Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ubiquitin thioesterase OTUB1  

UniProtKB / Swiss-Prot ID :  OTUB1_HUMAN

Gene Name (Synonyms) : 
OTUB1, OTB1, OTU1 HSPC263  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (By similarity). 

Protein Function :  Hydrolase that can remove conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a nuch lower preference compared to 'Lys-48'- linked ubiquitin. 

Protein Sequence MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQ...
Predicted Secondary Structure CCCCCCCHHHCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCHHHHHHHHHHHHHCCCCHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAEEP
---CCCCCC
24.47UniProtKB
Link-
16PhosphoserineEPLGSDSEG
CCCCCHHHH
45.72HPRD
Link-
16PhosphoserineEPLGSDSEG
CCCCCHHHH
45.72PhosphoELM
Link-
16PhosphoserineEPLGSDSEG
CCCCCHHHH
45.72Phosphositeplus
Link-
16Phosphoserine.EPLGSDSEG
CCCCCHHHH
45.72UniProtKB
Link-
18PhosphoserineLGSDSEGVN
CCCHHHHHH
37.64HPRD
Link-
18PhosphoserineLGSDSEGVN
CCCHHHHHH
37.64Phosphositeplus
Link-
26PhosphotyrosineNCLAYDEAI
HHHHHHHHH
11.02Phosphositeplus
Link-
59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SVLYKEYAE
HHHHHHCCC
39.84Phosphositeplus
Link
71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IYQQKIKDL
HHHHHHHHH
35.88Phosphositeplus
Link
84Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SYIRKTRPD
HHHHEECCC
39.05Phosphositeplus
Link
109Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LDDSKELQR
HHHHHHHHH
70.23Phosphositeplus
Link
188Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QRESKFFEH
HHHHHHHHH
49.69Phosphositeplus
Link
188N6-acetyllysineQRESKFFEH
HHHHHHHHH
49.69HPRD
Link
188N6-acetyllysineQRESKFFEH
HHHHHHHHH
49.69Phosphositeplus
Link
188N6-acetyllysine.QRESKFFEH
HHHHHHHHH
49.69UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
UBIQ_HUMANphysical interactionMINT-50324MINT11689694
SMAD9_HUMANyeast 2-hybridHPRD:08493HPRD15231748
RN128_HUMANENSP00000301453STRING
BTD_HUMANENSP00000301453STRING
TMLH_HUMANENSP00000301453STRING
BPL1_HUMANENSP00000301453STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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-188, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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-16, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures