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Q9CQX0 (OTUB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Ubiquitin thioesterase OTUB2

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme OTUB2
OTU domain-containing ubiquitin aldehyde-binding protein 2
Otubain-2
Ubiquitin-specific-processing protease OTUB2
Gene names
Name:Otub2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains By similarity.

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).

Sequence similarities

Belongs to the peptidase C65 family.

Contains 1 OTU domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 234234Ubiquitin thioesterase OTUB2
PRO_0000221011

Regions

Domain40 – 231192OTU

Sites

Active site481 By similarity
Active site511Nucleophile By similarity
Active site2241 By similarity
Site2261Required to orient and stabilize the active site H-224 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CQX0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 4BE469C91CE4EAD4

FASTA23427,300
        10         20         30         40         50         60 
MSETSFNLIS EKCDILSILR DHPENRIYQR KIQELSKRFT SIRKTKGDGN CFYRALGYSY 

        70         80         90        100        110        120 
LESLLGKSRE ILKFKERVLQ TPNDLLAAGF EEHKFRNFFN AFYSVVELVE KDSSVSSLLK 

       130        140        150        160        170        180 
VFNDQSSSDR IVQFLRLLTS AFIRNRADFF RHFIDEEMDI KDFCTHEVEP MAMECDHVQI 

       190        200        210        220        230 
TALSQALNIA LQVEYVDEMD TALNHHVFPE AAIPSVYLLY KTSHYNILYA AEKH 

« Hide

References

[1]"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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Testis and Tongue.
[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].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK006054 mRNA. Translation: BAB24385.1.
AK006346 mRNA. Translation: BAB24539.1.
AK006469 mRNA. Translation: BAB24603.1.
AK019830 mRNA. Translation: BAB31872.1.
AK160505 mRNA. Translation: BAE35829.1.
BC049551 mRNA. Translation: AAH49551.1.
CCDSCCDS36528.1.
RefSeqNP_001171312.1. NM_001177841.1.
NP_080856.1. NM_026580.4.
UniGeneMm.127378.

3D structure databases

ProteinModelPortalQ9CQX0.
SMRQ9CQX0. Positions 2-232.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC65.002.

PTM databases

PhosphoSiteQ9CQX0.

Proteomic databases

PaxDbQ9CQX0.
PRIDEQ9CQX0.

Protocols and materials databases

DNASU68149.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021620; ENSMUSP00000021620; ENSMUSG00000021203.
GeneID68149.
KEGGmmu:68149.
UCSCuc007ovg.2. mouse.

Organism-specific databases

CTD78990.
MGIMGI:1915399. Otub2.

Phylogenomic databases

eggNOGNOG267426.
GeneTreeENSGT00390000006979.
HOGENOMHOG000019496.
HOVERGENHBG053383.
KOK09603.
OrthoDBEOG71K64D.
PhylomeDBQ9CQX0.
TreeFamTF314145.

Gene expression databases

ArrayExpressQ9CQX0.
BgeeQ9CQX0.
CleanExMM_OTUB2.
GenevestigatorQ9CQX0.

Family and domain databases

InterProIPR003323. OTU.
IPR019400. Peptidase_C65_otubain.
IPR016615. Ubiquitin_thioesterase_Otubain.
[Graphical view]
PfamPF10275. Peptidase_C65. 1 hit.
[Graphical view]
PIRSFPIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
PROSITEPS50802. OTU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio326534.
PROQ9CQX0.
SOURCESearch...

Entry information

Entry nameOTUB2_MOUSE
AccessionPrimary (citable) accession number: Q9CQX0
Secondary accession number(s): Q3TUZ2, Q9D4K8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot