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 Q8R5H1

Entry ID Method Resolution Chain Position Source
AF-Q8R5H1-F1 Predicted AlphaFoldDB

33 variants for Q8R5H1

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389126451 40 Q>L No EVA
rs3389140768 55 M>T No EVA
rs3389126454 58 Q>P No EVA
rs3389131893 59 N>I No EVA
rs3389139899 115 R>G No EVA
rs1134168249 116 K>R No EVA
rs3389102084 141 N>T No EVA
rs3389131949 142 G>R No EVA
rs3389131980 199 Q>H No EVA
rs3389128322 263 Y>F No EVA
rs3389122841 330 N>D No EVA
rs3389130047 342 Y>* No EVA
rs3389126472 349 M>I No EVA
rs3389126465 448 C>Y No EVA
rs3389107403 471 K>T No EVA
rs3389107528 474 R>C No EVA
rs3389095119 482 R>* No EVA
rs3389132738 543 I>S No EVA
rs3389126464 553 E>G No EVA
rs3389126464 553 E>V No EVA
rs251191698 559 A>T No EVA
rs3389135526 597 I>L No EVA
rs3389132654 634 C>Y No EVA
rs3389071099 659 D>Y No EVA
rs3389095037 672 P>H No EVA
rs3389126429 758 K>N No EVA
rs3389126475 810 P>T No EVA
rs3389126462 854 F>I No EVA
rs3389135443 878 I>N No EVA
rs3389139930 903 K>* No EVA
rs3389132733 936 F>L No EVA
rs3389128116 958 P>A No EVA
rs3389128116 958 P>S No EVA

No associated diseases with Q8R5H1

7 regional properties for Q8R5H1

Type Name Position InterPro Accession
domain Peptidase C19, ubiquitin carboxyl-terminal hydrolase 289 - 930 IPR001394
domain Peptidase C19, ubiquitin-specific peptidase, DUSP domain 7 - 121 IPR006615
conserved_site Ubiquitin specific protease, conserved site 290 - 305 IPR018200-1
conserved_site Ubiquitin specific protease, conserved site 875 - 892 IPR018200-2
domain Ubiquitin-like domain, USP-type 136 - 222 IPR028135
domain Ubiquitin specific protease domain 289 - 933 IPR028889
domain Ubiquitin carboxyl-terminal hydrolase, C-terminal 472 - 600 IPR029346

Functions

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

6 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
nuclear body Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
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.

7 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.
cysteine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-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.
identical protein binding Binding to an identical protein or proteins.
Lys48-specific deubiquitinase activity Hydrolysis of Lys48-linked ubiquitin unit(s) from a ubiquitinated protein.
SMAD binding Binding to a SMAD signaling protein.
transforming growth factor beta receptor binding Binding to a transforming growth factor beta receptor.
ubiquitin modification-dependent histone binding Binding to a histone protein in which a residue has been modified by ubiquitination.

10 GO annotations of biological process

Name Definition
BMP signaling pathway The series of molecular signals initiated by the binding of a member of the BMP (bone morphogenetic protein) family to a receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription.
histone H2B conserved C-terminal lysine deubiquitination A histone deubiquitination process in which a ubiquitin monomer is removed from a conserved lysine residue in the C-terminus of histone H2B. The conserved lysine residue is K119 in fission yeast, K123 in budding yeast, or K120 in mammals.
monoubiquitinated protein deubiquitination The removal of the ubiquitin group from a monoubiquitinated protein.
negative regulation of antifungal innate immune response Any process that stops, prevents or reduces the frequency, rate or extent of an antifungal innate immune response.
pathway-restricted SMAD protein phosphorylation The process of introducing a phosphate group on to a pathway restricted SMAD protein. A pathway restricted SMAD protein is an effector protein that acts directly downstream of the transforming growth factor family receptor.
positive regulation of RIG-I signaling pathway Any process that activates or increases the frequency, rate or extent of RIG-I signaling pathway.
protein deubiquitination The removal of one or more ubiquitin groups from a protein.
protein K27-linked deubiquitination A protein deubiquitination process in which a K27-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 27 of the ubiquitin monomers, is removed from a protein.
transforming growth factor beta receptor signaling pathway The series of molecular signals initiated by an extracellular ligand binding to a transforming growth factor beta receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription.
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 a ubiquitin group, or multiple ubiquitin groups, to the protein.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9Y2K6 USP20 Ubiquitin carboxyl-terminal hydrolase 20 Homo sapiens (Human) PR
P51784 USP11 Ubiquitin carboxyl-terminal hydrolase 11 Homo sapiens (Human) PR
Q8R5K2 Usp33 Ubiquitin carboxyl-terminal hydrolase 33 Mus musculus (Mouse) PR
Q80U87 Usp8 Ubiquitin carboxyl-terminal hydrolase 8 Mus musculus (Mouse) PR
O88623 Usp2 Ubiquitin carboxyl-terminal hydrolase 2 Mus musculus (Mouse) PR
Q8K387 Usp45 Ubiquitin carboxyl-terminal hydrolase 45 Mus musculus (Mouse) PR
Q3TIX9 Usp39 U4/U6.U5 tri-snRNP-associated protein 2 Mus musculus (Mouse) PR
Q9SX68 RPL18 50S ribosomal protein L18, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
F6Z5C0 usp15 Ubiquitin carboxyl-terminal hydrolase 15 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW DKYQMGDQNV
70 80 90 100 110 120
YPGPIDNSGL LKDGDAQSLK EHLIDELDYI LLPTEGWNKL VSWYTLMEGQ EPIARKVVEQ
130 140 150 160 170 180
GMFVKHCKVE VYLTELKLCE NGNMNNVVTR RFSKADTIDT IEKEIRKIFN IPDEKEARLW
190 200 210 220 230 240
NKYMSNTFEP LNKPDSTIQD AGLYQGQVLV IEQKNEDGTW PRGPSTPKSP GASNFSTLPK
250 260 270 280 290 300
ISPSSLSNNY NNINNRNVKN SNYCLPSYTA YKNYDYSEPG RNNEQPGLCG LSNLGNTCFM
310 320 330 340 350 360
NSAIQCLSNT PPLTEYFLND KYQEELNFDN PLGMRGEIAK SYAELIKQMW SGKFSYVTPR
370 380 390 400 410 420
AFKTQVGRFA PQFSGYQQQD CQELLAFLLD GLHEDLNRIR KKPYIQLKDA DGRPDKVVAE
430 440 450 460 470 480
EAWENHLKRN DSIIVDIFHG LFKSTLVCPE CAKISVTFDP FCYLTLPLPM KKERSLEVYL
490 500 510 520 530 540
VRMDPLAKPM QYKVIVPKIG NILDLCTALS ALSGVPADKM IVTDIYNHRF HRIFAVDENL
550 560 570 580 590 600
SSIMERDDIY VFEININRAE DTEHVVIPVC LREKFRHSSY THHTGSSLFG QPFLMAIPRN
610 620 630 640 650 660
NTEDKLYNLL LLRMCRYVKM STETEETDGH LRCCEDQNIN GNGPNGLHEE GSPSEMETDE
670 680 690 700 710 720
PDDESSQDQE LPSENENSQS EDSVGGDNDS ENGLCTEETC KGQLTGHKKR LFTFQFNNLG
730 740 750 760 770 780
NNDINYIKDD TSHIRFDDRQ LRLDERSFLA LDWDPDLKKR YFDENAAEDF EKHESVEYKP
790 800 810 820 830 840
PKRPFVKLKD CIELFTTKEK LGAEDPWYCP NCKEHQQATK KLDLWSLPPV LVVHLKRFSY
850 860 870 880 890 900
SRYMRDKLDT LVDFPISDLD MSEFLINPNA GPCRYNLIAV SNHYGGMGGG HYTAFAKNKD
910 920 930 940 950 960
DGKWYYFDDS SVSTASEDQI VSKAAYVLFY QRQDTFSGTG FFPLDRETKG ASAATGIPLE
970 980
SDEDSNDNDN DLENENCMHT N