Q86T82 · UBP37_HUMAN
- ProteinUbiquitin carboxyl-terminal hydrolase 37
- GeneUSP37
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids979 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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) (PubMed:21596315).
Plays an important role in the regulation of DNA replication by stabilizing the licensing factor CDT1 (PubMed:27296872).
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 (PubMed:34509474).
Sustains the DNA damage response (DDR) by deubiquitinating and stabilizing the ATP-dependent DNA helicase BLM (PubMed:34606619).
Mechanistically, DNA double-strand breaks (DSB) promotes ATM-mediated phosphorylation of USP37 and enhances the binding between USP37 and BLM (PubMed:34606619).
Promotes cell migration by deubiquitinating and stabilizing the epithelial-mesenchymal transition (EMT)-inducing transcription factor SNAI (PubMed:31911859).
Plays a role in the regulation of mitotic spindle assembly and mitotic progression by associating with chromatin-associated WAPL and stabilizing it through deubiquitination (PubMed:26299517).
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 350 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 906 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | cysteine-type deubiquitinase activity | |
Molecular Function | cysteine-type endopeptidase activity | |
Molecular Function | protein kinase binding | |
Biological Process | cell division | |
Biological Process | G1/S transition of mitotic cell cycle | |
Biological Process | protein deubiquitination | |
Biological Process | protein K11-linked deubiquitination | |
Biological Process | protein K48-linked deubiquitination | |
Biological Process | proteolysis | |
Biological Process | regulation of DNA replication |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUbiquitin carboxyl-terminal hydrolase 37
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ86T82
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 32-34 | No effect. | ||||
Sequence: KEN → AAA | ||||||
Mutagenesis | 71-74 | No effect. | ||||
Sequence: RLML → ALMA | ||||||
Mutagenesis | 96-99 | No effect. | ||||
Sequence: RLFL → ALFA | ||||||
Mutagenesis | 114 | Loss of phosphorylation following cisplatin treatment. | ||||
Sequence: S → A | ||||||
Mutagenesis | 160-163 | No effect. | ||||
Sequence: RKVL → AKVA | ||||||
Mutagenesis | 221-223 | No effect. | ||||
Sequence: KEN → AAA | ||||||
Mutagenesis | 350 | Abolishes deubiquitinase activity. | ||||
Sequence: C → A | ||||||
Mutagenesis | 350 | Abolishes deubiquitinase activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 628 | Abolishes phosphorylation by CDK2, leading to lower deubiquitinase activity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 782-784 | Impaired interaction with FZR1/CDH1 and subsequent ubiquitination. | ||||
Sequence: KEN → AAA | ||||||
Natural variant | VAR_059752 | 979 | in dbSNP:rs6436058 | |||
Sequence: L → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 965 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000080667 | 1-979 | UniProt | Ubiquitin carboxyl-terminal hydrolase 37 | |||
Sequence: MSPLKIHGPIRIRSMQTGITKWKEGSFEIVEKENKVSLVVHYNTGGIPRIFQLSHNIKNVVLRPSGAKQSRLMLTLQDNSFLSIDKVPSKDAEEMRLFLDAVHQNRLPAAMKPSQGSGSFGAILGSRTSQKETSRQLSYSDNQASAKRGSLETKDDIPFRKVLGNPGRGSIKTVAGSGIARTIPSLTSTSTPLRSGLLENRTEKRKRMISTGSELNEDYPKENDSSSNNKAMTDPSRKYLTSSREKQLSLKQSEENRTSGLLPLQSSSFYGSRAGSKEHSSGGTNLDRTNVSSQTPSAKRSLGFLPQPVPLSVKKLRCNQDYTGWNKPRVPLSSHQQQQLQGFSNLGNTCYMNAILQSLFSLQSFANDLLKQGIPWKKIPLNALIRRFAHLLVKKDICNSETKKDLLKKVKNAISATAERFSGYMQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVSGEENSPDISATRAYTCPVITNLEFEVQHSIICKACGEIIPKREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKCALVRHKFNRLPRVLILHLKRYSFNVALSLNNKIGQQVIIPRYLTLSSHCTENTKPPFTLGWSAHMAISRPLKASQMVNSCITSPSTPSKKFTFKSKSSLALCLDSDSEDELKRSVALSQRLCEMLGNEQQQEDLEKDSKLCPIEPDKSELENSGFDRMSEEELLAAVLEISKRDASPSLSHEDDDKPTSSPDTGFAEDDIQEMPENPDTMETEKPKTITELDPASFTEITKDCDENKENKTPEGSQGEVDWLQQYDMEREREEQELQQALAQSLQEQEAWEQKEDDDLKRATELSLQEFNNSFVDALGSDEDSGNEDVFDMEYTEAEAEELKRNAETGNLPHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSDRDRSGYIFFYMHKEIFDELLETEKNSQSLSTEVGKTTRQAL | |||||||
Modified residue | 114 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 170 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 191 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 210 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 210 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 213 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 301 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 312 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 457 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 462 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 628 | UniProt | Phosphoserine; by CDK2 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 628 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 630 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 631 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 633 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 650 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 650 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 652 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 652 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 770 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 770 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated at Ser-114 by ATM following DNA damage, which in turn increases its deubiquitination activity towards BLM (PubMed:34606619).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Developmental stage
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for motif, region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 32-34 | KEN box 1 | ||||
Sequence: KEN | ||||||
Motif | 71-79 | D-box 1 | ||||
Sequence: RLMLTLQDN | ||||||
Motif | 96-105 | D-box 2 | ||||
Sequence: RLFLDAVHQN | ||||||
Region | 110-153 | Disordered | ||||
Sequence: AMKPSQGSGSFGAILGSRTSQKETSRQLSYSDNQASAKRGSLET | ||||||
Compositional bias | 119-147 | Polar residues | ||||
Sequence: SFGAILGSRTSQKETSRQLSYSDNQASAK | ||||||
Motif | 160-168 | D-box 3 | ||||
Sequence: RKVLGNPGR | ||||||
Compositional bias | 183-197 | Polar residues | ||||
Sequence: IPSLTSTSTPLRSGL | ||||||
Region | 183-304 | Disordered | ||||
Sequence: IPSLTSTSTPLRSGLLENRTEKRKRMISTGSELNEDYPKENDSSSNNKAMTDPSRKYLTSSREKQLSLKQSEENRTSGLLPLQSSSFYGSRAGSKEHSSGGTNLDRTNVSSQTPSAKRSLGF | ||||||
Compositional bias | 198-224 | Basic and acidic residues | ||||
Sequence: LENRTEKRKRMISTGSELNEDYPKEND | ||||||
Motif | 221-223 | KEN box 2 | ||||
Sequence: KEN | ||||||
Compositional bias | 225-301 | Polar residues | ||||
Sequence: SSSNNKAMTDPSRKYLTSSREKQLSLKQSEENRTSGLLPLQSSSFYGSRAGSKEHSSGGTNLDRTNVSSQTPSAKRS | ||||||
Domain | 341-951 | USP | ||||
Sequence: QGFSNLGNTCYMNAILQSLFSLQSFANDLLKQGIPWKKIPLNALIRRFAHLLVKKDICNSETKKDLLKKVKNAISATAERFSGYMQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVSGEENSPDISATRAYTCPVITNLEFEVQHSIICKACGEIIPKREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKCALVRHKFNRLPRVLILHLKRYSFNVALSLNNKIGQQVIIPRYLTLSSHCTENTKPPFTLGWSAHMAISRPLKASQMVNSCITSPSTPSKKFTFKSKSSLALCLDSDSEDELKRSVALSQRLCEMLGNEQQQEDLEKDSKLCPIEPDKSELENSGFDRMSEEELLAAVLEISKRDASPSLSHEDDDKPTSSPDTGFAEDDIQEMPENPDTMETEKPKTITELDPASFTEITKDCDENKENKTPEGSQGEVDWLQQYDMEREREEQELQQALAQSLQEQEAWEQKEDDDLKRATELSLQEFNNSFVDALGSDEDSGNEDVFDMEYTEAEAEELKRNAETGNLPHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSDRDRSGYIFFYMHK | ||||||
Region | 673-701 | Disordered | ||||
Sequence: EQQQEDLEKDSKLCPIEPDKSELENSGFD | ||||||
Compositional bias | 674-701 | Basic and acidic residues | ||||
Sequence: QQQEDLEKDSKLCPIEPDKSELENSGFD | ||||||
Domain | 704-723 | UIM 1 | ||||
Sequence: SEEELLAAVLEISKRDASPS | ||||||
Region | 719-795 | Disordered | ||||
Sequence: DASPSLSHEDDDKPTSSPDTGFAEDDIQEMPENPDTMETEKPKTITELDPASFTEITKDCDENKENKTPEGSQGEVD | ||||||
Compositional bias | 720-737 | Basic and acidic residues | ||||
Sequence: ASPSLSHEDDDKPTSSPD | ||||||
Compositional bias | 772-789 | Basic and acidic residues | ||||
Sequence: TEITKDCDENKENKTPEG | ||||||
Motif | 782-784 | KEN box 3 | ||||
Sequence: KEN | ||||||
Domain | 806-825 | UIM 2 | ||||
Sequence: REEQELQQALAQSLQEQEAW | ||||||
Domain | 828-847 | UIM 3 | ||||
Sequence: KEDDDLKRATELSLQEFNNS |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q86T82-1
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.
- Name1
- Length979
- Mass (Da)110,170
- Last updated2010-07-13 v2
- Checksum9F47F06A744EA449
Q86T82-2
- Name2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q86W68 | Q86W68_HUMAN | USP37 | 302 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_041740 | 1-72 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 119-147 | Polar residues | ||||
Sequence: SFGAILGSRTSQKETSRQLSYSDNQASAK | ||||||
Compositional bias | 183-197 | Polar residues | ||||
Sequence: IPSLTSTSTPLRSGL | ||||||
Compositional bias | 198-224 | Basic and acidic residues | ||||
Sequence: LENRTEKRKRMISTGSELNEDYPKEND | ||||||
Sequence conflict | 223-224 | in Ref. 1; CAD89955 | ||||
Sequence: ND → DG | ||||||
Compositional bias | 225-301 | Polar residues | ||||
Sequence: SSSNNKAMTDPSRKYLTSSREKQLSLKQSEENRTSGLLPLQSSSFYGSRAGSKEHSSGGTNLDRTNVSSQTPSAKRS | ||||||
Sequence conflict | 345 | in Ref. 1; CAD97970 | ||||
Sequence: N → K | ||||||
Sequence conflict | 456 | in Ref. 1; CAD89955 | ||||
Sequence: V → I | ||||||
Sequence conflict | 552 | in Ref. 4; AAI44250 | ||||
Sequence: F → I | ||||||
Sequence conflict | 567 | in Ref. 4; AAI44253 | ||||
Sequence: S → I | ||||||
Sequence conflict | 576 | in Ref. 4; AAI44253 | ||||
Sequence: N → Y | ||||||
Alternative sequence | VSP_041741 | 612-634 | in isoform 2 | |||
Sequence: ISRPLKASQMVNSCITSPSTPSK → M | ||||||
Compositional bias | 674-701 | Basic and acidic residues | ||||
Sequence: QQQEDLEKDSKLCPIEPDKSELENSGFD | ||||||
Compositional bias | 720-737 | Basic and acidic residues | ||||
Sequence: ASPSLSHEDDDKPTSSPD | ||||||
Sequence conflict | 731 | in Ref. 1; CAD97970 | ||||
Sequence: K → E | ||||||
Compositional bias | 772-789 | Basic and acidic residues | ||||
Sequence: TEITKDCDENKENKTPEG | ||||||
Sequence conflict | 905 | in Ref. 1; CAD97970 | ||||
Sequence: G → D |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL832645 EMBL· GenBank· DDBJ | CAD89955.1 EMBL· GenBank· DDBJ | mRNA | ||
BX538024 EMBL· GenBank· DDBJ | CAD97970.1 EMBL· GenBank· DDBJ | mRNA | ||
AC012510 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC073838 EMBL· GenBank· DDBJ | AAY14887.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CH471063 EMBL· GenBank· DDBJ | EAW70621.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC112901 EMBL· GenBank· DDBJ | AAI12902.1 EMBL· GenBank· DDBJ | mRNA | ||
BC133007 EMBL· GenBank· DDBJ | AAI33008.1 EMBL· GenBank· DDBJ | mRNA | ||
BC133009 EMBL· GenBank· DDBJ | AAI33010.1 EMBL· GenBank· DDBJ | mRNA | ||
BC144249 EMBL· GenBank· DDBJ | AAI44250.1 EMBL· GenBank· DDBJ | mRNA | ||
BC144252 EMBL· GenBank· DDBJ | AAI44253.1 EMBL· GenBank· DDBJ | mRNA | ||
AB046814 EMBL· GenBank· DDBJ | BAB13420.1 EMBL· GenBank· DDBJ | mRNA |