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Q96DC9

- OTUB2_HUMAN

UniProt

Q96DC9 - OTUB2_HUMAN

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Protein

Ubiquitin thioesterase OTUB2

Gene

OTUB2

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 in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains.3 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).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei48 – 481By similarity
Active sitei51 – 511NucleophileCurated
Active sitei224 – 2241
Sitei226 – 2261Required to orient and stabilize the active site H-224

GO - Molecular functioni

  1. omega peptidase activity Source: InterPro
  2. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. cellular amino acid metabolic process Source: UniProtKB
  2. protein deubiquitination Source: UniProtKB
  3. protein K11-linked deubiquitination Source: UniProtKB
  4. protein K48-linked deubiquitination Source: UniProtKB
  5. protein K63-linked deubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Protein family/group databases

MEROPSiC65.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin thioesterase OTUB2 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme OTUB2
OTU domain-containing ubiquitin aldehyde-binding protein 2
Otubain-2
Ubiquitin-specific-processing protease OTUB2
Gene namesi
Name:OTUB2
Synonyms:C14orf137, OTB2, OTU2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:20351. OTUB2.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471G → P: Affects its ability to cleave 'K63'-linked ubiquitin. 1 Publication
Mutagenesisi51 – 511C → S: Loss of function in vitro. 1 Publication
Mutagenesisi226 – 2261N → A: Abolishes deubiquitinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA134861658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 234234Ubiquitin thioesterase OTUB2PRO_0000221010Add
BLAST

Proteomic databases

MaxQBiQ96DC9.
PaxDbiQ96DC9.
PeptideAtlasiQ96DC9.
PRIDEiQ96DC9.

PTM databases

PhosphoSiteiQ96DC9.

Expressioni

Tissue specificityi

Widely expressed. Expressed at higher level in brain.1 Publication

Gene expression databases

BgeeiQ96DC9.
CleanExiHS_OTUB2.
GenevestigatoriQ96DC9.

Organism-specific databases

HPAiHPA002329.

Interactioni

Protein-protein interaction databases

BioGridi122461. 27 interactions.
IntActiQ96DC9. 3 interactions.
STRINGi9606.ENSP00000203664.

Structurei

Secondary structure

1
234
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Helixi15 – 217Combined sources
Helixi26 – 3510Combined sources
Turni36 – 383Combined sources
Beta strandi39 – 435Combined sources
Beta strandi47 – 493Combined sources
Helixi51 – 6414Combined sources
Helixi68 – 8720Combined sources
Helixi92 – 11019Combined sources
Helixi115 – 1228Combined sources
Helixi125 – 14420Combined sources
Helixi147 – 1504Combined sources
Helixi151 – 1533Combined sources
Helixi160 – 1678Combined sources
Helixi177 – 18711Combined sources
Beta strandi191 – 1966Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi204 – 2096Combined sources
Beta strandi215 – 2239Combined sources
Beta strandi225 – 2306Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TFFX-ray2.10A1-234[»]
4FJVX-ray2.05A/C1-234[»]
ProteinModelPortaliQ96DC9.
SMRiQ96DC9. Positions 2-232.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96DC9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 231192OTUPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C65 family.Curated
Contains 1 OTU domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG267426.
GeneTreeiENSGT00390000006979.
HOGENOMiHOG000019496.
HOVERGENiHBG053383.
InParanoidiQ96DC9.
KOiK09603.
OMAiVFSEAAC.
OrthoDBiEOG71K64D.
PhylomeDBiQ96DC9.
TreeFamiTF314145.

Family and domain databases

InterProiIPR003323. OTU.
IPR019400. Peptidase_C65_otubain.
IPR016615. Ubiquitin_thioesterase_Otubain.
[Graphical view]
PfamiPF10275. Peptidase_C65. 1 hit.
[Graphical view]
PIRSFiPIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
PROSITEiPS50802. OTU. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96DC9-1) [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
MSETSFNLIS EKCDILSILR DHPENRIYRR KIEELSKRFT AIRKTKGDGN
60 70 80 90 100
CFYRALGYSY LESLLGKSRE IFKFKERVLQ TPNDLLAAGF EEHKFRNFFN
110 120 130 140 150
AFYSVVELVE KDGSVSSLLK VFNDQSASDH IVQFLRLLTS AFIRNRADFF
160 170 180 190 200
RHFIDEEMDI KDFCTHEVEP MATECDHIQI TALSQALSIA LQVEYVDEMD
210 220 230
TALNHHVFPE AATPSVYLLY KTSHYNILYA ADKH
Length:234
Mass (Da):27,213
Last modified:March 1, 2004 - v2
Checksum:iDF2DBD32A78F9929
GO
Isoform 2 (identifier: Q96DC9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-234: Missing.

Note: No experimental confirmation available.

Show »
Length:73
Mass (Da):8,637
Checksum:iD3382B36FCD3C74A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei74 – 234161Missing in isoform 2. 1 PublicationVSP_009465Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY177201 mRNA. Translation: AAO27703.1.
AK025569 mRNA. Translation: BAB15172.1.
CR457345 mRNA. Translation: CAG33626.1.
AL079302 Genomic DNA. No translation available.
BC009615 mRNA. Translation: AAH09615.1.
BC068058 mRNA. Translation: AAH68058.1.
CCDSiCCDS9917.1. [Q96DC9-1]
RefSeqiNP_075601.1. NM_023112.3. [Q96DC9-1]
UniGeneiHs.278815.

Genome annotation databases

EnsembliENST00000203664; ENSP00000203664; ENSG00000089723. [Q96DC9-1]
ENST00000553723; ENSP00000451283; ENSG00000089723. [Q96DC9-2]
ENST00000617748; ENSP00000478628; ENSG00000277276. [Q96DC9-1]
GeneIDi78990.
KEGGihsa:78990.
UCSCiuc001yci.3. human. [Q96DC9-1]

Polymorphism databases

DMDMi44888285.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY177201 mRNA. Translation: AAO27703.1 .
AK025569 mRNA. Translation: BAB15172.1 .
CR457345 mRNA. Translation: CAG33626.1 .
AL079302 Genomic DNA. No translation available.
BC009615 mRNA. Translation: AAH09615.1 .
BC068058 mRNA. Translation: AAH68058.1 .
CCDSi CCDS9917.1. [Q96DC9-1 ]
RefSeqi NP_075601.1. NM_023112.3. [Q96DC9-1 ]
UniGenei Hs.278815.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TFF X-ray 2.10 A 1-234 [» ]
4FJV X-ray 2.05 A/C 1-234 [» ]
ProteinModelPortali Q96DC9.
SMRi Q96DC9. Positions 2-232.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122461. 27 interactions.
IntActi Q96DC9. 3 interactions.
STRINGi 9606.ENSP00000203664.

Protein family/group databases

MEROPSi C65.002.

PTM databases

PhosphoSitei Q96DC9.

Polymorphism databases

DMDMi 44888285.

Proteomic databases

MaxQBi Q96DC9.
PaxDbi Q96DC9.
PeptideAtlasi Q96DC9.
PRIDEi Q96DC9.

Protocols and materials databases

DNASUi 78990.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000203664 ; ENSP00000203664 ; ENSG00000089723 . [Q96DC9-1 ]
ENST00000553723 ; ENSP00000451283 ; ENSG00000089723 . [Q96DC9-2 ]
ENST00000617748 ; ENSP00000478628 ; ENSG00000277276 . [Q96DC9-1 ]
GeneIDi 78990.
KEGGi hsa:78990.
UCSCi uc001yci.3. human. [Q96DC9-1 ]

Organism-specific databases

CTDi 78990.
GeneCardsi GC14P094492.
HGNCi HGNC:20351. OTUB2.
HPAi HPA002329.
MIMi 608338. gene.
neXtProti NX_Q96DC9.
PharmGKBi PA134861658.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG267426.
GeneTreei ENSGT00390000006979.
HOGENOMi HOG000019496.
HOVERGENi HBG053383.
InParanoidi Q96DC9.
KOi K09603.
OMAi VFSEAAC.
OrthoDBi EOG71K64D.
PhylomeDBi Q96DC9.
TreeFami TF314145.

Miscellaneous databases

ChiTaRSi OTUB2. human.
EvolutionaryTracei Q96DC9.
GeneWikii OTUB2.
GenomeRNAii 78990.
NextBioi 67574.
PROi Q96DC9.
SOURCEi Search...

Gene expression databases

Bgeei Q96DC9.
CleanExi HS_OTUB2.
Genevestigatori Q96DC9.

Family and domain databases

InterProi IPR003323. OTU.
IPR019400. Peptidase_C65_otubain.
IPR016615. Ubiquitin_thioesterase_Otubain.
[Graphical view ]
Pfami PF10275. Peptidase_C65. 1 hit.
[Graphical view ]
PIRSFi PIRSF013503. Ubiquitin_thioesterase_Otubain. 1 hit.
PROSITEi PS50802. OTU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 CYS-51.
    Tissue: Cervix carcinoma.
  2. "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 1).
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Eye and Lung.
  6. "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: FUNCTION, MUTAGENESIS OF GLY-47.
  7. "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.
  8. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), MUTAGENESIS OF ASN-226.

Entry informationi

Entry nameiOTUB2_HUMAN
AccessioniPrimary (citable) accession number: Q96DC9
Secondary accession number(s): Q6IA10, Q9H6T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: November 26, 2014
This is version 113 of the entry and version 2 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

Miscellaneous

In the structure described by PubMed:15258613, the Asp-48 active site of the catalytic triad is located too far to interact directly with the active site His-224. A possible explanation is that OTUB2 is in inactive conformation in absence of ubiquitin and a conformation change may move Asp-48 in the proximity of His-224 in presence of ubiquitin substrate.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3