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Q5VVQ6

- OTU1_HUMAN

UniProt

Q5VVQ6 - OTU1_HUMAN

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Protein

Ubiquitin thioesterase OTU1

Gene

YOD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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.2 Publications

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).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei157 – 1571By similarity
Active sitei160 – 1601NucleophileCurated
Binding sitei266 – 2661Substrate; via carbonyl oxygen
Active sitei267 – 2671By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri318 – 34225C2H2-typeAdd
BLAST

GO - Molecular functioni

  1. Lys48-specific deubiquitinase activity Source: ParkinsonsUK-UCL
  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)
Alternative name(s):
DUBA-8
HIV-1-induced protease 7
Short name:
HIN-7
Short name:
HsHIN7
OTU domain-containing protein 2
Gene namesi
Name:YOD1
Synonyms:DUBA8, HIN7, OTUD2
ORF Names:PRO0907
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:25035. YOD1.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi160 – 1601C → S: Abolishes deubiquitinase activity without affecting interaction with VCP. Specifically blocks a step in the course of dislocation and/or degradation of endoplasmic reticulum-resident proteins destined for proteasomal degradation. 1 Publication
Mutagenesisi292 – 2921I → Q: Does not affect activity or specificity. Impairs ability to cleave longer 'Lys-11'-linked ubiquitin chains; when associated with Q-295. 1 Publication
Mutagenesisi295 – 2951V → Q: Does not affect activity or specificity. Impairs ability to cleave longer 'Lys-11'-linked ubiquitin chains; when associated with Q-292. 1 Publication
Mutagenesisi336 – 3361H → A: Reduced activity toward 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked ubiquitin without affecting activity toward 'Lys-11'-linked ubiquitin; when associated with A-342. 1 Publication
Mutagenesisi342 – 3421H → A: Reduced activity toward 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked ubiquitin without affecting activity toward 'Lys-11'-linked ubiquitin; when associated with A-336. 1 Publication

Organism-specific databases

PharmGKBiPA142670552.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348Ubiquitin thioesterase OTU1PRO_0000282356Add
BLAST

Proteomic databases

MaxQBiQ5VVQ6.
PaxDbiQ5VVQ6.
PRIDEiQ5VVQ6.

PTM databases

PhosphoSiteiQ5VVQ6.

Expressioni

Gene expression databases

BgeeiQ5VVQ6.
CleanExiHS_YOD1.
GenevestigatoriQ5VVQ6.

Organism-specific databases

HPAiHPA028400.
HPA028439.

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.2 Publications

Protein-protein interaction databases

BioGridi120666. 22 interactions.
IntActiQ5VVQ6. 2 interactions.
STRINGi9606.ENSP00000326813.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi138 – 1403
Beta strandi148 – 1514
Helixi160 – 16910
Helixi176 – 1783
Helixi179 – 19214
Turni194 – 1963
Helixi199 – 2024
Helixi206 – 2138
Beta strandi215 – 2173
Helixi222 – 23211
Beta strandi234 – 2407
Turni241 – 2444
Beta strandi245 – 2495
Turni250 – 2523
Beta strandi256 – 2638
Beta strandi268 – 2747
Beta strandi276 – 2805
Beta strandi285 – 2873
Helixi292 – 30817

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BOQX-ray1.47A132-314[»]
4BOSX-ray2.35A/B147-314[»]
4BOZX-ray3.03A/D132-314[»]
ProteinModelPortaliQ5VVQ6.
SMRiQ5VVQ6. Positions 47-132, 135-309.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini149 – 274126OTUPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 12879UBX-likeAdd
BLAST
Regioni154 – 1607Cys-loopBy similarity
Regioni213 – 22311Variable-loopBy similarityAdd
BLAST
Regioni263 – 2675His-loopBy similarity
Regioni291 – 2966S2 site

Domaini

The UBAX-like region mediates the interaction with VCP. According to PubMed:19818707, it corresponds to a UBX domain, which is a hallmark for VCP-associated proteins. However, no canonical UBX is detected by prediction tools such as Pfam or PROSITE.
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 (PubMed:23827681).1 Publication

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 fingeri318 – 34225C2H2-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5539.
GeneTreeiENSGT00390000009989.
HOGENOMiHOG000193461.
HOVERGENiHBG097006.
InParanoidiQ5VVQ6.
KOiK13719.
OMAiKSSRQFT.
OrthoDBiEOG7J1808.
PhylomeDBiQ5VVQ6.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5VVQ6-1) [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

        10         20         30         40         50
MFGPAKGRHF GVHPAPGFPG GVSQQAAGTK AGPAGAWPVG SRTDTMWRLR
60 70 80 90 100
CKAKDGTHVL QGLSSRTRVR ELQGQIAAIT GIAPGGQRIL VGYPPECLDL
110 120 130 140 150
SNGDTILEDL PIQSGDMLII EEDQTRPRSS PAFTKRGASS YVRETLPVLT
160 170 180 190 200
RTVVPADNSC LFTSVYYVVE GGVLNPACAP EMRRLIAQIV ASDPDFYSEA
210 220 230 240 250
ILGKTNQEYC DWIKRDDTWG GAIEISILSK FYQCEICVVD TQTVRIDRFG
260 270 280 290 300
EDAGYTKRVL LIYDGIHYDP LQRNFPDPDT PPLTIFSSND DIVLVQALEL
310 320 330 340
ADEARRRRQF TDVNRFTLRC MVCQKGLTGQ AEAREHAKET GHTNFGEV
Length:348
Mass (Da):38,322
Last modified:December 7, 2004 - v1
Checksum:i91DBD25BE85B1CCC
GO
Isoform 2 (identifier: Q5VVQ6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MFGPAKGRHF...KAKDGTHVLQ → METLHIIYSEAKSFTVE

Note: No experimental confirmation available.

Show »
Length:304
Mass (Da):33,979
Checksum:i8055467E0FD819CA
GO

Sequence cautioni

The sequence EAW93510.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81R → G in CAD89975. (PubMed:17974005)Curated
Sequence conflicti90 – 901L → F in BAC87233. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6161MFGPA…THVLQ → METLHIIYSEAKSFTVE in isoform 2. 1 PublicationVSP_024122Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK128014 mRNA. Translation: BAC87233.1.
AL445493 Genomic DNA. Translation: CAH70775.1.
AL445493 Genomic DNA. Translation: CAH70776.1.
CH471100 Genomic DNA. Translation: EAW93509.1.
CH471100 Genomic DNA. Translation: EAW93510.1. Sequence problems.
BC137166 mRNA. Translation: AAI37167.1.
BC137167 mRNA. Translation: AAI37168.1.
AL833081 mRNA. Translation: CAD89975.1.
AF116608 mRNA. Translation: AAF71033.1. Sequence problems.
CCDSiCCDS31002.1. [Q5VVQ6-1]
CCDS60402.1. [Q5VVQ6-2]
RefSeqiNP_001263249.1. NM_001276320.1. [Q5VVQ6-2]
NP_061036.3. NM_018566.3. [Q5VVQ6-1]
UniGeneiHs.567533.
Hs.745490.

Genome annotation databases

EnsembliENST00000315927; ENSP00000326813; ENSG00000180667. [Q5VVQ6-1]
ENST00000367084; ENSP00000356051; ENSG00000180667. [Q5VVQ6-2]
GeneIDi55432.
KEGGihsa:55432.
UCSCiuc001hfe.1. human. [Q5VVQ6-1]
uc001hff.1. human. [Q5VVQ6-2]

Polymorphism databases

DMDMi74747276.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK128014 mRNA. Translation: BAC87233.1 .
AL445493 Genomic DNA. Translation: CAH70775.1 .
AL445493 Genomic DNA. Translation: CAH70776.1 .
CH471100 Genomic DNA. Translation: EAW93509.1 .
CH471100 Genomic DNA. Translation: EAW93510.1 . Sequence problems.
BC137166 mRNA. Translation: AAI37167.1 .
BC137167 mRNA. Translation: AAI37168.1 .
AL833081 mRNA. Translation: CAD89975.1 .
AF116608 mRNA. Translation: AAF71033.1 . Sequence problems.
CCDSi CCDS31002.1. [Q5VVQ6-1 ]
CCDS60402.1. [Q5VVQ6-2 ]
RefSeqi NP_001263249.1. NM_001276320.1. [Q5VVQ6-2 ]
NP_061036.3. NM_018566.3. [Q5VVQ6-1 ]
UniGenei Hs.567533.
Hs.745490.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BOQ X-ray 1.47 A 132-314 [» ]
4BOS X-ray 2.35 A/B 147-314 [» ]
4BOZ X-ray 3.03 A/D 132-314 [» ]
ProteinModelPortali Q5VVQ6.
SMRi Q5VVQ6. Positions 47-132, 135-309.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120666. 22 interactions.
IntActi Q5VVQ6. 2 interactions.
STRINGi 9606.ENSP00000326813.

Protein family/group databases

MEROPSi C85.007.

PTM databases

PhosphoSitei Q5VVQ6.

Polymorphism databases

DMDMi 74747276.

Proteomic databases

MaxQBi Q5VVQ6.
PaxDbi Q5VVQ6.
PRIDEi Q5VVQ6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000315927 ; ENSP00000326813 ; ENSG00000180667 . [Q5VVQ6-1 ]
ENST00000367084 ; ENSP00000356051 ; ENSG00000180667 . [Q5VVQ6-2 ]
GeneIDi 55432.
KEGGi hsa:55432.
UCSCi uc001hfe.1. human. [Q5VVQ6-1 ]
uc001hff.1. human. [Q5VVQ6-2 ]

Organism-specific databases

CTDi 55432.
GeneCardsi GC01M207217.
HGNCi HGNC:25035. YOD1.
HPAi HPA028400.
HPA028439.
MIMi 612023. gene.
neXtProti NX_Q5VVQ6.
PharmGKBi PA142670552.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5539.
GeneTreei ENSGT00390000009989.
HOGENOMi HOG000193461.
HOVERGENi HBG097006.
InParanoidi Q5VVQ6.
KOi K13719.
OMAi KSSRQFT.
OrthoDBi EOG7J1808.
PhylomeDBi Q5VVQ6.
TreeFami TF323700.

Miscellaneous databases

GenomeRNAii 55432.
NextBioi 59830.
PROi Q5VVQ6.
SOURCEi Search...

Gene expression databases

Bgeei Q5VVQ6.
CleanExi HS_YOD1.
Genevestigatori Q5VVQ6.

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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 1).
    Tissue: Brain and Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-348.
    Tissue: Spinal cord.
  6. "Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs."
    Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.
    Genome Res. 11:1392-1403(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 267-348.
    Tissue: Fetal liver.
  7. "The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER."
    Ernst R., Mueller B., Ploegh H.L., Schlieker C.
    Mol. Cell 36:28-38(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME ACTIVITY, INTERACTION WITH FAF2; DERL1 AND VCP, MUTAGENESIS OF CYS-160.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
    Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
    Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 132-314 IN COMPLEX WITH UBIQUITINATED SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-292; VAL-295; HIS-336 AND HIS-342.

Entry informationi

Entry nameiOTU1_HUMAN
AccessioniPrimary (citable) accession number: Q5VVQ6
Secondary accession number(s): B2RNX3
, Q5VVQ5, Q6ZRS6, Q86T63, Q9P1L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 7, 2004
Last modified: October 29, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3