SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q96G74

- OTUD5_HUMAN

UniProt

Q96G74 - OTUD5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
OTU domain-containing protein 5
Gene
OTUD5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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).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

Enzyme regulationi

Inhibited by N-ethyl-maleimide (NEM).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei221 – 2211 Reviewed prediction
Active sitei224 – 2241Nucleophile1 Publication
Active sitei334 – 3341 Inferred

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: UniProtKB

GO - Biological processi

  1. innate immune response Source: Reactome
  2. negative regulation of type I interferon production Source: Reactome
  3. protein K48-linked deubiquitination Source: UniProtKB
  4. protein K63-linked deubiquitination Source: UniProtKB
  5. response to lipopolysaccharide Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_25271. Negative regulators of RIG-I/MDA5 signaling.

Protein family/group databases

MEROPSiC85.001.

Names & Taxonomyi

Protein namesi
Recommended name:
OTU domain-containing protein 5 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme A
Short name:
DUBA
Gene namesi
Name:OTUD5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:25402. OTUD5.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi177 – 1771S → D or E: Loss of deubiquitinase activity. Abolishes activation by protein kinases. 1 Publication
Mutagenesisi224 – 2241C → S: Loss of deubiquitinase activity. Loss of suppression of IFN production. 2 Publications
Mutagenesisi542 – 5421L → A: Loss of 'K-48'- and 'K-63'-linked polyubiquitin chain binding. Partial loss of TRAF3 deubiquitination; when associated with A-549. 1 Publication
Mutagenesisi549 – 5491S → A: Loss of 'K-48'- and 'K-63'-linked polyubiquitin chain binding. Partial loss of TRAF3 deubiquitination; when associated with A-542. 1 Publication

Organism-specific databases

PharmGKBiPA142671217.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 571571OTU domain-containing protein 5
PRO_0000278223Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Phosphoserine3 Publications
Modified residuei165 – 1651Phosphoserine4 Publications
Modified residuei175 – 1751Phosphotyrosine1 Publication
Modified residuei177 – 1771Phosphoserine3 Publications
Modified residuei452 – 4521Phosphoserine1 Publication
Modified residuei507 – 5071Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylation at Ser-177 is required for deubiquitinating activity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96G74.
PaxDbiQ96G74.
PRIDEiQ96G74.

PTM databases

PhosphoSiteiQ96G74.

Expressioni

Tissue specificityi

Expressed in various tissues, including the liver and placenta, as well as in peripheral blood leukocytes.1 Publication

Inductioni

Up-regulated by bacterial lipopolysaccharide (LPS) in bone marrow-derived macrophages.1 Publication

Gene expression databases

ArrayExpressiQ96G74.
BgeeiQ96G74.
CleanExiHS_OTUD5.
GenevestigatoriQ96G74.

Organism-specific databases

HPAiHPA017375.

Interactioni

Subunit structurei

Interacts with TRAF3.1 Publication

Protein-protein interaction databases

BioGridi120738. 17 interactions.
DIPiDIP-53541N.
IntActiQ96G74. 16 interactions.
MINTiMINT-1408843.
STRINGi9606.ENSP00000156084.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi178 – 1803
Helixi181 – 1866
Helixi193 – 21119
Beta strandi214 – 2163
Helixi224 – 23411
Helixi237 – 2393
Helixi240 – 25314
Helixi255 – 2584
Helixi259 – 2613
Helixi266 – 2738
Helixi282 – 29211
Beta strandi296 – 3016
Beta strandi303 – 3053
Beta strandi311 – 3144
Beta strandi325 – 3306
Turni331 – 3333
Beta strandi334 – 3396

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PFYX-ray1.70A172-344[»]
3TMOX-ray2.20A172-351[»]
3TMPX-ray1.91A/C/E/G172-351[»]
ProteinModelPortaliQ96G74.
SMRiQ96G74. Positions 173-341.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini213 – 341129OTU
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni218 – 2247Cys-loop By similarity
Regioni273 – 28311Variable-loop By similarity
Add
BLAST
Regioni329 – 3346His-loop By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 113109Pro-rich
Add
BLAST
Compositional biasi33 – 174142Gly-rich
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase C85 family.
Contains 1 OTU domain.

Phylogenomic databases

eggNOGiNOG286112.
HOGENOMiHOG000231360.
HOVERGENiHBG060214.
InParanoidiQ96G74.
KOiK12655.
OMAiWEDDEIL.
OrthoDBiEOG77Q4X0.
PhylomeDBiQ96G74.
TreeFamiTF326812.

Family and domain databases

InterProiIPR003323. OTU.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
[Graphical view]
PROSITEiPS50802. OTU. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96G74-1) [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

MTILPKKKPP PPDADPANEP PPPGPMPPAP RRGGGVGVGG GGTGVGGGDR    50
DRDSGVVGAR PRASPPPQGP LPGPPGALHR WALAVPPGAV AGPRPQQASP 100
PPCGGPGGPG GGPGDALGAA AAGVGAAGVV VGVGGAVGVG GCCSGPGHSK 150
RRRQAPGVGA VGGGSPEREE VGAGYNSEDE YEAAAARIEA MDPATVEQQE 200
HWFEKALRDK KGFIIKQMKE DGACLFRAVA DQVYGDQDMH EVVRKHCMDY 250
LMKNADYFSN YVTEDFTTYI NRKRKNNCHG NHIEMQAMAE MYNRPVEVYQ 300
YSTGTSAVEP INTFHGIHQN EDEPIRVSYH RNIHYNSVVN PNKATIGVGL 350
GLPSFKPGFA EQSLMKNAIK TSEESWIEQQ MLEDKKRATD WEATNEAIEE 400
QVARESYLQW LRDQEKQARQ VRGPSQPRKA SATCSSATAA ASSGLEEWTS 450
RSPRQRSSAS SPEHPELHAE LGMKPPSPGT VLALAKPPSP CAPGTSSQFS 500
AGADRATSPL VSLYPALECR ALIQQMSPSA FGLNDWDDDE ILASVLAVSQ 550
QEYLDSMKKN KVHRDPPPDK S 571
Length:571
Mass (Da):60,626
Last modified:December 1, 2001 - v1
Checksum:iF4B2B385B84ABC46
GO
Isoform 2 (identifier: Q96G74-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:542
Mass (Da):58,007
Checksum:iFB641E44937EC3F2
GO
Isoform 3 (identifier: Q96G74-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:561
Mass (Da):59,640
Checksum:i9C931880385CF8CB
GO
Isoform 4 (identifier: Q96G74-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-217: Missing.
     304-308: Missing.

Note: No experimental confirmation available.

Show »
Length:349
Mass (Da):39,185
Checksum:i555902ECCA9C52E4
GO
Isoform 5 (identifier: Q96G74-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:566
Mass (Da):60,210
Checksum:i46EBC6634CD55DA2
GO

Sequence cautioni

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 sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 217217Missing in isoform 4.
VSP_045185Add
BLAST
Alternative sequencei17 – 4024Missing in isoform 2.
VSP_023195Add
BLAST
Alternative sequencei304 – 3085Missing in isoform 2, isoform 3, isoform 4 and isoform 5.
VSP_023192
Alternative sequencei563 – 5664HRDP → PCRC in isoform 3.
VSP_023193
Alternative sequencei567 – 5715Missing in isoform 3.
VSP_023194

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14313.1. [Q96G74-1]
CCDS48104.1. [Q96G74-5]
CCDS48105.1. [Q96G74-4]
PIRiT46265.
RefSeqiNP_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]
UniGeneiHs.496098.

Genome annotation databases

EnsembliENST00000156084; 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]
GeneIDi55593.
KEGGihsa:55593.
UCSCiuc004dlt.4. human.
uc004dlu.3. human. [Q96G74-1]
uc011mmp.2. human.

Polymorphism databases

DMDMi74731791.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14313.1. [Q96G74-1 ]
CCDS48104.1. [Q96G74-5 ]
CCDS48105.1. [Q96G74-4 ]
PIRi T46265.
RefSeqi NP_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 ]
UniGenei Hs.496098.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3PFY X-ray 1.70 A 172-344 [» ]
3TMO X-ray 2.20 A 172-351 [» ]
3TMP X-ray 1.91 A/C/E/G 172-351 [» ]
ProteinModelPortali Q96G74.
SMRi Q96G74. Positions 173-341.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120738. 17 interactions.
DIPi DIP-53541N.
IntActi Q96G74. 16 interactions.
MINTi MINT-1408843.
STRINGi 9606.ENSP00000156084.

Protein family/group databases

MEROPSi C85.001.

PTM databases

PhosphoSitei Q96G74.

Polymorphism databases

DMDMi 74731791.

Proteomic databases

MaxQBi Q96G74.
PaxDbi Q96G74.
PRIDEi Q96G74.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000156084 ; 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 ]
GeneIDi 55593.
KEGGi hsa:55593.
UCSCi uc004dlt.4. human.
uc004dlu.3. human. [Q96G74-1 ]
uc011mmp.2. human.

Organism-specific databases

CTDi 55593.
GeneCardsi GC0XM048779.
HGNCi HGNC:25402. OTUD5.
HPAi HPA017375.
MIMi 300713. gene.
neXtProti NX_Q96G74.
PharmGKBi PA142671217.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG286112.
HOGENOMi HOG000231360.
HOVERGENi HBG060214.
InParanoidi Q96G74.
KOi K12655.
OMAi WEDDEIL.
OrthoDBi EOG77Q4X0.
PhylomeDBi Q96G74.
TreeFami TF326812.

Enzyme and pathway databases

Reactomei REACT_25271. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

ChiTaRSi OTUD5. human.
GenomeRNAii 55593.
NextBioi 60126.
PROi Q96G74.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q96G74.
Bgeei Q96G74.
CleanExi HS_OTUD5.
Genevestigatori Q96G74.

Family and domain databases

InterProi IPR003323. OTU.
[Graphical view ]
Pfami PF02338. OTU. 1 hit.
[Graphical view ]
PROSITEi PS50802. OTU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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.
    , 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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiOTUD5_HUMAN
AccessioniPrimary (citable) accession number: Q96G74
Secondary accession number(s): B4DGG7
, G5E9D7, Q4KMN9, Q8N6T5, Q9H650, Q9H9U0, Q9NT65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: December 1, 2001
Last modified: September 3, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

Similar proteinsi