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Ubiquitin carboxyl-terminal hydrolase 46 (EC 3.4.19.12) (Deubiquitinating enzyme 46) (Ubiquitin thioesterase 46) (Ubiquitin-specific-processing protease 46)

 UBP46_HUMAN             Reviewed;         366 AA.
P62068; B7Z3Y7; B7Z675; B7Z7S3; G8ACC7; Q80V95; Q9H7U4; Q9H9T8;
21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
21-JUN-2004, sequence version 1.
12-SEP-2018, entry version 121.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 46;
EC=3.4.19.12 {ECO:0000269|PubMed:14715245, ECO:0000269|PubMed:19075014, ECO:0000269|PubMed:26388029};
AltName: Full=Deubiquitinating enzyme 46;
AltName: Full=Ubiquitin thioesterase 46;
AltName: Full=Ubiquitin-specific-processing protease 46;
Name=USP46;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, ACTIVE
SITE, AND MUTAGENESIS OF CYS-44.
PubMed=22043315; DOI=10.1371/journal.pone.0026297;
Zhang W., Tian Q.B., Li Q.K., Wang J.M., Wang C.N., Liu T., Liu D.W.,
Wang M.W.;
"Lysine 92 amino acid residue of USP46, a gene associated with
'behavioral despair' in mice, influences the deubiquitinating enzyme
activity.";
PLoS ONE 6:E26297-E26297(2011).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Brain, Placenta, Teratocarcinoma, Testis, and Thalamus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
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).
[5]
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION, AND
INTERACTION WITH WDR48.
PubMed=19075014; DOI=10.1074/jbc.M808430200;
Cohn M.A., Kee Y., Haas W., Gygi S.P., D'Andrea A.D.;
"UAF1 is a subunit of multiple deubiquitinating enzyme complexes.";
J. Biol. Chem. 284:5343-5351(2009).
[7]
INTERACTION WITH WRD20.
PubMed=20147737; DOI=10.1074/jbc.M109.095141;
Kee Y., Yang K., Cohn M.A., Haas W., Gygi S.P., D'Andrea A.D.;
"WDR20 regulates activity of the USP12 x UAF1 deubiquitinating enzyme
complex.";
J. Biol. Chem. 285:11252-11257(2010).
[8] {ECO:0000244|PDB:5CVM, ECO:0000244|PDB:5CVN, ECO:0000244|PDB:5CVO}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 25-366 IN COMPLEXES WITH
WDR48 AND UBIQUITIN, ZINC-BINDING, INTERACTION WITH WDR48, FUNCTION,
ACTIVITY REGULATION, ACTIVE SITE, CATALYTIC ACTIVITY, AND MUTAGENESIS
OF CYS-44.
PubMed=26388029; DOI=10.1016/j.str.2015.08.010;
Yin J., Schoeffler A.J., Wickliffe K., Newton K., Starovasnik M.A.,
Dueber E.C., Harris S.F.;
"Structural insights into WD-repeat 48 activation of ubiquitin-
specific protease 46.";
Structure 23:2043-2054(2015).
[9] {ECO:0000244|PDB:5L8H}
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 8-366 IN COMPLEX WITH
UBIQUITIN, AND ZINC-BINDING.
PubMed=27650958; DOI=10.1016/j.jsb.2016.09.011;
Dharadhar S., Clerici M., van Dijk W.J., Fish A., Sixma T.K.;
"A conserved two-step binding for the UAF1 regulator to the USP12
deubiquitinating enzyme.";
J. Struct. Biol. 196:437-447(2016).
-!- FUNCTION: Deubiquitinating enzyme that plays a role in behavior,
possibly by regulating GABA action. May act by mediating the
deubiquitination of GAD1/GAD67 (By similarity). Has almost no
deubiquitinating activity by itself and requires the interaction
with WDR48 to have a high activity (PubMed:19075014,
PubMed:26388029). Not involved in deubiquitination of
monoubiquitinated FANCD2 (PubMed:19075014).
{ECO:0000250|UniProtKB:P62069, ECO:0000269|PubMed:19075014,
ECO:0000269|PubMed:26388029}.
-!- 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:0000269|PubMed:14715245, ECO:0000269|PubMed:19075014,
ECO:0000269|PubMed:26388029}.
-!- ACTIVITY REGULATION: Activated by interaction with WDR48.
{ECO:0000269|PubMed:26388029}.
-!- SUBUNIT: Interacts with WDR48 (PubMed:19075014, PubMed:26388029).
Interacts with WDR20 (PubMed:20147737).
{ECO:0000269|PubMed:19075014, ECO:0000269|PubMed:20147737,
ECO:0000269|PubMed:26388029}.
-!- INTERACTION:
Q8TBZ3:WDR20; NbExp=3; IntAct=EBI-2512753, EBI-2511486;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P62068-1; Sequence=Displayed;
Name=2;
IsoId=P62068-2; Sequence=VSP_037618, VSP_037621;
Note=No experimental confirmation available.;
Name=3;
IsoId=P62068-3; Sequence=VSP_037619;
Note=No experimental confirmation available.;
Name=4;
IsoId=P62068-4; Sequence=VSP_037620;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Broadly expressed.
