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Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10)

 UBP10_MOUSE             Reviewed;         792 AA.
P52479; Q3T9L4; Q3TNN5; Q3TZB8; Q3U5E0; Q6ZQG9; Q91VY7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-MAR-2010, sequence version 3.
25-APR-2018, entry version 151.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 10;
EC=3.4.19.12 {ECO:0000250|UniProtKB:Q14694};
AltName: Full=Deubiquitinating enzyme 10;
AltName: Full=Ubiquitin thioesterase 10;
AltName: Full=Ubiquitin-specific-processing protease 10;
Name=Usp10; Synonyms=Kiaa0190, Ode-1, Uchrp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Ito M., Hitomi K., Tsukagoshi N.;
"Cloning from a mouse osteoblastic cell line of a gene, encoding a
ubiquitin carboxyl-terminal hydrolase related polypeptide, down
regulated during ascorbic acid dependent differentiation.";
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, Spleen, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Mammary tumor;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-223; SER-359;
THR-566 AND SER-570, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from
target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an
essential regulator of p53/TP53 stability: in unstressed cells,
specifically deubiquitinates p53/TP53 in the cytoplasm, leading to
counteract MDM2 action and stabilize p53/TP53. Following DNA
damage, translocates to the nucleus and deubiquitinates p53/TP53,
leading to regulate the p53/TP53-dependent DNA damage response.
Component of a regulatory loop that controls autophagy and
p53/TP53 levels: mediates deubiquitination of BECN1, a key
regulator of autophagy, leading to stabilize the PIK3C3/VPS34-
containing complexes. In turn, PIK3C3/VPS34-containing complexes
regulate USP10 stability, suggesting the existence of a regulatory
system by which PIK3C3/VPS34-containing complexes regulate
p53/TP53 protein levels via USP10 and USP13. Does not
deubiquitinate MDM2. Deubiquitinates CFTR in early endosomes,
enhancing its endocytic recycling. Involved in a TANK-dependent
negative feedback response to attenuate NF-kappaB activation via
deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta
(IL1B) stimulation or upon DNA damage. Deubiquitinates TBX21
leading to its stabilization. {ECO:0000250|UniProtKB:Q14694}.
-!- CATALYTIC ACTIVITY: 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).
{ECO:0000250|UniProtKB:Q14694}.
-!- ENZYME REGULATION: Specifically inhibited by spautin-1 (specific
and potent autophagy inhibitor-1), a derivative of MBCQ that binds
to USP10 and inhibits deubiquitinase activity. Regulated by
PIK3C3/VPS34-containing complexes (By similarity). {ECO:0000250}.
-!- SUBUNIT: Found in a deubiquitination complex with TANK, USP10 and
ZC3H12A; this complex inhibits genotoxic stress- or interleukin-1-
beta (IL1B)-mediated NF-kappaB activation by promoting IKBKG or
TRAF6 deubiquitination. Interacts with IKBKG; this interaction
increases in response to DNA damage. Interacts with TANK; this
interaction increases in response to DNA damage. Interacts with
TRAF6; this interaction increases in response to DNA damage.
Interacts with ZC3H12A; this interaction increases in response to
DNA damage. Interacts with G3BP, which may regulate its function.
Interacts with p53/TP53, SNX3 and CFTR. Interacts with TBX21.
{ECO:0000250|UniProtKB:Q14694}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14694}.
Nucleus {ECO:0000250|UniProtKB:Q14694}. Early endosome
{ECO:0000250|UniProtKB:Q14694}. Note=Cytoplasmic in normal
conditions (By similarity). After DNA damage, translocates to the
nucleus following phosphorylation by ATM (By similarity).
{ECO:0000250|UniProtKB:Q14694}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P52479-1; Sequence=Displayed;
Name=2;
IsoId=P52479-2; Sequence=VSP_038870;
-!- PTM: Phosphorylated by ATM following DNA damage, leading to
stablization and translocation it to the nucleus. {ECO:0000250}.
-!- PTM: Ubiquitinated. Deubiquitinated by USP13 (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C19 family. USP10 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC97893.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; D84096; BAA12220.1; -; mRNA.
EMBL; AK129083; BAC97893.1; ALT_INIT; mRNA.
EMBL; AK153675; BAE32139.1; -; mRNA.
EMBL; AK157970; BAE34291.1; -; mRNA.
EMBL; AK165156; BAE38053.1; -; mRNA.
EMBL; AK172443; BAE43006.1; -; mRNA.
EMBL; CH466525; EDL11620.1; -; Genomic_DNA.
EMBL; BC007134; AAH07134.1; -; mRNA.
