OTUL_HUMAN - dbPTM
OTUL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OTUL_HUMAN
UniProt AC Q96BN8
Protein Name Ubiquitin thioesterase otulin {ECO:0000305}
Gene Name OTULIN {ECO:0000303|PubMed:23806334, ECO:0000312|HGNC:HGNC:25118}
Organism Homo sapiens (Human).
Sequence Length 352
Subcellular Localization Cytoplasm .
Protein Description Deubiquitinase that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. [PubMed: 23708998]
Protein Sequence MSRGTMPQPEAWPGASCAETPAREAAATARDGGKAAASGQPRPEMQCPAEHEEDMYRAADEIEKEKELLIHERGASEPRLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFTSIRRVRGDNYCALRATLFQAMSQAVGLPPWLQDPELMLLPEKLISKYNWIKQWKLGLKFDGKNEDLVDKIKESLTLLRKKWAGLAEMRTAEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYNDKEKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKDWPVVTLIAEDDRHYNIPVRVCEETSL
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
20PhosphorylationPGASCAETPAREAAA
CCCCCCCCHHHHHHH
28555341
31UbiquitinationEAAATARDGGKAAAS
HHHHHHHCCCCCCCC
23000965
34UbiquitinationATARDGGKAAASGQP
HHHHCCCCCCCCCCC
21963094
38PhosphorylationDGGKAAASGQPRPEM
CCCCCCCCCCCCCCC
28555341
56PhosphorylationAEHEEDMYRAADEIE
CCCHHHHHHHHHHHH
28674151
64UbiquitinationRAADEIEKEKELLIH
HHHHHHHHHHHHHHH
23000965
66UbiquitinationADEIEKEKELLIHER
HHHHHHHHHHHHHCC
23000965
76PhosphorylationLIHERGASEPRLSVA
HHHCCCCCCCCCCCC
25159151
91UbiquitinationPEMDIMDYCKKEWRG
CCCCHHHHHHHHHCC
22817900
93UbiquitinationMDIMDYCKKEWRGNT
CCHHHHHHHHHCCCC
32015554
94UbiquitinationDIMDYCKKEWRGNTQ
CHHHHHHHHHCCCCC
-
95UbiquitinationIMDYCKKEWRGNTQK
HHHHHHHHHCCCCCH
22817900
102UbiquitinationEWRGNTQKATCMKMG
HHCCCCCHHHHHHCC
29967540
104PhosphorylationRGNTQKATCMKMGYE
CCCCCHHHHHHCCHH
-
107UbiquitinationTQKATCMKMGYEEVS
CCHHHHHHCCHHHHH
32015554
110PhosphorylationATCMKMGYEEVSQKF
HHHHHCCHHHHHHHH
27642862
116UbiquitinationGYEEVSQKFTSIRRV
CHHHHHHHHHCHHHH
23000965
119PhosphorylationEVSQKFTSIRRVRGD
HHHHHHHCHHHHCCC
29496963
164AcetylationLPEKLISKYNWIKQW
CCHHHHHHCCHHHHH
25953088
164UbiquitinationLPEKLISKYNWIKQW
CCHHHHHHCCHHHHH
29967540
169UbiquitinationISKYNWIKQWKLGLK
HHHCCHHHHHHCCCE
29967540
176UbiquitinationKQWKLGLKFDGKNED
HHHHCCCEECCCCHH
22817900
176AcetylationKQWKLGLKFDGKNED
HHHHCCCEECCCCHH
12433833
180UbiquitinationLGLKFDGKNEDLVDK
CCCEECCCCHHHHHH
21906983
180AcetylationLGLKFDGKNEDLVDK
CCCEECCCCHHHHHH
12433843
187AcetylationKNEDLVDKIKESLTL
CCHHHHHHHHHHHHH
12433853
187UbiquitinationKNEDLVDKIKESLTL
CCHHHHHHHHHHHHH
29967540
1892-HydroxyisobutyrylationEDLVDKIKESLTLLR
HHHHHHHHHHHHHHH
-
189UbiquitinationEDLVDKIKESLTLLR
HHHHHHHHHHHHHHH
29967540
193PhosphorylationDKIKESLTLLRKKWA
HHHHHHHHHHHHHHH
24260401
244PhosphorylationLNRAIELYNDKEKGK
HHHHHHHHCCHHCCC
-
2472-HydroxyisobutyrylationAIELYNDKEKGKEVP
HHHHHCCHHCCCCCC
-
257PhosphorylationGKEVPFFSVLLFARD
CCCCCCEEEEEEECC
-
305PhosphorylationVRHTIQVYRLSKYNT
HHHHHHHEECCCCCC
-
350PhosphorylationPVRVCEETSL-----
CCEEEECCCC-----
28060719
351PhosphorylationVRVCEETSL------
CEEEECCCC------
28060719

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 OTUL_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OTUL_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 OTUL_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_HUMANUBCphysical
23746843
UBC_HUMANUBCphysical
23708998
RNF31_HUMANRNF31physical
23708998
HOIL1_HUMANRBCK1physical
23708998
DVL2_HUMANDVL2physical
23708998
RNF31_HUMANRNF31physical
24726327
HOIL1_HUMANRBCK1physical
24726327
UBC_HUMANUBCphysical
24726327
TERA_HUMANVCPphysical
24726323
RNF31_HUMANRNF31physical
24726323
HOIL1_HUMANRBCK1physical
24726323
SHRPN_HUMANSHARPINphysical
24726323
UBC_HUMANUBCphysical
23827681
SBP1_HUMANSELENBP1physical
26186194
DUS14_HUMANDUSP14physical
26186194
LRC15_HUMANLRRC15physical
26186194
UBC_HUMANUBCphysical
25527291
RNF31_HUMANRNF31physical
26670046
HOIL1_HUMANRBCK1physical
26670046
SHRPN_HUMANSHARPINphysical
26670046
BCL10_HUMANBCL10physical
27777308
LAMP2_HUMANLAMP2physical
28514442
DUS14_HUMANDUSP14physical
28514442
RNF31_HUMANRNF31physical
27591049
RNF31_HUMANRNF31physical
28244869
UBC_HUMANUBCphysical
28319114

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 OTUL_HUMAN

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Related Literatures of Post-Translational Modification

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