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Q9CUB6

- OTUD1_MOUSE

UniProt

Q9CUB6 - OTUD1_MOUSE

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Protein
OTU domain-containing protein 1
Gene
Otud1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei290 – 2901 By similarity
Active sitei293 – 2931Nucleophile By similarity
Active sitei404 – 4041 By 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)
Gene namesi
Name:Otud1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1918448. Otud1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454OTU domain-containing protein 1
PRO_0000271019Add
BLAST

Proteomic databases

PRIDEiQ9CUB6.

PTM databases

PhosphoSiteiQ9CUB6.

Expressioni

Gene expression databases

BgeeiQ9CUB6.
GenevestigatoriQ9CUB6.

Structurei

3D structure databases

ProteinModelPortaliQ9CUB6.
SMRiQ9CUB6. Positions 261-410.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini282 – 411130OTU
Add
BLAST
Repeati430 – 44920UIM
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni287 – 2937Cys-loop By similarity
Regioni342 – 35211His-loop By similarity
Add
BLAST
Regioni399 – 4046Variable-loop By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi20 – 8869Ala-rich
Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 OTU domain.

Phylogenomic databases

eggNOGiNOG327202.
GeneTreeiENSGT00510000049635.
HOGENOMiHOG000115304.
HOVERGENiHBG080487.
InParanoidiQ9CUB6.
KOiK13716.
OMAiNFRLSEH.
OrthoDBiEOG7TBC35.
PhylomeDBiQ9CUB6.
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.

Q9CUB6-1 [UniParc]FASTAAdd to Basket

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MQLYSSVCTH YPAGTPGPTA AAPPATAAAA FKVSLQSASP AAAAPEPDTG    50
ERPPAAATEP REAAAAAAMP AFSACFERSG SAAAPPGACS KPPLPPHFTS 100
TAHIAVRALG AERLLLPPPS APSPPRRGSS AWLLEELLRP DEPAAPNAVR 150
DAPDRNFRLS EHRQALAASQ HRAPAPAPVG PEPGAGPGSG PWGEERRAER 200
SSRGWDRASG RSDASGSDAL RRQDPEAEAH PVPAPARSSG EPAQNGEGEA 250
VGTSRADPRD EKLALYLAEV ERQDKYLRQR NKYRFHIIPD GNCLYRAVSK 300
TVYGDQSLHR ELREQTVHYI ADHLDHFSPL IEGDVGEFII AAAQDGAWAG 350
YPELLAMGQM LNVNIHLTTG GRLESPTVST MIHYLGPEDS LRPSIWLSWL 400
SNGHYDAVFD HSYPNPEYDN WCKQTQIQKK RDEELAKSMA ISLSKMYIEQ 450
NACS 454
Length:454
Mass (Da):48,823
Last modified:January 9, 2007 - v2
Checksum:iBAF1702C35D1EF89
GO

Sequence cautioni

The sequence BAB30530.1 differs from that shown. Reason: Frameshift at position 62.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL928877 Genomic DNA. Translation: CAM25812.1.
AK016972 mRNA. Translation: BAB30530.1. Frameshift.
CCDSiCCDS50508.1.
RefSeqiNP_081991.1. NM_027715.1.
UniGeneiMm.83981.

Genome annotation databases

EnsembliENSMUST00000052168; ENSMUSP00000100617; ENSMUSG00000043415.
GeneIDi71198.
KEGGimmu:71198.
UCSCiuc008imj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL928877 Genomic DNA. Translation: CAM25812.1 .
AK016972 mRNA. Translation: BAB30530.1 . Frameshift.
CCDSi CCDS50508.1.
RefSeqi NP_081991.1. NM_027715.1.
UniGenei Mm.83981.

3D structure databases

ProteinModelPortali Q9CUB6.
SMRi Q9CUB6. Positions 261-410.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C85.004.

PTM databases

PhosphoSitei Q9CUB6.

Proteomic databases

PRIDEi Q9CUB6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000052168 ; ENSMUSP00000100617 ; ENSMUSG00000043415 .
GeneIDi 71198.
KEGGi mmu:71198.
UCSCi uc008imj.2. mouse.

Organism-specific databases

CTDi 220213.
MGIi MGI:1918448. Otud1.

Phylogenomic databases

eggNOGi NOG327202.
GeneTreei ENSGT00510000049635.
HOGENOMi HOG000115304.
HOVERGENi HBG080487.
InParanoidi Q9CUB6.
KOi K13716.
OMAi NFRLSEH.
OrthoDBi EOG7TBC35.
PhylomeDBi Q9CUB6.
TreeFami TF338508.

Miscellaneous databases

NextBioi 333266.
PROi Q9CUB6.
SOURCEi Search...

Gene expression databases

Bgeei Q9CUB6.
Genevestigatori Q9CUB6.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 232-454.
    Strain: C57BL/6J.
    Tissue: Testis.

Entry informationi

Entry nameiOTUD1_MOUSE
AccessioniPrimary (citable) accession number: Q9CUB6
Secondary accession number(s): A2ATK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: July 9, 2014
This is version 73 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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