CCDS; CCDS40495.1; -. [P52479-2]
CCDS; CCDS80938.1; -. [P52479-1]
RefSeq; NP_001297559.1; NM_001310630.1. [P52479-1]
RefSeq; NP_033488.1; NM_009462.2. [P52479-2]
UniGene; Mm.256910; -.
UniGene; Mm.421337; -.
ProteinModelPortal; P52479; -.
BioGrid; 204424; 8.
IntAct; P52479; 7.
MINT; P52479; -.
STRING; 10090.ENSMUSP00000123590; -.
MEROPS; C19.018; -.
iPTMnet; P52479; -.
PhosphoSitePlus; P52479; -.
MaxQB; P52479; -.
PaxDb; P52479; -.
PeptideAtlas; P52479; -.
PRIDE; P52479; -.
DNASU; 22224; -.
Ensembl; ENSMUST00000108988; ENSMUSP00000104616; ENSMUSG00000031826. [P52479-1]
Ensembl; ENSMUST00000144458; ENSMUSP00000123590; ENSMUSG00000031826. [P52479-2]
GeneID; 22224; -.
KEGG; mmu:22224; -.
UCSC; uc009nqn.1; mouse. [P52479-2]
UCSC; uc009nqo.1; mouse. [P52479-1]
CTD; 9100; -.
MGI; MGI:894652; Usp10.
eggNOG; KOG1871; Eukaryota.
eggNOG; ENOG410XSIH; LUCA.
GeneTree; ENSGT00550000074994; -.
HOVERGEN; HBG059823; -.
InParanoid; P52479; -.
KO; K11841; -.
OMA; GQEYQRI; -.
OrthoDB; EOG091G023X; -.
PhylomeDB; P52479; -.
TreeFam; TF323203; -.
Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
ChiTaRS; Usp10; mouse.
PRO; PR:P52479; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031826; -.
CleanEx; MM_USP10; -.
ExpressionAtlas; P52479; baseline and differential.
Genevisible; P52479; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005769; C:early endosome; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0044325; F:ion channel binding; ISS:UniProtKB.
GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; ISS:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; ISS:UniProtKB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
InterPro; IPR009818; Ataxin-2_C.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF07145; PAM2; 1.
Pfam; PF00443; UCH; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Autophagy; Complete proteome;
Cytoplasm; DNA damage; DNA repair; Endosome; Hydrolase; Nucleus;
Phosphoprotein; Protease; Reference proteome; Thiol protease;
Ubl conjugation; Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q14694}.
CHAIN 2 792 Ubiquitin carboxyl-terminal hydrolase 10.
/FTId=PRO_0000080630.
DOMAIN 409 789 USP.
REGION 2 99 Interaction with p53/TP53. {ECO:0000250}.
ACT_SITE 418 418 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
ACT_SITE 743 743 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q14694}.
MOD_RES 24 24 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14694}.
MOD_RES 208 208 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000250|UniProtKB:Q14694}.
MOD_RES 330 330 Phosphoserine; by ATM.
{ECO:0000250|UniProtKB:Q14694}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:21183079}.
MOD_RES 364 364 Phosphoserine.
{ECO:0000250|UniProtKB:Q14694}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000250|UniProtKB:Q14694}.
MOD_RES 566 566 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 49 49 D -> DA (in isoform 2).
{ECO:0000303|PubMed:16141072,
ECO:0000303|Ref.1}.
/FTId=VSP_038870.
CONFLICT 72 72 P -> R (in Ref. 5; AAH07134).
{ECO:0000305}.
CONFLICT 101 101 E -> D (in Ref. 5; AAH07134).
{ECO:0000305}.
CONFLICT 293 293 N -> S (in Ref. 5; AAH07134).
{ECO:0000305}.
CONFLICT 347 347 A -> S (in Ref. 5; AAH07134).
{ECO:0000305}.
CONFLICT 448 448 R -> G (in Ref. 3; BAE34291).
{ECO:0000305}.
CONFLICT 472 472 P -> T (in Ref. 3; BAE32139).
{ECO:0000305}.
CONFLICT 528 528 G -> R (in Ref. 3; BAE38053).
{ECO:0000305}.
SEQUENCE 792 AA; 87022 MW; 02D07A8194215D09 CRC64;
MALHNPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTLCS IQAEDELPDG QEHQRIEFGV
DEVIEPSEGL PPTPSYSISS TLNPQAPEFI LGCTTSKKIP EAVEKDETYS SIDQYPASAL
ALESNSNAEA ETLENDSGAG GLGQRERKKK KKRPPGYYSY LKDGGEDSAS PATLVNGHAT
SVGTSGEAVE DAEFMDVLPP VMPRTCDSPQ NPVDFISGPV PDSPFPRTLG GDARTAGLCE
GCHEADFEQP CLPADSLLRT AGTQPYVGTD TTENFAVANG KILESPGEDT AANGAELHTD
EGADLDPAKP ESQSPPAESA LSASGAIPIS QPAKSWASLF HDSKPSASSP MAYVETKCSP
PVPSPLASEK QMEVKEGLVP VSEDPVAIKI AELLETVTLI HKPVSLQPRG LINKGNWCYI
NATLQALVAC PPMYHLMKFI PLYSKVQRPC TSTPMIDSFV RLMNEFTNMP VPPKPRQALG
DKIVRDIRPG AAFEPTYIYR LLTVIKSSLS EKGRQEDAEE YLGFILNGLH EEMLSLKKLL
SPTHEKHSVS NGPRSDLIED EELEDTGKGS EDEWEQVGPK NKTSITRQAD FVQTPITGIF
GGHIRSVVYQ QSSKESATLQ LFFTLQLDIQ SDKIRTVQDA LESLVARESV QGYTTKTKQE
VEVSRRVTLE KLPPVLVLHL KRFVYEKTGG CQKLVKNIDY PVDLEISREL LSPGIKNKNF
KCQRTYRLFA VVYHHGNSAT GGHYTTDVFQ IGLNGWLRID DQTVKVINQY QVVKPPADRT
AYLLYYRRVD LL


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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


 

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