RL32_HUMAN - dbPTM
RL32_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL32_HUMAN
UniProt AC P62910
Protein Name 60S ribosomal protein L32
Gene Name RPL32
Organism Homo sapiens (Human).
Sequence Length 135
Subcellular Localization
Protein Description
Protein Sequence MAALRPLVKPKIVKKRTKKFIRHQSDRYVKIKRNWRKPRGIDNRVRRRFKGQILMPNIGYGSNKKTKHMLPSGFRKFLVHNVKELEVLLMCNKSYCAEIAHNVSSKNRKAIVERAAQLAIRVTNPNARLRSEENE
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
9SumoylationAALRPLVKPKIVKKR
CCCCCCCCHHHHCHH
48.5628112733
9UbiquitinationAALRPLVKPKIVKKR
CCCCCCCCHHHHCHH
48.56-
22MethylationKRTKKFIRHQSDRYV
HHHHHHHHHCCCCEE
25.56115492073
25PhosphorylationKKFIRHQSDRYVKIK
HHHHHHCCCCEEEEC
20.2429514088
27MethylationFIRHQSDRYVKIKRN
HHHHCCCCEEEECCC
43.31115492089
37SumoylationKIKRNWRKPRGIDNR
EECCCCCCCCCCCHH
30.59-
50SuccinylationNRVRRRFKGQILMPN
HHHHHHHCCCEECCC
48.36-
50UbiquitinationNRVRRRFKGQILMPN
HHHHHHHCCCEECCC
48.36-
50AcetylationNRVRRRFKGQILMPN
HHHHHHHCCCEECCC
48.3625953088
50UbiquitinationNRVRRRFKGQILMPN
HHHHHHHCCCEECCC
48.3621890473
50SuccinylationNRVRRRFKGQILMPN
HHHHHHHCCCEECCC
48.3621890473
502-HydroxyisobutyrylationNRVRRRFKGQILMPN
HHHHHHHCCCEECCC
48.36-
55SulfoxidationRFKGQILMPNIGYGS
HHCCCEECCCCCCCC
2.2630846556
60PhosphorylationILMPNIGYGSNKKTK
EECCCCCCCCCCCCC
17.3728555341
62PhosphorylationMPNIGYGSNKKTKHM
CCCCCCCCCCCCCCC
36.6725159151
62O-linked_GlycosylationMPNIGYGSNKKTKHM
CCCCCCCCCCCCCCC
36.6728510447
64AcetylationNIGYGSNKKTKHMLP
CCCCCCCCCCCCCCC
64.6125953088
66PhosphorylationGYGSNKKTKHMLPSG
CCCCCCCCCCCCCCH
28.0020068231
672-HydroxyisobutyrylationYGSNKKTKHMLPSGF
CCCCCCCCCCCCCHH
35.58-
67AcetylationYGSNKKTKHMLPSGF
CCCCCCCCCCCCCHH
35.5826051181
67UbiquitinationYGSNKKTKHMLPSGF
CCCCCCCCCCCCCHH
35.58-
69SulfoxidationSNKKTKHMLPSGFRK
CCCCCCCCCCCHHHH
6.6628183972
72PhosphorylationKTKHMLPSGFRKFLV
CCCCCCCCHHHHHHH
46.7520068231
75MethylationHMLPSGFRKFLVHNV
CCCCCHHHHHHHCCH
32.13115492081
76UbiquitinationMLPSGFRKFLVHNVK
CCCCHHHHHHHCCHH
40.57-
762-HydroxyisobutyrylationMLPSGFRKFLVHNVK
CCCCHHHHHHHCCHH
40.57-
76AcetylationMLPSGFRKFLVHNVK
CCCCHHHHHHHCCHH
40.5725825284
83MethylationKFLVHNVKELEVLLM
HHHHCCHHHHHHHHH
63.0030993909
83UbiquitinationKFLVHNVKELEVLLM
HHHHCCHHHHHHHHH
63.00-
83AcetylationKFLVHNVKELEVLLM
HHHHCCHHHHHHHHH
63.0026051181
91S-nitrosocysteineELEVLLMCNKSYCAE
HHHHHHHCCCHHHHH
6.14-
91GlutathionylationELEVLLMCNKSYCAE
HHHHHHHCCCHHHHH
6.1422555962
91S-nitrosylationELEVLLMCNKSYCAE
HHHHHHHCCCHHHHH
6.1419483679
932-HydroxyisobutyrylationEVLLMCNKSYCAEIA
HHHHHCCCHHHHHHH
37.56-
93AcetylationEVLLMCNKSYCAEIA
HHHHHCCCHHHHHHH
37.5626051181
94PhosphorylationVLLMCNKSYCAEIAH
HHHHCCCHHHHHHHH
16.0828152594
95PhosphorylationLLMCNKSYCAEIAHN
HHHCCCHHHHHHHHH
9.4028152594
95NitrationLLMCNKSYCAEIAHN
HHHCCCHHHHHHHHH
9.40-
96GlutathionylationLMCNKSYCAEIAHNV
HHCCCHHHHHHHHHC
3.3722555962
96S-nitrosylationLMCNKSYCAEIAHNV
HHCCCHHHHHHHHHC
3.372212679
96S-palmitoylationLMCNKSYCAEIAHNV
HHCCCHHHHHHHHHC
3.3726865113
104PhosphorylationAEIAHNVSSKNRKAI
HHHHHHCCCCCHHHH
40.6928985074
105PhosphorylationEIAHNVSSKNRKAIV
HHHHHCCCCCHHHHH
29.6623312004
1062-HydroxyisobutyrylationIAHNVSSKNRKAIVE
HHHHCCCCCHHHHHH
53.95-
106UbiquitinationIAHNVSSKNRKAIVE
HHHHCCCCCHHHHHH
53.95-
106AcetylationIAHNVSSKNRKAIVE
HHHHCCCCCHHHHHH
53.9526051181
114MethylationNRKAIVERAAQLAIR
CHHHHHHHHHHHHHH
25.08115492065
128MethylationRVTNPNARLRSEENE
HHCCCCHHHCCCCCC
36.96115492097
131PhosphorylationNPNARLRSEENE---
CCCHHHCCCCCC---
54.5829743597

