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Q6GQQ9

- OTU7B_HUMAN

UniProt

Q6GQQ9 - OTU7B_HUMAN

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Protein

OTU domain-containing protein 7B

Gene

OTUD7B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF-kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Negatively regulates mucosal immunity against infections. Mediates deubiquitination of EGFR. Has deubiquitinating activity toward 'Lys-11', 'Lys-48' or 'Lys-63'-linked polyubiquitin chains. In vitro, has preference for 'Lys-11'-linked polyubiquitin chains; however such data are unsure in vivo. Hydrolyzes both linear and branched forms of polyubiquitin.6 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

Deubiquitinase activity is inhibited following interactin with PARK7.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei191 – 1911By similarity
Active sitei194 – 1941NucleophileCurated
Active sitei358 – 3581Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri796 – 83136A20-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB
  2. DNA binding Source: InterPro
  3. Lys48-specific deubiquitinase activity Source: ParkinsonsUK-UCL
  4. ubiquitin-specific protease activity Source: UniProtKB
  5. ubiquitin thiolesterase activity Source: UniProtKB
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. mucosal immune response Source: UniProtKB
  2. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: HGNC
  3. negative regulation of interleukin-8 production Source: ParkinsonsUK-UCL
  4. negative regulation of protein localization to nucleus Source: ParkinsonsUK-UCL
  5. negative regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
  6. protein K11-linked deubiquitination Source: UniProtKB
  7. protein K48-linked deubiquitination Source: UniProtKB
  8. protein K63-linked deubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Immunity, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ6GQQ9.

Protein family/group databases

MEROPSiC64.001.

Names & Taxonomyi

Protein namesi
Recommended name:
OTU domain-containing protein 7B (EC:3.4.19.12)
Alternative name(s):
Cellular zinc finger anti-NF-kappa-B protein
Zinc finger A20 domain-containing protein 1
Zinc finger protein Cezanne
Gene namesi
Name:OTUD7B
Synonyms:ZA20D1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16683. OTUD7B.

Subcellular locationi

Cytoplasm. Nucleus
Note: Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner.

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi194 – 1941C → A: Increased ability to interact with polyubiquitin. 3 Publications
Mutagenesisi194 – 1941C → S: Loss of deubiquitinating activity. 3 Publications
Mutagenesisi809 – 8091F → A: Does not affect interaction with EGFR. 1 Publication
Mutagenesisi810 – 8101Y → A: Impairs interaction with EGFR. 1 Publication

Organism-specific databases

PharmGKBiPA134873802.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 843843OTU domain-containing protein 7BPRO_0000188788Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated by EGFR.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6GQQ9.
PaxDbiQ6GQQ9.
PRIDEiQ6GQQ9.

PTM databases

PhosphoSiteiQ6GQQ9.

Expressioni

Tissue specificityi

Widely expressed. Abundant in kidney, heart and fetal liver. Expressed differentially among B-cells at distinct developmental stages. Higher expression seen in primary immature B-cells as compared to the mature cells.2 Publications

Inductioni

By TNF-alpha.1 Publication

Gene expression databases

BgeeiQ6GQQ9.
CleanExiHS_OTUD7B.
ExpressionAtlasiQ6GQQ9. differential.
GenevestigatoriQ6GQQ9.

Organism-specific databases

HPAiHPA027045.

Interactioni

Subunit structurei

Interacts with TRAF3 and TRAF6. Interacts with PARK7, leading to inhibit deubiquitinase activity. Interacts with EGFR, ITCH and NEDD4.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC50Q8IVM05EBI-527784,EBI-723996
PARK7Q994973EBI-527784,EBI-1164361

Protein-protein interaction databases

BioGridi121281. 13 interactions.
DIPiDIP-33805N.
IntActiQ6GQQ9. 13 interactions.
STRINGi9606.ENSP00000358131.

Structurei

3D structure databases

ProteinModelPortaliQ6GQQ9.
SMRiQ6GQQ9. Positions 1-61, 147-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 365183OTUPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni152 – 401250TRAF-bindingAdd
BLAST
Regioni167 – 440274CatalyticAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi483 – 49816Nuclear localization signalSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C64 family.Curated
Contains 1 A20-type zinc finger.PROSITE-ProRule annotation
Contains 1 OTU domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri796 – 83136A20-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG282016.
GeneTreeiENSGT00530000062989.
HOGENOMiHOG000048103.
HOVERGENiHBG050904.
InParanoidiQ6GQQ9.
KOiK11860.
OMAiYATFPRQ.
OrthoDBiEOG7JHM57.
PhylomeDBiQ6GQQ9.
TreeFamiTF323312.

