OTU1_HUMAN - dbPTM
OTU1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OTU1_HUMAN
UniProt AC Q5VVQ6
Protein Name Ubiquitin thioesterase OTU1
Gene Name YOD1
Organism Homo sapiens (Human).
Sequence Length 348
Subcellular Localization Cytoplasm . Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains.
Protein Description Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains. Cleaves both polyubiquitin and di-ubiquitin. May play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes. May recruit PLAA, UBXN6 and VCP to damaged lysosome membranes decorated with K48-linked ubiquitin chains and remove these chains allowing autophagosome formation. [PubMed: 27753622]
Protein Sequence MFGPAKGRHFGVHPAPGFPGGVSQQAAGTKAGPAGAWPVGSRTDTMWRLRCKAKDGTHVLQGLSSRTRVRELQGQIAAITGIAPGGQRILVGYPPECLDLSNGDTILEDLPIQSGDMLIIEEDQTRPRSSPAFTKRGASSYVRETLPVLTRTVVPADNSCLFTSVYYVVEGGVLNPACAPEMRRLIAQIVASDPDFYSEAILGKTNQEYCDWIKRDDTWGGAIEISILSKFYQCEICVVDTQTVRIDRFGEDAGYTKRVLLIYDGIHYDPLQRNFPDPDTPPLTIFSSNDDIVLVQALELADEARRRRQFTDVNRFTLRCMVCQKGLTGQAEAREHAKETGHTNFGEV
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
54UbiquitinationWRLRCKAKDGTHVLQ
EEEEEEECCCCCCCC
42.0322053931
91UbiquitinationPGGQRILVGYPPECL
CCCCEEEEECCHHHC
6.8532142685
129PhosphorylationEDQTRPRSSPAFTKR
CCCCCCCCCCCCHHH
43.2723403867
130PhosphorylationDQTRPRSSPAFTKRG
CCCCCCCCCCCHHHC
22.8727794612
135UbiquitinationRSSPAFTKRGASSYV
CCCCCCHHHCHHHHH
42.2432142685
139PhosphorylationAFTKRGASSYVRETL
CCHHHCHHHHHHHHC
25.6528857561
140PhosphorylationFTKRGASSYVRETLP
CHHHCHHHHHHHHCC
27.4126434776
145PhosphorylationASSYVRETLPVLTRT
HHHHHHHHCCEEEEE
26.2922985185
150PhosphorylationRETLPVLTRTVVPAD
HHHCCEEEEEEECCC
25.2420068231
213 (in isoform 2)Ubiquitination-1.3521906983
213UbiquitinationNQEYCDWIKRDDTWG
CHHHCHHHHCCCCCC
1.3522053931
226PhosphorylationWGGAIEISILSKFYQ
CCCCEEEEHHHHCCC
12.5124719451
257 (in isoform 1)Ubiquitination-31.8321906983
257UbiquitinationGEDAGYTKRVLLIYD
CCCCCCCCEEEEEEC
31.8332142685
281UbiquitinationNFPDPDTPPLTIFSS
CCCCCCCCCEEEECC
29.3222505724
317PhosphorylationFTDVNRFTLRCMVCQ
CCCCCHHHHHHHHCC
15.2824719451
325UbiquitinationLRCMVCQKGLTGQAE
HHHHHCCCCCCCHHH
51.2422505724
328PhosphorylationMVCQKGLTGQAEARE
HHCCCCCCCHHHHHH
35.6023403867

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 OTU1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OTU1_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 OTU1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BL1S5_HUMANBLOC1S5physical
19615732
THOC3_HUMANTHOC3physical
19615732
TERA_HUMANVCPphysical
19818707
UBC_HUMANUBCphysical
19818707
DERL1_HUMANDERL1physical
19818707
FAF2_HUMANFAF2physical
19818707
SYVN1_HUMANSYVN1physical
24068323
AMFR_HUMANAMFRphysical
24068323
TERA_HUMANVCPphysical
24417208
UBC_HUMANUBCphysical
23827681
UBE3A_HUMANUBE3Aphysical
23827681
NEDD4_HUMANNEDD4physical
23827681
RIPK1_HUMANRIPK1physical
23827681
NPL4_HUMANNPLOC4physical
19818707
UFD1_HUMANUFD1Lphysical
19818707
FA98B_HUMANFAM98Bphysical
26344197
UBC_HUMANUBCphysical
27066941
TRAF6_HUMANTRAF6physical
28244869
TERA_HUMANVCPphysical
28244869
BIRC3_HUMANBIRC3physical
28244869
SHRPN_HUMANSHARPINphysical
28244869

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 OTU1_HUMAN

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Related Literatures of Post-Translational Modification

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