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F1N5V1 (UBP37_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 19. 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length981 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-630 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-630 by CDK2 during G1/S phase but not during mitosis; phosphorylation at Ser-630 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 – 981981Ubiquitin carboxyl-terminal hydrolase 37
PRO_0000412644

Regions

Domain343 – 953611USP
Repeat706 – 72520UIM 1
Repeat808 – 82720UIM 2
Repeat830 – 84920UIM 3
Motif32 – 343KEN box 1 By similarity
Motif71 – 799D-box 1 By similarity
Motif96 – 10510D-box 2 By similarity
Motif160 – 1689D-box 3 By similarity
Motif223 – 2253KEN box 2 By similarity
Motif784 – 7863KEN box 3 By similarity

Sites

Active site3521Nucleophile By similarity
Active site9081Proton acceptor By similarity

Amino acid modifications

Modified residue6301Phosphoserine; by CDK2 By similarity
Modified residue6521Phosphoserine By similarity
Modified residue6541Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
F1N5V1 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 4F678FE4C1D0B5E3

FASTA981110,398
        10         20         30         40         50         60 
MSPLKIHGPI RIRSMQTGIT KWKEGSFEVV EKENKVSLVV HYNTGGIPRI FQLSHNIKNV 

        70         80         90        100        110        120 
VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLNAA MKPSQGSGSF 

       130        140        150        160        170        180 
GAILGSRTSQ KETNRQLSYS DNQVSSKRGS LETKDDTPFR KVLGNPSRGS IKAAAGNGVT 

       190        200        210        220        230        240 
PARTIPSLTS TSTPLRSGLL ENRTEKRKRM LSSGSELNED YPKENDSSSN NKAMTDPSRK 

       250        260        270        280        290        300 
YLTSSREKQL SLKQSEENRT SGLLPLQSSS FYGSRTAAKD YSPGSTNLDR TNISSQTPSA 

       310        320        330        340        350        360 
KRSLGFLPQP APLSVKKLRC NQDYTGWNKP RVPLSSHQQQ QLQGFSNLGN TCYMNAILQS 

       370        380        390        400        410        420 
LFSLQSFAND LLKQGIPWKK IPLNALIRRF AHLLVKKDIC NSETKKDLLK KVKNAISATA 

       430        440        450        460        470        480 
ERFSGYMQND AHEFLSQCLD QLKEDMEKLN KTWKIEPVPG EENSPDISAT RVYTCPVITN 

       490        500        510        520        530        540 
LEFEVQHSII CKVCGEIIPK REQFNDLSID LPRRKKPLPP RSIQDSLDLF FRAEELEYSC 

       550        560        570        580        590        600 
EKCGGKCALV RHKFNRLPRI LILHLKRYSF NVALSLNNKI GQQVIIPRYL TLSSHCTENT 

       610        620        630        640        650        660 
KPPFNLGWSA QMAVSRPLKA SQMVNSCITS PSTPSKNFTF KSKTSLALSL DSDSEDELKR 

       670        680        690        700        710        720 
SVALSHRLCE MSGSEQQQED LEKDSKSCRI EPDKSELENS GFDGMSEEEL LAAVLEISKR 

       730        740        750        760        770        780 
EASPSLSHED DDKPTSSPDT GFAEDDIQEM PENPDSVETE KPKTITEPDP ASFTEITKDC 

       790        800        810        820        830        840 
DENKENKTPE GSQGEVDWLQ QYDMEREREE QELQQALAQS LQEQEAWEQK EDDDLKRATE 

       850        860        870        880        890        900 
LSLQEFNNSF VDSLGSDEDS GNEDVLDMEY TEAEAEELKR NAETGNLPHS YRLISVVSHI 

       910        920        930        940        950        960 
GSTSSSGHYI SDVYDIKKQA WFTYNDLEVS KIQEASVQSD RDRSGYIFFY MHKEIFDELL 

       970        980 
ETEKNSQALN LEVGKTTRQV S 

« Hide

References

[1]"The genome sequence of taurine cattle: a window to ruminant biology and evolution."
The bovine genome sequencing and analysis consortium
Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFC03077731 Genomic DNA. No translation available.
AAFC03103854 Genomic DNA. No translation available.
AAFC03103857 Genomic DNA. No translation available.
RefSeqNP_001258921.1. NM_001271992.1.
XP_005202866.1. XM_005202809.1.
XP_005202867.1. XM_005202810.1.
UniGeneBt.25209.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEF1N5V1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000038243; ENSBTAP00000038058; ENSBTAG00000016572.
GeneID407168.
KEGGbta:407168.

Organism-specific databases

CTD57695.

Phylogenomic databases

GeneTreeENSGT00440000033542.
KOK11850.
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. 4 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...

Other

NextBio20818424.

Entry information

Entry nameUBP37_BOVIN
AccessionPrimary (citable) accession number: F1N5V1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: May 3, 2011
Last modified: April 16, 2014
This is version 19 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