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Ubiquitin carboxyl-terminal hydrolase 36 (EC 3 4 19 12) (Deubiquitinating enzyme 36) (Ubiquitin thioesterase 36) (Ubiquitin-specific-processing protease 36)

 UBP36_HUMAN             Reviewed;        1123 AA.
Q9P275; Q05C98; Q05DD0; Q6IQ38; Q8NDM8; Q9NVC8;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 4.
29-SEP-2021, entry version 179.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 36 {ECO:0000305};
EC=3.4.19.12;
AltName: Full=Deubiquitinating enzyme 36;
AltName: Full=Ubiquitin thioesterase 36;
AltName: Full=Ubiquitin-specific-processing protease 36;
Name=USP36 {ECO:0000312|HGNC:HGNC:20062}; Synonyms=KIAA1453;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-806; CYS-828 AND
959-LYS-LYS-960 DEL.
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII. The
complete sequences of 100 new cDNA clones from brain which code for large
proteins in vitro.";
DNA Res. 7:143-150(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-271; ARG-806 AND
PRO-887.
TISSUE=Cervix, Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-954, AND VARIANTS ARG-806 AND
CYS-828.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 494-1123.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[6]
TISSUE SPECIFICITY, AND ENZYME ACTIVITY.
PubMed=14715245; DOI=10.1016/j.bbrc.2003.12.050;
Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S.,
Lopez-Otin C.;
"Cloning and enzymatic analysis of 22 novel human ubiquitin-specific
proteases.";
Biochem. Biophys. Res. Commun. 314:54-62(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-952, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464; SER-582 AND SER-667, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-131, AND ACTIVE SITE.
PubMed=19208757; DOI=10.1242/jcs.044461;
Endo A., Matsumoto M., Inada T., Yamamoto A., Nakayama K.I., Kitamura N.,
Komada M.;
"Nucleolar structure and function are regulated by the deubiquitylating
enzyme USP36.";
J. Cell Sci. 122:678-686(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667 AND SER-682, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582; SER-713; SER-742 AND
SER-952, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF CYS-131.
PubMed=21268071; DOI=10.1002/jcb.22940;
Kim M.S., Ramakrishna S., Lim K.H., Kim J.H., Baek K.H.;
"Protein stability of mitochondrial superoxide dismutase SOD2 is regulated
by USP36.";
J. Cell. Biochem. 112:498-508(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-742, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
FUNCTION.
PubMed=22622177; DOI=10.4161/auto.19381;
Taillebourg E., Gregoire I., Viargues P., Jacomin A.C., Thevenon D.,
Faure M., Fauvarque M.O.;
"The deubiquitinating enzyme USP36 controls selective autophagy activation
by ubiquitinated proteins.";
Autophagy 8:767-779(2012).
[16]
FUNCTION.
PubMed=22902402; DOI=10.1016/j.celrep.2012.07.009;
Richardson L.A., Reed B.J., Charette J.M., Freed E.F., Fredrickson E.K.,
Locke M.N., Baserga S.J., Gardner R.G.;
"A conserved deubiquitinating enzyme controls cell growth by regulating RNA
polymerase I stability.";
Cell Rep. 2:372-385(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-464; SER-546;
SER-582; SER-667; SER-682; SER-713 AND SER-952, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
FUNCTION, SUBCELLULAR LOCATION, ACTIVE SITE, AND MUTAGENESIS OF CYS-131.
PubMed=25775507; DOI=10.1073/pnas.1411713112;
Sun X.X., He X., Yin L., Komada M., Sears R.C., Dai M.S.;
"The nucleolar ubiquitin-specific protease USP36 deubiquitinates and
stabilizes c-Myc.";
Proc. Natl. Acad. Sci. U.S.A. 112:3734-3739(2015).
[19]
FUNCTION, SUBCELLULAR LOCATION, ACTIVE SITE, INTERACTION WITH NEDD4L AND
NTRK1, MUTAGENESIS OF CYS-131, AND UBIQUITINATION.
PubMed=27445338; DOI=10.1074/jbc.m116.722637;
Anta B., Martin-Rodriguez C., Gomis-Perez C., Calvo L., Lopez-Benito S.,
Calderon-Garcia A.A., Vicente-Garcia C., Villarroel A., Arevalo J.C.;
"Ubiquitin-specific Protease 36 (USP36) Controls Neuronal Precursor Cell-
expressed Developmentally Down-regulated 4-2 (Nedd4-2) Actions over the
Neurotrophin Receptor TrkA and Potassium Voltage-gated Channels 7.2/3
(Kv7.2/3).";
J. Biol. Chem. 291:19132-19145(2016).
[20]
FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF CYS-131.
PubMed=29274341; DOI=10.1016/j.bbrc.2017.12.107;
DeVine T., Sears R.C., Dai M.S.;
"The ubiquitin-specific protease USP36 is a conserved histone H2B
deubiquitinase.";
Biochem. Biophys. Res. Commun. 495:2363-2368(2018).
[21]
FUNCTION.
PubMed=29273634; DOI=10.1074/jbc.m117.788430;
Fraile J.M., Campos-Iglesias D., Rodriguez F., Astudillo A.,
Vilarrasa-Blasi R., Verdaguer-Dot N., Prado M.A., Paulo J.A., Gygi S.P.,
Martin-Subero J.I., Freije J.M.P., Lopez-Otin C.;
"Loss of the deubiquitinase USP36 destabilizes the RNA helicase DHX33 and
causes preimplantation lethality in mice.";
J. Biol. Chem. 293:2183-2194(2018).
-!- FUNCTION: Deubiquitinase essential for the regulation of nucleolar
structure and function. Required for cell and organism viability. Plays
an important role in ribosomal RNA processing and protein synthesis,
which is mediated, at least in part, through deubiquitination of DHX33,
NPM1 and FBL, regulating their protein stability (PubMed:29273634,
PubMed:19208757, PubMed:22902402). Functions as a transcriptional
repressor by deubiquiting histone H2B at the promoters of genes
critical for cellular differentiation, such as CDKN1A, thereby
preventing histone H3 'Lys-4' trimethylation (H3K4) (PubMed:29274341).
Specifically deubiquitinates MYC in the nucleolus, leading to prevent
MYC degradation by the proteasome: acts by specifically interacting
with isoform 3 of FBXW7 (FBW7gamma) in the nucleolus and counteracting
ubiquitination of MYC by the SCF(FBW7) complex. In contrast, it does
not interact with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm
(PubMed:25775507). Interacts to and regulates the actions of E3
ubiquitin-protein ligase NEDD4L over substrates such as NTRK1, KCNQ2
and KCNQ3, affecting their expression an functions (PubMed:27445338).
Deubiquitinates SOD2, regulates SOD2 protein stability
(PubMed:21268071). Deubiquitinase activity is required to control
selective autophagy activation by ubiquitinated proteins
(PubMed:22622177). {ECO:0000269|PubMed:19208757,
ECO:0000269|PubMed:21268071, ECO:0000269|PubMed:22622177,
ECO:0000269|PubMed:22902402, ECO:0000269|PubMed:25775507,
ECO:0000269|PubMed:27445338, ECO:0000269|PubMed:29273634,
ECO:0000269|PubMed:29274341}.
-!- CATALYTIC ACTIVITY:
Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
residue protein attached to proteins as an intracellular targeting
signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:14715245};
-!- SUBUNIT: Interacts with isoform 3 of FBXW7; the interaction inhibits
MYC degradation induced by SCF(FBW7) complex (PubMed:25775507).
Interacts with NTRK1; USP36 does not deubiquitinate NTRK1
(PubMed:27445338). Interacts with NEDD4L (via domains WW1, 3 and 4);
the interaction inhibits ubiquitination of, at least, NTRK1, KCNQ2 and
KCNQ3 by NEDD4L (PubMed:27445338). {ECO:0000269|PubMed:25775507,
ECO:0000269|PubMed:27445338}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
ECO:0000269|PubMed:19208757, ECO:0000269|PubMed:25775507,
ECO:0000269|PubMed:27445338}. Cytoplasm {ECO:0000269|PubMed:27445338}.
-!- TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:14715245}.
-!- PTM: Polyubiquitinated by NEDD4L, no effect on USP36 protein levels.
Both proteins interact with and regulate each other's ubiquitination
levels. {ECO:0000269|PubMed:27445338}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH16487.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA95977.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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EMBL; AB040886; BAA95977.1; ALT_INIT; mRNA.
EMBL; BC016487; AAH16487.1; ALT_SEQ; mRNA.
EMBL; BC027992; AAH27992.1; -; mRNA.
EMBL; BC071582; AAH71582.1; -; mRNA.
EMBL; AK001671; BAA91825.1; -; mRNA.
EMBL; AL833835; CAD38695.1; -; mRNA.
CCDS; CCDS32755.1; -.
RefSeq; NP_001308220.1; NM_001321291.1.
RefSeq; XP_005257599.1; XM_005257542.2.
RefSeq; XP_005257600.1; XM_005257543.2.
RefSeq; XP_016880389.1; XM_017024900.1.
SMR; Q9P275; -.
BioGRID; 121651; 78.
IntAct; Q9P275; 35.
STRING; 9606.ENSP00000441214; -.
MEROPS; C19.042; -.
CarbonylDB; Q9P275; -.
iPTMnet; Q9P275; -.
PhosphoSitePlus; Q9P275; -.
SwissPalm; Q9P275; -.
BioMuta; USP36; -.
DMDM; 124056592; -.
SWISS-2DPAGE; Q9P275; -.
EPD; Q9P275; -.
jPOST; Q9P275; -.
MassIVE; Q9P275; -.
PaxDb; Q9P275; -.
PeptideAtlas; Q9P275; -.
PRIDE; Q9P275; -.
Antibodypedia; 1709; 238 antibodies.
DNASU; 57602; -.
Ensembl; ENST00000312010; ENSP00000310590; ENSG00000055483.
Ensembl; ENST00000542802; ENSP00000441214; ENSG00000055483.
Ensembl; ENST00000589225; ENSP00000467280; ENSG00000055483.
GeneID; 57602; -.
KEGG; hsa:57602; -.
UCSC; uc002jvz.2; human.
CTD; 57602; -.
DisGeNET; 57602; -.
GeneCards; USP36; -.
HGNC; HGNC:20062; USP36.
HPA; ENSG00000055483; Low tissue specificity.
MIM; 612543; gene.
neXtProt; NX_Q9P275; -.
OpenTargets; ENSG00000055483; -.
PharmGKB; PA134949090; -.
VEuPathDB; HostDB:ENSG00000055483; -.
eggNOG; KOG1865; Eukaryota.
GeneTree; ENSGT00940000157948; -.
InParanoid; Q9P275; -.
OMA; SETCLPQ; -.
OrthoDB; 929408at2759; -.
PhylomeDB; Q9P275; -.
TreeFam; TF315281; -.
PathwayCommons; Q9P275; -.
BioGRID-ORCS; 57602; 559 hits in 1029 CRISPR screens.
ChiTaRS; USP36; human.
GeneWiki; USP36; -.
GenomeRNAi; 57602; -.
Pharos; Q9P275; Tbio.
PRO; PR:Q9P275; -.
Proteomes; UP000005640; Chromosome 17.
RNAct; Q9P275; protein.
Bgee; ENSG00000055483; Expressed in adenohypophysis and 226 other tissues.
ExpressionAtlas; Q9P275; baseline and differential.
Genevisible; Q9P275; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent deubiquitinase; IDA:FlyBase.
GO; GO:0016578; P:histone deubiquitination; IMP:UniProtKB.
GO; GO:0016242; P:negative regulation of macroautophagy; IMP:UniProtKB.
GO; GO:0007000; P:nucleolus organization; ISS:UniProtKB.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; HMP:ParkinsonsUK-UCL.
GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
GO; GO:2000232; P:regulation of rRNA processing; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
InterPro; IPR038765; Papain-like_cys_pep_sf.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF00443; UCH; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protease;
Reference proteome; Thiol protease; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1..1123
/note="Ubiquitin carboxyl-terminal hydrolase 36"
/id="PRO_0000080666"
DOMAIN 122..423
/note="USP"
REGION 1..22
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 67..95
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 430..577
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 589..999
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 70..89
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 432..446
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 457..471
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 487..501
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 549..577
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 605..681
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 742..758
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 765..788
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 858..872
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 886..906
/note="Polar residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 917..932
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 964..979
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
ACT_SITE 131
/note="Nucleophile"
/evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
ECO:0000255|PROSITE-ProRule:PRU10093,
ECO:0000269|PubMed:19208757, ECO:0000269|PubMed:21268071,
ECO:0000269|PubMed:25775507, ECO:0000269|PubMed:27445338,
ECO:0000269|PubMed:29274341"
ACT_SITE 382
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
ECO:0000255|PROSITE-ProRule:PRU10093"
MOD_RES 429
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 464
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:23186163"
MOD_RES 546
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:23186163"
MOD_RES 582
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
MOD_RES 667
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:18669648,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
MOD_RES 682
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19690332,
ECO:0007744|PubMed:23186163"
MOD_RES 713
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:23186163"
MOD_RES 742
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692"
MOD_RES 952
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:17081983,
ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
VARIANT 271
/note="V -> I (in dbSNP:rs3744793)"
/evidence="ECO:0000269|PubMed:15489334"
/id="VAR_037277"
VARIANT 489
/note="I -> M (in dbSNP:rs3744795)"
/id="VAR_037278"
VARIANT 775
/note="R -> Q (in dbSNP:rs9889908)"
/id="VAR_037279"
VARIANT 806
/note="Q -> R (in dbSNP:rs3088040)"
/evidence="ECO:0000269|PubMed:10819331,
ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
/id="VAR_037280"
VARIANT 814
/note="K -> N (in dbSNP:rs3744797)"
/id="VAR_037281"
VARIANT 828
/note="R -> C (in dbSNP:rs1057040)"
/evidence="ECO:0000269|PubMed:10819331,
ECO:0000269|PubMed:14702039"
/id="VAR_037282"
VARIANT 887
/note="R -> P (in dbSNP:rs61760231)"
/evidence="ECO:0000269|PubMed:15489334"
/id="VAR_058034"
VARIANT 959..960
/note="Missing (in dbSNP:rs866027510)"
/evidence="ECO:0000269|PubMed:10819331"
/id="VAR_080193"
MUTAGEN 131
/note="C->A,S: Abolishes deubiquitinase activity. No effect
on NTRK1 ubiquitination levels."
/evidence="ECO:0000269|PubMed:19208757,
ECO:0000269|PubMed:21268071, ECO:0000269|PubMed:25775507,
ECO:0000269|PubMed:27445338, ECO:0000269|PubMed:29274341"
CONFLICT 82
/note="R -> G (in Ref. 2; AAH71582)"
/evidence="ECO:0000305"
CONFLICT 573
/note="D -> G (in Ref. 3; BAA91825)"
/evidence="ECO:0000305"
SEQUENCE 1123 AA; 122908 MW; 65CD93C1B8655319 CRC64;
MPIVDKLKEA LKPGRKDSAD DGELGKLLAS SAKKVLLQKI EFEPASKSFS YQLEALKSKY
VLLNPKTEGA SRHKSGDDPP ARRQGSEHTY ESCGDGVPAP QKVLFPTERL SLRWERVFRV
GAGLHNLGNT CFLNATIQCL TYTPPLANYL LSKEHARSCH QGSFCMLCVM QNHIVQAFAN
SGNAIKPVSF IRDLKKIARH FRFGNQEDAH EFLRYTIDAM QKACLNGCAK LDRQTQATTL
VHQIFGGYLR SRVKCSVCKS VSDTYDPYLD VALEIRQAAN IVRALELFVK ADVLSGENAY
MCAKCKKKVP ASKRFTIHRT SNVLTLSLKR FANFSGGKIT KDVGYPEFLN IRPYMSQNNG
DPVMYGLYAV LVHSGYSCHA GHYYCYVKAS NGQWYQMNDS LVHSSNVKVV LNQQAYVLFY
LRIPGSKKSP EGLISRTGSS SLPGRPSVIP DHSKKNIGNG IISSPLTGKR QDSGTMKKPH
TTEEIGVPIS RNGSTLGLKS QNGCIPPKLP SGSPSPKLSQ TPTHMPTILD DPGKKVKKPA
PPQHFSPRTA QGLPGTSNSN SSRSGSQRQG SWDSRDVVLS TSPKLLATAT ANGHGLKGND
ESAGLDRRGS SSSSPEHSAS SDSTKAPQTP RSGAAHLCDS QETNCSTAGH SKTPPSGADS
KTVKLKSPVL SNTTTEPAST MSPPPAKKLA LSAKKASTLW RATGNDLRPP PPSPSSDLTH
PMKTSHPVVA STWPVHRARA VSPAPQSSSR LQPPFSPHPT LLSSTPKPPG TSEPRSCSSI
STALPQVNED LVSLPHQLPE ASEPPQSPSE KRKKTFVGEP QRLGSETRLP QHIREATAAP
HGKRKRKKKK RPEDTAASAL QEGQTQRQPG SPMYRREGQA QLPAVRRQED GTQPQVNGQQ
VGCVTDGHHA SSRKRRRKGA EGLGEEGGLH QDPLRHSCSP MGDGDPEAME ESPRKKKKKK
RKQETQRAVE EDGHLKCPRS AKPQDAVVPE SSSCAPSANG WCPGDRMGLS QAPPVSWNGE
RESDVVQELL KYSSDKAYGR KVLTWDGKMS AVSQDAIEDS RQARTETVVD DWDEEFDRGK
EKKIKKFKRE KRRNFNAFQK LQTRRNFWSV THPAKAASLS YRR


Related products :

Catalog number Product name Quantity
EIAAB45096 Deubiquitinating enzyme 7,HAUSP,Herpesvirus-associated ubiquitin-specific protease,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-processing pro
EIAAB45055 Deubiquitinating enzyme 4,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 4,Ubiquitin thioesterase 4,Ubiquitin-specific-processing protease 4,Usp4
EIAAB44991 Deubiquitinating enzyme 16,Homo sapiens,Human,MSTP039,Ubiquitin carboxyl-terminal hydrolase 16,Ubiquitin thiolesterase 16,Ubiquitin-processing protease UBP-M,Ubiquitin-specific-processing protease 16,
EIAAB45002 41 kDa ubiquitin-specific protease,Deubiquitinating enzyme 2,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,Ubiquitin-
EIAAB45093 Chicken,Deubiquitinating enzyme 7,Gallus gallus,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-processing protease 7,USP7
EIAAB45022 Deubiquitinating enzyme 27,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 22-like,Ubiquitin carboxyl-terminal hydrolase 27,Ubiquitin thiolesterase 27,Ubiquitin-specific-processing protease 2
EIAAB45023 Deubiquitinating enzyme 27,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 27,Ubiquitin thiolesterase 27,Ubiquitin-specific-processing protease 27,Usp27,Usp27x,X-linked ubiquitin carboxyl-ter
EIAAB44981 Deubiquitinating enzyme 12,Mouse,Mus musculus,Ubh1,Ubiquitin carboxyl-terminal hydrolase 12,Ubiquitin thiolesterase 12,Ubiquitin-hydrolyzing enzyme 1,Ubiquitin-specific-processing protease 12,Usp12
EIAAB45005 41 kDa ubiquitin-specific protease,Deubiquitinating enzyme 2,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,UBP41,USP2
EIAAB45001 41 kDa ubiquitin-specific protease,Bos taurus,Bovine,Deubiquitinating enzyme 2,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,UBP41,USP2
EIAAB45004 41 kDa ubiquitin-specific protease,Deubiquitinating enzyme 2,MNCb-0190,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,Ubp
EIAAB45076 Deubiquitinating enzyme 48,Rat,Rattus norvegicus,Synaptic ubiquitin-specific protease,synUSP,Ubiquitin carboxyl-terminal hydrolase 48,Ubiquitin thiolesterase 48,Ubiquitin-specific-processing protease
EIAAB45095 Deubiquitinating enzyme 7,Hausp,Herpesvirus-associated ubiquitin-specific protease,mHAUSP,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-process
EIAAB45094 Deubiquitinating enzyme 7,Hausp,Herpesvirus-associated ubiquitin-specific protease,Rat,Rattus norvegicus,rHAUSP,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-proc
EIAAB44983 Deubiquitinating enzyme 12,Homo sapiens,Human,UBH1,Ubiquitin carboxyl-terminal hydrolase 12,Ubiquitin thiolesterase 12,Ubiquitin-hydrolyzing enzyme 1,Ubiquitin-specific-processing protease 12,USP12,US
EIAAB45098 Deubiquitinating enzyme 8,Kiaa0055,Mouse,mUBPy,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 8,Ubiquitin isopeptidase Y,Ubiquitin thiolesterase 8,Ubiquitin-specific-processing protease 8,Ubpy,Usp
EIAAB45039 Deubiquitinating enzyme 33,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 33,Ubiquitin thiolesterase 33,Ubiquitin-specific-processing protease 33,Usp33,Vdu1,VHL-interacting deubiquitinating
EIAAB45097 Deubiquitinating enzyme 8,Homo sapiens,hUBPy,Human,KIAA0055,Ubiquitin carboxyl-terminal hydrolase 8,Ubiquitin isopeptidase Y,Ubiquitin thiolesterase 8,Ubiquitin-specific-processing protease 8,UBPY,USP
EIAAB45050 Deubiquitinating enzyme 37,Pig,Sus scrofa,Ubiquitin carboxyl-terminal hydrolase 37,Ubiquitin thiolesterase 37,Ubiquitin-specific-processing protease 37,USP37
EIAAB45067 Inactive deubiquitinating enzyme 44,Inactive ubiquitin carboxyl-terminal hydrolase 44,Inactive ubiquitin thioesterase 44,Inactive ubiquitin-specific-processing protease 44,Mouse,Mus musculus,Usp44
EIAAB45052 Deubiquitinating enzyme 38,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 38,Ubiquitin thiolesterase 38,Ubiquitin-specific-processing protease 38,Usp38
EIAAB45069 Deubiquitinating enzyme 45,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 45,Ubiquitin thiolesterase 45,Ubiquitin-specific-processing protease 45,Usp45
EIAAB45066 Deubiquitinating enzyme 43,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 43,Ubiquitin thiolesterase 43,Ubiquitin-specific-processing protease 43,Usp43
EIAAB45072 Deubiquitinating enzyme 46,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 46,Ubiquitin thiolesterase 46,Ubiquitin-specific-processing protease 46,Usp46
EIAAB45073 Deubiquitinating enzyme 47,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 47,Ubiquitin thiolesterase 47,Ubiquitin-specific-processing protease 47,Usp47
Pathways :
WP2199: Seed Development
WP211: BMP signaling pathway
WP2292: Chemokine signaling pathway
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP2344: vitamin B6 (pyridoxine, pyridoxal, pyridoxamine) biosynthesis and salvage pathway
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP142: mRNA processing
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP1000: Arachidonate Epoxygenase Epoxide Hydrolase
WP793: mRNA processing
WP1142: mRNA processing
WP2328: Allograft rejection
WP1250: Arachidonate Epoxygenase Epoxide Hydrolase
WP1493: Carbon assimilation C4 pathway
WP310: mRNA processing
WP470: Proteasome Degradation
WP1838: Interleukin-1 processing
WP1890: Processing of Capped Intronless Pre-mRNA
WP678: Arachidonate Epoxygenase / Epoxide Hydrolase
WP1116: Arachidonate Epoxygenase Epoxide Hydrolase
WP906: mRNA processing
WP123: mRNA processing
WP467: mRNA processing
WP1830: Insulin Synthesis and Processing

Related Genes :
[scny Usp36 CG5505] Ubiquitin carboxyl-terminal hydrolase 36 (EC 3.4.19.12) (Deubiquitinating enzyme 36) (Protein scrawny) (Ubiquitin thioesterase 36) (Ubiquitin-specific-processing protease 36)
[USP7 HAUSP] Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Deubiquitinating enzyme 7) (Herpesvirus-associated ubiquitin-specific protease) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7)
[USP15 KIAA0529] Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) (Deubiquitinating enzyme 15) (Ubiquitin thioesterase 15) (Ubiquitin-specific-processing protease 15) (Unph-2) (Unph4)
[USP25 USP21] Ubiquitin carboxyl-terminal hydrolase 25 (EC 3.4.19.12) (Deubiquitinating enzyme 25) (USP on chromosome 21) (Ubiquitin thioesterase 25) (Ubiquitin-specific-processing protease 25)
[USP10 KIAA0190] Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10)
[USP17L2 DUB3 USP17 USP17H USP17I USP17J USP17K USP17L USP17M] Ubiquitin carboxyl-terminal hydrolase 17 (USP17) (EC 3.4.19.12) (Deubiquitinating enzyme 17-like protein 2) (Deubiquitinating protein 3) (DUB-3) (Ubiquitin carboxyl-terminal hydrolase 17-like protein 2) (Ubiquitin thioesterase 17-like protein 2) (Ubiquitin-specific-processing protease 17-like protein 2)
