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 B4JW98

Entry ID Method Resolution Chain Position Source
AF-B4JW98-F1 Predicted AlphaFoldDB

No variants for B4JW98

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B4JW98

No associated diseases with B4JW98

15 regional properties for B4JW98

Type Name Position InterPro Accession
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 203 - 387 IPR005479-1
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 738 - 801 IPR005479-2
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 828 - 961 IPR005479-3
domain Carbamoyl-phosphate synthetase, large subunit oligomerisation domain 480 - 602 IPR005480
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 631 - 645 IPR005483-1
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 660 - 670 IPR005483-2
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 778 - 790 IPR005483-3
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 835 - 854 IPR005483-4
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 869 - 886 IPR005483-5
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 924 - 953 IPR005483-6
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 1003 - 1021 IPR005483-7
domain Methylglyoxal synthase-like domain 1027 - 1163 IPR011607
domain ATP-grasp fold 185 - 381 IPR011761-1
domain ATP-grasp fold 743 - 955 IPR011761-2
domain Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain 1033 - 1134 IPR033937

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

2 GO annotations of cellular component

Name Definition
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
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.

4 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.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSVAGGSIST AAGNAGKNNA LPMAQLADGW LELESDPGLF TLLLEDFGCH DVQVEEVYDL
70 80 90 100 110 120
QKPIESPYGF IFLFRWIEER RARRKIVETT AEIFVKDEEA ISSIFFAQQV VPNSCATHAL
130 140 150 160 170 180
LSVLLNCNEN NLQLGETLGR LKAHTKGMSP ENKGLAIGNT PELACAHNSH AMPQARRRLE
190 200 210 220 230 240
RTGAGVASCR FTGEAFHFVS FVPINGQLFE LDGLKPYPMN HGCWEEHEDW TDKFRRVMAE
250 260 270 280 290 300
RLGIATGEQD IRFNLMAVVP DRRIAITHKL KMLRTNQAIV SGTLQKLLKA DEQGERDEQQ
310 320 330 340 350 360
RPDTPTTLLE PSAFTARDLQ SLLKNLDTEI AINEQHLADE NDRRQMFKVD ASRRTHNYDK
370 380 390 400 410 420
FICTFLSMLA HQGVLGELVS QHLLPSKKIA NRLNRQTNAA TAAANAANTN VAGTNAAGSK
430 440 450 460
SQQQQQQTQQ QPQQTQTAKN GKSPGKTPGR RRKGRNKCRK RK