Q8C0R0 · UBP37_MOUSE

  • Protein
    Ubiquitin carboxyl-terminal hydrolase 37
  • Gene
    Usp37
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Deubiquitinase that plays a role in different processes including cell cycle regulation, DNA replication or DNA damage response. Antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). Plays an important role in the regulation of DNA replication by stabilizing the licensing factor CDT1. Plays also an essential role beyond S-phase entry to promote the efficiency and fidelity of replication by deubiquitinating checkpoint kinase 1/CHK1, promoting its stability. Sustains the DNA damage response (DDR) by deubiquitinating and stabilizing the ATP-dependent DNA helicase BLM. Mechanistically, DNA double-strand breaks (DSB) promotes ATM-mediated phosphorylation of USP37 and enhances the binding between USP37 and BLM. Promotes cell migration by deubiquitinating and stabilizing the epithelial-mesenchymal transition (EMT)-inducing transcription factor SNAI. Plays a role in the regulation of mitotic spindle assembly and mitotic progression by associating with chromatin-associated WAPL and stabilizing it through deubiquitination.

Catalytic activity

  • Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
    EC:3.4.19.12 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site350Nucleophile
Active site906Proton acceptor

GO annotations

AspectTerm
Cellular Componentchromosome
Cellular Componentcytosol
Cellular Componentnucleus
Molecular Functioncysteine-type deubiquitinase activity
Molecular Functioncysteine-type endopeptidase activity
Biological Processcell division
Biological ProcessG1/S transition of mitotic cell cycle
Biological Processprotein deubiquitination
Biological Processprotein K11-linked deubiquitination
Biological Processprotein K48-linked deubiquitination
Biological Processproteolysis
Biological Processregulation of DNA replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ubiquitin carboxyl-terminal hydrolase 37
  • EC number
  • Alternative names
    • Deubiquitinating enzyme 37
    • Ubiquitin thioesterase 37
    • Ubiquitin-specific-processing protease 37

Gene names

    • Name
      Usp37
    • Synonyms
      Kiaa1594

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8C0R0
  • Secondary accessions
    • B2RT12
    • Q69ZF6
    • Q8BZE6

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002596101-979Ubiquitin carboxyl-terminal hydrolase 37
Modified residue114Phosphoserine
Modified residue212Phosphoserine
Modified residue628Phosphoserine; by CDK2
Modified residue650Phosphoserine
Modified residue652Phosphoserine
Modified residue770Phosphoserine

Post-translational modification

Polyubiquitinated via 'Lys-11'-linked ubiquitin by the APC(CDH1) complex during late mitosis, leading to its degradation. Able to mediate auto-deubiquitination.
Phosphorylated at Ser-628 by CDK2 during G1/S phase but not during mitosis; phosphorylation at Ser-628 is required for deubiquitinase activity. Also polyubiquitinated during early G1 phase, without leading to degradation. Phosphorylated at Ser-114 by ATM following DNA damage, which in turn increases its deubiquitination activity towards BLM.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with FZR1/CDH1. Interacts with CDT1.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif, compositional bias, region, domain.

TypeIDPosition(s)Description
Motif32-34KEN box 1
Motif71-79D-box 1
Motif96-105D-box 2
Compositional bias116-147Polar residues
Region116-178Disordered
Motif160-168D-box 3
Region192-240Disordered
Compositional bias200-225Basic and acidic residues
Motif222-224KEN box 2
Compositional bias226-240Polar residues
Domain341-951USP
Domain704-723UIM 1
Region719-795Disordered
Compositional bias721-737Basic and acidic residues
Compositional bias775-789Basic and acidic residues
Motif782-784KEN box 3
Domain806-825UIM 2
Domain828-847UIM 3

Domain

The KEN box 3 is required for interaction with FZR1/CDH1 and is essential for APC(CDH1)-mediated ubiquitination.

Sequence similarities

Belongs to the peptidase C19 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q8C0R0-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    979
  • Mass (Da)
    110,063
  • Last updated
    2003-03-01 v1
  • Checksum
    FF11DB673C1CA902
MSPLKIYGPIRIRSMQTGITKWKEGSFEIVEKDNRVSLLVHYNTGGIPRVFQLSHNIKNVVLRPSGIKQSRLMLTLQDNSFLSIDKVPSKDAEEMRLFLDAVHQNRLHAAMKASQGSGSFGTILGSRTSQKETNRQLSYSDNQASSKRGSLETKDEIPFRKVLGSPGRGPIKTVTGGGMAVTRTIPSLTLTSTPLRSGLLENRTEKRKRMLSGSELTEDYPKENDSSSNNKAMTDPSRKYLTSCREKQLSLKQAEENRTSGLLPLQSSSFYGSRAGSKDYSSGVTNLDRCNVSSQTPSAKRSLGFLPQPTPLSVKKLRCNQDYAGWNRPRVPLSSHQQQLQGFSNLGNTCYMNAILQSLFSLQSFANDLLKQSIPWKKIPFNALIRRFANLLIKKDICNSETKKELLKKVKNAISATAERFSGYVQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVLGEENLPDTSATKVFTCPVITNLEFEVQHSIICKACGETIPKREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKCALVRHKFNRLPRVLILHLKRYSFNVALSLNNKLGQQVIIPRFLTLASHCTESTKPPVTLGWSAPVAISRPLRACQMMNSCITSPSAPSKKFTFKSKSSVTSCLDSDSEDELKRSVVLSQRLCDLPGNEQYQEDVEKDLKLCRLEPGKAELENSGFDRMSEEEVLAAVLEISRREASPVLSPEDDDKPTSSPDTGFAEDDIPEMPENPDAMEIEKSKTITEPGPASFTEITKDCDENKENKTPEGSQGEVDWLQQYDVDREREEQELQQALAQSLQEQEAWEQKEDDDLKRATELSLQEFNNSFLDSLGSDEDSGNEDVFDMEYTEAEAEELKRNAETGALPHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSDRDRSGYIFFYMHKEIFDELLETEKTSQALSMEVGRAARQAS

Q8C0R0-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 612-634: ISRPLRACQMMNSCITSPSAPSK → M

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0R4J2D0A0A0R4J2D0_MOUSEUsp37979
A0A087WQE4A0A087WQE4_MOUSEUsp3722

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias116-147Polar residues
Compositional bias200-225Basic and acidic residues
Compositional bias226-240Polar residues
Alternative sequenceVSP_052196612-634in isoform 2
Sequence conflict622in Ref. 2; AAI39092
Compositional bias721-737Basic and acidic residues
Compositional bias775-789Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK030013
EMBL· GenBank· DDBJ
BAC26734.1
EMBL· GenBank· DDBJ
mRNA
AK035640
EMBL· GenBank· DDBJ
BAC29135.1
EMBL· GenBank· DDBJ
mRNA
AK173210
EMBL· GenBank· DDBJ
BAD32488.1
EMBL· GenBank· DDBJ
mRNA
BC139091
EMBL· GenBank· DDBJ
AAI39092.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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