U17PB_MOUSE
ID U17PB_MOUSE Reviewed; 468 AA.
AC E9Q9U0; B7ZN74; E9QMF1; Q6X3X0;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17-like protein B {ECO:0000305};
DE Short=USP17-B {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000269|PubMed:14583620};
DE AltName: Full=Deubiquitinating enzyme 1A {ECO:0000303|PubMed:14583620};
GN Name=Usp17lb {ECO:0000312|MGI:MGI:3051498};
GN Synonyms=Dub1a {ECO:0000303|PubMed:14583620};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:AAP81046.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVE SITE, ACTIVITY REGULATION, TISSUE SPECIFICITY, INDUCTION,
RP UBIQUITINATION, AND MUTAGENESIS OF CYS-60.
RX PubMed=14583620; DOI=10.1074/jbc.m304774200;
RA Baek K.H., Kim M.S., Kim Y.S., Shin J.M., Choi H.K.;
RT "DUB-1A, a novel deubiquitinating enzyme subfamily member, is
RT polyubiquitinated and cytokine-inducible in B-lymphocytes.";
RL J. Biol. Chem. 279:2368-2376(2004).
RN [2] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000312|EMBL:AAI45059.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:AAI45059.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000269|PubMed:14583620}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:14583620};
CC -!- ACTIVITY REGULATION: Inhibited by ubiquitin aldehyde.
CC {ECO:0000269|PubMed:14583620}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E9Q9U0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9Q9U0-2; Sequence=VSP_058560;
CC -!- TISSUE SPECIFICITY: Detected in brain, heart, liver, lung, kidney,
CC ovary and spleen. {ECO:0000269|PubMed:14583620}.
CC -!- INDUCTION: Up-regulated by interleukin-3 (IL-3) in the B-lymphocyte
CC cell line Ba/F3. May also be up-regulated in response to JAK2.
CC {ECO:0000269|PubMed:14583620}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:14583620}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP17 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY257250; AAP81046.1; -; mRNA.
DR EMBL; AC110621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137942; AAI37943.1; -; mRNA.
DR EMBL; BC145058; AAI45059.1; -; mRNA.
DR CCDS; CCDS21628.1; -. [E9Q9U0-1]
DR CCDS; CCDS90298.1; -. [E9Q9U0-2]
DR RefSeq; NP_958811.2; NM_201409.2. [E9Q9U0-1]
DR RefSeq; XP_011240140.1; XM_011241838.1.
DR AlphaFoldDB; E9Q9U0; -.
DR SMR; E9Q9U0; -.
DR STRING; 10090.ENSMUSP00000075822; -.
DR MEROPS; C19.085; -.
DR iPTMnet; E9Q9U0; -.
DR PhosphoSitePlus; E9Q9U0; -.
DR PaxDb; E9Q9U0; -.
DR PRIDE; E9Q9U0; -.
DR DNASU; 381944; -.
DR Ensembl; ENSMUST00000076501; ENSMUSP00000075822; ENSMUSG00000062369. [E9Q9U0-1]
DR Ensembl; ENSMUST00000106814; ENSMUSP00000102427; ENSMUSG00000062369. [E9Q9U0-2]
DR GeneID; 381944; -.
DR KEGG; mmu:381944; -.
DR UCSC; uc009iwy.1; mouse. [E9Q9U0-1]
DR CTD; 381944; -.
DR MGI; MGI:3051498; Usp17lb.
DR VEuPathDB; HostDB:ENSMUSG00000062369; -.
DR eggNOG; KOG1865; Eukaryota.
DR GeneTree; ENSGT00940000162665; -.
DR HOGENOM; CLU_008279_10_0_1; -.
DR InParanoid; E9Q9U0; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; E9Q9U0; -.
DR TreeFam; TF315281; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 381944; 2 hits in 71 CRISPR screens.
DR PRO; PR:E9Q9U0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9Q9U0; protein.
DR Bgee; ENSMUSG00000062369; Expressed in morula and 2 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IDA:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..468
FT /note="Ubiquitin carboxyl-terminal hydrolase 17-like
FT protein B"
FT /id="PRO_0000437666"
FT DOMAIN 51..348
FT /note="USP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 60
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035,
FT ECO:0000305|PubMed:14583620"
FT ACT_SITE 307
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT VAR_SEQ 10
FT /note="Missing (in isoform 2)"
FT /id="VSP_058560"
FT MUTAGEN 60
FT /note="C->S: Loss of deubiquitinating activity."
FT /evidence="ECO:0000269|PubMed:14583620"
FT CONFLICT 121
FT /note="N -> I (in Ref. 3; AAI37943/AAI45059)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="Missing (in Ref. 1; AAP81046)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="K -> E (in Ref. 3; AAI37943/AAI45059)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="E -> Q (in Ref. 3; AAI37943/AAI45059)"
FT /evidence="ECO:0000305"
FT CONFLICT 454..457
FT /note="LSGA -> PS (in Ref. 1; AAP81046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 52114 MW; B887AD560A813CA8 CRC64;
MVVALSFPEA DPAMSPPSAP ELHQDEAQVV EELAANGKHS LSWESPQGPG CGLQNTGNSC
YLNAALQCLT HTPPLADYML SQEHSQTCCS PEGCKMCAME AHVTQSLLHT HSGDVMKPSQ
NLTSAFHKRK QEDAHEFLMF TLETMHESCL QVHRQSEPTS EDSSPIHDIF GGWWRSQIKC
HHCQGTSYSY DPFLDIPLDI SSVQSVKQAL QDTEKAEELC GENSYYCGRC RQKKPASKTL
KLYSAPKVLM LVLKRFSGSM GKKLDRKVSY PEFLDLKPYL SQPTGGPLPY ALYAVLVHEG
ATCHSGHYFC CVKAGHGKWY KMDDTKVTSC DVTSVLNENA YVLFYVQQND LKKGSINMPE
GRIHEVLDAK YQLKKSGEKK HNKSPCTEDA GEPCENREKR SSKETSLGEG KVLQEQDHQK
AGQKQENTKL TPQEQNHEKG GQNLRNTEGE LDRLSGAIVV YQPICTAN
