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Protein

OTU domain-containing protein 1

Gene

OTUD1

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

Functioni

Deubiquitinating enzyme that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin.1 Publication

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 sitei317 – 3171By similarity
Active sitei320 – 3201NucleophileBy similarity
Active sitei431 – 4311By similarity

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. protein K63-linked deubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC85.004.

Names & Taxonomyi

Protein namesi
Recommended name:
OTU domain-containing protein 1 (EC:3.4.19.12)
Alternative name(s):
DUBA-7
Gene namesi
Name:OTUD1
Synonyms:DUBA7, OTDC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:27346. OTUD1.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134932304.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 481481OTU domain-containing protein 1PRO_0000271018Add
BLAST

Proteomic databases

MaxQBiQ5VV17.
PaxDbiQ5VV17.
PRIDEiQ5VV17.

PTM databases

PhosphoSiteiQ5VV17.

Expressioni

Gene expression databases

BgeeiQ5VV17.
CleanExiHS_OTUD1.
GenevestigatoriQ5VV17.

Organism-specific databases

HPAiHPA038504.

Interactioni

Protein-protein interaction databases

BioGridi128638. 8 interactions.
IntActiQ5VV17. 10 interactions.
STRINGi9606.ENSP00000365678.

Structurei

Secondary structure

1
481
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi289 – 30618Combined sources
Beta strandi310 – 3123Combined sources
Helixi320 – 33011Combined sources
Helixi333 – 3353Combined sources
Helixi336 – 34914Combined sources
Helixi351 – 3544Combined sources
Helixi355 – 3573Combined sources
Helixi362 – 3698Combined sources
Helixi378 – 38811Combined sources
Beta strandi391 – 3999Combined sources
Beta strandi402 – 4109Combined sources
Beta strandi412 – 4143Combined sources
Beta strandi421 – 4277Combined sources
Turni428 – 4303Combined sources
Beta strandi431 – 4366Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BOPX-ray2.10A/B287-437[»]
ProteinModelPortaliQ5VV17.
SMRiQ5VV17. Positions 288-437.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini309 – 438130OTUPROSITE-ProRule annotationAdd
BLAST
Domaini457 – 47620UIMCuratedAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni314 – 3207Cys-loop
Regioni369 – 37911His-loopAdd
BLAST
Regioni426 – 4316Variable-loop

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi13 – 155143Ala-richAdd
BLAST

Domaini

The UIM repeat increases the specificity and efficiency of the enzyme toward 'Lys-63'-linked polyubiquitin.1 Publication
Specificity is not given by the S1' ubiquitin-binding site within the OTU domain (composed of the Cys-, His- and Variable-loops).1 Publication

Sequence similaritiesi

Contains 1 OTU domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG327202.
GeneTreeiENSGT00510000049635.
HOGENOMiHOG000115304.
HOVERGENiHBG080487.
InParanoidiQ5VV17.
KOiK13716.
OMAiPHYTSTA.
OrthoDBiEOG7TBC35.
PhylomeDBiQ5VV17.
TreeFamiTF338508.

Family and domain databases

InterProiIPR003323. OTU.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
[Graphical view]
PROSITEiPS50802. OTU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5VV17-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLYSSVCTH YPAGAPGPTA AAPAPPAAAT PFKVSLQPPG AAGAAPEPET
60 70 80 90 100
GECQPAAAAE HREAAAVPAA KMPAFSSCFE VVSGAAAPAS AAAGPPGASC
110 120 130 140 150
KPPLPPHYTS TAQITVRALG ADRLLLHGPD PVPGAAGSAA APRGRCLLLA
160 170 180 190 200
PAPAAPVPPR RGSSAWLLEE LLRPDCPEPA GLDATREGPD RNFRLSEHRQ
210 220 230 240 250
ALAAAKHRGP AATPGSPDPG PGPWGEEHLA ERGPRGWERG GDRCDAPGGD
260 270 280 290 300
AARRPDPEAE APPAGSIEAA PSSAAEPVIV SRSDPRDEKL ALYLAEVEKQ
310 320 330 340 350
DKYLRQRNKY RFHIIPDGNC LYRAVSKTVY GDQSLHRELR EQTVHYIADH
360 370 380 390 400
LDHFSPLIEG DVGEFIIAAA QDGAWAGYPE LLAMGQMLNV NIHLTTGGRL
410 420 430 440 450
ESPTVSTMIH YLGPEDSLRP SIWLSWLSNG HYDAVFDHSY PNPEYDNWCK
460 470 480
QTQVQRKRDE ELAKSMAISL SKMYIEQNAC S
Length:481
Mass (Da):51,063
Last modified:December 7, 2004 - v1
Checksum:i37B3AEB0B3851982
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL512603 Genomic DNA. Translation: CAH73715.1.
CCDSiCCDS44366.1.
RefSeqiNP_001138845.1. NM_001145373.2.
UniGeneiHs.499042.

Genome annotation databases

EnsembliENST00000376495; ENSP00000365678; ENSG00000165312.
GeneIDi220213.
KEGGihsa:220213.
UCSCiuc001irr.2. human.

Polymorphism databases

DMDMi74747188.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL512603 Genomic DNA. Translation: CAH73715.1.
CCDSiCCDS44366.1.
RefSeqiNP_001138845.1. NM_001145373.2.
UniGeneiHs.499042.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BOPX-ray2.10A/B287-437[»]
ProteinModelPortaliQ5VV17.
SMRiQ5VV17. Positions 288-437.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128638. 8 interactions.
IntActiQ5VV17. 10 interactions.
STRINGi9606.ENSP00000365678.

Protein family/group databases

MEROPSiC85.004.

PTM databases

PhosphoSiteiQ5VV17.

Polymorphism databases

DMDMi74747188.

Proteomic databases

MaxQBiQ5VV17.
PaxDbiQ5VV17.
PRIDEiQ5VV17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376495; ENSP00000365678; ENSG00000165312.
GeneIDi220213.
KEGGihsa:220213.
UCSCiuc001irr.2. human.

Organism-specific databases

CTDi220213.
GeneCardsiGC10P023728.
HGNCiHGNC:27346. OTUD1.
HPAiHPA038504.
MIMi612022. gene.
neXtProtiNX_Q5VV17.
PharmGKBiPA134932304.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG327202.
GeneTreeiENSGT00510000049635.
HOGENOMiHOG000115304.
HOVERGENiHBG080487.
InParanoidiQ5VV17.
KOiK13716.
OMAiPHYTSTA.
OrthoDBiEOG7TBC35.
PhylomeDBiQ5VV17.
TreeFamiTF338508.

Miscellaneous databases

GenomeRNAii220213.
NextBioi91030.
PROiQ5VV17.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VV17.
CleanExiHS_OTUD1.
GenevestigatoriQ5VV17.

Family and domain databases

InterProiIPR003323. OTU.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
[Graphical view]
PROSITEiPS50802. OTU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiOTUD1_HUMAN
AccessioniPrimary (citable) accession number: Q5VV17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: December 7, 2004
Last modified: February 4, 2015
This is version 74 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.