Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8CB27

- OTU1_MOUSE

UniProt

Q8CB27 - OTU1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ubiquitin thioesterase OTU1

Gene

Yod1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.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 sitei152 – 1521By similarity
Active sitei155 – 1551NucleophileBy similarity
Binding sitei261 – 2611Substrate; via carbonyl oxygenBy similarity
Active sitei262 – 2621By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri313 – 33725C2H2-typeAdd
BLAST

GO - Molecular functioni

  1. Lys48-specific deubiquitinase activity Source: Ensembl
  2. metal ion binding Source: UniProtKB-KW
  3. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. cellular amino acid metabolic process Source: UniProtKB
  2. endoplasmic reticulum unfolded protein response Source: UniProtKB
  3. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  4. protein K11-linked deubiquitination Source: UniProtKB
  5. protein K27-linked deubiquitination Source: UniProtKB
  6. protein K29-linked deubiquitination Source: UniProtKB
  7. protein K33-linked deubiquitination Source: UniProtKB
  8. protein K48-linked deubiquitination Source: UniProtKB
  9. protein K63-linked deubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway, Unfolded protein response

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiC85.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin thioesterase OTU1 (EC:3.4.19.12)
Gene namesi
Name:Yod1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:2442596. Yod1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 343343Ubiquitin thioesterase OTU1PRO_0000282357Add
BLAST

Proteomic databases

PaxDbiQ8CB27.
PRIDEiQ8CB27.

PTM databases

PhosphoSiteiQ8CB27.

Expressioni

Gene expression databases

BgeeiQ8CB27.
ExpressionAtlasiQ8CB27. baseline and differential.
GenevestigatoriQ8CB27.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000055318.

Structurei

Secondary structure

1
343
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 485
Beta strandi51 – 555
Helixi64 – 7411
Turni79 – 813
Beta strandi85 – 884
Turni102 – 1043
Beta strandi112 – 1143

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KZRNMR-A42-126[»]
ProteinModelPortaliQ8CB27.
SMRiQ8CB27. Positions 42-127, 142-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini144 – 269126OTUPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 12379UBX-likeAdd
BLAST
Regioni149 – 1557Cys-loopBy similarity
Regioni208 – 21811Variable-loopBy similarityAdd
BLAST
Regioni258 – 2625His-loopBy similarity
Regioni286 – 2916S2 siteBy similarity

Domaini

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.By similarity

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.Curated
Contains 1 OTU domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri313 – 33725C2H2-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5539.
GeneTreeiENSGT00390000009989.
HOGENOMiHOG000193461.
HOVERGENiHBG097006.
InParanoidiQ8CB27.
KOiK13719.
OMAiKSSRQFT.
OrthoDBiEOG7J1808.
PhylomeDBiQ8CB27.
TreeFamiTF323700.

Family and domain databases

InterProiIPR003323. OTU.
IPR029071. Ubiquitin-rel_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50802. OTU. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CB27-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFGGAKGGHF GVPPAGYSGA VPQSEAGTKA GPAGGRPADT MWRVRCKAKG
60 70 80 90 100
GTHLLQGLSS RTRLRELQGQ IAAITGIAPG SQRILVGYPP ECLDLSDRDI
110 120 130 140 150
TLGDLPIQSG DMLIVEEDQT RPKASPAFSK YGAPSYVREA LPVLTRTAVP
160 170 180 190 200
ADNSCLFTSV YYVVEGGVLN PACAPEMRRL IAQIVASDPV LYSEAILGKT
210 220 230 240 250
NEDYCDWIRR DDTWGGAIEI SILSKFYQCE ICVVDTQTVR IDRFGEDAGY
260 270 280 290 300
TKRVLLIYDG IHYDPLQRNF PDPDTPPLTI FSSNDDIVLV QALELADEAR
310 320 330 340
RKRQFTDVNR FTLRCMICQK GLTGQAEARD HARETGHTNF GEV
Length:343
Mass (Da):37,485
Last modified:March 1, 2003 - v1
Checksum:iC07F3F69F1CA86D8
GO

Sequence cautioni

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 databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK036938 mRNA. Translation: BAC29646.1.
AK036991 mRNA. Translation: BAC29661.1. Frameshift.
AK053730 mRNA. Translation: BAC35495.1. Sequence problems.
BC139034 mRNA. Translation: AAI39035.1.
CCDSiCCDS48351.1.
RefSeqiNP_848806.2. NM_178691.4.
UniGeneiMm.106553.

Genome annotation databases

EnsembliENSMUST00000049813; ENSMUSP00000055318; ENSMUSG00000046404.
GeneIDi226418.
KEGGimmu:226418.
UCSCiuc007cmh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK036938 mRNA. Translation: BAC29646.1 .
AK036991 mRNA. Translation: BAC29661.1 . Frameshift.
AK053730 mRNA. Translation: BAC35495.1 . Sequence problems.
BC139034 mRNA. Translation: AAI39035.1 .
CCDSi CCDS48351.1.
RefSeqi NP_848806.2. NM_178691.4.
UniGenei Mm.106553.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2KZR NMR - A 42-126 [» ]
ProteinModelPortali Q8CB27.
SMRi Q8CB27. Positions 42-127, 142-306.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000055318.

Protein family/group databases

MEROPSi C85.007.

PTM databases

PhosphoSitei Q8CB27.

Proteomic databases

PaxDbi Q8CB27.
PRIDEi Q8CB27.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049813 ; ENSMUSP00000055318 ; ENSMUSG00000046404 .
GeneIDi 226418.
KEGGi mmu:226418.
UCSCi uc007cmh.2. mouse.

Organism-specific databases

CTDi 55432.
MGIi MGI:2442596. Yod1.

Phylogenomic databases

eggNOGi COG5539.
GeneTreei ENSGT00390000009989.
HOGENOMi HOG000193461.
HOVERGENi HBG097006.
InParanoidi Q8CB27.
KOi K13719.
OMAi KSSRQFT.
OrthoDBi EOG7J1808.
PhylomeDBi Q8CB27.
TreeFami TF323700.

Miscellaneous databases

NextBioi 378144.
PROi Q8CB27.
SOURCEi Search...

Gene expression databases

Bgeei Q8CB27.
ExpressionAtlasi Q8CB27. baseline and differential.
Genevestigatori Q8CB27.

Family and domain databases

InterProi IPR003323. OTU.
IPR029071. Ubiquitin-rel_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
[Graphical view ]
Pfami PF02338. OTU. 1 hit.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS50802. OTU. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiOTU1_MOUSE
AccessioniPrimary (citable) accession number: Q8CB27
Secondary accession number(s): B2RSW9, Q8BPM9, Q8CB24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: March 1, 2003
Last modified: October 29, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3