ID   UBP19_MOUSE             Reviewed;        1360 AA.
AC   Q3UJD6; Q3TAC9; Q3TUE6; Q6P9T0; Q80TP5; Q80ZW5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 19;
DE            EC=3.1.2.15;
DE   AltName: Full=Ubiquitin thioesterase 19;
DE   AltName: Full=Ubiquitin-specific-processing protease 19;
DE   AltName: Full=Deubiquitinating enzyme 19;
GN   Name=Usp19; Synonyms=Kiaa0891;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, Kidney, and Spleen;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 395-1360 (ISOFORM 2).
RC   STRAIN=C57BL/6; 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in the ubiquitin-dependent proteolytic pathway
CC       in conjunction with the 26S proteasome (By similarity).
CC   -!- CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H(2)O =
CC       ubiquitin + a thiol.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UJD6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UJD6-2; Sequence=VSP_026769, VSP_026770;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 2 CS domains.
CC   -!- SIMILARITY: Contains 1 MYND-type zinc finger.
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DR   EMBL; AK122396; BAC65678.4; ALT_INIT; mRNA.
DR   EMBL; AK146504; BAE27219.1; -; mRNA.
DR   EMBL; AK160807; BAE36025.1; -; mRNA.
DR   EMBL; AK171942; BAE42739.1; -; mRNA.
DR   EMBL; BC046824; AAH46824.1; -; mRNA.
DR   EMBL; BC060613; AAH60613.1; -; mRNA.
DR   IPI; IPI00420483; -.
DR   IPI; IPI00457619; -.
DR   RefSeq; NP_082080.2; -.
DR   UniGene; Mm.289706; -.
DR   SMR; Q3UJD6; 306-439.
DR   MEROPS; C19.024; -.
DR   PhosphoSite; Q3UJD6; -.
DR   PRIDE; Q3UJD6; -.
DR   Ensembl; ENSMUSG00000006676; Mus musculus.
DR   GeneID; 71472; -.
DR   KEGG; mmu:71472; -.
DR   MGI; MGI:1918722; Usp19.
DR   HOGENOM; Q3UJD6; -.
DR   HOVERGEN; Q3UJD6; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 333851; -.
DR   ArrayExpress; Q3UJD6; -.
DR   Bgee; Q3UJD6; -.
DR   CleanEx; MM_USP19; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043161; P:proteasomal ubiquitin-dependent protein cat...; IEA:InterPro.
DR   InterPro; IPR017447; CS.
DR   InterPro; IPR007052; CS_domain.
DR   InterPro; IPR015054; DUF1872.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR002893; Znf_MYND.
DR   Pfam; PF04969; CS; 1.
DR   Pfam; PF08959; DUF1872; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   PROSITE; PS51203; CS; 2.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Metal-binding; Phosphoprotein;
KW   Protease; Repeat; Thiol protease; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1360       Ubiquitin carboxyl-terminal hydrolase 19.
FT                                /FTId=PRO_0000295157.
FT   DOMAIN       51    140       CS 1.
FT   DOMAIN      322    424       CS 2.
FT   ZN_FING     833    875       MYND-type.
FT   COMPBIAS    524    530       Poly-Glu.
FT   ACT_SITE    548    548       By similarity.
FT   ACT_SITE   1199   1199       By similarity.
FT   ACT_SITE   1207   1207       By similarity.
FT   MOD_RES    1284   1284       Phosphoserine (By similarity).
FT   VAR_SEQ    1286   1340       ASRIWQELEAEEEMVPEGPGPLGPWGPQDWVGPPPRGPTTP
FT                                DEGCLRYFVLGTVA -> GLGPGQAPEVAPTRTAPERFAPP
FT                                VDRPAPTYSNMEEVD (in isoform 2).
FT                                /FTId=VSP_026769.
FT   VAR_SEQ    1341   1360       Missing (in isoform 2).
FT                                /FTId=VSP_026770.
FT   CONFLICT    140    140       L -> LK (in Ref. 2; BAE42739).
FT   CONFLICT    142    142       P -> S (in Ref. 3; AAH60613).
FT   CONFLICT    430    431       Missing (in Ref. 2; BAE42739).
FT   CONFLICT    669    669       A -> T (in Ref. 2; BAE42739).
FT   CONFLICT   1058   1058       D -> E (in Ref. 2; BAE42739).
SQ   SEQUENCE   1360 AA;  150549 MW;  FE9C3020D2CD9AED CRC64;
     MSAGASATGP RRGPPGLEEA TSKKKQKDRA NLESKDGDAR RVSLPRKEPT KDELLLDWRQ
     SADEVIVKLR VGTGPVRLED VDAAFTDTDC VVRLPDGRQW GGVFFAEIQS SCTKVQARKG
     GLLQLVLPKK VPLLTWPSLL KPLGTQELVP GLQCQENGQE LSPIALEPGS EPRRAKQEAR
     NQKRAQGRGE VGSGAGPGTQ AGPSAKRAVH LRRGPEGEGS MDGPGPQGDA PSFLSDSATQ
     VEAEEKLCAP PMNTQTSLLS SEKSLALLTV EKTVSPRNDP VAPVMVQDRD PEPEQEDQVK
     EEMALGADPT ALVEEPESMV NLAFVKNDSY EKGPDSVVVH VYVKEIRRDS SRVLFREQDF
     TLIFQTRDGN FLRLHPGCGP HTIFRWQVKL RNLIEPEQCT FCFTASRIDI CLRKRQSQRW
     GGLEAPATRG AVGGAKVAVP TGPTPLDSTP PGGGPHPLTG QEEARAVEKE KPKARSEDSG
     LDGVVARTPL EHVAPKPDPH LASPKPTCMV PPMPHSPVSG DSVEEDEEEE KKVCLPGFTG
     LVNLGNTCFM NSVIQSLSNT RELRDFFHDR SFEAEINYNN PLGTGGRLAI GFAVLLRALW
     KGTHQAFQPS KLKAIVASKA SQFTGYAQHD AQEFMAFLLD GLHEDLNRIQ NKPYTETVDS
     DGRPDEVVAE EAWQRHKMRN DSFIVDLFQG QYKSKLVCPV CAKVSITFDP FLYLPVPLPQ
     KQKVLPIFYF AREPHSKPIK FLVSVSKENS SASEVLDSLS QSVHVKPENL RLAEVIKNRF
     HRVFLPSHSL DAVSPTDVLL CFELLSPELA KERVVVLEVQ QRPQVPSIPI SKCAACQRKQ
     QSEEEKLKRC TRCYRVGYCN QFCQKTHWPD HKGLCRPENI GYPFLVSVPA SRLTYARLAQ
     LLEGYARYSV SVFQPPFQPG RMALESQSPG CTTLLSTSSL EAGDSEREPI QPSELQLVTP
     VAEGDTGAHR VWPPADRGPV PSTSGLSSEM LASGPIEGCP LLAGERVSRP EAAVPGYQHS
     SESVNTHTPQ FFIYKIDASN REQRLEDKGE TPLELGDDCS LALVWRNNER LQEFVLVASK
     ELECAEDPGS AGEAARAGHF TLDQCLNLFT RPEVLAPEEA WYCPQCKQHR EASKQLLLWR
     LPNVLIVQLK RFSFRSFIWR DKINDLVEFP VRNLDLSKFC IGQKEEQLPS YDLYAVINHY
     GGMIGGHYTA CARLPNDRSS QRSDVGWRLF DDSTVTTVDE SQVVTRYAYV LFYRRRNSPV
     ERPPRASHSE HHPDLGPAAE AAASQASRIW QELEAEEEMV PEGPGPLGPW GPQDWVGPPP
     RGPTTPDEGC LRYFVLGTVA ALVALVLNVF YPLVSQSRWR
//