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Q96G74 (OTUD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
OTU domain-containing protein 5

EC=3.4.19.12
Alternative name(s):
Deubiquitinating enzyme A
Short name=DUBA
Gene names
Name:OTUD5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Deubiquitinating enzyme that functions as negative regulator of the innate immune system. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro). Ref.7 Ref.13 Ref.15

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

Inhibited by N-ethyl-maleimide (NEM).

Subunit structure

Interacts with TRAF3. Ref.7

Tissue specificity

Expressed in various tissues, including the liver and placenta, as well as in peripheral blood leukocytes. Ref.7

Induction

Up-regulated by bacterial lipopolysaccharide (LPS) in bone marrow-derived macrophages. Ref.15

Post-translational modification

Phosphorylation at Ser-177 is required for deubiquitinating activity.

Sequence similarities

Belongs to the peptidase C85 family.

Contains 1 OTU domain.

Sequence caution

The sequence BAB14131.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB15416.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96G74-1)

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: Q96G74-2)

The sequence of this isoform differs from the canonical sequence as follows:
     17-40: Missing.
     304-308: Missing.
Note: No experimental confirmation available. Dubious isoform produced through aberrant splice sites.
Isoform 3 (identifier: Q96G74-3)

The sequence of this isoform differs from the canonical sequence as follows:
     304-308: Missing.
     563-566: HRDP → PCRC
     567-571: Missing.
Note: No experimental confirmation available. Dubious isoform produced through aberrant splice sites.
Isoform 4 (identifier: Q96G74-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-217: Missing.
     304-308: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q96G74-5)

The sequence of this isoform differs from the canonical sequence as follows:
     304-308: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 571571OTU domain-containing protein 5
PRO_0000278223

Regions

Domain213 – 341129OTU
Region218 – 2247Cys-loop By similarity
Region273 – 28311Variable-loop By similarity
Region329 – 3346His-loop By similarity
Compositional bias5 – 113109Pro-rich
Compositional bias33 – 174142Gly-rich

Sites

Active site2211 Potential
Active site2241Nucleophile Ref.15
Active site3341 Probable

Amino acid modifications

Modified residue641Phosphoserine Ref.8 Ref.12 Ref.15
Modified residue1651Phosphoserine Ref.9 Ref.11 Ref.12 Ref.15
Modified residue1751Phosphotyrosine Ref.15
Modified residue1771Phosphoserine Ref.9 Ref.11 Ref.15
Modified residue4521Phosphoserine Ref.9
Modified residue5071Phosphothreonine Ref.15

Natural variations

Alternative sequence1 – 217217Missing in isoform 4.
VSP_045185
Alternative sequence17 – 4024Missing in isoform 2.
VSP_023195
Alternative sequence304 – 3085Missing in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_023192
Alternative sequence563 – 5664HRDP → PCRC in isoform 3.
VSP_023193
Alternative sequence567 – 5715Missing in isoform 3.
VSP_023194

Experimental info

Mutagenesis1771S → D or E: Loss of deubiquitinase activity. Abolishes activation by protein kinases. Ref.15
Mutagenesis2241C → S: Loss of deubiquitinase activity. Loss of suppression of IFN production. Ref.7 Ref.15
Mutagenesis5421L → A: Loss of 'K-48'- and 'K-63'-linked polyubiquitin chain binding. Partial loss of TRAF3 deubiquitination; when associated with A-549. Ref.7
Mutagenesis5491S → A: Loss of 'K-48'- and 'K-63'-linked polyubiquitin chain binding. Partial loss of TRAF3 deubiquitination; when associated with A-542. Ref.7

Secondary structure

.............................. 571
Helix Strand Turn

Details...

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: F4B2B385B84ABC46

FASTA57160,626
        10         20         30         40         50         60 
MTILPKKKPP PPDADPANEP PPPGPMPPAP RRGGGVGVGG GGTGVGGGDR DRDSGVVGAR 

        70         80         90        100        110        120 
PRASPPPQGP LPGPPGALHR WALAVPPGAV AGPRPQQASP PPCGGPGGPG GGPGDALGAA 

       130        140        150        160        170        180 
AAGVGAAGVV VGVGGAVGVG GCCSGPGHSK RRRQAPGVGA VGGGSPEREE VGAGYNSEDE 

       190        200        210        220        230        240 
YEAAAARIEA MDPATVEQQE HWFEKALRDK KGFIIKQMKE DGACLFRAVA DQVYGDQDMH 

       250        260        270        280        290        300 
EVVRKHCMDY LMKNADYFSN YVTEDFTTYI NRKRKNNCHG NHIEMQAMAE MYNRPVEVYQ 

       310        320        330        340        350        360 
YSTGTSAVEP INTFHGIHQN EDEPIRVSYH RNIHYNSVVN PNKATIGVGL GLPSFKPGFA 

       370        380        390        400        410        420 
EQSLMKNAIK TSEESWIEQQ MLEDKKRATD WEATNEAIEE QVARESYLQW LRDQEKQARQ 

       430        440        450        460        470        480 
VRGPSQPRKA SATCSSATAA ASSGLEEWTS RSPRQRSSAS SPEHPELHAE LGMKPPSPGT 

       490        500        510        520        530        540 
VLALAKPPSP CAPGTSSQFS AGADRATSPL VSLYPALECR ALIQQMSPSA FGLNDWDDDE 

       550        560        570 
ILASVLAVSQ QEYLDSMKKN KVHRDPPPDK S 

« Hide

Isoform 2 [UniParc].

Checksum: FB641E44937EC3F2
Show »

FASTA54258,007
Isoform 3 [UniParc].

Checksum: 9C931880385CF8CB
Show »

FASTA56159,640
Isoform 4 [UniParc].

Checksum: 555902ECCA9C52E4
Show »

FASTA34939,185
Isoform 5 [UniParc].

Checksum: 46EBC6634CD55DA2
Show »

FASTA56660,210

References

« Hide 'large scale' references
[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. 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 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-571 (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-571 (ISOFORM 1).
Tissue: Brain and Small intestine.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORMS 1; 2 AND 3).
Tissue: Kidney and Skin.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 140-571 (ISOFORM 5).
Tissue: Amygdala.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"DUBA: a deubiquitinase that regulates type I interferon production."
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.
Science 318:1628-1632(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TRAF3, MUTAGENESIS OF CYS-224; LEU-542 AND SER-549.
[8]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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-165; SER-177 AND SER-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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.
[14]"The catalytic domain of human OTUD5."
Structural genomics consortium (SGC)
Submitted (DEC-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 172-339.
[15]"Phosphorylation-dependent activity of the deubiquitinase DUBA."
Huang O.W., Ma X., Yin J., Flinders J., Maurer T., Kayagaki N., Phung Q., Bosanac I., Arnott D., Dixit V.M., Hymowitz S.G., Starovasnik M.A., Cochran A.G.
Nat. Struct. Mol. Biol. 19:171-175(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 172-351 IN COMPLEX WITH UBIQUITIN, CATALYTIC ACTIVITY, FUNCTION, INDUCTION, PHOSPHORYLATION AT SER-64; SER-165; TYR-175; SER-177 AND THR-507, MUTAGENESIS OF SER-177 AND CYS-224, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK022612 mRNA. Translation: BAB14131.1. Different initiation.
AK026260 mRNA. Translation: BAB15416.1. Different initiation.
AK294590 mRNA. Translation: BAG57778.1.
AF207550 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50724.1.
BC009917 mRNA. Translation: AAH09917.1.
BC028225 mRNA. Translation: AAH28225.1.
BC098440 mRNA. Translation: AAH98440.1.
AL137509 mRNA. Translation: CAB70778.1.
CCDSCCDS14313.1. [Q96G74-1]
CCDS48105.1. [Q96G74-4]
PIRT46265.
RefSeqNP_001129629.1. NM_001136157.1. [Q96G74-5]
NP_001129630.1. NM_001136158.1. [Q96G74-5]
NP_001129631.1. NM_001136159.1. [Q96G74-4]
NP_060072.1. NM_017602.3. [Q96G74-1]
XP_006724600.1. XM_006724537.1. [Q96G74-1]
UniGeneHs.496098.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PFYX-ray1.70A172-344[»]
3TMOX-ray2.20A172-351[»]
3TMPX-ray1.91A/C/E/G172-351[»]
ProteinModelPortalQ96G74.
SMRQ96G74. Positions 173-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120738. 17 interactions.
DIPDIP-53541N.
IntActQ96G74. 16 interactions.
MINTMINT-1408843.
STRING9606.ENSP00000156084.

Protein family/group databases

MEROPSC85.001.

PTM databases

PhosphoSiteQ96G74.

Polymorphism databases

DMDM74731791.

Proteomic databases

MaxQBQ96G74.
PaxDbQ96G74.
PRIDEQ96G74.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000156084; ENSP00000156084; ENSG00000068308. [Q96G74-1]
ENST00000376488; ENSP00000365671; ENSG00000068308.
ENST00000396743; ENSP00000379969; ENSG00000068308.
ENST00000428668; ENSP00000401629; ENSG00000068308. [Q96G74-4]
ENST00000594822; ENSP00000472254; ENSG00000267983. [Q96G74-4]
ENST00000597676; ENSP00000471884; ENSG00000267983. [Q96G74-1]
GeneID55593.
KEGGhsa:55593.
UCSCuc004dlt.4. human.
uc004dlu.3. human. [Q96G74-1]
uc011mmp.2. human.

Organism-specific databases

CTD55593.
GeneCardsGC0XM048779.
HGNCHGNC:25402. OTUD5.
HPAHPA017375.
MIM300713. gene.
neXtProtNX_Q96G74.
PharmGKBPA142671217.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG286112.
HOGENOMHOG000231360.
HOVERGENHBG060214.
InParanoidQ96G74.
KOK12655.
OMAWEDDEIL.
OrthoDBEOG77Q4X0.
PhylomeDBQ96G74.
TreeFamTF326812.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ96G74.
BgeeQ96G74.
CleanExHS_OTUD5.
GenevestigatorQ96G74.

Family and domain databases

InterProIPR003323. OTU.
[Graphical view]
PfamPF02338. OTU. 1 hit.
[Graphical view]
PROSITEPS50802. OTU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSOTUD5. human.
GenomeRNAi55593.
NextBio60126.
PROQ96G74.
SOURCESearch...

Entry information

Entry nameOTUD5_HUMAN
AccessionPrimary (citable) accession number: Q96G74
Secondary accession number(s): B4DGG7 expand/collapse secondary AC list , G5E9D7, Q4KMN9, Q8N6T5, Q9H650, Q9H9U0, Q9NT65
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 101 of the entry and version 1 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 X

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