UBP37_MOUSE
ID UBP37_MOUSE Reviewed; 979 AA.
AC Q8C0R0; B2RT12; Q69ZF6; Q8BZE6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 37;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q86T82};
DE AltName: Full=Deubiquitinating enzyme 37;
DE AltName: Full=Ubiquitin thioesterase 37;
DE AltName: Full=Ubiquitin-specific-processing protease 37;
GN Name=Usp37 {ECO:0000312|MGI:MGI:2442483};
GN Synonyms=Kiaa1594 {ECO:0000312|EMBL:BAD32488.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAC26734.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-779 (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26734.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC26734.1}, and
RC Urinary bladder {ECO:0000312|EMBL:BAC29135.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAD32488.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-979 (ISOFORM 2).
RC TISSUE=Pancreatic islet {ECO:0000312|EMBL:BAD32488.1};
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650 AND SER-652, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, 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: Deubiquitinase that antagonizes the anaphase-promoting
CC complex (APC/C) during G1/S transition by mediating deubiquitination of
CC cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry.
CC Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin
CC chains, a specific ubiquitin-linkage type mediated by the APC/C
CC complex. Also mediates deubiquitination of 'Lys-48'-linked
CC polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S
CC phase maximizes the deubiquitinase activity, leading to prevent
CC degradation of cyclin-A (CCNA1 and CCNA2). Plays an important role in
CC the regulation of DNA replication by stabilizing the licensing factor
CC CDT1. {ECO:0000250|UniProtKB:Q86T82}.
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:Q86T82};
CC -!- SUBUNIT: Interacts with FZR1/CDH1. Interacts with CDT1.
CC {ECO:0000250|UniProtKB:Q86T82}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8C0R0-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15368895, ECO:0000269|PubMed:16141072};
CC IsoId=Q8C0R0-2; Sequence=VSP_052196;
CC -!- DOMAIN: The KEN box 3 is required for interaction with FZR1/CDH1 and is
CC essential for APC(CDH1)-mediated ubiquitination.
CC {ECO:0000250|UniProtKB:Q86T82}.
CC -!- PTM: Polyubiquitinated via 'Lys-11'-linked ubiquitin by the APC(CDH1)
CC complex during late mitosis, leading to its degradation. Able to
CC mediate auto-deubiquitination. {ECO:0000250|UniProtKB:Q86T82}.
CC -!- PTM: Phosphorylated at Ser-628 by CDK2 during G1/S phase but not during
CC mitosis; phosphorylation at Ser-628 is required for deubiquitinase
CC activity. Also polyubiquitinated during early G1 phase, without leading
CC to degradation. {ECO:0000250|UniProtKB:Q86T82}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000255}.
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DR EMBL; AK030013; BAC26734.1; -; mRNA.
DR EMBL; AK035640; BAC29135.1; -; mRNA.
DR EMBL; AK173210; BAD32488.1; -; mRNA.
DR EMBL; BC139091; AAI39092.1; -; mRNA.
DR CCDS; CCDS15050.1; -. [Q8C0R0-1]
DR CCDS; CCDS78616.1; -. [Q8C0R0-2]
DR RefSeq; NP_001297591.1; NM_001310662.1. [Q8C0R0-2]
DR RefSeq; NP_795946.2; NM_176972.4.
DR RefSeq; XP_006496117.1; XM_006496054.3.
DR AlphaFoldDB; Q8C0R0; -.
DR SMR; Q8C0R0; -.
DR BioGRID; 235424; 2.
DR STRING; 10090.ENSMUSP00000140670; -.
DR iPTMnet; Q8C0R0; -.
DR PhosphoSitePlus; Q8C0R0; -.
DR EPD; Q8C0R0; -.
DR jPOST; Q8C0R0; -.
DR MaxQB; Q8C0R0; -.
DR PaxDb; Q8C0R0; -.
DR PeptideAtlas; Q8C0R0; -.
DR PRIDE; Q8C0R0; -.
DR ProteomicsDB; 298361; -. [Q8C0R0-1]
DR ProteomicsDB; 298362; -. [Q8C0R0-2]
DR Antibodypedia; 34273; 168 antibodies from 26 providers.
DR DNASU; 319651; -.
DR Ensembl; ENSMUST00000044260; ENSMUSP00000035445; ENSMUSG00000033364. [Q8C0R0-2]
DR GeneID; 319651; -.
DR KEGG; mmu:319651; -.
DR UCSC; uc007bmc.2; mouse. [Q8C0R0-2]
DR UCSC; uc007bmd.2; mouse. [Q8C0R0-1]
DR CTD; 57695; -.
DR MGI; MGI:2442483; Usp37.
DR VEuPathDB; HostDB:ENSMUSG00000033364; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000158091; -.
DR HOGENOM; CLU_012557_0_0_1; -.
DR InParanoid; Q8C0R0; -.
DR OrthoDB; 129045at2759; -.
DR PhylomeDB; Q8C0R0; -.
DR TreeFam; TF323032; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 319651; 13 hits in 72 CRISPR screens.
DR ChiTaRS; Usp37; mouse.
DR PRO; PR:Q8C0R0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8C0R0; protein.
DR Bgee; ENSMUSG00000033364; Expressed in spermatocyte and 226 other tissues.
DR ExpressionAtlas; Q8C0R0; baseline and differential.
DR Genevisible; Q8C0R0; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
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:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd13312; PH_USP37_like; 1.
DR Gene3D; 2.30.29.180; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR032069; USP37-like_PH.
DR InterPro; IPR038093; USP37-like_PH_sf.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 1.
DR Pfam; PF02809; UIM; 3.
DR SMART; SM00726; UIM; 3.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50330; UIM; 2.
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 Alternative splicing; Cell cycle; Cell division; Hydrolase; Mitosis;
KW Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..979
FT /note="Ubiquitin carboxyl-terminal hydrolase 37"
FT /id="PRO_0000259610"
FT DOMAIN 341..951
FT /note="USP"
FT DOMAIN 704..723
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 806..825
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 828..847
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 116..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 32..34
FT /note="KEN box 1"
FT /evidence="ECO:0000250"
FT MOTIF 71..79
FT /note="D-box 1"
FT /evidence="ECO:0000250"
FT MOTIF 96..105
FT /note="D-box 2"
FT /evidence="ECO:0000250"
FT MOTIF 160..168
FT /note="D-box 3"
FT /evidence="ECO:0000250"
FT MOTIF 222..224
FT /note="KEN box 2"
FT /evidence="ECO:0000250"
FT MOTIF 782..784
FT /note="KEN box 3"
FT /evidence="ECO:0000250"
FT COMPBIAS 116..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q86T82,
FT ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-
FT ProRule:PRU10093"
FT ACT_SITE 906
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 628
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT VAR_SEQ 612..634
FT /note="ISRPLRACQMMNSCITSPSAPSK -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052196"
FT CONFLICT 622
FT /note="M -> V (in Ref. 2; AAI39092)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 979 AA; 110063 MW; FF11DB673C1CA902 CRC64;
MSPLKIYGPI RIRSMQTGIT KWKEGSFEIV EKDNRVSLLV HYNTGGIPRV FQLSHNIKNV
VLRPSGIKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLHAA MKASQGSGSF
GTILGSRTSQ KETNRQLSYS DNQASSKRGS LETKDEIPFR KVLGSPGRGP IKTVTGGGMA
VTRTIPSLTL TSTPLRSGLL ENRTEKRKRM LSGSELTEDY PKENDSSSNN KAMTDPSRKY
LTSCREKQLS LKQAEENRTS GLLPLQSSSF YGSRAGSKDY SSGVTNLDRC NVSSQTPSAK
RSLGFLPQPT PLSVKKLRCN QDYAGWNRPR VPLSSHQQQL QGFSNLGNTC YMNAILQSLF
SLQSFANDLL KQSIPWKKIP FNALIRRFAN LLIKKDICNS ETKKELLKKV KNAISATAER
FSGYVQNDAH EFLSQCLDQL KEDMEKLNKT WKTEPVLGEE NLPDTSATKV FTCPVITNLE
FEVQHSIICK ACGETIPKRE QFNDLSIDLP RRKKPLPPRS IQDSLDLFFR AEELEYSCEK
CGGKCALVRH KFNRLPRVLI LHLKRYSFNV ALSLNNKLGQ QVIIPRFLTL ASHCTESTKP
PVTLGWSAPV AISRPLRACQ MMNSCITSPS APSKKFTFKS KSSVTSCLDS DSEDELKRSV
VLSQRLCDLP GNEQYQEDVE KDLKLCRLEP GKAELENSGF DRMSEEEVLA AVLEISRREA
SPVLSPEDDD KPTSSPDTGF AEDDIPEMPE NPDAMEIEKS KTITEPGPAS FTEITKDCDE
NKENKTPEGS QGEVDWLQQY DVDREREEQE LQQALAQSLQ EQEAWEQKED DDLKRATELS
LQEFNNSFLD SLGSDEDSGN EDVFDMEYTE AEAEELKRNA ETGALPHSYR LISVVSHIGS
TSSSGHYISD VYDIKKQAWF TYNDLEVSKI QEAAVQSDRD RSGYIFFYMH KEIFDELLET
EKTSQALSME VGRAARQAS