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 RL32_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL32_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 RL32_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL5_HUMANRPL5physical
22939629
RL7_HUMANRPL7physical
22939629
RL8_HUMANRPL8physical
22939629
RL9_HUMANRPL9physical
22939629
RS23_HUMANRPS23physical
22939629
RS26_HUMANRPS26physical
22939629
RS2_HUMANRPS2physical
22939629
RS3_HUMANRPS3physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS6_HUMANRPS6physical
22939629
RL7A_HUMANRPL7Aphysical
22939629
RS8_HUMANRPS8physical
22939629
RL4_HUMANRPL4physical
22939629
RSSA_HUMANRPSAphysical
22939629
RS20_HUMANRPS20physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RS16_HUMANRPS16physical
22939629
RS3A_HUMANRPS3Aphysical
22939629
RL3_HUMANRPL3physical
22939629
RL17_HUMANRPL17physical
26344197
RL23A_HUMANRPL23Aphysical
26344197
RL27A_HUMANRPL27Aphysical
26344197
RL35A_HUMANRPL35Aphysical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RL39_HUMANRPL39physical
26344197
RL4_HUMANRPL4physical
26344197
RL5_HUMANRPL5physical
26344197
RL7_HUMANRPL7physical
26344197
RL7A_HUMANRPL7Aphysical
26344197
RL9_HUMANRPL9physical
26344197
RS13_HUMANRPS13physical
26344197
RS16_HUMANRPS16physical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS6_HUMANRPS6physical
26344197
RL40_HUMANUBA52physical
26344197
THOC4_HUMANALYREFphysical
27173435
UBIM_HUMANFAUphysical
27173435
LSM4_HUMANLSM4physical
27173435
LSM8_HUMANLSM8physical
27173435
SART3_HUMANSART3physical
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 RL32_HUMAN

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Related Literatures of Post-Translational Modification

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