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F1SRY5 (UBP37_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin carboxyl-terminal hydrolase 37

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 37
Ubiquitin thioesterase 37
Ubiquitin-specific-processing protease 37
Gene names
Name:USP37
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length982 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Deubiquitinase that 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. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-631 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2) By similarity.

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).

Subunit structure

Interacts with FZR1/CDH1 By similarity.

Domain

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

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 By similarity.

Phosphorylated at Ser-631 by CDK2 during G1/S phase but not during mitosis; phosphorylation at Ser-631 is required for deubiquitinase activity. Also polyubiquitinated during early G1 phase, without leading to degradation By similarity.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 3 UIM (ubiquitin-interacting motif) repeats.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 982982Ubiquitin carboxyl-terminal hydrolase 37
PRO_0000412646

Regions

Domain343 – 954612USP
Repeat707 – 72620UIM 1
Repeat809 – 82820UIM 2
Repeat831 – 85020UIM 3
Motif32 – 343KEN box 1 By similarity
Motif71 – 799D-box 1 By similarity
Motif96 – 10510D-box 2 By similarity
Motif161 – 1699D-box 3 By similarity
Motif224 – 2263KEN box 2 By similarity
Motif785 – 7873KEN box 3 By similarity

Sites

Active site3521Nucleophile By similarity
Active site9091Proton acceptor By similarity

Amino acid modifications

Modified residue6311Phosphoserine; by CDK2 By similarity
Modified residue6531Phosphoserine By similarity
Modified residue6551Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
F1SRY5 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 3B09ABDE42E07AFF

FASTA982110,483
        10         20         30         40         50         60 
MSPLKIQGPI RIRSMQTGIT KWKEGSFEIV EKENKVSLVV HYNTGGIPRI FQLSHNIKNV 

        70         80         90        100        110        120 
VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLNAV AMKPSQGSGS 

       130        140        150        160        170        180 
FGAILGSRTS QKETHRQLSY SDNQVSSKRG SLETKDDIPF RKVLGNPGRA SIKTAAGSGI 

       190        200        210        220        230        240 
TATRTIPSLT STSTPLRSGL LENRTEKRKR MLSSGSELNE DYPKENDSSS NNKAMTDPSR 

       250        260        270        280        290        300 
KYLTSSREKQ LSLKQSEENR TSGLLPLQSS SFYGSRAASK DYSPSSTNLD RTNISSQTPS 

       310        320        330        340        350        360 
AKRSLGFLPQ PAPLSVKKLR CNQDYTGWNK PRLPLSSHQQ QLQGFSNLGN TCYMNAILQS 

       370        380        390        400        410        420 
LFSLQSFAND LLKQGIPWKK IPLNALISRR FAHLLVKKDI CNSETKKDLL KKVKNAISAT 

       430        440        450        460        470        480 
AERFSGYMQN DAHEFLSQCL DQLKEDMEKL NKTWKTEPVP GEENSPDVTA TRVYTCPVIT 

       490        500        510        520        530        540 
NLEFEVQHSI ICKACGEIIP KREQFNDLSI DLPRRKKPLP PRSIQDSLDL FFRAEELEYS 

       550        560        570        580        590        600 
CEKCGGKCAL VRHKFNRLPR ILILHLKRYS FNVALSLNNK IGQQVIIPRY LTLSSHCTEN 

       610        620        630        640        650        660 
TKPPFNLGWS AQMAISRPLK ASQMVNSCIT SPSTPSKNFT FKSKSSLALS LDSDSEDELK 

       670        680        690        700        710        720 
RSVALSQRLC EISSSEQQQE DLEKDSKSCK LEPDKSELEN SGFDAMSEEE LLAAVLEISK 

       730        740        750        760        770        780 
REASPSPSHE DDDKPTSSPD TGFAEDDIQE MPENPDPMET EKPKTITEPD PASFTEITKD 

       790        800        810        820        830        840 
CDENKENKTP EGSQGEVDWL QQYDMERERE EQELQQALAQ SLQEQEAWEQ KEDDDLKRAT 

       850        860        870        880        890        900 
ELSLQEFNNS FLDSLGSDED SGNEDVLDME YTEAEAEELK RNAETGNLPH SYRLISVVSH 

       910        920        930        940        950        960 
IGSTSSSGHY ISDVYDIKKQ AWFTYNDLEV SKIQEASVQS DRDRSGYIFF YMHKEIFDEL 

       970        980 
LETEKNSQAL SMEVGKTTRQ AS 

« Hide

References

[1]Swine Genome Sequencing Consortium.
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Landrace.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU570813 Genomic DNA. No translation available.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000017635; ENSSSCP00000017157; ENSSSCG00000016194.

Phylogenomic databases

GeneTreeENSGT00440000033542.
OMALQEFNNS.
OrthoDBEOG7HMS09.
TreeFamTF323032.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR003903. Ubiquitin-int_motif.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
PF02809. UIM. 3 hits.
[Graphical view]
SMARTSM00726. UIM. 3 hits.
[Graphical view]
PROSITEPS50330. UIM. 3 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUBP37_PIG
AccessionPrimary (citable) accession number: F1SRY5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: May 3, 2011
Last modified: April 16, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries