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Q5T2D3 (OTUD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 3

EC=3.4.19.12
Gene names
Name:OTUD3
Synonyms:KIAA0459
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deubiquitinating enzyme that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. Also hydrolyzes heterotypic (mixed and branched) and homotypic chains. Ref.4

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.4

Domain

The UBA-like domain has no influence on ubiquitin hydrolysis (Ref.4).

Specificity is given by the S1' ubiquitin-binding site within the OTU domain composed of the Cys-, His- and Variable-loops (Ref.4).

Sequence similarities

Contains 1 OTU domain.

Contains 1 UBA-like domain.

Sequence caution

The sequence BAA32304.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein K11-linked deubiquitination

Inferred from direct assay Ref.4. Source: UniProtKB

protein K6-linked deubiquitination

Inferred from direct assay Ref.4. Source: UniProtKB

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionubiquitin-specific protease activity

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398OTU domain-containing protein 3
PRO_0000058103

Regions

Domain65 – 189125OTU
Domain230 – 27041UBA-like
Region70 – 767Cys-loop
Region127 – 13711Variable-loop
Region177 – 1826His-loop

Sites

Active site731 By similarity
Active site761Nucleophile By similarity
Active site1821 By similarity

Natural variations

Natural variant3211N → S.
Corresponds to variant rs2298110 [ dbSNP | Ensembl ].
VAR_051258
Natural variant3331A → T.
Corresponds to variant rs10916668 [ dbSNP | Ensembl ].
VAR_051259

Experimental info

Mutagenesis178 – 1814RYGE → LSNG: Impaired activity. Ref.4

Secondary structure

......................... 398
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5T2D3 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 9C16E610CF1E3C5A

FASTA39845,124
        10         20         30         40         50         60 
MSRKQAAKSR PGSGSRKAEA ERKRDERAAR RALAKERRNR PESGGGGGCE EEFVSFANQL 

        70         80         90        100        110        120 
QALGLKLREV PGDGNCLFRA LGDQLEGHSR NHLKHRQETV DYMIKQREDF EPFVEDDIPF 

       130        140        150        160        170        180 
EKHVASLAKP GTFAGNDAIV AFARNHQLNV VIHQLNAPLW QIRGTEKSSV RELHIAYRYG 

       190        200        210        220        230        240 
EHYDSVRRIN DNSEAPAHLQ TDFQMLHQDE SNKREKIKTK GMDSEDDLRD EVEDAVQKVC 

       250        260        270        280        290        300 
NATGCSDFNL IVQNLEAENY NIESAIIAVL RMNQGKRNNA EENLEPSGRV LKQCGPLWEE 

       310        320        330        340        350        360 
GGSGARIFGN QGLNEGRTEN NKAQASPSEE NKANKNQLAK VTNKQRREQQ WMEKKKRQEE 

       370        380        390 
RHRHKALESR GSHRDNNRSE AEANTQVTLV KTFAALNI 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[4]"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 (1.55 ANGSTROMS) OF 52-209, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF 178-ARG--GLU-181.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB007928 mRNA. Translation: BAA32304.2. Different initiation.
AL391883 Genomic DNA. Translation: CAI17041.1.
RefSeqNP_056022.1. NM_015207.1.
UniGeneHs.374987.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BOUX-ray1.55A52-209[»]
ProteinModelPortalQ5T2D3.
SMRQ5T2D3. Positions 52-190.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116856. 2 interactions.
STRING9606.ENSP00000364261.

Protein family/group databases

MEROPSC85.003.

PTM databases

PhosphoSiteQ5T2D3.

Proteomic databases

PaxDbQ5T2D3.
PRIDEQ5T2D3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375120; ENSP00000364261; ENSG00000169914.
GeneID23252.
KEGGhsa:23252.
UCSCuc001bcs.4. human.

Organism-specific databases

CTD23252.
GeneCardsGC01P020208.
HGNCHGNC:29038. OTUD3.
HPAHPA028543.
HPA028544.
MIM611758. gene.
neXtProtNX_Q5T2D3.
PharmGKBPA142671215.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG136081.
HOGENOMHOG000049263.
HOVERGENHBG056738.
InParanoidQ5T2D3.
KOK13717.
OMAANKNQLP.
OrthoDBEOG70ZZNW.
PhylomeDBQ5T2D3.
TreeFamTF329594.

Gene expression databases

ArrayExpressQ5T2D3.
BgeeQ5T2D3.
CleanExHS_OTUD3.
GenevestigatorQ5T2D3.

Family and domain databases

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

Other

GenomeRNAi23252.
NextBio44955.
PROQ5T2D3.
SOURCESearch...

Entry information

Entry nameOTUD3_HUMAN
AccessionPrimary (citable) accession number: Q5T2D3
Secondary accession number(s): O75047
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 72 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM