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E7F6T8 (UBP37_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 26. 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
ORF Names:zgc:152882, zgc:153999
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length937 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of APC/C target proteins, 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 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).

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 – 937937Ubiquitin carboxyl-terminal hydrolase 37
PRO_0000412648

Regions

Domain322 – 911590USP
Repeat672 – 69120UIM 1
Repeat766 – 78520UIM 2
Repeat788 – 80720UIM 3
Motif38 – 403KEN box 1 By similarity
Motif76 – 849D-box 1 By similarity
Motif101 – 11010D-box 2 By similarity
Motif162 – 1709D-box 3 By similarity
Motif204 – 2063KEN box 2 By similarity
Motif742 – 7443KEN box 3 By similarity

Sites

Active site3311Nucleophile By similarity
Active site8661Proton acceptor By similarity

Experimental info

Sequence conflict791L → Q in AAI24597. Ref.2
Sequence conflict1061T → N in AAI24597. Ref.2
Sequence conflict1061T → N in AAI29041. Ref.2
Sequence conflict1551S → N in AAI24597. Ref.2
Sequence conflict1551S → N in AAI29041. Ref.2
Sequence conflict1801L → F in AAI24597. Ref.2
Sequence conflict1801L → F in AAI29041. Ref.2
Sequence conflict4451T → M in AAI24597. Ref.2
Sequence conflict4451T → M in AAI29041. Ref.2
Sequence conflict5311A → V in AAI24597. Ref.2
Sequence conflict5311A → V in AAI29041. Ref.2
Sequence conflict6151R → K in AAI24597. Ref.2
Sequence conflict6151R → K in AAI29041. Ref.2
Sequence conflict6341E → V in AAI24597. Ref.2
Sequence conflict6531E → EQ in AAI24597. Ref.2
Sequence conflict654 – 6563LQQ → HHH in AAI29041. Ref.2
Sequence conflict654 – 6563LQQ → HHH in AAI24597. Ref.2
Sequence conflict7341L → P in AAI24597. Ref.2

Sequences

Sequence LengthMass (Da)Tools
E7F6T8 [UniParc].

Last modified March 8, 2011. Version 1.
Checksum: 6B483279C5C4EB83

FASTA937105,264
        10         20         30         40         50         60 
MAAAVPRLTS GGAVRIRIRC GELGTTKWRE GVIEIQERDN KINLLVKFNS GGAPRVFQLS 

        70         80         90        100        110        120 
HNVKSVSWFQ THGPNRMTLT LKDSCIVMMD KLNMLVAKKM KEYLETVKLG KPAVFKTNQG 

       130        140        150        160        170        180 
SASFGLVLGN RTAQNDSGLS PSDKQSAPRR SSLDSREDST PRKPLGSPSR VTSTPARGSL 

       190        200        210        220        230        240 
SEIRSEKRKR LMNSDGDLTE DYPKENDSSS NNKAITDSSR KFLLSCKDKL KQSEENRASA 

       250        260        270        280        290        300 
PHTPAPLQPT SFYGSRTGAK DYTQTHSFLD RPSSTGSCPS AKRSLVLPNH STPFKKVRPT 

       310        320        330        340        350        360 
LDYGGWNKPR PSVLAQPQPP LQGFSNLGNT CYMNAILQSL FSLPSFSNDL LKQGIPWKRV 

       370        380        390        400        410        420 
PINALLRRFA HLLAKKDISP PEVKKDLLRR VKNAISSTAE RFSGYMQNDA HEFLSQCLDQ 

       430        440        450        460        470        480 
LKEDVEKINK SWKNEPSAWD EPQSTRLADE VDTSRIYTCP VTVNMEFEVQ HTITCKSCGE 

       490        500        510        520        530        540 
VVLKREQFND LSIDLPRRRK TLPMRSIQDS LDLFFRMEEI EYSCEKCSGK AATVSHKFSR 

       550        560        570        580        590        600 
LPRVLILHLK RYSYNTQLSL NSKLGQQVLI PKYLTLLSHC TDATRSPLSL GWSAQNALSR 

       610        620        630        640        650        660 
TLKISQSVNS STLRRASQRP ESSGSVLCDS DSDEELVRKV ARKHHPDDDR ADELQQHHPH 

       670        680        690        700        710        720 
AAVEQSEFNG INDEEMLAAV LEMSRHDTSL CAGPDEEPSS SPDTGFGDAD AHDLTQHLEL 

       730        740        750        760        770        780 
LDAEKQPTDA LESLDLTMDE NKENQTPDGL QGELDWVQQY SLEQEREEQE LQQALAQSLQ 

       790        800        810        820        830        840 
EQEAREMRED DDLKRATELS LQEFNNSLPE LLCSDEDSGN EDGLDMEYSE AEAEELKKNA 

       850        860        870        880        890        900 
ETGELPNSFR LISVVSHIGS SSSSGHYISD VYDMKKQSWL TYNDLDVSRT QESTVQRDRD 

       910        920        930 
RSGYIFFYMH KDVFEELSEL EKAGVNTDGG RTVLQPL 

« Hide

References

[1]"The zebrafish reference genome sequence and its relationship to the human genome."
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J. expand/collapse author list , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CT583711 Genomic DNA. No translation available.
BC124596 mRNA. Translation: AAI24597.1.
BC129040 mRNA. Translation: AAI29041.1.
RefSeqNP_001070811.1. NM_001077343.1.
UniGeneDr.150626.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000076736.

Protein family/group databases

MEROPSC19.053.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000129632; ENSDARP00000110966; ENSDARG00000040990.
GeneID768201.
KEGGdre:768201.

Organism-specific databases

CTD57695.
ZFINZDB-GENE-061013-802. usp37.

Phylogenomic databases

eggNOGCOG5560.
GeneTreeENSGT00440000033542.
HOGENOMHOG000060197.
HOVERGENHBG055893.
InParanoidQ08BR8.
KOK11850.

Gene expression databases

BgeeE7F6T8.

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. 2 hits.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20918515.
PROE7F6T8.

Entry information

Entry nameUBP37_DANRE
AccessionPrimary (citable) accession number: E7F6T8
Secondary accession number(s): A1L1F9 expand/collapse secondary AC list , E7FBK6, F1QUQ3, Q08BR8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: March 8, 2011
Last modified: April 16, 2014
This is version 26 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