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Q5T2D3

- OTUD3_HUMAN

UniProt

Q5T2D3 - OTUD3_HUMAN

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Protein
OTU domain-containing protein 3
Gene
OTUD3, KIAA0459
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Deubiquitinating enzyme that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. Also hydrolyzes heterotypic (mixed and branched) and homotypic chains.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 sitei73 – 731 By similarity
Active sitei76 – 761Nucleophile By similarity
Active sitei182 – 1821 By similarity

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. protein K11-linked deubiquitination Source: UniProtKB
  2. protein K6-linked deubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC85.003.

Names & Taxonomyi

Protein namesi
Recommended name:
OTU domain-containing protein 3 (EC:3.4.19.12)
Gene namesi
Name:OTUD3
Synonyms:KIAA0459
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:29038. OTUD3.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi178 – 1814RYGE → LSNG: Impaired activity. 1 Publication

Organism-specific databases

PharmGKBiPA142671215.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398OTU domain-containing protein 3
PRO_0000058103Add
BLAST

Proteomic databases

MaxQBiQ5T2D3.
PaxDbiQ5T2D3.
PRIDEiQ5T2D3.

PTM databases

PhosphoSiteiQ5T2D3.

Expressioni

Gene expression databases

ArrayExpressiQ5T2D3.
BgeeiQ5T2D3.
CleanExiHS_OTUD3.
GenevestigatoriQ5T2D3.

Organism-specific databases

HPAiHPA028543.
HPA028544.

Interactioni

Protein-protein interaction databases

BioGridi116856. 2 interactions.
STRINGi9606.ENSP00000364261.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 627
Beta strandi65 – 684
Helixi76 – 8611
Beta strandi87 – 893
Helixi92 – 10514
Helixi107 – 1104
Helixi111 – 1133
Helixi120 – 1289
Helixi136 – 14510
Beta strandi149 – 1535
Beta strandi160 – 1667
Beta strandi172 – 1787
Turni179 – 1813
Beta strandi182 – 1887

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BOUX-ray1.55A52-209[»]
ProteinModelPortaliQ5T2D3.
SMRiQ5T2D3. Positions 52-190.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 189125OTU
Add
BLAST
Domaini230 – 27041UBA-like
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 767Cys-loop
Regioni127 – 13711Variable-loop
Add
BLAST
Regioni177 – 1826His-loop

Domaini

The UBA-like domain has no influence on ubiquitin hydrolysis (1 Publication).
Specificity is 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.
Contains 1 UBA-like domain.

Phylogenomic databases

eggNOGiNOG136081.
HOGENOMiHOG000049263.
HOVERGENiHBG056738.
InParanoidiQ5T2D3.
KOiK13717.
OMAiANKNQLP.
OrthoDBiEOG70ZZNW.
PhylomeDBiQ5T2D3.
TreeFamiTF329594.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q5T2D3-1 [UniParc]FASTAAdd to Basket

« Hide

MSRKQAAKSR PGSGSRKAEA ERKRDERAAR RALAKERRNR PESGGGGGCE    50
EEFVSFANQL QALGLKLREV PGDGNCLFRA LGDQLEGHSR NHLKHRQETV 100
DYMIKQREDF EPFVEDDIPF EKHVASLAKP GTFAGNDAIV AFARNHQLNV 150
VIHQLNAPLW QIRGTEKSSV RELHIAYRYG EHYDSVRRIN DNSEAPAHLQ 200
TDFQMLHQDE SNKREKIKTK GMDSEDDLRD EVEDAVQKVC NATGCSDFNL 250
IVQNLEAENY NIESAIIAVL RMNQGKRNNA EENLEPSGRV LKQCGPLWEE 300
GGSGARIFGN QGLNEGRTEN NKAQASPSEE NKANKNQLAK VTNKQRREQQ 350
WMEKKKRQEE RHRHKALESR GSHRDNNRSE AEANTQVTLV KTFAALNI 398
Length:398
Mass (Da):45,124
Last modified:December 21, 2004 - v1
Checksum:i9C16E610CF1E3C5A
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti321 – 3211N → S.
Corresponds to variant rs2298110 [ dbSNP | Ensembl ].
VAR_051258
Natural varianti333 – 3331A → T.
Corresponds to variant rs10916668 [ dbSNP | Ensembl ].
VAR_051259

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB007928 mRNA. Translation: BAA32304.2. Different initiation.
AL391883 Genomic DNA. Translation: CAI17041.1.
CCDSiCCDS41279.1.
RefSeqiNP_056022.1. NM_015207.1.
UniGeneiHs.374987.

Genome annotation databases

EnsembliENST00000375120; ENSP00000364261; ENSG00000169914.
GeneIDi23252.
KEGGihsa:23252.
UCSCiuc001bcs.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB007928 mRNA. Translation: BAA32304.2 . Different initiation.
AL391883 Genomic DNA. Translation: CAI17041.1 .
CCDSi CCDS41279.1.
RefSeqi NP_056022.1. NM_015207.1.
UniGenei Hs.374987.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BOU X-ray 1.55 A 52-209 [» ]
ProteinModelPortali Q5T2D3.
SMRi Q5T2D3. Positions 52-190.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116856. 2 interactions.
STRINGi 9606.ENSP00000364261.

Protein family/group databases

MEROPSi C85.003.

PTM databases

PhosphoSitei Q5T2D3.

Proteomic databases

MaxQBi Q5T2D3.
PaxDbi Q5T2D3.
PRIDEi Q5T2D3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375120 ; ENSP00000364261 ; ENSG00000169914 .
GeneIDi 23252.
KEGGi hsa:23252.
UCSCi uc001bcs.4. human.

Organism-specific databases

CTDi 23252.
GeneCardsi GC01P020208.
HGNCi HGNC:29038. OTUD3.
HPAi HPA028543.
HPA028544.
MIMi 611758. gene.
neXtProti NX_Q5T2D3.
PharmGKBi PA142671215.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG136081.
HOGENOMi HOG000049263.
HOVERGENi HBG056738.
InParanoidi Q5T2D3.
KOi K13717.
OMAi ANKNQLP.
OrthoDBi EOG70ZZNW.
PhylomeDBi Q5T2D3.
TreeFami TF329594.

Miscellaneous databases

GenomeRNAii 23252.
NextBioi 44955.
PROi Q5T2D3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q5T2D3.
Bgeei Q5T2D3.
CleanExi HS_OTUD3.
Genevestigatori Q5T2D3.

Family and domain databases

InterProi IPR003323. OTU.
[Graphical view ]
Pfami PF02338. OTU. 1 hit.
[Graphical view ]
PROSITEi PS50802. OTU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiOTUD3_HUMAN
AccessioniPrimary (citable) accession number: Q5T2D3
Secondary accession number(s): O75047
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: December 21, 2004
Last modified: July 9, 2014
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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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