Full text data of YOD1
YOD1
(DUBA8, HIN7, OTUD2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ubiquitin thioesterase OTU1; 3.4.19.12 (DUBA-8; HIV-1-induced protease 7; HIN-7; HsHIN7; OTU domain-containing protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin thioesterase OTU1; 3.4.19.12 (DUBA-8; HIV-1-induced protease 7; HIN-7; HsHIN7; OTU domain-containing protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00183503
IPI00183503 OTU-like cysteine protease family protein Novel protein soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00183503 OTU-like cysteine protease family protein Novel protein soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q5VVQ6
ID OTU1_HUMAN Reviewed; 348 AA.
AC Q5VVQ6; B2RNX3; Q5VVQ5; Q6ZRS6; Q86T63; Q9P1L8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 78.
DE RecName: Full=Ubiquitin thioesterase OTU1;
DE EC=3.4.19.12;
DE AltName: Full=DUBA-8;
DE AltName: Full=HIV-1-induced protease 7;
DE Short=HIN-7;
DE Short=HsHIN7;
DE AltName: Full=OTU domain-containing protein 2;
GN Name=YOD1; Synonyms=DUBA8, HIN7, OTUD2; ORFNames=PRO0907;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-348.
RC TISSUE=Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 267-348.
RC TISSUE=Fetal liver;
RX PubMed=11483580; DOI=10.1101/gr.175501;
RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C.,
RA Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C.,
RA He F.;
RT "Gene expression profiling in human fetal liver and identification of
RT tissue- and developmental-stage-specific genes through compiled
RT expression profiles and efficient cloning of full-length cDNAs.";
RL Genome Res. 11:1392-1403(2001).
RN [7]
RP FUNCTION, ENZYME ACTIVITY, INTERACTION WITH FAF2; DERL1 AND VCP, AND
RP MUTAGENESIS OF CYS-160.
RX PubMed=19818707; DOI=10.1016/j.molcel.2009.09.016;
RA Ernst R., Mueller B., Ploegh H.L., Schlieker C.;
RT "The otubain YOD1 is a deubiquitinating enzyme that associates with
RT p97 to facilitate protein dislocation from the ER.";
RL Mol. Cell 36:28-38(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 132-314 IN COMPLEX WITH
RP UBIQUITINATED SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF ILE-292; VAL-295; HIS-336 AND HIS-342.
RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F.,
RA Freund S.M., Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and
RT enable ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from
CC proteins and participates in endoplasmic reticulum-associated
CC degradation (ERAD) for misfolded lumenal proteins. May act by
CC triming the ubiquitin chain on the associated substrate to
CC facilitate their threading through the VCP/p97 pore. Ubiquitin
CC moieties on substrates may present a steric impediment to the
CC threading process when the substrate is transferred to the VCP
CC pore and threaded through VCP's axial channel. Mediates
CC deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked
CC polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked
CC ubiquitin chains. Cleaves both polyubiquitin and di-ubiquitin.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Interacts with VCP; the interaction is direct. Interacts
CC with FAF2/UBXD8. Interacts with DERL1; however interaction is
CC dependent on the UBAX-like region, suggesting that it may be
CC indirect.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VVQ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VVQ6-2; Sequence=VSP_024122;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The UBAX-like region mediates the interaction with VCP.
CC According to PubMed:19818707, it corresponds to a UBX domain,
CC which is a hallmark for VCP-associated proteins. However, no
CC canonical UBX is detected by prediction tools such as Pfam or
CC PROSITE.
CC -!- DOMAIN: The C2H2-type zinc finger mediates specificity for 'Lys-
CC 27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains but not
CC for 'Lys-11'-linked ubiquitin chains. Selectivity for 'Lys-11'-
CC linked ubiquitin chains is provided by recognition of the sequence
CC surrounding 'Lys-11' in ubiquitin. The S2 site region provides
CC specificity for longer 'Lys-11'-linked ubiquitin chains
CC (PubMed:23827681).
CC -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC -!- SIMILARITY: Contains 1 OTU domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF71033.1; Type=Erroneous translation; Note=Wrong choice of frame;
CC Sequence=EAW93510.1; Type=Erroneous gene model prediction;
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DR EMBL; AK128014; BAC87233.1; -; mRNA.
DR EMBL; AL445493; CAH70775.1; -; Genomic_DNA.
DR EMBL; AL445493; CAH70776.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93509.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93510.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC137166; AAI37167.1; -; mRNA.
DR EMBL; BC137167; AAI37168.1; -; mRNA.
DR EMBL; AL833081; CAD89975.1; -; mRNA.
DR EMBL; AF116608; AAF71033.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001263249.1; NM_001276320.1.
DR RefSeq; NP_061036.3; NM_018566.3.
DR UniGene; Hs.567533; -.
DR UniGene; Hs.745490; -.
DR PDB; 4BOQ; X-ray; 1.47 A; A=132-314.
DR PDB; 4BOS; X-ray; 2.35 A; A/B=147-314.
DR PDB; 4BOZ; X-ray; 3.03 A; A/D=132-314.
DR PDBsum; 4BOQ; -.
DR PDBsum; 4BOS; -.
DR PDBsum; 4BOZ; -.
DR ProteinModelPortal; Q5VVQ6; -.
DR SMR; Q5VVQ6; 47-132, 148-306.
DR IntAct; Q5VVQ6; 2.
DR STRING; 9606.ENSP00000326813; -.
DR MEROPS; C85.007; -.
DR PhosphoSite; Q5VVQ6; -.
DR DMDM; 74747276; -.
DR PaxDb; Q5VVQ6; -.
DR PRIDE; Q5VVQ6; -.
DR Ensembl; ENST00000315927; ENSP00000326813; ENSG00000180667.
DR Ensembl; ENST00000367084; ENSP00000356051; ENSG00000180667.
DR Ensembl; ENST00000391927; ENSP00000375793; ENSG00000180667.
DR GeneID; 55432; -.
DR KEGG; hsa:55432; -.
DR UCSC; uc001hfe.1; human.
DR CTD; 55432; -.
DR GeneCards; GC01M207217; -.
DR HGNC; HGNC:25035; YOD1.
DR HPA; HPA028400; -.
DR HPA; HPA028439; -.
DR MIM; 612023; gene.
DR neXtProt; NX_Q5VVQ6; -.
DR PharmGKB; PA142670552; -.
DR eggNOG; COG5539; -.
DR HOGENOM; HOG000193461; -.
DR HOVERGEN; HBG097006; -.
DR InParanoid; Q5VVQ6; -.
DR KO; K13719; -.
DR OMA; FDGIHYD; -.
DR OrthoDB; EOG7J1808; -.
DR GenomeRNAi; 55432; -.
DR NextBio; 59830; -.
DR PRO; PR:Q5VVQ6; -.
DR Bgee; Q5VVQ6; -.
DR CleanEx; HS_YOD1; -.
DR Genevestigator; Q5VVQ6; -.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:cellular amino acid metabolic process; ISS:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
DR GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:1990167; P:protein K27-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0035523; P:protein K29-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:1990168; P:protein K33-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
DR InterPro; IPR003323; OTU.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR Pfam; PF02338; OTU; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Hydrolase;
KW Metal-binding; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway; Unfolded protein response; Zinc; Zinc-finger.
FT CHAIN 1 348 Ubiquitin thioesterase OTU1.
FT /FTId=PRO_0000282356.
FT DOMAIN 149 274 OTU.
FT ZN_FING 318 342 C2H2-type.
FT REGION 50 128 UBX-like.
FT REGION 154 160 Cys-loop (By similarity).
FT REGION 213 223 Variable-loop (By similarity).
FT REGION 263 267 His-loop (By similarity).
FT REGION 291 296 S2 site.
FT ACT_SITE 157 157 By similarity.
FT ACT_SITE 160 160 Nucleophile (Probable).
FT ACT_SITE 267 267 By similarity.
FT BINDING 266 266 Substrate; via carbonyl oxygen.
FT VAR_SEQ 1 61 MFGPAKGRHFGVHPAPGFPGGVSQQAAGTKAGPAGAWPVGS
FT RTDTMWRLRCKAKDGTHVLQ -> METLHIIYSEAKSFTVE
FT (in isoform 2).
FT /FTId=VSP_024122.
FT MUTAGEN 160 160 C->S: Abolishes deubiquitinase activity
FT without affecting interaction with VCP.
FT Specifically blocks a step in the course
FT of dislocation and/or degradation of
FT endoplasmic reticulum-resident proteins
FT destined for proteasomal degradation.