Family and domain databases

InterProiIPR003323. OTU.
IPR002653. Znf_A20.
[Graphical view]
PfamiPF02338. OTU. 1 hit.
[Graphical view]
PROSITEiPS50802. OTU. 1 hit.
PS51036. ZF_A20. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6GQQ9) [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
MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDVNAALSD FEQLRQVHAG
60 70 80 90 100
NLPPSFSEGS GGSRTPEKGF SDREPTRPPR PILQRQDDIV QEKRLSRGIS
110 120 130 140 150
HASSSIVSLA RSHVSSNGGG GGSNEHPLEM PICAFQLPDL TVYNEDFRSF
160 170 180 190 200
IERDLIEQSM LVALEQAGRL NWWVSVDPTS QRLLPLATTG DGNCLLHAAS
210 220 230 240 250
LGMWGFHDRD LMLRKALYAL MEKGVEKEAL KRRWRWQQTQ QNKESGLVYT
260 270 280 290 300
EDEWQKEWNE LIKLASSEPR MHLGTNGANC GGVESSEEPV YESLEEFHVF
310 320 330 340 350
VLAHVLRRPI VVVADTMLRD SGGEAFAPIP FGGIYLPLEV PASQCHRSPL
360 370 380 390 400
VLAYDQAHFS ALVSMEQKEN TKEQAVIPLT DSEYKLLPLH FAVDPGKGWE
410 420 430 440 450
WGKDDSDNVR LASVILSLEV KLHLLHSYMN VKWIPLSSDA QAPLAQPESP
460 470 480 490 500
TASAGDEPRS TPESGDSDKE SVGSSSTSNE GGRRKEKSKR DREKDKKRAD
510 520 530 540 550
SVANKLGSFG KTLGSKLKKN MGGLMHSKGS KPGGVGTGLG GSSGTETLEK
560 570 580 590 600
KKKNSLKSWK GGKEEAAGDG PVSEKPPAES VGNGGSKYSQ EVMQSLSILR
610 620 630 640 650
TAMQGEGKFI FVGTLKMGHR HQYQEEMIQR YLSDAEERFL AEQKQKEAER
660 670 680 690 700
KIMNGGIGGG PPPAKKPEPD AREEQPTGPP AESRAMAFST GYPGDFTIPR
710 720 730 740 750
PSGGGVHCQE PRRQLAGGPC VGGLPPYATF PRQCPPGRPY PHQDSIPSLE
760 770 780 790 800
PGSHSKDGLH RGALLPPPYR VADSYSNGYR EPPEPDGWAG GLRGLPPTQT
810 820 830 840
KCKQPNCSFY GHPETNNFCS CCYREELRRR EREPDGELLV HRF
Length:843
Mass (Da):92,526
Last modified:July 19, 2004 - v1
Checksum:i6D386C864B12EE57
GO
Isoform 2 (identifier: Q6GQQ9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     805-833: Missing.

Show »
Length:814
Mass (Da):88,947
Checksum:i26C3BFE215BEC0D3
GO

Sequence cautioni

The sequence CAB97494.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti243 – 2431K → E in AAH20622. (PubMed:15489334)Curated
Sequence conflicti421 – 4211K → R in AAH20622. (PubMed:15489334)Curated
Sequence conflicti791 – 7911G → S in BAH13129. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei805 – 83329Missing in isoform 2. 1 PublicationVSP_046015Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ293573 mRNA. Translation: CAB97494.1. Different initiation.
AK299790 mRNA. Translation: BAH13129.1.
AL590487 Genomic DNA. Translation: CAI12651.1.
CH471121 Genomic DNA. Translation: EAW53586.1.
CH471121 Genomic DNA. Translation: EAW53587.1.
BC020622 mRNA. Translation: AAH20622.1.
BC072681 mRNA. Translation: AAH72681.1.
AL122102 mRNA. Translation: CAB59268.1.
CCDSiCCDS72903.1. [Q6GQQ9-1]
PIRiT34535.
RefSeqiNP_064590.2. NM_020205.3. [Q6GQQ9-1]
XP_006711524.1. XM_006711461.1. [Q6GQQ9-1]
XP_006711525.1. XM_006711462.1. [Q6GQQ9-1]
XP_006711526.1. XM_006711463.1. [Q6GQQ9-1]
UniGeneiHs.98322.

Genome annotation databases

EnsembliENST00000581312; ENSP00000462729; ENSG00000264522. [Q6GQQ9-1]
GeneIDi56957.
KEGGihsa:56957.
UCSCiuc001etn.3. human. [Q6GQQ9-1]

Polymorphism databases

DMDMi51701318.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ293573 mRNA. Translation: CAB97494.1 . Different initiation.
AK299790 mRNA. Translation: BAH13129.1 .
AL590487 Genomic DNA. Translation: CAI12651.1 .
CH471121 Genomic DNA. Translation: EAW53586.1 .
CH471121 Genomic DNA. Translation: EAW53587.1 .
BC020622 mRNA. Translation: AAH20622.1 .
BC072681 mRNA. Translation: AAH72681.1 .
AL122102 mRNA. Translation: CAB59268.1 .
CCDSi CCDS72903.1. [Q6GQQ9-1 ]
PIRi T34535.
RefSeqi NP_064590.2. NM_020205.3. [Q6GQQ9-1 ]
XP_006711524.1. XM_006711461.1. [Q6GQQ9-1 ]
XP_006711525.1. XM_006711462.1. [Q6GQQ9-1 ]
XP_006711526.1. XM_006711463.1. [Q6GQQ9-1 ]
UniGenei Hs.98322.

