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 Q6A4J8

Entry ID Method Resolution Chain Position Source
AF-Q6A4J8-F1 Predicted AlphaFoldDB

No variants for Q6A4J8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6A4J8

No associated diseases with Q6A4J8

2 regional properties for Q6A4J8

Type Name Position InterPro Accession
domain Protein kinase domain 123 - 456 IPR000719
active_site Serine/threonine-protein kinase, active site 244 - 256 IPR008271

Functions

Description
EC Number 3.4.19.12 Omega peptidases
Subcellular Localization
  • Nucleus
  • Cytoplasm
  • Nucleus, PML body
  • Chromosome
  • Present in a minority of ND10 nuclear bodies
  • Association with ICP0/VMW110 at early times of infection leads to an increased proportion of USP7-containing ND10
  • Colocalizes with ATXN1 in the nucleus
  • Colocalized with DAXX in speckled structures
  • Colocalized with PML and PTEN in promyelocytic leukemia protein (PML) nuclear bodies
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.
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.
PML body A class of nuclear body; they react against SP100 auto-antibodies (PML, promyelocytic leukemia); cells typically contain 10-30 PML bodies per nucleus; alterations in the localization of PML bodies occurs after viral infection.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
XY body A structure found in a male mammalian spermatocyte containing an unpaired X chromosome that has become densely heterochromatic, silenced and localized at the nuclear periphery.

8 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.
deubiquitinase activity An isopeptidase activity that cleaves ubiquitin from a target protein to which it is conjugated.
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.
p53 binding Binding to one of the p53 family of proteins.
protein C-terminus binding Binding to a protein C-terminus, the end of a peptide chain at which the 1-carboxyl function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
ubiquitin protein ligase binding Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.

18 GO annotations of biological process

Name Definition
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.
maintenance of DNA methylation Any process involved in maintaining the methylation state of a nucleotide sequence.
monoubiquitinated protein deubiquitination The removal of the ubiquitin group from a monoubiquitinated protein.
negative regulation of NF-kappaB transcription factor activity Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the transcription factor NF-kappaB.
negative regulation of proteasomal ubiquitin-dependent protein catabolic process Any process that stops, prevents, or reduces the frequency, rate or extent of 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.
positive regulation of apoptotic process Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
positive regulation of DNA demethylation Any process that activates or increases the frequency, rate or extent of DNA demethylation.
protein deubiquitination The removal of one or more ubiquitin groups 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.
protein stabilization Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
regulation of circadian rhythm Any process that modulates the frequency, rate or extent of a circadian rhythm. A circadian rhythm is a biological process in an organism that recurs with a regularity of approximately 24 hours.
regulation of DNA-binding transcription factor activity Any process that modulates the frequency, rate or extent of the activity of a transcription factor, any factor involved in the initiation or regulation of transcription.
regulation of gluconeogenesis Any process that modulates the frequency, rate or extent of gluconeogenesis, the formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.
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 retrograde transport, endosome to Golgi Any process that modulates the frequency, rate or extent of retrograde transport, endosome to Golgi.
rhythmic process Any process pertinent to the generation and maintenance of rhythms in the physiology of an organism.
transcription-coupled nucleotide-excision repair The nucleotide-excision repair process that carries out preferential repair of DNA lesions on the actively transcribed strand of the DNA duplex. In addition, the transcription-coupled nucleotide-excision repair pathway is required for the recognition and repair of a small subset of lesions that are not recognized by the global genome nucleotide excision repair pathway.
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.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P50101 UBP15 Ubiquitin carboxyl-terminal hydrolase 15 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9UHP3 USP25 Ubiquitin carboxyl-terminal hydrolase 25 Homo sapiens (Human) EV
Q93009 USP7 Ubiquitin carboxyl-terminal hydrolase 7 Homo sapiens (Human) PR
P57080 Usp25 Ubiquitin carboxyl-terminal hydrolase 25 Mus musculus (Mouse) SS
P56399 Usp5 Ubiquitin carboxyl-terminal hydrolase 5 Mus musculus (Mouse) PR
10 20 30 40 50 60
MNHQQQQQQQ QKAGEQQLSE PEDMEMEAGD TDDPPRITQN PVINGNVTLS DGHSNAEEDM
70 80 90 100 110 120
EDDTSWRSEA TFQFTVERFS RLSESVLSPP CFVRNLPWKI MVMPRFYPDR PHQKSVGFFL
130 140 150 160 170 180
QCNAESDSTS WSCHAQAVLK IINYRDDDKS FSRRISHLFF HEENDWGFSN FMAWSEVTDP
190 200 210 220 230 240
EKGFIDDDKV TFEVFVQADA PHGVAWDSKK HTGYVGLKNQ GATCYMNSLL QTLFFTNQLR
250 260 270 280 290 300
KAVYMMPTEG DDSSKSVPLA LQRVFYELQH SDKPVGTKKL TKSFGWETLD SFMQHDVQEL
310 320 330 340 350 360
CRVLLDNVEN KMKGTCVEGT IPKLFRGKMV SYIQCKDVDY RSDRREDYYD IQLSIKGKKN
370 380 390 400 410 420
IFESFVDYVA VEQLDGDNKY DAGEHGLQEA EKGVKFLTLP PVLHLQLMRF MYDPQTDQNI
430 440 450 460 470 480
KINDRFEFPE QLPLDEFLQK TDPKDPANYI LHAVLVHSGD NHGGHYVVYL NPKGDGKWCK
490 500 510 520 530 540
FDDDVVSRCT KEEAIEHNYG GHDDDLSVRH CTNAYMLVYI RESKLSEVLQ AVTDHDIPQQ
550 560 570 580 590 600
LVERLQEEKR IEAQKRKERQ EAHLYMQVQI VAEDQFCGHQ GNDMYDEEKV RYTVFKVLKN
610 620 630 640 650 660
SSLAEFVQSL SQTMGFPQDQ IRLWPMQARS NGTKRPAMLD NEADGNKTMI ELSDNENPWT
670 680 690 700 710 720
IFLETVDPEL AASGATLPKF DKDHDVMLFL KMYDPKTRSL NYCGHIYTPI SCKIRDLLPV
730 740 750 760 770 780
MCDRAGFIQD TSLILYEEVK PNLTERIQDY DVSLDKALDE LMDGDIIVFQ KDDPENDNSE
790 800 810 820 830 840
LPTAKEYFRD LYHRVDVIFC DKTIPNDPGF VVTLSNRMNY FQVAKTVAQR LNTDPMLLQF
850 860 870 880 890 900
FKSQGYRDGP GNPLRHNYEG TLRDLLQFFK PRQPKKLYYQ QLKMKITDFE NRRSFKCIWL
910 920 930 940 950 960
NSQFREEEIT LYPDKHGCVR DLLEECKKAV ELGDKASGRL RLLEIVSYKI IGVHQEDELL
970 980 990 1000 1010 1020
ECLSPATSRT FRIEEIPLDQ VDIDKENEML ITVAHFHKEV FGTFGIPFLL RIHQGEHFRE
1030 1040 1050 1060 1070 1080
VMKRIQSLLD IQEKEFEKFK FAIVMMGRHQ YINEDEYEVN LKDFEPQPGN MSHPRPWLGL
1090 1100
DHFNKAPKRS RYTYLEKAIK IHN