CPLM-019082

Genbank Nucleotide ID

Ubiquitin thioesterase otulin

Protein Synonyms/Alias

Deubiquitinating enzyme otulin; OTU domain-containing deubiquitinase with linear linkage specificity; Ubiquitin thioesterase Gumby

Homo sapiens (Human)

Position	Peptide	Type	References
34	ATARDGGKAAASGQP	ubiquitination	[1, 2]
64	RAADEIEKEKELLIH	ubiquitination	[1, 2, 3, 4, 5, 6]
66	ADEIEKEKELLIHER	ubiquitination	[2, 6, 7]
94	DIMDYCKKEWRGNTQ	ubiquitination	[2]
116	GYEEVSQKFTSIRRV	ubiquitination	[2, 4, 7]
180	LGLKFDGKNEDLVDK	ubiquitination	[4]

[1] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]

Functional Description

Deubiquitinase that specifically removes linear ('M-1'- linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis. Associates with the LUBAC complex via direct interaction with RNF31 and counteracts its action by cleaving linear polyubiquitin chains to substrates. Required during angiogenesis, craniofacial and neuronal development by regulating the canonical Wnt signaling together with the LUBAC complex. Acts as a negative regulator of NF-kappa-B by counteracting activity of the LUBAC complex.

DOMAIN 118 346 OTU.
REGION 95 96 Linear diubiquitin binding.
REGION 124 126 Linear diubiquitin binding.
REGION 255 259 Linear diubiquitin binding.
REGION 283 289 Linear diubiquitin binding.
REGION 336 338 Linear diubiquitin binding.
ACT_SITE 126 126 By similarity.
ACT_SITE 129 129 Nucleophile.
ACT_SITE 339 339
BINDING 314 314 Linear diubiquitin.

3D-structure; Acetylation; Angiogenesis; Coiled coil; Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein; Polymorphism; Protease; Reference proteome; Thiol protease; Ubl conjugation; Ubl conjugation pathway; Wnt signaling pathway.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

IPR023235; FAM105.
IPR023237; FAM105B.

PR02055; PROTEINF105.
PR02057; PROTEINF105B.