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 Q12021

Entry ID Method Resolution Chain Position Source
AF-Q12021-F1 Predicted AlphaFoldDB

14 variants for Q12021

Variant ID(s) Position Change Description Diseaes Association Provenance
s04-503246 9 V>L No SGRP
s04-503209 21 T>S No SGRP
s04-503111 54 T>A No SGRP
s04-502925 116 D>N No SGRP
s04-502897 125 Y>S No SGRP
s04-502874 133 N>D No SGRP
s04-502864 136 N>S No SGRP
s04-502723 183 S>F No SGRP
s04-502475 266 I>V No SGRP
s04-502412 287 Q>K No SGRP
s04-502274 333 R>G No SGRP
s04-502094 393 L>M No SGRP
s04-501959 438 V>I No SGRP
s04-501914 453 E>K No SGRP

No associated diseases with Q12021

7 regional properties for Q12021

Type Name Position InterPro Accession
repeat WD40 repeat 52 - 85 IPR001680-1
repeat WD40 repeat 184 - 233 IPR001680-2
repeat WD40 repeat 280 - 316 IPR001680-3
repeat WD40 repeat 352 - 387 IPR001680-4
repeat G-protein beta WD-40 repeat 72 - 86 IPR020472-1
repeat G-protein beta WD-40 repeat 211 - 225 IPR020472-2
repeat G-protein beta WD-40 repeat 303 - 317 IPR020472-3

Functions

Description
EC Number
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
Cul4A-RING E3 ubiquitin ligase complex A ubiquitin ligase complex in which a cullin from the Cul4A subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein.
nucleotide-excision repair complex Any complex formed of proteins that act in nucleotide-excision repair.
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.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

4 GO annotations of biological process

Name Definition
DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
proteasome-mediated 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 ubiquitin, and mediated by the proteasome.
protein polyubiquitination Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDPFLEFRVG NISLNEFYRR TIQSEFERIL EDPLSNMKNY RFSKQSNYST KEKTPLSIGV
70 80 90 100 110 120
NCLDIDDTGQ VLLGGGDDGS LSIWGLDESL HRNDEGEQEL INKRLNYIKR QPHQSDDEPA
130 140 150 160 170 180
QIMGYKNKRT RINDNNTMRL VHSFQTQRNK YRMYRQSSAA VPVQRSHISN KTDSPIGFSE
190 200 210 220 230 240
TLSETDSEAS ISHHKYGITT LKWYKADNGM FFTGSNDKTV KIWDTNRFEA VQDINLGYKI
250 260 270 280 290 300
NQIDNNVVDD SSLLVVASED YYPRLIDLRT MNSGVTALGM GNQTRMQSEI LCCKFNPVRE
310 320 330 340 350 360
QIIACGDMEG GVKLWDLRMR NRLYSELKRN KNRFKTINND DNDDQSDVYF SSNQSKAHLR
370 380 390 400 410 420
CCSDIVWNSE GSELCSVGMD GKLNVWRPFT EILQPEGLAS YSQLGTQDLS RIKYKKRVSR
430 440 450 460 470 480
RLLWFDKFLL CITDNGEVEI YNTEEKKLWN KLEYPMVNQV KKNQASHCQF SSMIVQTNIM
490 500
NSVGLKLFFG TNNNTVSDGG SIFECS