OTUB2_MOUSE
ID OTUB2_MOUSE Reviewed; 234 AA.
AC Q9CQX0; Q3TUZ2; Q9D4K8;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ubiquitin thioesterase OTUB2;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q96DC9};
DE AltName: Full=Deubiquitinating enzyme OTUB2;
DE AltName: Full=OTU domain-containing ubiquitin aldehyde-binding protein 2;
DE AltName: Full=Otubain-2;
DE AltName: Full=Ubiquitin-specific-processing protease OTUB2;
GN Name=Otub2;
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].
RC STRAIN=C57BL/6J; TISSUE=Testis, and Tongue;
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].
RC TISSUE=Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC in vitro and may therefore play an important regulatory role at the
CC level of protein turnover by preventing degradation. Mediates
CC deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked
CC polyubiquitin chains, with a preference for 'Lys-63'-linked
CC polyubiquitin chains (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; Evidence={ECO:0000250|UniProtKB:Q96DC9};
CC -!- SIMILARITY: Belongs to the peptidase C65 family. {ECO:0000305}.
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DR EMBL; AK006054; BAB24385.1; -; mRNA.
DR EMBL; AK006346; BAB24539.1; -; mRNA.
DR EMBL; AK006469; BAB24603.1; -; mRNA.
DR EMBL; AK019830; BAB31872.1; -; mRNA.
DR EMBL; AK160505; BAE35829.1; -; mRNA.
DR EMBL; BC049551; AAH49551.1; -; mRNA.
DR CCDS; CCDS36528.1; -.
DR RefSeq; NP_001171312.1; NM_001177841.1.
DR RefSeq; NP_080856.1; NM_026580.4.
DR AlphaFoldDB; Q9CQX0; -.
DR SMR; Q9CQX0; -.
DR STRING; 10090.ENSMUSP00000021620; -.
DR iPTMnet; Q9CQX0; -.
DR PhosphoSitePlus; Q9CQX0; -.
DR MaxQB; Q9CQX0; -.
DR PaxDb; Q9CQX0; -.
DR PRIDE; Q9CQX0; -.
DR ProteomicsDB; 295490; -.
DR Antibodypedia; 103; 420 antibodies from 33 providers.
DR DNASU; 68149; -.
DR Ensembl; ENSMUST00000021620; ENSMUSP00000021620; ENSMUSG00000021203.
DR GeneID; 68149; -.
DR KEGG; mmu:68149; -.
DR UCSC; uc007ovg.2; mouse.
DR CTD; 78990; -.
DR MGI; MGI:1915399; Otub2.
DR VEuPathDB; HostDB:ENSMUSG00000021203; -.
DR eggNOG; KOG3991; Eukaryota.
DR GeneTree; ENSGT00390000006979; -.
DR HOGENOM; CLU_014832_3_2_1; -.
DR InParanoid; Q9CQX0; -.
DR OMA; EAPDLHV; -.
DR OrthoDB; 1257066at2759; -.
DR PhylomeDB; Q9CQX0; -.
DR TreeFam; TF314145; -.
DR Reactome; R-MMU-5689896; Ovarian tumor domain proteases.
DR BioGRID-ORCS; 68149; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Otub2; mouse.
DR PRO; PR:Q9CQX0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9CQX0; protein.
DR Bgee; ENSMUSG00000021203; Expressed in seminiferous tubule of testis and 208 other tissues.
DR ExpressionAtlas; Q9CQX0; baseline and differential.
DR Genevisible; Q9CQX0; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:2000780; P:negative regulation of double-strand break repair; IBA:GO_Central.
DR GO; GO:1901315; P:negative regulation of histone H2A K63-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR Gene3D; 1.20.1300.20; -; 1.
DR Gene3D; 3.30.200.60; -; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR030299; OTUB2.
DR InterPro; IPR016615; Otubain.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR019400; Peptidase_C65_otubain.
DR InterPro; IPR042468; Peptidase_C65_otubain_sub1.
DR InterPro; IPR042467; Peptidase_C65_otubain_sub2.
DR PANTHER; PTHR12931; PTHR12931; 1.
DR PANTHER; PTHR12931:SF3; PTHR12931:SF3; 1.
DR Pfam; PF10275; Peptidase_C65; 1.
DR PIRSF; PIRSF013503; Ubiquitin_thioesterase_Otubain; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..234
FT /note="Ubiquitin thioesterase OTUB2"
FT /id="PRO_0000221011"
FT DOMAIN 40..231
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT ACT_SITE 48
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT ACT_SITE 51
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT ACT_SITE 205
FT /evidence="ECO:0000250|UniProtKB:Q96FW1"
FT ACT_SITE 224
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
FT SITE 226
FT /note="Required to orient and stabilize the active site H-
FT 224"
FT /evidence="ECO:0000250|UniProtKB:Q96DC9"
SQ SEQUENCE 234 AA; 27300 MW; 4BE469C91CE4EAD4 CRC64;
MSETSFNLIS EKCDILSILR DHPENRIYQR KIQELSKRFT SIRKTKGDGN CFYRALGYSY
LESLLGKSRE ILKFKERVLQ TPNDLLAAGF EEHKFRNFFN AFYSVVELVE KDSSVSSLLK
VFNDQSSSDR IVQFLRLLTS AFIRNRADFF RHFIDEEMDI KDFCTHEVEP MAMECDHVQI
TALSQALNIA LQVEYVDEMD TALNHHVFPE AAIPSVYLLY KTSHYNILYA AEKH