{ECO:0000269|PubMed:14715245}.
-!- SIMILARITY: Belongs to the peptidase C19 family. USP12/USP46
subfamily. {ECO:0000305}.
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EMBL; GU455414; ADV57651.1; -; mRNA.
EMBL; AK022614; BAB14133.1; -; mRNA.
EMBL; AK024318; BAB14881.1; -; mRNA.
EMBL; AK296493; BAH12373.1; -; mRNA.
EMBL; AK299883; BAH13161.1; -; mRNA.
EMBL; AK302438; BAH13709.1; -; mRNA.
EMBL; CH471057; EAX05435.1; -; Genomic_DNA.
EMBL; BC037574; AAH37574.1; -; mRNA.
CCDS; CCDS47053.1; -. [P62068-1]
CCDS; CCDS47054.1; -. [P62068-3]
RefSeq; NP_001127695.1; NM_001134223.1. [P62068-3]
RefSeq; NP_001273696.1; NM_001286767.1. [P62068-4]
RefSeq; NP_001273697.1; NM_001286768.1. [P62068-2]
RefSeq; NP_073743.2; NM_022832.3. [P62068-1]
UniGene; Hs.7966; -.
PDB; 5CVM; X-ray; 1.90 A; A=25-366.
PDB; 5CVN; X-ray; 3.36 A; B=25-366.
PDB; 5CVO; X-ray; 3.88 A; B/E=25-366.
PDB; 5L8H; X-ray; 1.85 A; A=8-366.
PDBsum; 5CVM; -.
PDBsum; 5CVN; -.
PDBsum; 5CVO; -.
PDBsum; 5L8H; -.
ProteinModelPortal; P62068; -.
SMR; P62068; -.
BioGrid; 122327; 40.
CORUM; P62068; -.
DIP; DIP-53590N; -.
IntAct; P62068; 20.
STRING; 9606.ENSP00000407818; -.
MEROPS; C19.052; -.
PhosphoSitePlus; P62068; -.
BioMuta; USP46; -.
DMDM; 49065850; -.
EPD; P62068; -.
MaxQB; P62068; -.
PaxDb; P62068; -.
PeptideAtlas; P62068; -.
PRIDE; P62068; -.
ProteomicsDB; 57356; -.
ProteomicsDB; 57357; -. [P62068-2]
ProteomicsDB; 57358; -. [P62068-3]
ProteomicsDB; 57359; -. [P62068-4]
DNASU; 64854; -.
Ensembl; ENST00000441222; ENSP00000407818; ENSG00000109189. [P62068-1]
Ensembl; ENST00000508499; ENSP00000423244; ENSG00000109189. [P62068-3]
GeneID; 64854; -.
KEGG; hsa:64854; -.
UCSC; uc003gzm.5; human. [P62068-1]
CTD; 64854; -.
DisGeNET; 64854; -.
EuPathDB; HostDB:ENSG00000109189.12; -.
GeneCards; USP46; -.
HGNC; HGNC:20075; USP46.
HPA; CAB076369; -.
HPA; CAB076370; -.
HPA; HPA007288; -.
MIM; 612849; gene.
neXtProt; NX_P62068; -.
OpenTargets; ENSG00000109189; -.
PharmGKB; PA134922048; -.
eggNOG; KOG1864; Eukaryota.
eggNOG; ENOG410XQ81; LUCA.
GeneTree; ENSGT00890000139367; -.
HOVERGEN; HBG054038; -.
InParanoid; P62068; -.
KO; K11842; -.
OMA; SYKAQQK; -.
OrthoDB; EOG091G0FC5; -.
PhylomeDB; P62068; -.
TreeFam; TF314144; -.
ChiTaRS; USP46; human.
GenomeRNAi; 64854; -.
PRO; PR:P62068; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109189; Expressed in 225 organ(s), highest expression level in substantia nigra.
CleanEx; HS_USP46; -.
ExpressionAtlas; P62068; baseline and differential.
Genevisible; P62068; HS.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IDA:UniProtKB.
GO; GO:0008343; P:adult feeding behavior; IEA:Ensembl.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISS:UniProtKB.
GO; GO:0060013; P:righting reflex; IEA:Ensembl.
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;
3D-structure; Alternative splicing; Behavior; Complete proteome;
Hydrolase; Metal-binding; Polymorphism; Protease; Reference proteome;
Thiol protease; Ubl conjugation pathway; Zinc.
CHAIN 1 366 Ubiquitin carboxyl-terminal hydrolase 46.
/FTId=PRO_0000080674.
DOMAIN 35 365 USP.
ACT_SITE 44 44 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093,
ECO:0000269|PubMed:26388029,
ECO:0000305|PubMed:22043315}.
ACT_SITE 313 313 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
METAL 182 182 Zinc. {ECO:0000244|PDB:5CVM,
ECO:0000244|PDB:5CVN,
ECO:0000244|PDB:5CVO,
ECO:0000244|PDB:5L8H}.
METAL 185 185 Zinc. {ECO:0000244|PDB:5CVM,
ECO:0000244|PDB:5CVN,
ECO:0000244|PDB:5CVO,
ECO:0000244|PDB:5L8H}.
METAL 229 229 Zinc. {ECO:0000244|PDB:5CVM,
ECO:0000244|PDB:5CVN,
ECO:0000244|PDB:5CVO,
ECO:0000244|PDB:5L8H}.
METAL 232 232 Zinc. {ECO:0000244|PDB:5CVM,
ECO:0000244|PDB:5CVN,
ECO:0000244|PDB:5CVO,
ECO:0000244|PDB:5L8H}.
VAR_SEQ 1 116 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037618.
VAR_SEQ 1 12 MTVRNIASICNM -> MNCFQ (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037619.
VAR_SEQ 40 51 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037620.
VAR_SEQ 334 366 KIDAQAIEEFYGLTSDISKNSESGYILFYQSRE -> VGLQ
IILQ (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037621.
VARIANT 81 81 A -> V (in dbSNP:rs17475800).
/FTId=VAR_051540.
MUTAGEN 44 44 C->S: Abolishes enzyme activity.
{ECO:0000269|PubMed:22043315,
ECO:0000269|PubMed:26388029}.
CONFLICT 177 177 T -> A (in Ref. 2; BAH13161).
{ECO:0000305}.
CONFLICT 250 250 I -> V (in Ref. 2; BAB14133).
{ECO:0000305}.
CONFLICT 265 265 H -> R (in Ref. 2; BAB14133).
{ECO:0000305}.
STRAND 34 37 {ECO:0000244|PDB:5L8H}.
STRAND 40 42 {ECO:0000244|PDB:5L8H}.
HELIX 44 54 {ECO:0000244|PDB:5L8H}.
HELIX 57 69 {ECO:0000244|PDB:5L8H}.
HELIX 76 89 {ECO:0000244|PDB:5L8H}.
STRAND 91 97 {ECO:0000244|PDB:5L8H}.
HELIX 100 109 {ECO:0000244|PDB:5L8H}.
HELIX 111 113 {ECO:0000244|PDB:5L8H}.
STRAND 114 117 {ECO:0000244|PDB:5L8H}.
HELIX 121 140 {ECO:0000244|PDB:5L8H}.
HELIX 167 172 {ECO:0000244|PDB:5L8H}.
STRAND 174 182 {ECO:0000244|PDB:5L8H}.
TURN 183 185 {ECO:0000244|PDB:5L8H}.
STRAND 188 200 {ECO:0000244|PDB:5L8H}.
STRAND 204 207 {ECO:0000244|PDB:5L8H}.
HELIX 208 215 {ECO:0000244|PDB:5L8H}.
STRAND 219 221 {ECO:0000244|PDB:5L8H}.
HELIX 223 225 {ECO:0000244|PDB:5L8H}.
STRAND 227 229 {ECO:0000244|PDB:5L8H}.
TURN 230 233 {ECO:0000244|PDB:5L8H}.
STRAND 234 236 {ECO:0000244|PDB:5L8H}.
STRAND 238 246 {ECO:0000244|PDB:5L8H}.
STRAND 249 255 {ECO:0000244|PDB:5L8H}.
STRAND 258 261 {ECO:0000244|PDB:5L8H}.
TURN 262 265 {ECO:0000244|PDB:5L8H}.
STRAND 266 269 {ECO:0000244|PDB:5L8H}.
STRAND 278 283 {ECO:0000244|PDB:5L8H}.
STRAND 286 290 {ECO:0000244|PDB:5CVN}.
STRAND 293 311 {ECO:0000244|PDB:5L8H}.
STRAND 313 320 {ECO:0000244|PDB:5L8H}.
STRAND 323 328 {ECO:0000244|PDB:5L8H}.
STRAND 331 335 {ECO:0000244|PDB:5L8H}.
HELIX 337 344 {ECO:0000244|PDB:5L8H}.
STRAND 346 349 {ECO:0000244|PDB:5L8H}.
STRAND 354 364 {ECO:0000244|PDB:5L8H}.
SEQUENCE 366 AA; 42442 MW; 67BB113FC4081C46 CRC64;
MTVRNIASIC NMGTNASALE KDIGPEQFPI NEHYFGLVNF GNTCYCNSVL QALYFCRPFR
ENVLAYKAQQ KKKENLLTCL ADLFHSIATQ KKKVGVIPPK KFISRLRKEN DLFDNYMQQD
AHEFLNYLLN TIADILQEEK KQEKQNGKLK NGNMNEPAEN NKPELTWVHE IFQGTLTNET
RCLNCETVSS KDEDFLDLSV DVEQNTSITH CLRDFSNTET LCSEQKYYCE TCCSKQEAQK
RMRVKKLPMI LALHLKRFKY MEQLHRYTKL SYRVVFPLEL RLFNTSSDAV NLDRMYDLVA
VVVHCGSGPN RGHYITIVKS HGFWLLFDDD IVEKIDAQAI EEFYGLTSDI SKNSESGYIL
FYQSRE


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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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