Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

F1QFS9 (UBP13_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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 13

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 13
Ubiquitin thioesterase 13
Ubiquitin-specific-processing protease 13
Gene names
Name:usp13
ORF Names:wu:fc61g08
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length860 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Deubiquitinase that mediates deubiquitination of target proteins and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD) 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).

Enzyme regulation

Specifically inhibited by spautin-1 (specific and potent autophagy inhibitor-1), a derivative of MBCQ that binds to usp13 and inhibits deubiquitinase activity By similarity.

Domain

The UBP-type zinc finger has lost its ability to bind ubiquitin and usp13 is not activated by unanchored ubiquitin By similarity.

The UBA domains mediate binding to ubiquitin By similarity.

Sequence similarities

Belongs to the peptidase C19 family.

Contains 2 UBA domains.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 860860Ubiquitin carboxyl-terminal hydrolase 13
PRO_0000418013

Regions

Domain318 – 857540USP
Domain635 – 67642UBA 1
Domain710 – 75041UBA 2
Zinc finger190 – 26273UBP-type

Sites

Active site3271Nucleophile By similarity
Active site8191Proton acceptor By similarity

Experimental info

Sequence conflict7311Q → R in AAI41801. Ref.2

Sequences

Sequence LengthMass (Da)Tools
F1QFS9 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 456C6827F7D0DCC1

FASTA86097,452
        10         20         30         40         50         60 
MATDLGELLV PYMPTIRVPR TGDRVFKSEC AFSYDSPESE GGLYVCMNSF LGFGREHVER 

        70         80         90        100        110        120 
HYRKTGQSVY MHLKRHVKEK ATGAAGGAIP RRRNGKVFLD LELNRDFNGD DYEYEDEAKL 

       130        140        150        160        170        180 
VIFPDHYEIP LPNIEELPAL VTIACDAVLN APSPYKKQES DSWEEEIQVS RHARSLRQLD 

       190        200        210        220        230        240 
NGVRIPPSGW KCAKCEMREN LWLNLTDGSV LCGKWFFDGS GGNGHALEHY RESNFPLAVK 

       250        260        270        280        290        300 
LNTITPDGAD IYSFDEEEAV LDPHISEHLL HFGIDMLQMQ RTENGHHTDN HVQPRISDWE 

       310        320        330        340        350        360 
VIQEAGLKLK PVYGSGYTGI KNLGNSCYLS TTMQVLFSIP EFQRAYAGNL QRIFDYSPLD 

       370        380        390        400        410        420 
PTQDFNTQMA KLGHGLLSGQ YSKPPMKSEL IEQVMKEEHK QQQQRGISPK MFKALVSKGH 

       430        440        450        460        470        480 
PEFSSNRQQD AHEFLLHLIN LVERNNSGSE NPSDVFRFIV EERTQCCQSQ KVRYTQRVDY 

       490        500        510        520        530        540 
LMQLPVPLEA ASNREELIAY EGKRKEAEEN MRPLPEVVRA RVPFTACLQA FTEPENVPDF 

       550        560        570        580        590        600 
WSSALQAKSA GVKTSRFATF PEYMIVQLKK FTFGVDWVPK KLDMSVDVPD FLDLNRLRAT 

       610        620        630        640        650        660 
GLQAGEEELP DLTPPIVIPE DTRDSSTNNS LESPEIDESS VMQLAEMGFP LEACRKAVYY 

       670        680        690        700        710        720 
TGNMGAEMAF NWIIAHMEEP DFAEPLAVPT YMESDLPSPS LPTTSALDNQ PPEESISILT 

       730        740        750        760        770        780 
SMGFPRHHTI QALKASNNNL ERALDWIFTH PDCEDESEAM SDTADTEPND NSFSNANAHT 

       790        800        810        820        830        840 
DSSLSPDQDL SSPRVRDGPG RYELFAFISH MGTSTMSGHY VCHIKKEGRW LIYNDHKVCL 

       850        860 
SERPPKDLGY MYFYRRLSSC 

« 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 (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL928701 Genomic DNA. No translation available.
CU459215 Genomic DNA. No translation available.
BC141800 mRNA. Translation: AAI41801.1.
RefSeqNP_001091856.1. NM_001098386.1.
UniGeneDr.115281.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING7955.ENSDARP00000095070.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000065293; ENSDARP00000065292; ENSDARG00000079198.
GeneID558011.
KEGGdre:558011.

Organism-specific databases

CTD8975.
ZFINZDB-GENE-080724-7. usp13.

Phylogenomic databases

GeneTreeENSGT00390000000874.
KOK11836.
OMAPRMFKAF.
OrthoDBEOG7CNZF3.
TreeFamTF300576.

Gene expression databases

BgeeF1QFS9.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
IPR016652. Ubiquitinyl_hydrolase.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00627. UBA. 2 hits.
PF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PIRSFPIRSF016308. UBP. 1 hit.
SMARTSM00165. UBA. 2 hits.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
PROSITEPS50030. UBA. 2 hits.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20882266.

Entry information

Entry nameUBP13_DANRE
AccessionPrimary (citable) accession number: F1QFS9
Secondary accession number(s): A5D8T1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: May 3, 2011
Last modified: May 14, 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