHHHHH
53.2725953088
1532-HydroxyisobutyrylationKADKARKKLLADQAE
HHHHHHHHHHHHHHH
43.08-
153UbiquitinationKADKARKKLLADQAE
HHHHHHHHHHHHHHH
43.0821890473
153MalonylationKADKARKKLLADQAE
HHHHHHHHHHHHHHH
43.0826320211
162MethylationLADQAEARRSKTKEA
HHHHHHHHHHHHHHH
34.60115491841
164PhosphorylationDQAEARRSKTKEARK
HHHHHHHHHHHHHHH
38.8428985074
165UbiquitinationQAEARRSKTKEARKR
HHHHHHHHHHHHHHH
62.90-
167MethylationEARRSKTKEARKRRE
HHHHHHHHHHHHHHH
53.78116252551
180AcetylationREERLQAKKEEIIKT
HHHHHHHHHHHHHHH
47.9923749302
180UbiquitinationREERLQAKKEEIIKT
HHHHHHHHHHHHHHH
47.9919608861
181SumoylationEERLQAKKEEIIKTL
HHHHHHHHHHHHHHH
64.6925114211
181AcetylationEERLQAKKEEIIKTL
HHHHHHHHHHHHHHH
64.6926051181
181UbiquitinationEERLQAKKEEIIKTL
HHHHHHHHHHHHHHH
64.6921890473
1862-HydroxyisobutyrylationAKKEEIIKTLSKEEE
HHHHHHHHHHCHHHH
49.42-
186AcetylationAKKEEIIKTLSKEEE
HHHHHHHHHHCHHHH
49.4226051181
186UbiquitinationAKKEEIIKTLSKEEE
HHHHHHHHHHCHHHH
49.4221906983
187PhosphorylationKKEEIIKTLSKEEET
HHHHHHHHHCHHHHH
26.3427794612
189PhosphorylationEEIIKTLSKEEETKK
HHHHHHHCHHHHHCC
43.1623401153
190UbiquitinationEIIKTLSKEEETKK-
HHHHHHCHHHHHCC-
72.721906983
190AcetylationEIIKTLSKEEETKK-
HHHHHHCHHHHHCC-
72.7223749302
1902-HydroxyisobutyrylationEIIKTLSKEEETKK-
HHHHHHCHHHHHCC-
72.72-
194PhosphorylationTLSKEEETKK-----
HHCHHHHHCC-----
47.6223403867
195UbiquitinationLSKEEETKK------
HCHHHHHCC------
60.8221906983
196UbiquitinationSKEEETKK-------
CHHHHHCC-------
73.35-

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
12SPhosphorylationKinaseCHEK1O14757
GPS
56TPhosphorylationKinaseCHEK1O14757
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL19_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 RL19_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL21_HUMANRPL21physical
22939629
RL22_HUMANRPL22physical
22939629
RL23_HUMANRPL23physical
22939629
RL24_HUMANRPL24physical
22939629
RL27A_HUMANRPL27Aphysical
22939629
RL30_HUMANRPL30physical
22939629
RL31_HUMANRPL31physical
22939629
RL37A_HUMANRPL37Aphysical
22939629
RL3_HUMANRPL3physical
22939629
RL4_HUMANRPL4physical
22939629
RL5_HUMANRPL5physical
22939629
RL6_HUMANRPL6physical
22939629
RL7A_HUMANRPL7Aphysical
22939629
RL7_HUMANRPL7physical
22939629
RL9_HUMANRPL9physical
22939629
RS13_HUMANRPS13physical
22939629
RS14_HUMANRPS14physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RS16_HUMANRPS16physical
22939629
RS17_HUMANRPS17physical
22939629
RS19_HUMANRPS19physical
22939629
RS23_HUMANRPS23physical
22939629
RS25_HUMANRPS25physical
22939629
RS26_HUMANRPS26physical
22939629
RS2_HUMANRPS2physical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RS3_HUMANRPS3physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS5_HUMANRPS5physical
22939629
RS6_HUMANRPS6physical
22939629
RS7_HUMANRPS7physical
22939629
RS8_HUMANRPS8physical
22939629
RSSA_HUMANRPSAphysical
22939629
RL8_HUMANRPL8physical
22939629
RL23A_HUMANRPL23Aphysical
22939629
RS24_HUMANRPS24physical
22939629
RS11_HUMANRPS11physical
22939629
RS28_HUMANRPS28physical
22939629
RS20_HUMANRPS20physical
22939629
RS12_HUMANRPS12physical
22939629
RLA0_HUMANRPLP0physical
22939629
RL36_HUMANRPL36physical
22939629
RL27_HUMANRPL27physical
22939629
RS9_HUMANRPS9physical
22939629
RL32_HUMANRPL32physical
22939629
RS27A_HUMANRPS27Aphysical
22939629
RS21_HUMANRPS21physical
22939629
RL1D1_HUMANRSL1D1physical
22939629
SRP14_HUMANSRP14physical
22939629
RS27L_HUMANRPS27Lphysical
22939629
RRS1_HUMANRRS1physical
22939629
SND1_HUMANSND1physical
22939629
TEBP_HUMANPTGES3physical
22939629
RM12_HUMANMRPL12physical
22939629
HNRPM_HUMANHNRNPMphysical
22863883
SYK_HUMANKARSphysical
22863883
NMT1_HUMANNMT1physical
22863883
SYQ_HUMANQARSphysical
22863883
RL10_HUMANRPL10physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL11_HUMANRPL11physical
26344197
RL12_HUMANRPL12physical
26344197
RL13_HUMANRPL13physical
26344197
RL13A_HUMANRPL13Aphysical
26344197
RL15_HUMANRPL15physical
26344197
RL17_HUMANRPL17physical
26344197
RL21_HUMANRPL21physical
26344197
RL22_HUMANRPL22physical
26344197
RL23_HUMANRPL23physical
26344197
RL23A_HUMANRPL23Aphysical
26344197
RL24_HUMANRPL24physical
26344197
RL26_HUMANRPL26physical
26344197
RL27_HUMANRPL27physical
26344197
RL27A_HUMANRPL27Aphysical
26344197
RL28_HUMANRPL28physical
26344197
RL30_HUMANRPL30physical
26344197
RL31_HUMANRPL31physical
26344197
RL32_HUMANRPL32physical
26344197
RL34_HUMANRPL34physical
26344197
RL35_HUMANRPL35physical
26344197
RL35A_HUMANRPL35Aphysical
26344197
RL36_HUMANRPL36physical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL3L_HUMANRPL3Lphysical
26344197
RL4_HUMANRPL4physical
26344197
RL5_HUMANRPL5physical
26344197
RL7_HUMANRPL7physical
26344197
RL7A_HUMANRPL7Aphysical
26344197
RL8_HUMANRPL8physical
26344197
RL9_HUMANRPL9physical
26344197
RLA1_HUMANRPLP1physical
26344197
RLA2_HUMANRPLP2physical
26344197
RS10_HUMANRPS10physical
26344197
RS11_HUMANRPS11physical
26344197
RS12_HUMANRPS12physical
26344197
RS13_HUMANRPS13physical
26344197
RS14_HUMANRPS14physical
26344197
RS15_HUMANRPS15physical
26344197
RS15A_HUMANRPS15Aphysical
26344197
RS16_HUMANRPS16physical
26344197
RS18_HUMANRPS18physical
26344197
RS2_HUMANRPS2physical
26344197
RS23_HUMANRPS23physical
26344197
RS25_HUMANRPS25physical
26344197
RS26_HUMANRPS26physical
26344197
RS3_HUMANRPS3physical
26344197
RS3A_HUMANRPS3Aphysical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS5_HUMANRPS5physical
26344197
RS6_HUMANRPS6physical
26344197
RS7_HUMANRPS7physical
26344197
RS8_HUMANRPS8physical
26344197
RS9_HUMANRPS9physical
26344197
RSSA_HUMANRPSAphysical
26344197
S61A1_HUMANSEC61A1physical
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 RL19_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-80, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND THR-187, AND MASSSPECTROMETRY.

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