3D structure databases

ProteinModelPortali Q6GQQ9.
SMRi Q6GQQ9. Positions 1-61, 147-395.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121281. 13 interactions.
DIPi DIP-33805N.
IntActi Q6GQQ9. 13 interactions.
STRINGi 9606.ENSP00000358131.

Protein family/group databases

MEROPSi C64.001.

PTM databases

PhosphoSitei Q6GQQ9.

Polymorphism databases

DMDMi 51701318.

Proteomic databases

MaxQBi Q6GQQ9.
PaxDbi Q6GQQ9.
PRIDEi Q6GQQ9.

Protocols and materials databases

DNASUi 56957.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000581312 ; ENSP00000462729 ; ENSG00000264522 . [Q6GQQ9-1 ]
GeneIDi 56957.
KEGGi hsa:56957.
UCSCi uc001etn.3. human. [Q6GQQ9-1 ]

Organism-specific databases

CTDi 56957.
GeneCardsi GC01M149912.
HGNCi HGNC:16683. OTUD7B.
HPAi HPA027045.
MIMi 611748. gene.
neXtProti NX_Q6GQQ9.
PharmGKBi PA134873802.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG282016.
GeneTreei ENSGT00530000062989.
HOGENOMi HOG000048103.
HOVERGENi HBG050904.
InParanoidi Q6GQQ9.
KOi K11860.
OMAi YATFPRQ.
OrthoDBi EOG7JHM57.
PhylomeDBi Q6GQQ9.
TreeFami TF323312.

Enzyme and pathway databases

SignaLinki Q6GQQ9.

Miscellaneous databases

ChiTaRSi OTUD7B. human.
GeneWikii OTUD7B.
GenomeRNAii 56957.
NextBioi 35479876.
PROi Q6GQQ9.
SOURCEi Search...

Gene expression databases

Bgeei Q6GQQ9.
CleanExi HS_OTUD7B.
ExpressionAtlasi Q6GQQ9. differential.
Genevestigatori Q6GQQ9.

Family and domain databases

InterProi IPR003323. OTU.
IPR002653. Znf_A20.
[Graphical view ]
Pfami PF02338. OTU. 1 hit.
[Graphical view ]
PROSITEi PS50802. OTU. 1 hit.
PS51036. ZF_A20. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of two novel A20-like proteins."
    Evans P.C., Taylor E.R., Coadwell J., Heyninck K., Beyaert R., Kilshaw P.J.
    Biochem. J. 357:617-623(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH TRAF6.
    Tissue: Lymphocyte.
  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 2).
    Tissue: Brain.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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].
    Tissue: Eye and Prostate.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 437-843.
    Tissue: Testis.
  7. Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-194.
  8. "Zinc-finger protein A20, a regulator of inflammation and cell survival, has de-ubiquitinating activity."
    Evans P.C., Ovaa H., Hamon M., Kilshaw P.J., Hamm S., Bauer S., Ploegh H.L., Smith T.S.
    Biochem. J. 378:727-734(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-194.
  9. "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.
  10. "NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling."
    Enesa K., Zakkar M., Chaudhury H., Luong le A., Rawlinson L., Mason J.C., Haskard D.O., Dean J.L., Evans P.C.
    J. Biol. Chem. 283:7036-7045(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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].
  14. "Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne."
    Bremm A., Freund S.M., Komander D.
    Nat. Struct. Mol. Biol. 17:939-947(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "DJ-1 enhances cell survival through the binding of cezanne, a negative regulator of NF-{kappa}B."
    McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A., Mak T.W., Ting J.P.
    J. Biol. Chem. 286:4098-4106(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH PARK7.
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "A global survey of CRM1-dependent nuclear export sequences in the human deubiquitinase family."
    Garcia-Santisteban I., Banuelos S., Rodriguez J.A.
    Biochem. J. 441:209-217(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  20. Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH EGFR; ITCH AND NEDD4, MUTAGENESIS OF CYS-194; PHE-809 AND TYR-810.
  21. "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.

Entry informationi

Entry nameiOTU7B_HUMAN
AccessioniPrimary (citable) accession number: Q6GQQ9
Secondary accession number(s): B7Z643
, D3DUZ8, Q5SZ60, Q8WWA7, Q9NQ53, Q9UFF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 19, 2004
Last modified: October 29, 2014
This is version 114 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3