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Reviewed, UniProtKB/Swiss-Prot Q96G74 (OTUD5_HUMAN)

Last modified January 19, 2010. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    OTU domain-containing protein 5
    EC=3.1.2.15
Alternative name(s):
    Deubiquinating enzyme A
      Short name=DUBA
Gene names
Name: OTUD5
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Negative regulator of innate immune system. Has deubiquitinating activity that is directed towards 'Lys-63'-linked polyubiquitin chains. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Ref.5

Catalytic activity

Ubiquitin C-terminal thioester + H2O = ubiquitin + a thiol.

Enzyme regulation

Inhibited by N-ethyl-maleimide (NEM).

Subunit structure

Interacts with TRAF3. Ref.5

Tissue specificity

Expressed in various tissues, including the liver and placenta, as well as in peripheral blood leukocytes. Ref.5

Induction

By bacterial lipopolysaccharides (LPS) in bone marrow-derived macrophages.

Sequence similarities

Belongs to the peptidase C85 family.

Contains 1 OTU domain.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmodification-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin thiolesterase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96G74-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96G74-2)

The sequence of this isoform differs from the canonical sequence as follows:
     17-40: Missing.
     304-308: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q96G74-3)

The sequence of this isoform differs from the canonical sequence as follows:
     304-308: Missing.
     563-566: HRDP → PCRC
     567-571: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 571571OTU domain-containing protein 5
PRO_0000278223

Regions

Domain213 – 341129OTU
Compositional bias5 – 113109Pro-rich
Compositional bias33 – 174142Gly-rich

Sites

Active site2211 Potential
Active site2241 Potential
Active site3341 Potential

Amino acid modifications

Modified residue641Phosphoserine Ref.4 Ref.6 Ref.7
Modified residue1651Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue1751Phosphotyrosine Ref.8
Modified residue1771Phosphoserine Ref.7 Ref.9
Modified residue4521Phosphoserine Ref.7
Modified residue5071Phosphothreonine Ref.8
Modified residue5081Phosphoserine Ref.8

Natural variations

Alternative sequence17 – 4024Missing in isoform 2.
VSP_023195
Alternative sequence304 – 3085Missing in isoform 2 and isoform 3.
VSP_023192
Alternative sequence563 – 5664HRDP → PCRC in isoform 3.
VSP_023193
Alternative sequence567 – 5715Missing in isoform 3.
VSP_023194

Experimental info

Mutagenesis2241C → S: Loss of suppression of IFN production. Ref.5
Mutagenesis5421L → A: Loss of 'K-48'- and 'K-63'-linked polyubiquitin chain binding. Partial loss of TRAF3 deubiquitination; when associated with A-549. Ref.5
Mutagenesis5491S → A: Loss of 'K-48'- and 'K-63'-linked polyubiquitin chain binding. Partial loss of TRAF3 deubiquitination; when associated with A-542. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F4B2B385B84ABC46

FASTA57160,626
        10         20         30         40         50         60 
MTILPKKKPP PPDADPANEP PPPGPMPPAP RRGGGVGVGG GGTGVGGGDR DRDSGVVGAR 

        70         80         90        100        110        120 
PRASPPPQGP LPGPPGALHR WALAVPPGAV AGPRPQQASP PPCGGPGGPG GGPGDALGAA 

       130        140        150        160        170        180 
AAGVGAAGVV VGVGGAVGVG GCCSGPGHSK RRRQAPGVGA VGGGSPEREE VGAGYNSEDE 

       190        200        210        220        230        240 
YEAAAARIEA MDPATVEQQE HWFEKALRDK KGFIIKQMKE DGACLFRAVA DQVYGDQDMH 

       250        260        270        280        290        300 
EVVRKHCMDY LMKNADYFSN YVTEDFTTYI NRKRKNNCHG NHIEMQAMAE MYNRPVEVYQ 

       310        320        330        340        350        360 
YSTGTSAVEP INTFHGIHQN EDEPIRVSYH RNIHYNSVVN PNKATIGVGL GLPSFKPGFA 

       370        380        390        400        410        420 
EQSLMKNAIK TSEESWIEQQ MLEDKKRATD WEATNEAIEE QVARESYLQW LRDQEKQARQ 

       430        440        450        460        470        480 
VRGPSQPRKA SATCSSATAA ASSGLEEWTS RSPRQRSSAS SPEHPELHAE LGMKPPSPGT 

       490        500        510        520        530        540 
VLALAKPPSP CAPGTSSQFS AGADRATSPL VSLYPALECR ALIQQMSPSA FGLNDWDDDE 

       550        560        570 
ILASVLAVSQ QEYLDSMKKN KVHRDPPPDK S 

« Hide

Isoform 2.

Checksum: FB641E44937EC3F2
Show »

FASTA54258,007
Isoform 3.

Checksum: 9C931880385CF8CB
Show »

FASTA56159,640

References

[1]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Kidney and Skin.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-571 (ISOFORM 2).
Tissue: Amygdala.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-571 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-571 (ISOFORM 1).
Tissue: Small intestine.
[4]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY.
Tissue: Epithelium.
[5]"DUBA: a deubiquitinase that regulates type I interferon production."
Kayagaki N., Phung Q., Chan S., Chaudhari R., Quan C., O'Rourke K.M., Eby M., Pietras E., Cheng G., Bazan J.F., Zhang Z., Arnott D., Dixit V.M.
Science 318:1628-1632(2007) [PubMed: 17991829] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRAF3, MUTAGENESIS OF CYS-224; LEU-542 AND SER-549.
[6]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY.
[7]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-165; SER-177 AND SER-452, MASS SPECTROMETRY.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; TYR-175; THR-507 AND SER-508, MASS SPECTROMETRY.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-177, MASS SPECTROMETRY.
Tissue: T-cell.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC009917 mRNA. Translation: AAH09917.1.
BC028225 mRNA. Translation: AAH28225.1.
BC098440 mRNA. Translation: AAH98440.1.
AL137509 mRNA. Translation: CAB70778.1.
AK022612 mRNA. Translation: BAB14131.1. Different initiation.
AK026260 mRNA. Translation: BAB15416.1. Different initiation.
IPIIPI00640364.
IPI00641956.
IPI00940013.
PIRT46265.
RefSeqNP_001129629.1.
NP_001129630.1.
NP_060072.1.
UniGeneHs.496098

3D structure databases

SMRQ96G74. Positions 208-340.
ModBaseSearch...

Protein-protein interaction databases

IntActQ96G74. 1 interaction.

Protein family/group databases

MEROPSC85.001.

PTM databases

PhosphoSiteQ96G74.

Proteomic databases

PRIDEQ96G74.

Genome annotation databases

EnsemblENST00000156084; ENSP00000156084; ENSG00000068308; Homo sapiens. [Genome view]
GeneID55593.
KEGGhsa:55593.
UCSCuc004dlt.2. human.
uc004dlu.1. human.

Organism-specific databases

CTD55593.
GeneCardsGC0XM048665.
HGNCHGNC:25402. OTUD5.
HPAHPA017375.
MIM300713. gene.
PharmGKBPA142671217.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG04829.
HOGENOMHBG717174.
HOVERGENQ96G74.
InParanoidQ96G74.
OMASPPPCGG.
PhylomeDBQ96G74.

Gene expression databases

ArrayExpressQ96G74.
BgeeQ96G74.
CleanExHS_OTUD5.
GenevestigatorQ96G74.

Family and domain databases

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

Other Resources

NextBio60126.
SOURCESearch...

Entry information

Entry nameOTUD5_HUMAN
AccessionPrimary (citable) accession number: Q96G74
Secondary accession number(s): Q4KMN9 expand/collapse secondary AC list , Q8N6T5, Q9H650, Q9H9U0, Q9NT65
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: December 1, 2001
Last modified: January 19, 2010
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome X

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

MIM cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents