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Protein

Ubiquitin thioesterase OTU1

Gene

YOD1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. endoplasmic reticulum unfolded protein response Source: UniProtKB
  2. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  3. protein K11-linked deubiquitination Source: UniProtKB
  4. protein K27-linked deubiquitination Source: UniProtKB
  5. protein K29-linked deubiquitination Source: UniProtKB
  6. protein K33-linked deubiquitination Source: UniProtKB
  7. protein K48-linked deubiquitination Source: UniProtKB
  8. 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 – 1403Combined sources
Beta strandi148 – 1514Combined sources
Helixi160 – 16910Combined sources
Helixi176 – 1783Combined sources
Helixi179 – 19214Combined sources
Turni194 – 1963Combined sources
Helixi199 – 2024Combined sources
Helixi206 – 2138Combined sources
Beta strandi215 – 2173Combined sources
Helixi222 – 23211Combined sources
Beta strandi234 – 2407Combined sources
Turni241 – 2444Combined sources
Beta strandi245 – 2495Combined sources
Turni250 – 2523Combined sources
Beta strandi256 – 2638Combined sources
Beta strandi268 – 2747Combined sources
Beta strandi276 – 2805Combined sources
Beta strandi285 – 2873Combined sources
Helixi292 – 30817Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiSNAEYCA.
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. AlignAdd to basket

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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiC85.007.

PTM databases

PhosphoSiteiQ5VVQ6.

Polymorphism databases

DMDMi74747276.

Proteomic databases

MaxQBiQ5VVQ6.
PaxDbiQ5VVQ6.
PRIDEiQ5VVQ6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi55432.
GeneCardsiGC01M207217.
HGNCiHGNC:25035. YOD1.
HPAiHPA028400.
HPA028439.
MIMi612023. gene.
neXtProtiNX_Q5VVQ6.
PharmGKBiPA142670552.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5539.
GeneTreeiENSGT00390000009989.
HOGENOMiHOG000193461.
HOVERGENiHBG097006.
InParanoidiQ5VVQ6.
KOiK13719.
OMAiSNAEYCA.
OrthoDBiEOG7J1808.
PhylomeDBiQ5VVQ6.
TreeFamiTF323700.

Miscellaneous databases

GenomeRNAii55432.
NextBioi59830.
PROiQ5VVQ6.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VVQ6.
CleanExiHS_YOD1.
GenevestigatoriQ5VVQ6.

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]
ProtoNetiSearch...

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: January 7, 2015
This is version 89 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.