Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q3U2S4

Entry ID Method Resolution Chain Position Source
AF-Q3U2S4-F1 Predicted AlphaFoldDB

25 variants for Q3U2S4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3409644573 71 L>R No EVA
rs3389544750 155 A>V No EVA
rs3408437448 187 R>P No EVA
rs3389562594 255 A>D No EVA
rs3389551481 289 A>P No EVA
rs3389544677 291 M>V No EVA
rs3389554982 317 D>N No EVA
rs3389552798 351 K>* No EVA
rs3389566942 353 G>R No EVA
rs3389459678 374 Q>K No EVA
rs3389518142 374 Q>R No EVA
rs3409332927 389 T>S No EVA
rs3413064415 390 N>I No EVA
rs3407474740 390 N>Y No EVA
rs3409332930 391 E>V No EVA
rs3389531312 401 S>C No EVA
rs3409460768 446 R>W No EVA
rs3389551416 447 S>F No EVA
rs3389546685 494 F>Y No EVA
rs3389566909 505 L>R No EVA
rs3409600992 528 L>Q No EVA
rs3389543911 545 Q>P No EVA
rs3389551478 547 E>K No EVA
rs3389546681 549 L>I No EVA
rs3389459646 553 K>M No EVA

No associated diseases with Q3U2S4

1 regional properties for Q3U2S4

Type Name Position InterPro Accession
domain OTU domain 213 - 336 IPR003323

Functions

Description
EC Number 3.4.19.12 Omega peptidases
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
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.

4 GO annotations of molecular function

Name Definition
cysteine-type deubiquitinase activity An thiol-dependent isopeptidase activity that cleaves ubiquitin from a target protein to which it is conjugated.
deubiquitinase activity An isopeptidase activity that cleaves ubiquitin from a target protein to which it is conjugated.
Lys48-specific deubiquitinase activity Hydrolysis of Lys48-linked ubiquitin unit(s) from a ubiquitinated protein.
Lys63-specific deubiquitinase activity Hydrolysis of Lys63-Linked ubiquitin unit(s) from a ubiquitinated protein.

14 GO annotations of biological process

Name Definition
CD8-positive, alpha-beta T cell differentiation The process in which a relatively unspecialized T cell acquires specialized features of a mature CD8-positive, alpha-beta T cell.
negative regulation of canonical Wnt signaling pathway Any process that decreases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes.
negative regulation of interleukin-17 production Any process that stops, prevents, or reduces the frequency, rate, or extent of production of any member of the interleukin-17 family of cytokines.
neural crest cell differentiation The process in which a relatively unspecialized cell acquires specialized features of a neural crest cell.
positive regulation of TORC1 signaling Any process that activates or increases the frequency, rate or extent of TORC1 signaling.
positive regulation of TORC2 signaling Any process that activates or increases the frequency, rate or extent of TORC2 signaling.
proteasome-mediated ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
protein deubiquitination The removal of one or more ubiquitin groups 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.
regulation of protein stability Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
regulation of T-helper 17 type immune response Any process that modulates the frequency, rate or extent of T-helper 17 type immune response.
response to lipopolysaccharide Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipopolysaccharide stimulus; lipopolysaccharide is a major component of the cell wall of gram-negative bacteria.
T-helper 17 cell lineage commitment The process in which a CD4-positive, alpha-beta T cell becomes committed to becoming a T-helper 17 cell, a CD4-positive, alpha-beta T cell with the phenotype RORgamma-t-positive that produces IL-17.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q96G74 OTUD5 OTU domain-containing protein 5 Homo sapiens (Human) PR
10 20 30 40 50 60
MTILPKKKPP PPDADPANEP PPPGPLPPAP RRGAGVGVGG GGTGVGGGER DRDSGVVGAR
70 80 90 100 110 120
PRASPPPQGP LPGPPGALHR WALAVPPGAV AGPRPQQASP PPCGGPGGPG GGPGDALGAT
130 140 150 160 170 180
TAGVGAAGVV VGVGGTVGVG GCCSGPGHSK RRRQAPGVGA VGGASPEREE 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
YSTEPINTFH GIHQNEDEPI RVSYHRNIHY NSVVNPNKAT IGVGLGLPSF KPGFAEQSLM
370 380 390 400 410 420
KNAIKTSEES WIEQQMLEDK KRATDWEATN EAIEEQVARE SYLQWLRDQE KQARQVRGPS
430 440 450 460 470 480
QPRKASATCS SATAAASSGL EEWTSRSPRQ RSSASSPEHP ELHAELGIKP PSPGTVLALA
490 500 510 520 530 540
KPPSPCAPGT SSQFSAGGDR ATSPLVSLYP ALECRALIQQ MSPSAFGLND WDDDEILASV
550 560
LAVSQQEYLD SMKKNKVHRE PPPDKS