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Q96FW1 (OTUB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin thioesterase OTUB1

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme OTUB1
OTU domain-containing ubiquitin aldehyde-binding protein 1
Otubain-1
Short name=hOTU1
Ubiquitin-specific-processing protease OTUB1
Gene names
Name:OTUB1
Synonyms:OTB1, OTU1
ORF Names:HSPC263
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin. Ref.1 Ref.2 Ref.7 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16

Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain. Ref.1 Ref.2 Ref.7 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16

Catalytic activity

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). Ref.15

Enzyme regulation

By free ubiquitin: binding of free ubiquitin triggers conformational changes in the OTU domain and formation of a ubiquitin-binding helix in the N-terminus, promoting binding of the conjugated donor ubiquitin in UBE2N/UBC13 to OTUB1. Ref.17 Ref.18

Subunit structure

Isoform 1 and isoform 2 interact with RNF128. Isoform 1 forms a ternary complex with RNF128 and USP8. Isoform 1 interacts with the C-terminal UCH catalytic domain of USP8. Isoform 2 does not associate with USP8. Interacts with FUS, ESR1 and GNB2L1/RACK1. Interacts with UBE2N/UBC13. Ref.2 Ref.10 Ref.12 Ref.16

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Isoform 1 is ubiquitous. Isoform 2 is expressed only in lymphoid tissues such as tonsils, lymph nodes and spleen, as well as peripheral blood mononuclear cells. Ref.1 Ref.2

Domain

In addition to ubiquitin-binding at the Cys-91 active site, a proximal ubiquitin-binding site is also present at Cys-23 Occupancy of the active site is needed to enable tight binding to the second site. Distinct binding sites for the ubiquitins may allow to discriminate among different isopeptide linkages (i.e. 'Lys-48'-, 'Lys-63'-linked polyubiquitin) in polyubiquitin substrates and achieve linkage-specific deubiquitination. Ref.11

Miscellaneous

In the structure described by Ref.16, the His-265 active site of the catalytic triad is located too far to interact directly with the active site Cys-91. A possible explanation is that OTUB1 is in inactive conformation in absence of ubiquitin and a conformation change may move His-265 in the proximity of Cys-91 in presence of ubiquitin substrate.

Sequence similarities

Belongs to the peptidase C65 family.

Contains 1 OTU domain.

Sequence caution

The sequence AAF28941.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAdaptive immunity
DNA damage
DNA repair
Immunity
Ubl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from direct assay Ref.12. Source: UniProtKB

immune system process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of double-strand break repair

Inferred from mutant phenotype Ref.12. Source: UniProtKB

negative regulation of histone H2A K63-linked ubiquitination

Inferred from direct assay Ref.12. Source: UniProtKB

protein K48-linked deubiquitination

Inferred from direct assay Ref.16Ref.11Ref.15. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

   Molecular_functionNEDD8-specific protease activity

Inferred from direct assay Ref.16. Source: UniProtKB

omega peptidase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.16. Source: UniProtKB

ubiquitin binding

Inferred from direct assay Ref.11. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.12. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.16Ref.11Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96FW1-1)

Also known as: Otubain-1;

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.
Isoform 2 (identifier: Q96FW1-2)

Also known as: ARF-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: MAAEEPQQQK...ALLDDSKELQ → MMKPSWLSRT...MLGPPFHPTP
Note: Lacks the catalytic sites for protease activity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 271270Ubiquitin thioesterase OTUB1
PRO_0000221008

Regions

Domain80 – 271192OTU
Region130 – 1389Ubiquitin-conjugating enzyme E2 binding
Region169 – 1779Ubiquitin-conjugating enzyme E2 binding
Region189 – 1957Free ubiquitin binding
Region206 – 2138Ubiquitin-conjugating enzyme E2 binding
Region214 – 2218Free ubiquitin binding
Region245 – 2517Free ubiquitin binding

Sites

Active site881
Active site911Nucleophile
Active site2651
Binding site2211Free ubiquitin
Binding site2351Free ubiquitin
Binding site2371Free ubiquitin
Binding site2611Free ubiquitin
Binding site2661Free ubiquitin
Site231Required for proximal ubiquitin-binding

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.14
Modified residue161Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 112112MAAEE…SKELQ → MMKPSWLSRTEFSKRLLCRT LWCQSGWSSRSYTRSMLKMT TSINRRSRTSTKSTRTSARP GLTATVSIGLSDSPTWRHCW MTARSCSGEKGGHWAPRQVG VYLLPGRVGCVSSRVSPSFP GDGLDSGLARRGSAVSALAS GLVEEPMLGPPFHPTP in isoform 2.
VSP_009464

