ID UBP37_PIG Reviewed; 982 AA.
AC F1SRY5;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Landrace;
RG Swine Genome Sequencing Consortium.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinase that plays a role in different processes
CC including cell cycle regulation, DNA replication or DNA damage
CC response. Antagonizes the anaphase-promoting complex (APC/C) during
CC G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and
CC CCNA2), thereby promoting S phase entry. Specifically mediates
CC deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific
CC ubiquitin-linkage type mediated by the APC/C complex. Phosphorylation
CC at Ser-628 during G1/S phase maximizes the deubiquitinase activity,
CC leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). Plays an
CC important role in the regulation of DNA replication by stabilizing the
CC licensing factor CDT1. Plays also an essential role beyond S-phase
CC entry to promote the efficiency and fidelity of replication by
CC deubiquitinating checkpoint kinase 1/CHK1, promoting its stability.
CC Sustains the DNA damage response (DDR) by deubiquitinating and
CC stabilizing the ATP-dependent DNA helicase BLM. Mechanistically, DNA
CC double-strand breaks (DSB) promotes ATM-mediated phosphorylation of
CC USP37 and enhances the binding between USP37 and BLM. Promotes cell
CC migration by deubiquitinating and stabilizing the epithelial-
CC mesenchymal transition (EMT)-inducing transcription factor SNAI. Plays
CC a role in the regulation of mitotic spindle assembly and mitotic
CC progression by associating with chromatin-associated WAPL and
CC stabilizing it through deubiquitination.
CC {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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86T82}.
CC Chromosome {ECO:0000250|UniProtKB:Q86T82}.
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-631 by CDK2 during G1/S phase but not during
CC mitosis; phosphorylation at Ser-631 is required for deubiquitinase
CC activity. Also polyubiquitinated during early G1 phase, without leading
CC to degradation. Phosphorylated at Ser-115 by ATM following DNA damage,
CC which in turn increases its deubiquitination activity towards BLM.
CC {ECO:0000250|UniProtKB:Q86T82}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU570813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1SRY5; -.
DR SMR; F1SRY5; -.
DR STRING; 9823.ENSSSCP00000017157; -.
DR PaxDb; 9823-ENSSSCP00000017157; -.
DR eggNOG; KOG1868; Eukaryota.
DR InParanoid; F1SRY5; -.
DR TreeFam; TF323032; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR CDD; cd02257; Peptidase_C19; 2.
DR CDD; cd13312; PH_USP37_like; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 2.30.29.180; Ubiquitin carboxyl-terminal hydrolase 26/29/37, pleckstrin homology-like domain; 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 PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF23; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE USP2; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF16674; UCH_N; 1.
DR Pfam; PF02809; UIM; 3.
DR SMART; SM00726; UIM; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50330; UIM; 3.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Chromosome; Hydrolase; Mitosis; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..982
FT /note="Ubiquitin carboxyl-terminal hydrolase 37"
FT /id="PRO_0000412646"
FT DOMAIN 343..954
FT /note="USP"
FT DOMAIN 707..726
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 809..828
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 831..850
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 128..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..798
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 161..169
FT /note="D-box 3"
FT /evidence="ECO:0000250"
FT MOTIF 224..226
FT /note="KEN box 2"
FT /evidence="ECO:0000250"
FT MOTIF 785..787
FT /note="KEN box 3"
FT /evidence="ECO:0000250"
FT COMPBIAS 128..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 352
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q86T82,
FT ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-
FT ProRule:PRU10093"
FT ACT_SITE 909
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 631
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86T82"
SQ SEQUENCE 982 AA; 110483 MW; 3B09ABDE42E07AFF CRC64;
MSPLKIQGPI RIRSMQTGIT KWKEGSFEIV EKENKVSLVV HYNTGGIPRI FQLSHNIKNV
VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLNAV AMKPSQGSGS
FGAILGSRTS QKETHRQLSY SDNQVSSKRG SLETKDDIPF RKVLGNPGRA SIKTAAGSGI
TATRTIPSLT STSTPLRSGL LENRTEKRKR MLSSGSELNE DYPKENDSSS NNKAMTDPSR
KYLTSSREKQ LSLKQSEENR TSGLLPLQSS SFYGSRAASK DYSPSSTNLD RTNISSQTPS
AKRSLGFLPQ PAPLSVKKLR CNQDYTGWNK PRLPLSSHQQ QLQGFSNLGN TCYMNAILQS
LFSLQSFAND LLKQGIPWKK IPLNALISRR FAHLLVKKDI CNSETKKDLL KKVKNAISAT
AERFSGYMQN DAHEFLSQCL DQLKEDMEKL NKTWKTEPVP GEENSPDVTA TRVYTCPVIT
NLEFEVQHSI ICKACGEIIP KREQFNDLSI DLPRRKKPLP PRSIQDSLDL FFRAEELEYS
CEKCGGKCAL VRHKFNRLPR ILILHLKRYS FNVALSLNNK IGQQVIIPRY LTLSSHCTEN
TKPPFNLGWS AQMAISRPLK ASQMVNSCIT SPSTPSKNFT FKSKSSLALS LDSDSEDELK
RSVALSQRLC EISSSEQQQE DLEKDSKSCK LEPDKSELEN SGFDAMSEEE LLAAVLEISK
REASPSPSHE DDDKPTSSPD TGFAEDDIQE MPENPDPMET EKPKTITEPD PASFTEITKD
CDENKENKTP EGSQGEVDWL QQYDMERERE EQELQQALAQ SLQEQEAWEQ KEDDDLKRAT
ELSLQEFNNS FLDSLGSDED SGNEDVLDME YTEAEAEELK RNAETGNLPH SYRLISVVSH
IGSTSSSGHY ISDVYDIKKQ AWFTYNDLEV SKIQEASVQS DRDRSGYIFF YMHKEIFDEL
LETEKNSQAL SMEVGKTTRQ AS
//
