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Q70EK9 (UBP51_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 51

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme 51
Ubiquitin thioesterase 51
Ubiquitin-specific-processing protease 51
Gene names
Name:USP51
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length711 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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). Ref.1

Tissue specificity

Expressed in prostate, brain, lung, aorta and kidney. Ref.1

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 UBP-type zinc finger.

Contains 1 USP domain.

Sequence caution

The sequence AAH35907.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 711711Ubiquitin carboxyl-terminal hydrolase 51
PRO_0000080680

Regions

Domain363 – 706344USP
Zinc finger234 – 29461UBP-type
Compositional bias97 – 14448Pro-rich

Sites

Active site3721Nucleophile By similarity
Active site6651Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q70EK9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: B721E620AE7ACE86

FASTA71179,756
        10         20         30         40         50         60 
MAQVRETSLP SGSGVRWISG GGGGASPEEA VEKAGKMEEA AAGATKASSR REAEEMKLEP 

        70         80         90        100        110        120 
LQEREPAPEE NLTWSSSGGD EKVLPSIPLR CHSSSSPVCP RRKPRPRPQP RARSRSQPGL 

       130        140        150        160        170        180 
SAPPPPPARP PPPPPPPPPP APRPRAWRGS RRRSRPGSRP QTRRSCSGDL DGSGDPGGLG 

       190        200        210        220        230        240 
DWLLEVEFGQ GPTGCSHVES FKVGKNWQKN LRLIYQRFVW SGTPETRKRK AKSCICHVCS 

       250        260        270        280        290        300 
THMNRLHSCL SCVFFGCFTE KHIHKHAETK QHHLAVDLYH GVIYCFMCKD YVYDKDIEQI 

       310        320        330        340        350        360 
AKETKEKILR LLTSTSTDVS HQQFMTSGFE DKQSTCETKE QEPKLVKPKK KRRKKSVYTV 

       370        380        390        400        410        420 
GLRGLINLGN TCFMNCIVQA LTHIPLLKDF FLSDKHKCIM TSPSLCLVCE MSSLFHAMYS 

       430        440        450        460        470        480 
GSRTPHIPYK LLHLIWIHAE HLAGYRQQDA HEFLIAILDV LHRHSKDDSG GQEANNPNCC 

       490        500        510        520        530        540 
NCIIDQIFTG GLQSDVTCQA CHSVSTTIDP CWDISLDLPG SCATFDSQNP ERADSTVSRD 

       550        560        570        580        590        600 
DHIPGIPSLT DCLQWFTRPE HLGSSAKIKC NSCQSYQEST KQLTMKKLPI VACFHLKRFE 

       610        620        630        640        650        660 
HVGKQRRKIN TFISFPLELD MTPFLASTKE SRMKEGQPPT DCVPNENKYS LFAVINHHGT 

       670        680        690        700        710 
LESGHYTSFI RQQKDQWFSC DDAIITKATI EDLLYSEGYL LFYHKQGLEK D 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and enzymatic analysis of 22 novel human ubiquitin-specific proteases."
Quesada V., Diaz-Perales A., Gutierrez-Fernandez A., Garabaya C., Cal S., Lopez-Otin C.
Biochem. Biophys. Res. Commun. 314:54-62(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, ENZYME ACTIVITY.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-305.
Tissue: Mammary gland.
[4]"A genomic analysis of rat proteases and protease inhibitors."
Puente X.S., Lopez-Otin C.
Genome Res. 14:609-622(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ583823 mRNA. Translation: CAE47750.2.
AL732358 Genomic DNA. No translation available.
BC035907 mRNA. Translation: AAH35907.1. Sequence problems.
BN000340 mRNA. Translation: CAE48396.2.
RefSeqNP_958443.1. NM_201286.3.
XP_005262049.1. XM_005261992.1.
UniGeneHs.40061.
Hs.607524.

3D structure databases

ProteinModelPortalQ70EK9.
SMRQ70EK9. Positions 193-709.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127720. 4 interactions.

Protein family/group databases

MEROPSC19.065.

PTM databases

PhosphoSiteQ70EK9.

Polymorphism databases

DMDM52000873.

Proteomic databases

PRIDEQ70EK9.

Protocols and materials databases

DNASU158880.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000500968; ENSP00000423333; ENSG00000247746.
GeneID158880.
KEGGhsa:158880.
UCSCuc004dun.2. human.

Organism-specific databases

CTD158880.
GeneCardsGC0XM055511.
HGNCHGNC:23086. USP51.
HPAHPA001942.
neXtProtNX_Q70EK9.
PharmGKBPA134888611.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000007260.
HOVERGENHBG058014.
InParanoidQ70EK9.
KOK11366.
OMAWFSCDDA.
OrthoDBEOG7FR7G7.
PhylomeDBQ70EK9.
TreeFamTF323554.

Gene expression databases

BgeeQ70EK9.
CleanExHS_USP51.
GenevestigatorQ70EK9.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiUSP51.
GenomeRNAi158880.
NextBio87839.
PROQ70EK9.

Entry information

Entry nameUBP51_HUMAN
AccessionPrimary (citable) accession number: Q70EK9
Secondary accession number(s): Q8IWJ8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM