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Q2YDU3

- OTUD5_RAT

UniProt

Q2YDU3 - OTUD5_RAT

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Protein
OTU domain-containing protein 5
Gene
Otud5
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Deubiquitinating enzyme that functions as negative regulator of the innate immune system. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro) By similarity.

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).

Enzyme regulationi

Inhibited by N-ethyl-maleimide (NEM) By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei221 – 2211 Reviewed prediction
Active sitei224 – 2241Nucleophile By similarity
Active sitei329 – 3291 By similarity

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. protein K48-linked deubiquitination Source: UniProtKB
  2. protein K63-linked deubiquitination Source: UniProtKB
  3. response to lipopolysaccharide Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_198997. Negative regulators of RIG-I/MDA5 signaling.

Protein family/group databases

MEROPSiC85.001.

Names & Taxonomyi

Protein namesi
Recommended name:
OTU domain-containing protein 5 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme A
Short name:
DUBA
Gene namesi
Name:Otud5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome X

Organism-specific databases

RGDi1563027. Otud5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 566566OTU domain-containing protein 5
PRO_0000278225Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Phosphoserine By similarity
Modified residuei165 – 1651Phosphoserine By similarity
Modified residuei175 – 1751Phosphotyrosine By similarity
Modified residuei177 – 1771Phosphoserine By similarity
Modified residuei447 – 4471Phosphoserine By similarity
Modified residuei502 – 5021Phosphothreonine By similarity

Post-translational modificationi

Phosphorylation at Ser-177 is required for deubiquitinating activity By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ2YDU3.

Expressioni

Gene expression databases

GenevestigatoriQ2YDU3.

Interactioni

Subunit structurei

Interacts with TRAF3 By similarity.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000039455.

Structurei

3D structure databases

ProteinModelPortaliQ2YDU3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini213 – 336124OTU
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni218 – 2247Cys-loop By similarity
Regioni273 – 28311Variable-loop By similarity
Add
BLAST
Regioni324 – 3296His-loop By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 113109Pro-rich
Add
BLAST
Compositional biasi33 – 174142Gly-rich
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase C85 family.
Contains 1 OTU domain.

Phylogenomic databases

eggNOGiNOG286112.
GeneTreeiENSGT00510000048473.
HOGENOMiHOG000231360.
HOVERGENiHBG060214.
InParanoidiQ2YDU3.
KOiK12655.
OMAiWEDDEIL.
OrthoDBiEOG77Q4X0.
PhylomeDBiQ2YDU3.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q2YDU3-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MTILPKKKPP PPDADPANEP PPPGPLPPAP RRGGGVGVGG GGTGVGGGER    50
DRDSGVVGAR PRASPPPQGP LPGPPGALHR WALAVPPGAV AGPRPQQASP 100
PPCGGPGGPG GGPGDALGAT TAGVGAAGVV VGVGGPVGVG GCCSGPGHSK 150
RRRQAPGVGA VGGASPEREE VGAGYNSEDE YEAAAARIEA MDPATVEQQE 200
HWFEKALRDK KGFIIKQMKE DGACLFRAVA DQVYGDQDMH EVVRKHCMDY 250
LMKNADYFSN YVTEDFTTYI NRKRKNNCHG NHIEMQAMAE MYNRPVEVYQ 300
YSTEPINTFH GIHQNEDEPI RVSYHRNIHY NSVVNPNKAT IGVGLGLPSF 350
KPGFAEQSLM KNAIKTSEES WIEQQMLEDK KRATDWEATN EAIEEQVARE 400
SYLQWLRDQE KQARQVRGPS QPRKASATCS SATAAASSGL EEWTSRSPRQ 450
RSSASSPEHP ELHAELGIKP PSPGTVLALA KPPSPCAPGT SSQFSAGADR 500
ATSPLVSLYP ALECRALIQQ MSPSAFGLND WDDDEILASV LAVSQQEYLD 550
SMKKNKVHRD PPPDKS 566
Length:566
Mass (Da):60,288
Last modified:February 20, 2007 - v2
Checksum:i1B49AF4337634A07
GO
Isoform 2 (identifier: Q2YDU3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     118-160: Missing.

Show »
Length:523
Mass (Da):56,534
Checksum:iCB83BE543DEACE23
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei118 – 16043Missing in isoform 2.
VSP_023197Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03119131 Genomic DNA. No translation available.
BC110054 mRNA. Translation: AAI10055.1.
RefSeqiNP_001032585.1. NM_001037496.1. [Q2YDU3-2]
UniGeneiRn.97794.

Genome annotation databases

EnsembliENSRNOT00000006233; ENSRNOP00000006233; ENSRNOG00000008764. [Q2YDU3-2]
ENSRNOT00000044743; ENSRNOP00000039455; ENSRNOG00000008764. [Q2YDU3-1]
GeneIDi363452.
KEGGirno:363452.
UCSCiRGD:1563027. rat. [Q2YDU3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AABR03119131 Genomic DNA. No translation available.
BC110054 mRNA. Translation: AAI10055.1 .
RefSeqi NP_001032585.1. NM_001037496.1. [Q2YDU3-2 ]
UniGenei Rn.97794.

3D structure databases

ProteinModelPortali Q2YDU3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000039455.

Protein family/group databases

MEROPSi C85.001.

Proteomic databases

PaxDbi Q2YDU3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000006233 ; ENSRNOP00000006233 ; ENSRNOG00000008764 . [Q2YDU3-2 ]
ENSRNOT00000044743 ; ENSRNOP00000039455 ; ENSRNOG00000008764 . [Q2YDU3-1 ]
GeneIDi 363452.
KEGGi rno:363452.
UCSCi RGD:1563027. rat. [Q2YDU3-1 ]

Organism-specific databases

CTDi 55593.
RGDi 1563027. Otud5.

Phylogenomic databases

eggNOGi NOG286112.
GeneTreei ENSGT00510000048473.
HOGENOMi HOG000231360.
HOVERGENi HBG060214.
InParanoidi Q2YDU3.
KOi K12655.
OMAi WEDDEIL.
OrthoDBi EOG77Q4X0.
PhylomeDBi Q2YDU3.

Enzyme and pathway databases

Reactomei REACT_198997. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

NextBioi 683365.
PROi Q2YDU3.

Gene expression databases

Genevestigatori Q2YDU3.

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

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.

Entry informationi

Entry nameiOTUD5_RAT
AccessioniPrimary (citable) accession number: Q2YDU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 20, 2007
Last modified: September 3, 2014
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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