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Q8CB27 (OTU1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. 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 OTU1

EC=3.4.19.12
Gene names
Name:Yod1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains. Cleaves both polyubiquitin and di-ubiquitin 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).

Subunit structure

Interacts with VCP; the interaction is direct. Interacts with FAF2/UBXD8. Interacts with DERL1; however interaction is dependent on the UBAX-like region, suggesting that it may be indirect By similarity.

Domain

The UBAX-like region mediates the interaction with VCP By similarity.

The C2H2-type zinc finger mediates specificity for 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains but not for 'Lys-11'-linked ubiquitin chains. Selectivity for 'Lys-11'-linked ubiquitin chains is provided by recognition of the sequence surrounding 'Lys-11' in ubiquitin. The S2 site region provides specificity for longer 'Lys-11'-linked ubiquitin chains By similarity.

Sequence similarities

Contains 1 C2H2-type zinc finger.

Contains 1 OTU domain.

Sequence caution

The sequence BAC29661.1 differs from that shown. Reason: Frameshift at position 8.

The sequence BAC35495.1 differs from that shown. Reason: Erroneous termination at position 344. Translated as stop.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Ubiquitin thioesterase OTU1
PRO_0000282357

Regions

Domain144 – 269126OTU
Zinc finger313 – 33725C2H2-type
Region45 – 12379UBX-like
Region149 – 1557Cys-loop By similarity
Region208 – 21811Variable-loop By similarity
Region258 – 2625His-loop By similarity
Region286 – 2916S2 site By similarity

Sites

Active site1521 By similarity
Active site1551Nucleophile By similarity
Active site2621 By similarity
Binding site2611Substrate; via carbonyl oxygen By similarity

Secondary structure

............... 343
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8CB27 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C07F3F69F1CA86D8

FASTA34337,485
        10         20         30         40         50         60 
MFGGAKGGHF GVPPAGYSGA VPQSEAGTKA GPAGGRPADT MWRVRCKAKG GTHLLQGLSS 

        70         80         90        100        110        120 
RTRLRELQGQ IAAITGIAPG SQRILVGYPP ECLDLSDRDI TLGDLPIQSG DMLIVEEDQT 

       130        140        150        160        170        180 
RPKASPAFSK YGAPSYVREA LPVLTRTAVP ADNSCLFTSV YYVVEGGVLN PACAPEMRRL 

       190        200        210        220        230        240 
IAQIVASDPV LYSEAILGKT NEDYCDWIRR DDTWGGAIEI SILSKFYQCE ICVVDTQTVR 

       250        260        270        280        290        300 
IDRFGEDAGY TKRVLLIYDG IHYDPLQRNF PDPDTPPLTI FSSNDDIVLV QALELADEAR 

       310        320        330        340 
RKRQFTDVNR FTLRCMICQK GLTGQAEARD HARETGHTNF GEV 

« Hide

References

« Hide 'large scale' 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: Eye and Vagina.
[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: Brain.
[3]"Northeast structural genomics consortium target mmt2a."
Northeast structural genomics consortium (NESG)
Submitted (AUG-2010) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 42-126.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK036938 mRNA. Translation: BAC29646.1.
AK036991 mRNA. Translation: BAC29661.1. Frameshift.
AK053730 mRNA. Translation: BAC35495.1. Sequence problems.
BC139034 mRNA. Translation: AAI39035.1.
CCDSCCDS48351.1.
RefSeqNP_848806.2. NM_178691.4.
UniGeneMm.106553.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KZRNMR-A42-126[»]
ProteinModelPortalQ8CB27.
SMRQ8CB27. Positions 42-127, 142-306.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000055318.

Protein family/group databases

MEROPSC85.007.

PTM databases

PhosphoSiteQ8CB27.

Proteomic databases

PaxDbQ8CB27.
PRIDEQ8CB27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049813; ENSMUSP00000055318; ENSMUSG00000046404.
GeneID226418.
KEGGmmu:226418.
UCSCuc007cmh.2. mouse.

Organism-specific databases

CTD55432.
MGIMGI:2442596. Yod1.

Phylogenomic databases

eggNOGCOG5539.
GeneTreeENSGT00390000009989.
HOGENOMHOG000193461.
HOVERGENHBG097006.
InParanoidB2RSW9.
KOK13719.
OMAKSSRQFT.
OrthoDBEOG7J1808.
PhylomeDBQ8CB27.
TreeFamTF323700.

Gene expression databases

BgeeQ8CB27.
GenevestigatorQ8CB27.

Family and domain databases

InterProIPR003323. OTU.
IPR029071. Ubiquitin-rel_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamPF02338. OTU. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
PROSITEPS50802. OTU. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio378144.
PROQ8CB27.
SOURCESearch...

Entry information

Entry nameOTU1_MOUSE
AccessionPrimary (citable) accession number: Q8CB27
Secondary accession number(s): B2RSW9, Q8BPM9, Q8CB24
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 95 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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