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

0 structures for Q5UQR3

Entry ID Method Resolution Chain Position Source

No variants for Q5UQR3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5UQR3

No associated diseases with Q5UQR3

4 regional properties for Q5UQR3

Type Name Position InterPro Accession
domain Peptidase C19, ubiquitin carboxyl-terminal hydrolase 42 - 459 IPR001394
conserved_site Ubiquitin specific protease, conserved site 43 - 58 IPR018200-1
conserved_site Ubiquitin specific protease, conserved site 404 - 421 IPR018200-2
domain Ubiquitin specific protease domain 42 - 462 IPR028889

Functions

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

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

1 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.

2 GO annotations of biological process

Name Definition
protein deubiquitination The removal of one or more ubiquitin groups from a protein.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MQNMMNTSQS FQNDSVLIGD KNTLQSINKS VDNGSKNTHG ITGIMNLGNT CYMNSALQAL
70 80 90 100 110 120
SHNYLLINYL FMNKKQIIRT LLTNARKIFK DCDNFKIEST ISPIPLELRK KIQSENYHLS
130 140 150 160 170 180
MLTVEDVNIL LNNTITAQII RLFECMWKNN CVVVPTSFRK VFGEVRDKFF FGYEQHDAEE
190 200 210 220 230 240
AYSCIIQKMQ EELAEKRTIR FKTTRHSVGE YIKYMNDVKE KVSCLPNGKE KDIVMNKFKQ
250 260 270 280 290 300
IKKQMPRESL TAESFREMKK YYEQGYSYIT EIFSGYVHSS ICCPNTSCGF TNDRFDAFTH
310 320 330 340 350 360
LSLSIPVKNM YEQLNVYDCL REYFSQETLD ADNLWNCEGC HEKVQAIKKT KLWTTPYVLV
370 380 390 400 410 420
IQFKRFGMTR IAKDNRFINY PMDELDVSSV ICSQQFEDSV QTKYKLQCVI NHHGGLNNGH
430 440 450 460
YFTYSKIENT GEWYEFNDTY TGKVTDNHIV NQNAYILFYI RSDLFRSQ