Experimental info

Mutagenesis231C → A: Abolishes only ubiquitin-vinylsulfone adduct formation. Ref.11
Mutagenesis331Q → R: Impairs inhibition of UBE2N/UBC13. Ref.17
Mutagenesis371I → T: Impairs inhibition of UBE2N/UBC13. Ref.17
Mutagenesis391Q → L: Does not affect activity in DNA repair and ability to inhibit UBE2N/UBC13. Ref.17
Mutagenesis871P → G: Slightly improves ability to cleave 'K63'-linked ubiquitin. Ref.16
Mutagenesis881D → E: Abolishes hydrolase activity in vitro. Abolishes ability to inhibit RNF168; when associated with S-91 and A-265. Ref.1 Ref.12
Mutagenesis911C → A: Prevents RNF128 autoubiquitination, and stabilizes RNF128 in vivo. Abolishes both ubiquitin-binding and adduct formation with ubiquitin-vinylsulfone. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.16 Ref.17
Mutagenesis911C → S: Abolishes hydrolase activity in vitro. Does not affect ability to inhibit RNF168. Abolishes ability to inhibit RNF168; when associated with A-88 and A-265. Ref.1 Ref.2 Ref.10 Ref.11 Ref.12 Ref.16 Ref.17
Mutagenesis1161A → T: Does not affect ability to inhibit UBE2N/UBC13. Ref.17
Mutagenesis1341T → R: Impairs inhibition of UBE2N/UBC13. Ref.17
Mutagenesis1371D → G: Impairs inhibition of UBE2N/UBC13. Ref.17
Mutagenesis1761R → L: No effect on RNF128. Ref.2
Mutagenesis1901F → S: Fails to inhibit ubiquitin conjugation by UBE2N/UBC13. Ref.17
Mutagenesis2121C → A: No effect on RNF128. Ref.2 Ref.11
Mutagenesis2611Y → H: Impairs inhibition of UBE2N/UBC13. Ref.17
Mutagenesis2631P → L: Fails to inhibit ubiquitin conjugation by UBE2N/UBC13. Ref.17
Mutagenesis2651H → A: Abolishes ability to inhibit RNF168; when associated with A-88 and S-91. Ref.1 Ref.12
Mutagenesis2651H → R: Abolishes hydrolase activity in vitro. Ref.1 Ref.12
Sequence conflict611Y → C in AAH10368. Ref.6
Sequence conflict1511K → R in BAA90956. Ref.4

Secondary structure

......................................... 271
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Otubain-1) [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 63188EE1DC5FD66F

FASTA27131,284
        10         20         30         40         50         60 
MAAEEPQQQK QEPLGSDSEG VNCLAYDEAI MAQQDRIQQE IAVQNPLVSE RLELSVLYKE 

        70         80         90        100        110        120 
YAEDDNIYQQ KIKDLHKKYS YIRKTRPDGN CFYRAFGFSH LEALLDDSKE LQRFKAVSAK 

       130        140        150        160        170        180 
SKEDLVSQGF TEFTIEDFHN TFMDLIEQVE KQTSVADLLA SFNDQSTSDY LVVYLRLLTS 

       190        200        210        220        230        240 
GYLQRESKFF EHFIEGGRTV KEFCQQEVEP MCKESDHIHI IALAQALSVS IQVEYMDRGE 

       250        260        270 
GGTTNPHIFP EGSEPKVYLL YRPGHYDILY K 

« Hide

Isoform 2 (ARF-1) [UniParc].

Checksum: 3B37EB8F1B3B2404
Show »

FASTA31535,285

References

« Hide 'large scale' references
[1]"Otubains: a new family of cysteine proteases in the ubiquitin pathway."
Balakirev M.Y., Tcherniuk S.O., Jaquinod M., Chroboczek J.
EMBO Rep. 4:517-522(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-88; CYS-91 AND HIS-265.
Tissue: Cervix carcinoma.
[2]"Two isoforms of otubain 1 regulate T cell anergy via GRAIL."
Soares L., Seroogy C., Skrenta H., Anandasabapathy N., Lovelace P., Chung C.D., Engleman E., Fathman C.G.
Nat. Immunol. 5:45-54(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH RNF128 AND USP8, MUTAGENESIS OF CYS-91; ARG-176 AND CYS-212.
[3]"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. expand/collapse author list , Gu J., Chen S.-J., Chen Z.
Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Umbilical cord blood.
[4]"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. expand/collapse author list , 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 1).
Tissue: Colon.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Colon and Skin.
[7]"Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family."
Borodovsky A., Ovaa H., Kolli N., Gan-Erdene T., Wilkinson K.D., Ploegh H.L., Kessler B.M.
Chem. Biol. 9:1149-1159(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"OTU Domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) alpha and affects ERalpha transcriptional activity."
Stanisic V., Malovannaya A., Qin J., Lonard D.M., O'Malley B.W.
J. Biol. Chem. 284:16135-16145(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ESR1, MUTAGENESIS OF CYS-91.
[11]"Evidence for bidentate substrate binding as the basis for the K48 linkage specificity of otubain 1."
Wang T., Yin L., Cooper E.M., Lai M.-Y., Dickey S., Pickart C.M., Fushman D., Wilkinson K.D., Cohen R.E., Wolberger C.
J. Mol. Biol. 386:1011-1023(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITIN-BINDING, DOMAIN, MUTAGENESIS OF CYS-23; CYS-91 AND CYS-212.
[12]"Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1."
Nakada S., Tai I., Panier S., Al-Hakim A., Iemura S., Juang Y.C., O'Donnell L., Kumakubo A., Munro M., Sicheri F., Gingras A.C., Natsume T., Suda T., Durocher D.
Nature 466:941-946(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INHIBITION OF RNF168, INTERACTION WITH UBE2N/UBC13, MUTAGENESIS OF ASP-88; CYS-91 AND HIS-265.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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: FUNCTION, CATALYTIC ACTIVITY.
[16]"Structural basis and specificity of human otubain 1-mediated deubiquitination."
Edelmann M.J., Iphoefer A., Akutsu M., Altun M., di Gleria K., Kramer H.B., Fiebiger E., Dhe-Paganon S., Kessler B.M.
Biochem. J. 418:379-390(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 40-271, FUNCTION, INTERACTION WITH FUS AND GNB2L1, MUTAGENESIS OF PRO-87 AND CYS-91.
[17]"OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function."
Juang Y.C., Landry M.C., Sanches M., Vittal V., Leung C.C., Ceccarelli D.F., Mateo A.R., Pruneda J.N., Mao D.Y., Szilard R.K., Orlicky S., Munro M., Brzovic P.S., Klevit R.E., Sicheri F., Durocher D.
Mol. Cell 45:384-397(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-271 IN COMPLEX WITH UBE2V2 AND UBE2N, FREE UBIQUITIN-BINDING, ENZYME REGULATION, MUTAGENESIS OF GLN-33; ILE-37; GLN-39; CYS-91; ALA-116; THR-134; ASP-137; PHE-190; TYR-261 AND PRO-263.
[18]"The mechanism of OTUB1-mediated inhibition of ubiquitination."
Wiener R., Zhang X., Wang T., Wolberger C.
Nature 483:618-622(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF 1-45 IN COMPLEX WITH UBE2N AND UBIQUITIN, ENZYME REGULATION, FREE UBIQUITIN-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY177200 mRNA. Translation: AAO27702.1.
AF161381 mRNA. Translation: AAF28941.1. Different initiation.
AK000120 mRNA. Translation: BAA90956.1.
AP000721 Genomic DNA. No translation available.
BC007519 mRNA. Translation: AAH07519.1.
BC010368 mRNA. Translation: AAH10368.1.
BC107701 mRNA. Translation: AAI07702.1.
CCDSCCDS8055.1. [Q96FW1-1]
RefSeqNP_060140.2. NM_017670.2. [Q96FW1-1]
UniGeneHs.473788.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZFYX-ray1.69A40-271[»]
3VONX-ray3.15A/H/O/V/c/j45-271[»]
4DDGX-ray3.30A/B/C/J/K/L25-271[»]
4DDIX-ray3.80A/B/C25-271[»]
4DHZX-ray3.11A1-45[»]
4I6LX-ray2.49A45-271[»]
4LDTX-ray1.90A1-45[»]
ProteinModelPortalQ96FW1.
SMRQ96FW1. Positions 25-271.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120751. 58 interactions.
DIPDIP-41158N.
IntActQ96FW1. 26 interactions.
MINTMINT-5001867.
STRING9606.ENSP00000301453.

Protein family/group databases

MEROPSC65.001.

PTM databases

PhosphoSiteQ96FW1.

Polymorphism databases

DMDM44888286.

Proteomic databases

MaxQBQ96FW1.
PaxDbQ96FW1.
PRIDEQ96FW1.

Protocols and materials databases

DNASU55611.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000428192; ENSP00000402551; ENSG00000167770. [Q96FW1-1]
ENST00000538426; ENSP00000444357; ENSG00000167770. [Q96FW1-1]
GeneID55611.
KEGGhsa:55611.
UCSCuc001nyf.1. human. [Q96FW1-1]
uc001nyg.1. human. [Q96FW1-2]

Organism-specific databases

CTD55611.
GeneCardsGC11P063753.
HGNCHGNC:23077. OTUB1.
HPAHPA039176.
MIM608337. gene.
neXtProtNX_Q96FW1.
PharmGKBPA134988141.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267426.
HOVERGENHBG053383.
InParanoidQ96FW1.
KOK09602.
PhylomeDBQ96FW1.
TreeFamTF314145.

Gene expression databases

ArrayExpressQ96FW1.
BgeeQ96FW1.
CleanExHS_OTUB1.
GenevestigatorQ96FW1.

Family and domain databases

InterProIPR003323. OTU.
IPR019400. Peptidase_C65_otubain.
IPR016615. Ubiquitin_thioesterase_Otubain.
[Graphical view]
PfamPF10275. Peptidase_C65. 1 hit.
[Graphical view]
PIRSFPIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
PROSITEPS50802. OTU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSOTUB1. human.
EvolutionaryTraceQ96FW1.
GeneWikiOTUB1.
GenomeRNAi55611.
NextBio60179.
PROQ96FW1.
SOURCESearch...

Entry information

Entry nameOTUB1_HUMAN
AccessionPrimary (citable) accession number: Q96FW1
Secondary accession number(s): Q32Q78 expand/collapse secondary AC list , Q96II3, Q9NXQ4, Q9P0B8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: July 9, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM