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 27-MAR-2024, entry version 139. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000024779; -. DR ProteomicsDB; 297709; -. DR Antibodypedia; 35153; 115 antibodies from 23 providers. DR DNASU; 224836; -. DR Ensembl; ENSMUST00000024779.15; ENSMUSP00000024779.9; ENSMUSG00000090115.8. DR GeneID; 224836; -. DR KEGG; mmu:224836; -. DR UCSC; uc008cvv.1; mouse. DR AGR; MGI:2685391; -. 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; AWACLKC; -. DR OrthoDB; 227085at2759; -. DR PhylomeDB; Q6P9L4; -. DR TreeFam; TF315281; -. DR BioGRID-ORCS; 224836; 3 hits in 79 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 65 other cell types or tissues. DR ExpressionAtlas; Q6P9L4; baseline and differential. 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:0140936; F:histone H2B deubiquitinase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR21646:SF7; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 49; 1. DR Pfam; PF00443; UCH; 1. DR Pfam; PF02148; zf-UBP; 1. DR SMART; SM00290; ZnF_UBP; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF57850; RING/U-box; 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. DR Genevisible; Q6P9L4; MM. 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 //