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Q5VV17 (OTUD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
OTU domain-containing protein 1

EC=3.4.19.12
Alternative name(s):
DUBA-7
Gene names
Name:OTUD1
Synonyms:DUBA7, OTDC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deubiquitinating enzyme that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin. Ref.2

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.2

Domain

The UIM repeat increases the specificity and efficiency of the enzyme toward 'Lys-63'-linked polyubiquitin (Ref.2).

Specificity is not given by the S1' ubiquitin-binding site within the OTU domain (composed of the Cys-, His- and Variable-loops) (Ref.2).

Sequence similarities

Contains 1 OTU domain.

Contains 1 UIM (ubiquitin-interacting motif) repeat.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Molecular functionHydrolase
Protease
Thiol protease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein K63-linked deubiquitination

Inferred from direct assay Ref.2. Source: UniProtKB

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionubiquitin-specific protease activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481OTU domain-containing protein 1
PRO_0000271018

Regions

Domain309 – 438130OTU
Repeat457 – 47620UIM
Region314 – 3207Cys-loop
Region369 – 37911His-loop
Region426 – 4316Variable-loop
Compositional bias13 – 155143Ala-rich

Sites

Active site3171 By similarity
Active site3201Nucleophile By similarity
Active site4311 By similarity

Secondary structure

........................... 481
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5VV17 [UniParc].

Last modified December 7, 2004. Version 1.
Checksum: 37B3AEB0B3851982

FASTA48151,063
        10         20         30         40         50         60 
MQLYSSVCTH YPAGAPGPTA AAPAPPAAAT PFKVSLQPPG AAGAAPEPET GECQPAAAAE 

        70         80         90        100        110        120 
HREAAAVPAA KMPAFSSCFE VVSGAAAPAS AAAGPPGASC KPPLPPHYTS TAQITVRALG 

       130        140        150        160        170        180 
ADRLLLHGPD PVPGAAGSAA APRGRCLLLA PAPAAPVPPR RGSSAWLLEE LLRPDCPEPA 

       190        200        210        220        230        240 
GLDATREGPD RNFRLSEHRQ ALAAAKHRGP AATPGSPDPG PGPWGEEHLA ERGPRGWERG 

       250        260        270        280        290        300 
GDRCDAPGGD AARRPDPEAE APPAGSIEAA PSSAAEPVIV SRSDPRDEKL ALYLAEVEKQ 

       310        320        330        340        350        360 
DKYLRQRNKY RFHIIPDGNC LYRAVSKTVY GDQSLHRELR EQTVHYIADH LDHFSPLIEG 

       370        380        390        400        410        420 
DVGEFIIAAA QDGAWAGYPE LLAMGQMLNV NIHLTTGGRL ESPTVSTMIH YLGPEDSLRP 

       430        440        450        460        470        480 
SIWLSWLSNG HYDAVFDHSY PNPEYDNWCK QTQVQRKRDE ELAKSMAISL SKMYIEQNAC 


S 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 287-437, FUNCTION, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL512603 Genomic DNA. Translation: CAH73715.1.
RefSeqNP_001138845.1. NM_001145373.2.
UniGeneHs.499042.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BOPX-ray2.10A/B287-437[»]
ProteinModelPortalQ5VV17.
SMRQ5VV17. Positions 288-437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128638. 7 interactions.
IntActQ5VV17. 10 interactions.
STRING9606.ENSP00000365678.

Protein family/group databases

MEROPSC85.004.

PTM databases

PhosphoSiteQ5VV17.

Polymorphism databases

DMDM74747188.

Proteomic databases

PaxDbQ5VV17.
PRIDEQ5VV17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376495; ENSP00000365678; ENSG00000165312.
GeneID220213.
KEGGhsa:220213.
UCSCuc001irr.2. human.

Organism-specific databases

CTD220213.
GeneCardsGC10P023768.
HGNCHGNC:27346. OTUD1.
HPAHPA038504.
MIM612022. gene.
neXtProtNX_Q5VV17.
PharmGKBPA134932304.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327202.
HOGENOMHOG000115304.
HOVERGENHBG080487.
InParanoidQ5VV17.
KOK13716.
OMANFRLSEH.
OrthoDBEOG7TBC35.
TreeFamTF338508.

Gene expression databases

BgeeQ5VV17.
CleanExHS_OTUD1.
GenevestigatorQ5VV17.

Family and domain databases

InterProIPR003323. OTU.
[Graphical view]
PfamPF02338. OTU. 1 hit.
[Graphical view]
PROSITEPS50802. OTU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi220213.
NextBio91030.
PROQ5VV17.
SOURCESearch...

Entry information

Entry nameOTUD1_HUMAN
AccessionPrimary (citable) accession number: Q5VV17
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: December 7, 2004
Last modified: March 19, 2014
This is version 66 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM