UBP38_MOUSE
ID UBP38_MOUSE Reviewed; 1042 AA.
AC Q8BW70; Q8BWL1; Q8BX03;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 38;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 38;
DE AltName: Full=Ubiquitin thioesterase 38;
DE AltName: Full=Ubiquitin-specific-processing protease 38;
GN Name=Usp38;
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=Embryonic heart, Embryonic stem cell, and Oviduct;
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; TISSUE=Brain, Olfactory epithelium, and Retina;
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=Heart, Liver, Pancreas, 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).
CC -!- FUNCTION: Deubiquitinating enzyme exhibiting a preference towards 'Lys-
CC 63'-linked ubiquitin chains. {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 -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AK049287; BAC33659.2; -; mRNA.
DR EMBL; AK052219; BAC34890.1; -; mRNA.
DR EMBL; AK054116; BAC35661.1; -; mRNA.
DR EMBL; BC054404; AAH54404.1; -; mRNA.
DR EMBL; BC057122; AAH57122.1; -; mRNA.
DR EMBL; BC058784; AAH58784.1; -; mRNA.
DR CCDS; CCDS22444.1; -.
DR RefSeq; NP_081830.2; NM_027554.2.
DR AlphaFoldDB; Q8BW70; -.
DR SMR; Q8BW70; -.
DR BioGRID; 217020; 2.
DR STRING; 10090.ENSMUSP00000039943; -.
DR MEROPS; C19.056; -.
DR iPTMnet; Q8BW70; -.
DR PhosphoSitePlus; Q8BW70; -.
DR EPD; Q8BW70; -.
DR MaxQB; Q8BW70; -.
DR PaxDb; Q8BW70; -.
DR PRIDE; Q8BW70; -.
DR ProteomicsDB; 298461; -.
DR Antibodypedia; 27336; 139 antibodies from 26 providers.
DR DNASU; 74841; -.
DR Ensembl; ENSMUST00000042724; ENSMUSP00000039943; ENSMUSG00000038250.
DR GeneID; 74841; -.
DR KEGG; mmu:74841; -.
DR UCSC; uc009mjd.1; mouse.
DR CTD; 84640; -.
DR MGI; MGI:1922091; Usp38.
DR VEuPathDB; HostDB:ENSMUSG00000038250; -.
DR eggNOG; KOG1864; Eukaryota.
DR GeneTree; ENSGT00940000158403; -.
DR HOGENOM; CLU_010910_0_0_1; -.
DR InParanoid; Q8BW70; -.
DR OMA; AFVCDSV; -.
DR OrthoDB; 802596at2759; -.
DR PhylomeDB; Q8BW70; -.
DR TreeFam; TF324529; -.
DR BioGRID-ORCS; 74841; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Usp38; mouse.
DR PRO; PR:Q8BW70; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BW70; protein.
DR Bgee; ENSMUSG00000038250; Expressed in animal zygote and 237 other tissues.
DR Genevisible; Q8BW70; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; ISO:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd02664; Peptidase_C19H; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR033840; USP38.
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 1: Evidence at protein level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..1042
FT /note="Ubiquitin carboxyl-terminal hydrolase 38"
FT /id="PRO_0000080669"
FT DOMAIN 445..949
FT /note="USP"
FT ACT_SITE 454
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 857
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT CONFLICT 90
FT /note="Q -> H (in Ref. 1; BAC35661)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="S -> G (in Ref. 1; BAC33659)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="T -> A (in Ref. 1; BAC34890)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="V -> A (in Ref. 1; BAC33659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1042 AA; 116102 MW; B039BCA53E16B178 CRC64;
MDKILEGLVS SSHPLPLKRM IVRKVVEFAE HWLDEAQCEA MFDLTTRLIL EGQDPFQRQV
GHQVLEAYAR YHRPEFESFF NKTFVLGLLQ QGYHSVDRKD VAILDYIHNG LKLIMSCPSV
LDLFSLLQVE VLRMVCERPE PVLCARLSDL LTDFVQCVPK GKLSVTFCQQ LVRTIGHFQC
VSTQEKELRE YVSQVTKVST LLQNIWKAEP STLLPSLQEV FASISSTDAS FEPSVALASL
VQHIPLQMIT VLIRSLTTDP NVKDASMTQA LCRMIDWLSW PLAQHVDTWV IALLKGLAAV
QKFTILIDVT LLKIELVFNR LWFPLVRPGA LAVLSHMLLS FQHSPEAFHV IVPHIVNLVH
SFRSDGLPSS TAFLVQLTEL VHCMMYHYSG FPDLYEPILE AVKDFPKPSE EKIKLILNQS
AWTSQSNALA SCLSRLSGKS ETGKTGLINL GNTCYMNSVL QALFMATEFR RQVLSLNLNG
CNSLMKKLQH LFAFLAHTQR EAYAPRIFFE ASRPPWFTPR SQQDCSEYLR FLLDRLHEEE
KILRVQSSHK PSEGLDCAET CLQEVTSKVA VPTESPGTGD SEKTLIEKMF GGKLRTHICC
LNCGSTSHKV EAFTDLSLAF CPSPSVEDLS FQDTASLPSA QDDGLMQTSV ADPEEEPVVY
NPATAAFVCD SVVNQRVLGS PPVEFHCAES SSVPEESAKI LISKDVPQNP GGESTTSVTD
LLNYFLAPEV LTGENQYYCE SCASLQNAEK TMQITEEPEY LILTLLRFSY DQKYHVRRKI
LDNVSLPLVL ELPVKRTASF SSLSQSWSVD VDFTDINENL PKKLKPSGTE EAFCPKLVPY
LLSSVVVHSG VSSESGHYYS YARNITGTES SYQMCPQSES LALAPSQSCL LGVESPNTVI
EQDLENKEMS QEWFLFNDSR VTFTSFQSVQ KITSRFPKDT AYVLLYKKQS RANGIDSDNP
ASGVWANGDP PLQKELMDAI TKDNKLYLQE QELNARARAL QAASASCSFR PNGFDDNDPP
GSCGPTGGGG GGGFNTVGRL VF
