UBP49_MOUSE
ID UBP49_MOUSE Reviewed; 685 AA.
AC Q6P9L4;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 49;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 49;
DE AltName: Full=Ubiquitin thioesterase 49;
DE AltName: Full=Ubiquitin-specific-processing protease 49;
GN Name=Usp49;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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: Specifically deubiquitinates histone H2B at 'Lys-120'
CC (H2BK120Ub). H2BK120Ub is a specific tag for epigenetic transcriptional
CC activation and acts as a regulator of mRNA splicing. Deubiquitination
CC is required for efficient cotranscriptional splicing of a large set of
CC exons (By similarity). {ECO:0000250}.
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;
CC -!- SUBUNIT: Component of a complex with RUVBL1 and PSMC5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; GL456179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060712; AAH60712.1; -; mRNA.
DR CCDS; CCDS28852.1; -.
DR RefSeq; NP_940813.1; NM_198421.1.
DR AlphaFoldDB; Q6P9L4; -.
DR BioGRID; 230330; 2.
DR STRING; 10090.ENSMUSP00000024779; -.
DR MEROPS; C19.073; -.
DR iPTMnet; Q6P9L4; -.
DR PhosphoSitePlus; Q6P9L4; -.
DR jPOST; Q6P9L4; -.
DR PaxDb; Q6P9L4; -.
DR PRIDE; Q6P9L4; -.
DR ProteomicsDB; 297709; -.
DR Antibodypedia; 35153; 112 antibodies from 23 providers.
DR DNASU; 224836; -.
DR Ensembl; ENSMUST00000024779; ENSMUSP00000024779; ENSMUSG00000090115.
DR GeneID; 224836; -.
DR KEGG; mmu:224836; -.
DR UCSC; uc008cvv.1; mouse.
DR CTD; 25862; -.
DR MGI; MGI:2685391; Usp49.
DR VEuPathDB; HostDB:ENSMUSG00000090115; -.
DR eggNOG; KOG1867; Eukaryota.
DR GeneTree; ENSGT00940000157997; -.
DR HOGENOM; CLU_008279_13_1_1; -.
DR InParanoid; Q6P9L4; -.
DR OMA; LWFERSS; -.
DR OrthoDB; 1230415at2759; -.
DR PhylomeDB; Q6P9L4; -.
DR TreeFam; TF315281; -.
DR BioGRID-ORCS; 224836; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Usp49; mouse.
DR PRO; PR:Q6P9L4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6P9L4; protein.
DR Bgee; ENSMUSG00000090115; Expressed in secondary oocyte and 62 other tissues.
DR ExpressionAtlas; Q6P9L4; baseline and differential.
DR Genevisible; Q6P9L4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035616; P:histone H2B conserved C-terminal lysine deubiquitination; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 1.
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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Hydrolase; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..685
FT /note="Ubiquitin carboxyl-terminal hydrolase 49"
FT /id="PRO_0000080679"
FT DOMAIN 250..654
FT /note="USP"
FT ZN_FING 2..99
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT ACT_SITE 259
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 612
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 4
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
SQ SEQUENCE 685 AA; 78272 MW; 0E090343A481AE29 CRC64;
MDRCKHVGRL RLAQDHSILN PQKWCCLQCA TTESAWACLK CSHVACGRYI EDHALKHFEE
TGHPLAMEVR DLYVFCYLCK DYVLNDNPEG DLKLLRSSLL AVRGQKQDLL ARRGRTLRST
AAGEDVVPPQ RTPQGQPQML TALWYRRQRL LAKTLRLWFQ KSSRGRAQLE QRRQEEALER
KKEAARQRRR EVKRRLLEEL ASAPPRKSAR LLLHAPGPVA VRPATLATSR RLSAAALNPR
RQPAVAPGVT GLRNLGNTCY MNSILQVLSH LQKFRECFLN LDPSTSEHLF PQATNGKAQL
SGRPASSSAA ELSVRSVRAQ GCEPQGLCWS SGASISRSLE LIQNKEPSSK HISLCHELHT
LFRVMWSGKW ALVSPFAMLH SVWSLIPAFR GYDQQDAQEF LCELLHKVQQ ELESEGSTRR
ILIPFSQRKL TKQVLKVVNT IFHGQLLSQV TCISCNYKSN TIEPFWDLSL EFPERYHCIE
KGFVPLNQTE CLLTEMLAKF TETEALEGRI YACDQCNSKR RKSNPKPLVL SEARKQLMIY
RLPQVLRLHL KRFRWSGRNH REKIGVHVIF DQVLTMEPYC CRDMLSSLDK ETFAYDLSAV
VMHHGKGFGS GHYTAYCYNT EGGFWVHCND SKLDVCSVEE VCKTQAYILF YTRRTVQGSA
KLSEPHLQAQ VHSSSKDERR TYTLP