[USP44] Ubiquitin carboxyl-terminal hydrolase 44 (EC 3.4.19.12) (Deubiquitinating enzyme 44) (Ubiquitin thioesterase 44) (Ubiquitin-specific-processing protease 44)
[USP22 KIAA1063 USP3L] Ubiquitin carboxyl-terminal hydrolase 22 (EC 3.4.19.12) (Deubiquitinating enzyme 22) (Ubiquitin thioesterase 22) (Ubiquitin-specific-processing protease 22)
[USP9X DFFRX FAM USP9] Probable ubiquitin carboxyl-terminal hydrolase FAF-X (EC 3.4.19.12) (Deubiquitinating enzyme FAF-X) (Fat facets in mammals) (hFAM) (Fat facets protein-related, X-linked) (Ubiquitin thioesterase FAF-X) (Ubiquitin-specific protease 9, X chromosome) (Ubiquitin-specific-processing protease FAF-X)
[Cyld Cyld1 Kiaa0849] Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD)
[USP11 UHX1] Ubiquitin carboxyl-terminal hydrolase 11 (EC 3.4.19.12) (Deubiquitinating enzyme 11) (Ubiquitin thioesterase 11) (Ubiquitin-specific-processing protease 11)
[USP28 KIAA1515] Ubiquitin carboxyl-terminal hydrolase 28 (EC 3.4.19.12) (Deubiquitinating enzyme 28) (Ubiquitin thioesterase 28) (Ubiquitin-specific-processing protease 28)
[CYLD CYLD1 KIAA0849 HSPC057] Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD)
[Usp25] Ubiquitin carboxyl-terminal hydrolase 25 (EC 3.4.19.12) (Deubiquitinating enzyme 25) (Ubiquitin thioesterase 25) (Ubiquitin-specific-processing protease 25) (mUSP25)
[UBP3 YER151C] Ubiquitin carboxyl-terminal hydrolase 3 (EC 3.4.19.12) (Deubiquitinating enzyme 3) (Ubiquitin thioesterase 3) (Ubiquitin-specific-processing protease 3)
[USP6 HRP1 TRE2] Ubiquitin carboxyl-terminal hydrolase 6 (EC 3.4.19.12) (Deubiquitinating enzyme 6) (Proto-oncogene TRE-2) (Ubiquitin thioesterase 6) (Ubiquitin-specific-processing protease 6)
[UBP2 YOR124C O3281 YOR3281C] Ubiquitin carboxyl-terminal hydrolase 2 (EC 3.4.19.12) (Deubiquitinating enzyme 2) (Ubiquitin thioesterase 2) (Ubiquitin-specific-processing protease 2)
[USP24 KIAA1057] Ubiquitin carboxyl-terminal hydrolase 24 (EC 3.4.19.12) (Deubiquitinating enzyme 24) (Ubiquitin thioesterase 24) (Ubiquitin-specific-processing protease 24)
[USP45] Ubiquitin carboxyl-terminal hydrolase 45 (EC 3.4.19.12) (Deubiquitinating enzyme 45) (Ubiquitin thioesterase 45) (Ubiquitin-specific-processing protease 45)
[ubp9 SPBC1703.12] Probable ubiquitin carboxyl-terminal hydrolase 9 (EC 3.4.19.12) (Deubiquitinating enzyme 9) (Ubiquitin thioesterase 9) (Ubiquitin-specific-processing protease 9)
[Usp10 Kiaa0190 Ode-1 Uchrp] Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10)
[Usp44] Ubiquitin carboxyl-terminal hydrolase 44 (EC 3.4.19.12) (Deubiquitinating enzyme 44) (Ubiquitin thioesterase 44) (Ubiquitin-specific-processing protease 44)
[Cyld Cyld1] Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD)
[Usp28 Kiaa1515] Ubiquitin carboxyl-terminal hydrolase 28 (EC 3.4.19.12) (Deubiquitinating enzyme 28) (Ubiquitin thioesterase 28) (Ubiquitin-specific-processing protease 28)
[CYLD CYLD1] Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD)
[CYLD CYLD1] Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD)
[Usp15 ubp109] Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) (Deubiquitinating enzyme 15) (Ubiquitin carboxyl-terminal hydrolase of 109 kDa) (Ubiquitin thioesterase 15) (Ubiquitin-specific-processing protease 15)
[USP9Y DFFRY] Probable ubiquitin carboxyl-terminal hydrolase FAF-Y (EC 3.4.19.12) (Deubiquitinating enzyme FAF-Y) (Fat facets protein-related, Y-linked) (Ubiquitin thioesterase FAF-Y) (Ubiquitin-specific protease 9, Y chromosome) (Ubiquitin-specific-processing protease FAF-Y)
[Usp10] Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10)
[Usp15 Kiaa0529] Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) (Deubiquitinating enzyme 15) (Ubiquitin thioesterase 15) (Ubiquitin-specific-processing protease 15)

Bibliography :