FT MUTAGEN 292 292 I->Q: Does not affect activity or
FT specificity. Impairs ability to cleave
FT longer 'Lys-11'-linked ubiquitin chains;
FT when associated with Q-295.
FT MUTAGEN 295 295 V->Q: Does not affect activity or
FT specificity. Impairs ability to cleave
FT longer 'Lys-11'-linked ubiquitin chains;
FT when associated with Q-292.
FT MUTAGEN 336 336 H->A: Reduced activity toward 'Lys-27'-,
FT 'Lys-29'- and 'Lys-33'-linked ubiquitin
FT without affecting activity toward 'Lys-
FT 11'-linked ubiquitin; when associated
FT with A-342.
FT MUTAGEN 342 342 H->A: Reduced activity toward 'Lys-27'-,
FT 'Lys-29'- and 'Lys-33'-linked ubiquitin
FT without affecting activity toward 'Lys-
FT 11'-linked ubiquitin; when associated
FT with A-336.
FT CONFLICT 8 8 R -> G (in Ref. 5; CAD89975).
FT CONFLICT 90 90 L -> F (in Ref. 1; BAC87233).
FT HELIX 138 140
FT STRAND 148 151
FT HELIX 160 169
FT HELIX 176 178
FT HELIX 179 192
FT TURN 194 196
FT HELIX 199 202
FT HELIX 206 213
FT STRAND 215 217
FT HELIX 222 232
FT STRAND 234 240
FT TURN 241 244
FT STRAND 245 249
FT TURN 250 252
FT STRAND 256 263
FT STRAND 268 274
FT STRAND 276 280
FT STRAND 285 287
FT HELIX 292 308
SQ SEQUENCE 348 AA; 38322 MW; 91DBD25BE85B1CCC CRC64;
MFGPAKGRHF GVHPAPGFPG GVSQQAAGTK AGPAGAWPVG SRTDTMWRLR CKAKDGTHVL
QGLSSRTRVR ELQGQIAAIT GIAPGGQRIL VGYPPECLDL SNGDTILEDL PIQSGDMLII
EEDQTRPRSS PAFTKRGASS YVRETLPVLT RTVVPADNSC LFTSVYYVVE GGVLNPACAP
EMRRLIAQIV ASDPDFYSEA ILGKTNQEYC DWIKRDDTWG GAIEISILSK FYQCEICVVD
TQTVRIDRFG EDAGYTKRVL LIYDGIHYDP LQRNFPDPDT PPLTIFSSND DIVLVQALEL
ADEARRRRQF TDVNRFTLRC MVCQKGLTGQ AEAREHAKET GHTNFGEV
//
ID OTU1_HUMAN Reviewed; 348 AA.
AC Q5VVQ6; B2RNX3; Q5VVQ5; Q6ZRS6; Q86T63; Q9P1L8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-DEC-2004, sequence version 1.
DT 22-JAN-2014, entry version 78.
DE RecName: Full=Ubiquitin thioesterase OTU1;
DE EC=3.4.19.12;
DE AltName: Full=DUBA-8;
DE AltName: Full=HIV-1-induced protease 7;
DE Short=HIN-7;
DE Short=HsHIN7;
DE AltName: Full=OTU domain-containing protein 2;
GN Name=YOD1; Synonyms=DUBA8, HIN7, OTUD2; ORFNames=PRO0907;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-348.
RC TISSUE=Spinal cord;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 267-348.
RC TISSUE=Fetal liver;
RX PubMed=11483580; DOI=10.1101/gr.175501;
RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C.,
RA Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C.,
RA He F.;
RT "Gene expression profiling in human fetal liver and identification of
RT tissue- and developmental-stage-specific genes through compiled
RT expression profiles and efficient cloning of full-length cDNAs.";
RL Genome Res. 11:1392-1403(2001).
RN [7]
RP FUNCTION, ENZYME ACTIVITY, INTERACTION WITH FAF2; DERL1 AND VCP, AND
RP MUTAGENESIS OF CYS-160.
RX PubMed=19818707; DOI=10.1016/j.molcel.2009.09.016;
RA Ernst R., Mueller B., Ploegh H.L., Schlieker C.;
RT "The otubain YOD1 is a deubiquitinating enzyme that associates with
RT p97 to facilitate protein dislocation from the ER.";
RL Mol. Cell 36:28-38(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 132-314 IN COMPLEX WITH
RP UBIQUITINATED SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS
RP OF ILE-292; VAL-295; HIS-336 AND HIS-342.
RX PubMed=23827681; DOI=10.1016/j.cell.2013.05.046;
RA Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M.,
RA Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F.,
RA Freund S.M., Ovaa H., Komander D.;
RT "OTU deubiquitinases reveal mechanisms of linkage specificity and
RT enable ubiquitin chain restriction analysis.";
RL Cell 154:169-184(2013).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from
CC proteins and participates in endoplasmic reticulum-associated
CC degradation (ERAD) for misfolded lumenal proteins. May act by
CC triming the ubiquitin chain on the associated substrate to
CC facilitate their threading through the VCP/p97 pore. Ubiquitin
CC moieties on substrates may present a steric impediment to the
CC threading process when the substrate is transferred to the VCP
CC pore and threaded through VCP's axial channel. Mediates
CC deubiquitination of 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked
CC polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked
CC ubiquitin chains. Cleaves both polyubiquitin and di-ubiquitin.
CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC thioester, amide, peptide and isopeptide bonds formed by the C-
CC terminal Gly of ubiquitin (a 76-residue protein attached to
CC proteins as an intracellular targeting signal).
CC -!- SUBUNIT: Interacts with VCP; the interaction is direct. Interacts
CC with FAF2/UBXD8. Interacts with DERL1; however interaction is
CC dependent on the UBAX-like region, suggesting that it may be
CC indirect.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VVQ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VVQ6-2; Sequence=VSP_024122;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The UBAX-like region mediates the interaction with VCP.
CC According to PubMed:19818707, it corresponds to a UBX domain,
CC which is a hallmark for VCP-associated proteins. However, no
CC canonical UBX is detected by prediction tools such as Pfam or
CC PROSITE.
CC -!- DOMAIN: The C2H2-type zinc finger mediates specificity for 'Lys-
CC 27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains but not
CC for 'Lys-11'-linked ubiquitin chains. Selectivity for 'Lys-11'-
CC linked ubiquitin chains is provided by recognition of the sequence
CC surrounding 'Lys-11' in ubiquitin. The S2 site region provides
CC specificity for longer 'Lys-11'-linked ubiquitin chains
CC (PubMed:23827681).
CC -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC -!- SIMILARITY: Contains 1 OTU domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF71033.1; Type=Erroneous translation; Note=Wrong choice of frame;
CC Sequence=EAW93510.1; Type=Erroneous gene model prediction;
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DR EMBL; AK128014; BAC87233.1; -; mRNA.
DR EMBL; AL445493; CAH70775.1; -; Genomic_DNA.
DR EMBL; AL445493; CAH70776.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93509.1; -; Genomic_DNA.
DR EMBL; CH471100; EAW93510.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC137166; AAI37167.1; -; mRNA.
DR EMBL; BC137167; AAI37168.1; -; mRNA.
DR EMBL; AL833081; CAD89975.1; -; mRNA.
DR EMBL; AF116608; AAF71033.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001263249.1; NM_001276320.1.
DR RefSeq; NP_061036.3; NM_018566.3.
DR UniGene; Hs.567533; -.
DR UniGene; Hs.745490; -.
DR PDB; 4BOQ; X-ray; 1.47 A; A=132-314.
DR PDB; 4BOS; X-ray; 2.35 A; A/B=147-314.
DR PDB; 4BOZ; X-ray; 3.03 A; A/D=132-314.
DR PDBsum; 4BOQ; -.
DR PDBsum; 4BOS; -.
DR PDBsum; 4BOZ; -.
DR ProteinModelPortal; Q5VVQ6; -.
DR SMR; Q5VVQ6; 47-132, 148-306.
DR IntAct; Q5VVQ6; 2.
DR STRING; 9606.ENSP00000326813; -.
DR MEROPS; C85.007; -.
DR PhosphoSite; Q5VVQ6; -.
DR DMDM; 74747276; -.
DR PaxDb; Q5VVQ6; -.
DR PRIDE; Q5VVQ6; -.
DR Ensembl; ENST00000315927; ENSP00000326813; ENSG00000180667.
DR Ensembl; ENST00000367084; ENSP00000356051; ENSG00000180667.
DR Ensembl; ENST00000391927; ENSP00000375793; ENSG00000180667.
DR GeneID; 55432; -.
DR KEGG; hsa:55432; -.
DR UCSC; uc001hfe.1; human.
DR CTD; 55432; -.
DR GeneCards; GC01M207217; -.
DR HGNC; HGNC:25035; YOD1.
DR HPA; HPA028400; -.
DR HPA; HPA028439; -.
DR MIM; 612023; gene.
DR neXtProt; NX_Q5VVQ6; -.
DR PharmGKB; PA142670552; -.
DR eggNOG; COG5539; -.
DR HOGENOM; HOG000193461; -.
DR HOVERGEN; HBG097006; -.
DR InParanoid; Q5VVQ6; -.
DR KO; K13719; -.
DR OMA; FDGIHYD; -.
DR OrthoDB; EOG7J1808; -.
DR GenomeRNAi; 55432; -.
DR NextBio; 59830; -.
DR PRO; PR:Q5VVQ6; -.
DR Bgee; Q5VVQ6; -.
DR CleanEx; HS_YOD1; -.
DR Genevestigator; Q5VVQ6; -.
DR GO; GO:0004843; F:deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:cellular amino acid metabolic process; ISS:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
DR GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:1990167; P:protein K27-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0035523; P:protein K29-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:1990168; P:protein K33-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
DR InterPro; IPR003323; OTU.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR Pfam; PF02338; OTU; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Hydrolase;
KW Metal-binding; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway; Unfolded protein response; Zinc; Zinc-finger.
FT CHAIN 1 348 Ubiquitin thioesterase OTU1.
FT /FTId=PRO_0000282356.
FT DOMAIN 149 274 OTU.
FT ZN_FING 318 342 C2H2-type.
FT REGION 50 128 UBX-like.
FT REGION 154 160 Cys-loop (By similarity).
FT REGION 213 223 Variable-loop (By similarity).
FT REGION 263 267 His-loop (By similarity).
FT REGION 291 296 S2 site.
FT ACT_SITE 157 157 By similarity.
FT ACT_SITE 160 160 Nucleophile (Probable).
FT ACT_SITE 267 267 By similarity.
FT BINDING 266 266 Substrate; via carbonyl oxygen.
FT VAR_SEQ 1 61 MFGPAKGRHFGVHPAPGFPGGVSQQAAGTKAGPAGAWPVGS
FT RTDTMWRLRCKAKDGTHVLQ -> METLHIIYSEAKSFTVE
FT (in isoform 2).
FT /FTId=VSP_024122.
FT MUTAGEN 160 160 C->S: Abolishes deubiquitinase activity
FT without affecting interaction with VCP.
FT Specifically blocks a step in the course
FT of dislocation and/or degradation of
FT endoplasmic reticulum-resident proteins
FT destined for proteasomal degradation.
FT MUTAGEN 292 292 I->Q: Does not affect activity or
FT specificity. Impairs ability to cleave
FT longer 'Lys-11'-linked ubiquitin chains;
FT when associated with Q-295.
FT MUTAGEN 295 295 V->Q: Does not affect activity or
FT specificity. Impairs ability to cleave
FT longer 'Lys-11'-linked ubiquitin chains;
FT when associated with Q-292.
FT MUTAGEN 336 336 H->A: Reduced activity toward 'Lys-27'-,
FT 'Lys-29'- and 'Lys-33'-linked ubiquitin
FT without affecting activity toward 'Lys-
FT 11'-linked ubiquitin; when associated
FT with A-342.
FT MUTAGEN 342 342 H->A: Reduced activity toward 'Lys-27'-,
FT 'Lys-29'- and 'Lys-33'-linked ubiquitin
FT without affecting activity toward 'Lys-
FT 11'-linked ubiquitin; when associated
FT with A-336.
FT CONFLICT 8 8 R -> G (in Ref. 5; CAD89975).
FT CONFLICT 90 90 L -> F (in Ref. 1; BAC87233).
FT HELIX 138 140
FT STRAND 148 151
FT HELIX 160 169
FT HELIX 176 178
FT HELIX 179 192
FT TURN 194 196
FT HELIX 199 202
FT HELIX 206 213
FT STRAND 215 217
FT HELIX 222 232
FT STRAND 234 240
FT TURN 241 244
FT STRAND 245 249
FT TURN 250 252
FT STRAND 256 263
FT STRAND 268 274
FT STRAND 276 280
FT STRAND 285 287
FT HELIX 292 308
SQ SEQUENCE 348 AA; 38322 MW; 91DBD25BE85B1CCC CRC64;
MFGPAKGRHF GVHPAPGFPG GVSQQAAGTK AGPAGAWPVG SRTDTMWRLR CKAKDGTHVL
QGLSSRTRVR ELQGQIAAIT GIAPGGQRIL VGYPPECLDL SNGDTILEDL PIQSGDMLII
EEDQTRPRSS PAFTKRGASS YVRETLPVLT RTVVPADNSC LFTSVYYVVE GGVLNPACAP
EMRRLIAQIV ASDPDFYSEA ILGKTNQEYC DWIKRDDTWG GAIEISILSK FYQCEICVVD
TQTVRIDRFG EDAGYTKRVL LIYDGIHYDP LQRNFPDPDT PPLTIFSSND DIVLVQALEL
ADEARRRRQF TDVNRFTLRC MVCQKGLTGQ AEAREHAKET GHTNFGEV
//
MIM
612023
*RECORD*
*FIELD* NO
612023
*FIELD* TI
*612023 YOD1 OTU DEUBIQUITINATING ENZYME 1, S. CEREVISIAE, HOMOLOG OF; YOD1
;;OTU DOMAIN-CONTAINING PROTEIN 2; OTUD2;;
read moreDUBA8
*FIELD* TX
DESCRIPTION
Deubiquitinating enzymes (DUBs; see 603478) are proteases that
specifically cleave ubiquitin (191339) linkages, negating the action of
ubiquitin ligases. DUBA8 belongs to a DUB subfamily characterized by an
ovarian tumor (OTU) domain.
CLONING
Kayagaki et al. (2007) identified ovarian tumor domain (OTU)-containing
protein 2 (OTUD2) in a small interfering RNA (siRNA)-based screen for
OTU deubiquitinating enzyme (DUB) family members. The 6,265-basepair
mRNA contains an open reading frame (ORF) predicting a 348-amino acid
protein. In addition to an OTU domain, the protein includes a zinc
finger (ZNF) C2H2 domain.
MAPPING
The YOD1 gene maps to chromosome 1q32.1 (Kayagaki et al., 2007).
*FIELD* RF
1. Kayagaki, N.; Phung, Q.; Chan, S.; Chaudhari, R.; Quan, C.; O'Rourke,
K. M.; Eby, M.; Pietras, E.; Cheng, G.; Bazan, J. F.; Zhang, Z.; Arnott,
D.; Dixit, V. M.: DUBA: a deubiquitinase that regulates type I interferon
production. Science 318: 1628-1632, 2007.
*FIELD* CD
Ada Hamosh: 5/6/2008
*FIELD* ED
alopez: 05/07/2008
alopez: 5/6/2008
*RECORD*
*FIELD* NO
612023
*FIELD* TI
*612023 YOD1 OTU DEUBIQUITINATING ENZYME 1, S. CEREVISIAE, HOMOLOG OF; YOD1
;;OTU DOMAIN-CONTAINING PROTEIN 2; OTUD2;;
read moreDUBA8
*FIELD* TX
DESCRIPTION
Deubiquitinating enzymes (DUBs; see 603478) are proteases that
specifically cleave ubiquitin (191339) linkages, negating the action of
ubiquitin ligases. DUBA8 belongs to a DUB subfamily characterized by an
ovarian tumor (OTU) domain.
CLONING
Kayagaki et al. (2007) identified ovarian tumor domain (OTU)-containing
protein 2 (OTUD2) in a small interfering RNA (siRNA)-based screen for
OTU deubiquitinating enzyme (DUB) family members. The 6,265-basepair
mRNA contains an open reading frame (ORF) predicting a 348-amino acid
protein. In addition to an OTU domain, the protein includes a zinc
finger (ZNF) C2H2 domain.
MAPPING
The YOD1 gene maps to chromosome 1q32.1 (Kayagaki et al., 2007).
*FIELD* RF
1. Kayagaki, N.; Phung, Q.; Chan, S.; Chaudhari, R.; Quan, C.; O'Rourke,
K. M.; Eby, M.; Pietras, E.; Cheng, G.; Bazan, J. F.; Zhang, Z.; Arnott,
D.; Dixit, V. M.: DUBA: a deubiquitinase that regulates type I interferon
production. Science 318: 1628-1632, 2007.
*FIELD* CD
Ada Hamosh: 5/6/2008
*FIELD* ED
alopez: 05/07/2008
alopez: 5/6/2008