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

3 structures for Q7K5N4

Entry ID Method Resolution Chain Position Source
6CGA X-ray 350 A A/C 43-404 PDB
6HGC X-ray 302 A PDB
AF-Q7K5N4-F1 Predicted AlphaFoldDB

No variants for Q7K5N4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7K5N4

No associated diseases with Q7K5N4

2 regional properties for Q7K5N4

Type Name Position InterPro Accession
domain Peptidase C12, ubiquitin carboxyl-terminal hydrolase 44 - 277 IPR001578
domain Peptidase C12, C-terminal domain 348 - 393 IPR041507

Functions

Description
EC Number 3.4.19.12 Omega peptidases
Subcellular Localization
  • Nucleus
  • Localizes to PcG response elements (PREs)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
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.
PR-DUB complex A multimeric protein complex that removes monoubiquitin from histone H2A. In Drosophila and mammals, the core of the complex is composed of Calypso/BAP1 and Asx/ASXL1, respectively.

2 GO annotations of molecular function

Name Definition
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
cysteine-type deubiquitinase activity An thiol-dependent isopeptidase activity that cleaves ubiquitin from a target protein to which it is conjugated.

5 GO annotations of biological process

Name Definition
heterochromatin assembly An epigenetic gene silencing mechanism in which chromatin is compacted into heterochromatin, resulting in a chromatin conformation refractory to transcription. This process starts with heterochromatin nucleation, its spreading, and ends with heterochromatin boundary formation.
monoubiquitinated histone H2A deubiquitination The removal of the ubiquitin group from a monoubiquitinated histone H2A protein.
protein deubiquitination The removal of one or more ubiquitin groups from a protein.
specification of segmental identity, abdomen The specification of the characteristic structures of the abdominal segments following establishment of segment boundaries. Identity is considered to be the aggregate of characteristics by which a structure is recognized.
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.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9XSJ0 UCHL5 Ubiquitin carboxyl-terminal hydrolase isozyme L5 Bos taurus (Bovine) PR
Q9Y5K5 UCHL5 Ubiquitin carboxyl-terminal hydrolase isozyme L5 Homo sapiens (Human) PR
Q9WUP7 Uchl5 Ubiquitin carboxyl-terminal hydrolase isozyme L5 Mus musculus (Mouse) PR
Q06AT3 UCHL5 Ubiquitin carboxyl-terminal hydrolase isozyme L5 Sus scrofa (Pig) PR
10 20 30 40 50 60
MNAAGGGSGA QAAAVAAGNN SLSHNALLST ASGATTMPMA QLADGWLELE SDPGLFTLLL
70 80 90 100 110 120
KDFGCHDVQV EEVYDLQKPI ESPYGFIFLF RWIEERRARR KIVETTAEIF VKDEEAISSI
130 140 150 160 170 180
FFAQQVVPNS CATHALLSVL LNCNENNLQL GDTLSRLKTH TKGMSPENKG LAIGNTPELA
190 200 210 220 230 240
CAHNSHAMPQ ARRRLERTGA GVSSCRFTGE AFHFVSFVPI NGQLFELDGL KPYPMNHGGW
250 260 270 280 290 300
EDSEDWTDKF RRVMAERLGI ATGEQDIRFN LMAVVPDRRI AITHKLKMLR TNQAIVSGTL
310 320 330 340 350 360
QKLLKADEQG ESGNGDSQRP DTPTTLLEPS AFTARDLQSL LKNLDTEIAI NEQHLADEND
370 380 390 400 410 420
RRHMFKVDAS RRTHNYDKFI CTFLSMLAHQ GVLGELVSQH LLPSKKVSGQ GAANRISKQS
430 440 450 460 470
TTASAGGSTA AGTASTPKTQ QQQAAAAKNG KSPSKTPGRR RKGRNKCRKR K