DESI2_MOUSE
ID DESI2_MOUSE Reviewed; 194 AA.
AC Q9D291; Q3TUJ4;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Deubiquitinase DESI2 {ECO:0000250|UniProtKB:Q9BSY9};
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q9BSY9};
DE AltName: Full=Desumoylating isopeptidase 2;
DE Short=DeSI-2;
DE AltName: Full=PPPDE peptidase domain-containing protein 1;
DE AltName: Full=Protein FAM152A;
GN Name=Desi2; Synonyms=Fam152a, Pppde1;
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=Head, and Thymus;
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 STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
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).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22370726; DOI=10.1038/embor.2012.3;
RA Shin E.J., Shin H.M., Nam E., Kim W.S., Kim J.H., Oh B.H., Yun Y.;
RT "DeSUMOylating isopeptidase: a second class of SUMO protease.";
RL EMBO Rep. 13:339-346(2012).
CC -!- FUNCTION: Has deubiquitinating activity towards 'Lys-48'- and 'Lys-63'-
CC linked polyubiquitin chains. Deubiquitinates 'Lys-48'-linked
CC polyubiquitination of RPS7 leading to its stabilization.
CC {ECO:0000250|UniProtKB:Q9BSY9}.
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:Q9BSY9};
CC -!- SUBUNIT: Interacts with RPS7. {ECO:0000250|UniProtKB:Q9BSY9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22370726}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:22370726}.
CC -!- SIMILARITY: Belongs to the DeSI family. {ECO:0000305}.
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DR EMBL; AK020014; BAB31967.1; -; mRNA.
DR EMBL; AK049579; BAC33822.1; -; mRNA.
DR EMBL; AK160733; BAE35977.1; -; mRNA.
DR EMBL; BC002200; AAH02200.1; -; mRNA.
DR EMBL; BC046816; AAH46816.1; -; mRNA.
DR CCDS; CCDS35803.1; -.
DR RefSeq; NP_077244.1; NM_024282.3.
DR AlphaFoldDB; Q9D291; -.
DR SMR; Q9D291; -.
DR BioGRID; 219660; 2.
DR STRING; 10090.ENSMUSP00000027783; -.
DR MEROPS; C97.002; -.
DR iPTMnet; Q9D291; -.
DR PhosphoSitePlus; Q9D291; -.
DR SwissPalm; Q9D291; -.
DR EPD; Q9D291; -.
DR MaxQB; Q9D291; -.
DR PaxDb; Q9D291; -.
DR PRIDE; Q9D291; -.
DR ProteomicsDB; 279629; -.
DR Antibodypedia; 34714; 120 antibodies from 31 providers.
DR DNASU; 78825; -.
DR Ensembl; ENSMUST00000027783; ENSMUSP00000027783; ENSMUSG00000026502.
DR GeneID; 78825; -.
DR KEGG; mmu:78825; -.
DR UCSC; uc007dux.1; mouse.
DR CTD; 51029; -.
DR MGI; MGI:1926075; Desi2.
DR VEuPathDB; HostDB:ENSMUSG00000026502; -.
DR eggNOG; KOG0324; Eukaryota.
DR GeneTree; ENSGT00730000111005; -.
DR InParanoid; Q9D291; -.
DR OMA; GVYWTRP; -.
DR OrthoDB; 1300278at2759; -.
DR PhylomeDB; Q9D291; -.
DR TreeFam; TF313188; -.
DR BioGRID-ORCS; 78825; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Desi2; mouse.
DR PRO; PR:Q9D291; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9D291; protein.
DR Bgee; ENSMUSG00000026502; Expressed in animal zygote and 61 other tissues.
DR ExpressionAtlas; Q9D291; baseline and differential.
DR Genevisible; Q9D291; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISO:MGI.
DR GO; GO:0101005; F:deubiquitinase activity; IBA:GO_Central.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0070646; P:protein modification by small protein removal; IBA:GO_Central.
DR Gene3D; 3.90.1720.30; -; 1.
DR InterPro; IPR008580; PPPDE_dom.
DR InterPro; IPR042266; PPPDE_sf.
DR PANTHER; PTHR12378; PTHR12378; 1.
DR Pfam; PF05903; Peptidase_C97; 1.
DR SMART; SM01179; DUF862; 1.
DR PROSITE; PS51858; PPPDE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..194
FT /note="Deubiquitinase DESI2"
FT /id="PRO_0000221631"
FT DOMAIN 5..149
FT /note="PPPDE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT ACT_SITE 30
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT ACT_SITE 108
FT /evidence="ECO:0000250|UniProtKB:Q9BSY9,
FT ECO:0000255|PROSITE-ProRule:PRU01205"
SQ SEQUENCE 194 AA; 21434 MW; 677820432643E922 CRC64;
MGANQLVVLN VYDMYWMNEY TSSIGIGVFH SGIEVYGREF AYGGHPYPFS GIFEISPGNA
SELGETFKFK EAVVLGSTDF LEDDIEKIVE ELGKEYKGNA YHLMHKNCNH FSSALSEILC
GKEIPRWINR LAYFSSCIPF LQSCLPKEWL TPAALQSSVS QELQDELEEA EDAAASSAMA
SAAAGARTGR HTKL
