Descriptions

Deubiquitinating enzymes of the ovarian tumour (OTU) family regulate cellular signalling by targeting distinct linkage types within polyubiquitin. OTUD7B regulates inflammation and NK-kB signaling, T-cell activation, and EGFR trafficking. OTUD7B is autoinhibited by the Cys-loop (187-193) that occupies the channel that binds the C-terminal tail of distal ubiquitin.

Autoinhibitory domains (AIDs)

Target domain

183-365 (OTU domain)

Relief mechanism

Ligand binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for B2RUR8

Entry ID Method Resolution Chain Position Source
AF-B2RUR8-F1 Predicted AlphaFoldDB

7 variants for B2RUR8

Variant ID(s) Position Change Description Diseaes Association Provenance
rs33170355 51 N>S No Ensembl
rs252983493 176 M>L No Ensembl
rs222051347 179 T>P No Ensembl
rs260727626 478 G>S No Ensembl
rs221086198 587 S>N No Ensembl
rs1134803502 666 K>Q No Ensembl
rs240449752 684 P>S No Ensembl

No associated diseases with B2RUR8

2 regional properties for B2RUR8

Type Name Position InterPro Accession
domain Zinc finger, A20-type 793 - 828 IPR002653
domain OTU domain 183 - 365 IPR003323

Functions

Description
EC Number 3.4.19.12 Omega peptidases
Subcellular Localization
  • Cytoplasm
  • Nucleus
  • Shuttles be cytoplasm and the nucleus in a XPO1/CRM1-dependent manner
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

6 GO annotations of molecular function

Name Definition
cysteine-type peptidase activity Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
K63-linked polyubiquitin modification-dependent protein binding Binding to a protein upon poly-ubiquitination formed by linkages between lysine residues at position 63 in the target protein.
Lys48-specific deubiquitinase activity Hydrolysis of Lys48-linked ubiquitin unit(s) from a ubiquitinated protein.
thiol-dependent deubiquitinase An thiol-dependent isopeptidase activity that cleaves ubiquitin from a target protein to which it is conjugated.
zinc ion binding Binding to a zinc ion (Zn).

12 GO annotations of biological process

Name Definition
adaptive immune response An immune response mediated by cells expressing specific receptors for antigen produced through a somatic diversification process, and allowing for an enhanced secondary response to subsequent exposures to the same antigen (immunological memory).
in utero embryonic development The process whose specific outcome is the progression of the embryo in the uterus over time, from formation of the zygote in the oviduct, to birth. An example of this process is found in Mus musculus.
mucosal immune response An immune response taking place in mucosal tissues, including those of the intestinal tract, nasal and upper respiratory tract, and genital tract.
negative regulation of I-kappaB kinase/NF-kappaB signaling Any process that stops, prevents, or reduces the frequency, rate or extent of -kappaB kinase/NF-kappaB signaling.
negative regulation of interleukin-8 production Any process that stops, prevents, or reduces the frequency, rate, or extent of interleukin-8 production.
negative regulation of protein localization to nucleus Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to nucleus.
negative regulation of transcription by RNA polymerase II Any process that stops, prevents, or reduces the frequency, rate or extent of transcription mediated by RNA polymerase II.
protein deubiquitination The removal of one or more ubiquitin groups from a protein.
protein deubiquitination involved in ubiquitin-dependent protein catabolic process The removal of one or more ubiquitin groups from a protein as part of a process of ubiquitin-dependent protein catabolism.
protein K11-linked deubiquitination A protein deubiquitination process in which a K11-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 11 of the ubiquitin monomers, is removed from a protein.
protein K48-linked deubiquitination A protein deubiquitination process in which a K48-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 48 of the ubiquitin monomers, is removed from a protein.
protein K63-linked deubiquitination A protein deubiquitination process in which a K63-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is removed from a protein.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P21580 TNFAIP3 Tumor necrosis factor alpha-induced protein 3 Homo sapiens (Human) SS
Q8TE49 OTUD7A OTU domain-containing protein 7A Homo sapiens (Human) SS
Q6GQQ9 OTUD7B OTU domain-containing protein 7B Homo sapiens (Human) EV
Q60769 Tnfaip3 Tumor necrosis factor alpha-induced protein 3 Mus musculus (Mouse) SS
Q8R554 Otud7a OTU domain-containing protein 7A Mus musculus (Mouse) SS
10 20 30 40 50 60
MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDVSAALSD FEQLRQVHAG NLSPPFSGGS
70 80 90 100 110 120
TCPKTPEKGG SDREPTRPSR PILQRQDDVI QEKRLSRGIS HASSSIVSLA RSHVSSNGGG
130 140 150 160 170 180
GGSSEHPLEM PICAFQLPDL TVYKEDFRSF IERDLIEQSM LVALEQAGRL NWWVSMDSTC
190 200 210 220 230 240
QRLLPLATTG DGNCLLHAAS LGMWGFHDRD LVLRKALYAL MEKGVEKEAL RRRWRWQQTQ
250 260 270 280 290 300
QNKESGLVYT EDEWQKEWNE LIKLASSEPR MHLGSNGASG GGVESSEEPV YESLEEFHVF
310 320 330 340 350 360
VLAHVLKRPI VVVADTMLRD SGGEAFAPIP FGGIYLPLEV PASQCHRSPL VLAYDQAHFS
370 380 390 400 410 420
ALVSMEQKES AKEQAVIPLT DSEHKLLPLH FAVDPGKGWE WGKDDNDNVR LASIILSLEV
430 440 450 460 470 480
KLHLLHSYMN VKWIPLSSDS QAPLAQPESP TASAGDEPRS TPESGESDKE SVGSSSLGNE
490 500 510 520 530 540
GSRRKEKSKR DREKDKKRAD SVANKLGSFG KTLGSKLKKN MGGLMHSKGP KPGGLGSGSG
550 560 570 580 590 600
ISSGTETLEK KKKNNTLKSW KGGKEEAAGD GPVSEKPPSE SVGNGGSKYS QEVMQSLSTM
610 620 630 640 650 660
RIAMQGEGKY IFVGTLKMGH RHQYQEEMIQ RYLADAEERF LAEQKQKEVE RKIMNGGLVS
670 680 690 700 710 720
GPPPAKKPEP DGGEDQPSDS PAEPKAMAFS TAYPGGFTIP RPSGGGVHCQ EPRRQLAGGP
730 740 750 760 770 780
CVGGLPSYAT FPRQYPGRPY PHQDNIPALE PGKDGVHRGA LLPPQFRVAD SYSNGYREPP
790 800 810 820 830
EPDGWAGAPR GLPPTQTKCK QPNCSFYGHP ETNNLCSCCY REELRRRERE PGGELLAHRF