UBP12_MOUSE
ID UBP12_MOUSE Reviewed; 370 AA.
AC Q9D9M2; Q790B0; Q7TNV4; Q80Y43; Q8CBN8;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 12;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 12;
DE AltName: Full=Ubiquitin thioesterase 12;
DE AltName: Full=Ubiquitin-hydrolyzing enzyme 1;
DE AltName: Full=Ubiquitin-specific-processing protease 12;
GN Name=Usp12; Synonyms=Ubh1;
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 MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Liver;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-370 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=12391724; DOI=10.1080/10425170290023383;
RA Baek K.-H., Park K.-H., Kim Y.-S., Kim M.-S., Choi H.-K.;
RT "Molecular cloning and complete cDNA sequence of UBH1 in mouse testis.";
RL DNA Seq. 13:145-148(2002).
CC -!- FUNCTION: Deubiquitinating enzyme. Has almost no deubiquitinating
CC activity by itself and requires the interaction with WDR48 to have a
CC high activity. Not involved in deubiquitination of monoubiquitinated
CC FANCD2. {ECO:0000250|UniProtKB:O75317}.
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 -!- ACTIVITY REGULATION: Activated by interaction with WDR20 and WDR48
CC through different allosteric mechanisms.
CC {ECO:0000250|UniProtKB:O75317}.
CC -!- SUBUNIT: Interacts with WDR48. Interacts with WDR20. Component of the
CC USP12/WDR20/WDR48 deubiquitinating complex.
CC {ECO:0000250|UniProtKB:O75317}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D9M2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D9M2-2; Sequence=VSP_037617;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP12/USP46 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK006739; BAB24720.2; -; mRNA.
DR EMBL; AK035629; BAC29129.1; -; mRNA.
DR EMBL; AK167153; BAE39295.1; -; mRNA.
DR EMBL; BC049274; AAH49274.1; -; mRNA.
DR EMBL; BC055398; AAH55398.1; -; mRNA.
DR EMBL; BC068136; AAH68136.1; -; mRNA.
DR EMBL; AF441835; AAL86740.1; -; mRNA.
DR CCDS; CCDS39395.1; -. [Q9D9M2-1]
DR RefSeq; NP_035799.1; NM_011669.3. [Q9D9M2-1]
DR RefSeq; XP_006504881.1; XM_006504818.2.
DR AlphaFoldDB; Q9D9M2; -.
DR SMR; Q9D9M2; -.
DR BioGRID; 204419; 6.
DR IntAct; Q9D9M2; 1.
DR STRING; 10090.ENSMUSP00000082754; -.
DR MEROPS; C19.020; -.
DR iPTMnet; Q9D9M2; -.
DR PhosphoSitePlus; Q9D9M2; -.
DR SwissPalm; Q9D9M2; -.
DR EPD; Q9D9M2; -.
DR MaxQB; Q9D9M2; -.
DR PaxDb; Q9D9M2; -.
DR PeptideAtlas; Q9D9M2; -.
DR PRIDE; Q9D9M2; -.
DR ProteomicsDB; 298453; -. [Q9D9M2-1]
DR ProteomicsDB; 298454; -. [Q9D9M2-2]
DR Antibodypedia; 22631; 279 antibodies from 27 providers.
DR DNASU; 22217; -.
DR Ensembl; ENSMUST00000085614; ENSMUSP00000082754; ENSMUSG00000029640. [Q9D9M2-1]
DR GeneID; 22217; -.
DR KEGG; mmu:22217; -.
DR UCSC; uc009anj.1; mouse. [Q9D9M2-1]
DR CTD; 219333; -.
DR MGI; MGI:1270128; Usp12.
DR VEuPathDB; HostDB:ENSMUSG00000029640; -.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00940000153284; -.
DR HOGENOM; CLU_008279_2_0_1; -.
DR InParanoid; Q9D9M2; -.
DR OMA; ATVVHCG; -.
DR OrthoDB; 378361at2759; -.
DR PhylomeDB; Q9D9M2; -.
DR TreeFam; TF314144; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 22217; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Usp12; mouse.
DR PRO; PR:Q9D9M2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D9M2; protein.
DR Bgee; ENSMUSG00000029640; Expressed in retinal neural layer and 239 other tissues.
DR Genevisible; Q9D9M2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:0101005; F:deubiquitinase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; IDA:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc.
FT CHAIN 1..370
FT /note="Ubiquitin carboxyl-terminal hydrolase 12"
FT /id="PRO_0000260312"
FT DOMAIN 39..369
FT /note="USP"
FT REGION 146..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 48
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75317"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75317"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75317"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75317"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037617"
SQ SEQUENCE 370 AA; 42914 MW; B11AC16D9B12EBB8 CRC64;
MEILMTVSKF ASICTMGANA SALEKEIGPE QFPVNEHYFG LVNFGNTCYC NSVLQALYFC
RPFREKVLAY KSQPRKKENL LTCLADLFHS IATQKKKVGV IPPKKFITRL RKENELFDNY
MQQDAHEFLN YLLNTIADIL QEERKQEKQN GRLRNGDVDN EDNNSTPDPT WVHEIFQGTL
TNETRCLTCE TISSKDEDFL DLSVDVEQNT SITHCLRGFS NTETLCSEYK YYCEECRSKQ
EAHKRMKVKK LPLILALHLK RFKYMDQLHR YTKLSYRVVF PLELRLFNTS GDATNPDRMY
DLVAVVVHCG SGPNRGHYIA IVKSHDFWLL FDDDIVEKID AQAIEEFYGL TSDISKNSES
GYILFYQSRD
