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Protein

Ubiquitin carboxyl-terminal hydrolase 51

Gene

USP51

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei372 – 3721NucleophilePROSITE-ProRule annotation
Active sitei665 – 6651Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri234 – 29461UBP-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiC19.065.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:USP51
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:23086. USP51.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134888611.

Polymorphism and mutation databases

BioMutaiUSP51.
DMDMi52000873.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 711711Ubiquitin carboxyl-terminal hydrolase 51PRO_0000080680Add
BLAST

Proteomic databases

PRIDEiQ70EK9.

PTM databases

PhosphoSiteiQ70EK9.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ70EK9.
CleanExiHS_USP51.
GenevisibleiQ70EK9. HS.

Organism-specific databases

HPAiHPA001942.

Interactioni

Protein-protein interaction databases

BioGridi127720. 5 interactions.
STRINGi9606.ENSP00000423333.

Structurei

3D structure databases

ProteinModelPortaliQ70EK9.
SMRiQ70EK9. Positions 249-703.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini363 – 706344USPAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi97 – 14448Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated
Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri234 – 29461UBP-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00790000122966.
HOGENOMiHOG000007260.
HOVERGENiHBG058014.
InParanoidiQ70EK9.
KOiK11366.
OMAiWFSCDDA.
OrthoDBiEOG7FR7G7.
PhylomeDBiQ70EK9.
TreeFamiTF323554.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q70EK9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQVRETSLP SGSGVRWISG GGGGASPEEA VEKAGKMEEA AAGATKASSR
60 70 80 90 100
REAEEMKLEP LQEREPAPEE NLTWSSSGGD EKVLPSIPLR CHSSSSPVCP
110 120 130 140 150
RRKPRPRPQP RARSRSQPGL SAPPPPPARP PPPPPPPPPP APRPRAWRGS
160 170 180 190 200
RRRSRPGSRP QTRRSCSGDL DGSGDPGGLG DWLLEVEFGQ GPTGCSHVES
210 220 230 240 250
FKVGKNWQKN LRLIYQRFVW SGTPETRKRK AKSCICHVCS THMNRLHSCL
260 270 280 290 300
SCVFFGCFTE KHIHKHAETK QHHLAVDLYH GVIYCFMCKD YVYDKDIEQI
310 320 330 340 350
AKETKEKILR LLTSTSTDVS HQQFMTSGFE DKQSTCETKE QEPKLVKPKK
360 370 380 390 400
KRRKKSVYTV GLRGLINLGN TCFMNCIVQA LTHIPLLKDF FLSDKHKCIM
410 420 430 440 450
TSPSLCLVCE MSSLFHAMYS GSRTPHIPYK LLHLIWIHAE HLAGYRQQDA
460 470 480 490 500
HEFLIAILDV LHRHSKDDSG GQEANNPNCC NCIIDQIFTG GLQSDVTCQA
510 520 530 540 550
CHSVSTTIDP CWDISLDLPG SCATFDSQNP ERADSTVSRD DHIPGIPSLT
560 570 580 590 600
DCLQWFTRPE HLGSSAKIKC NSCQSYQEST KQLTMKKLPI VACFHLKRFE
610 620 630 640 650
HVGKQRRKIN TFISFPLELD MTPFLASTKE SRMKEGQPPT DCVPNENKYS
660 670 680 690 700
LFAVINHHGT LESGHYTSFI RQQKDQWFSC DDAIITKATI EDLLYSEGYL
710
LFYHKQGLEK D
Length:711
Mass (Da):79,756
Last modified:July 5, 2004 - v1
Checksum:iB721E620AE7ACE86
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ583823 mRNA. Translation: CAE47750.2.
AL732358 Genomic DNA. No translation available.
BC035907 mRNA. Translation: AAH35907.1. Sequence problems.
BN000340 mRNA. Translation: CAE48396.2.
CCDSiCCDS14370.1.
RefSeqiNP_958443.1. NM_201286.3.
UniGeneiHs.40061.
Hs.607524.

Genome annotation databases

EnsembliENST00000500968; ENSP00000423333; ENSG00000247746.
GeneIDi158880.
KEGGihsa:158880.
UCSCiuc004dun.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ583823 mRNA. Translation: CAE47750.2.
AL732358 Genomic DNA. No translation available.
BC035907 mRNA. Translation: AAH35907.1. Sequence problems.
BN000340 mRNA. Translation: CAE48396.2.
CCDSiCCDS14370.1.
RefSeqiNP_958443.1. NM_201286.3.
UniGeneiHs.40061.
Hs.607524.

3D structure databases

ProteinModelPortaliQ70EK9.
SMRiQ70EK9. Positions 249-703.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127720. 5 interactions.
STRINGi9606.ENSP00000423333.

Protein family/group databases

MEROPSiC19.065.

PTM databases

PhosphoSiteiQ70EK9.

Polymorphism and mutation databases

BioMutaiUSP51.
DMDMi52000873.

Proteomic databases

PRIDEiQ70EK9.

Protocols and materials databases

DNASUi158880.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000500968; ENSP00000423333; ENSG00000247746.
GeneIDi158880.
KEGGihsa:158880.
UCSCiuc004dun.2. human.

Organism-specific databases

CTDi158880.
GeneCardsiGC0XM055511.
HGNCiHGNC:23086. USP51.
HPAiHPA001942.
neXtProtiNX_Q70EK9.
PharmGKBiPA134888611.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00790000122966.
HOGENOMiHOG000007260.
HOVERGENiHBG058014.
InParanoidiQ70EK9.
KOiK11366.
OMAiWFSCDDA.
OrthoDBiEOG7FR7G7.
PhylomeDBiQ70EK9.
TreeFamiTF323554.

Miscellaneous databases

GeneWikiiUSP51.
GenomeRNAii158880.
NextBioi87839.
PROiQ70EK9.

Gene expression databases

BgeeiQ70EK9.
CleanExiHS_USP51.
GenevisibleiQ70EK9. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF00443. UCH. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
PROSITEiPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiUBP51_HUMAN
AccessioniPrimary (citable) accession number: Q70EK9
Secondary accession number(s): Q8IWJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.