Q17392

PR
Gene name
cul-4 (F45E12.3)
Protein name
Cullin-4
Names
CUL-4
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_F45E12.3
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-138 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q17392

Entry ID Method Resolution Chain Position Source
AF-Q17392-F1 Predicted AlphaFoldDB

No variants for Q17392

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q17392

No associated diseases with Q17392

4 regional properties for Q17392

Type Name Position InterPro Accession
domain Cullin, N-terminal 122 - 741 IPR001373
conserved_site Cullin, conserved site 813 - 840 IPR016157
domain Cullin homology domain 474 - 703 IPR016158
domain Cullin protein, neddylation domain 769 - 834 IPR019559

Functions

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

2 GO annotations of cellular component

Name Definition
Cul4-RING E3 ubiquitin ligase complex A ubiquitin ligase complex in which a cullin from the Cul4 family and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein.
cullin-RING ubiquitin ligase complex Any ubiquitin ligase complex in which the catalytic core consists of a member of the cullin family and a RING domain protein; the core is associated with one or more additional proteins that confer substrate specificity.

2 GO annotations of molecular function

Name Definition
protein-macromolecule adaptor activity The binding activity of a protein that brings together two or more macromolecules in contact, permitting those molecules to function in a coordinated way. The adaptor can bring together two proteins, or a protein and another macromolecule such as a lipid or a nucleic acid.
ubiquitin protein ligase binding Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins.

4 GO annotations of biological process

Name Definition
cellular response to DNA damage stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
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 ubiquitination The process in which one or more ubiquitin groups are added to a protein.
SCF-dependent proteasomal 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, with ubiquitin-protein ligation catalyzed by an SCF (Skp1/Cul1/F-box protein) complex, and mediated by the proteasome.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q13619 CUL4A Cullin-4A Homo sapiens (Human) PR
Q13620 CUL4B Cullin-4B Homo sapiens (Human) PR
Q3TCH7 Cul4a Cullin-4A Mus musculus (Mouse) PR
A2A432 Cul4b Cullin-4B Mus musculus (Mouse) PR
P0CH31 At1g43140 Putative cullin-like protein 1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MTSGAPPTIS TEKSRSKQLR KSSKRTASTV EGTEAKQMRG DTENRSDGEM DDVSTSSEIR
70 80 90 100 110 120
HGNGFIENFR SQTGNSSRTT ATNERIKKKL VIKNFKANAN QNDVAMGDTN IDSTDGSVGR
130 140 150 160 170 180
DWAVLSDNVF AILEDRKTVT TLEGLFSKVR SVCDKNQSKV LYDRLVAIVV QFAKSLKESL
190 200 210 220 230 240
NAVEQVPLAE DNCEQYLEKF GQIWQAYPVK INLIRNIFLH LDRIALGATD TEILPLWECF
250 260 270 280 290 300
MQIFQKTFFP NIFKEFKATK LFNALYMAMQ KIMQRYPVDS PLRSLVDMLQ TVHVSEEFAK
310 320 330 340 350 360
FLISQLREHY NNERIDKVPK MNCNDYMEYC EDQINRYSQL VKVNFDEPSA LKDVQATVTN
370 380 390 400 410 420
CLIQQAIPEI LTHDFDDLID SDNISDIGRM FNLCRQCVGG EDEVRTQFSK YLKKRGEKLI
430 440 450 460 470 480
ATCPDEDLVS ELLAFKKKVD FIMTGSFKSA NDPVKMRQCL SDAFESFVNK QVDRSAELIS
490 500 510 520 530 540
KHFHTLLHSS NKNVSDDTTL DQMVDEAIVL FRYLRGKDVF EAYYKRGLAK RLFLERSASV
550 560 570 580 590 600
DAEKMVLCKL KTECGSAFTY KLEGMFKDMD ASENYGRLFN QYLEHMNKEK ANFTARVITP
610 620 630 640 650 660
EYWPTYDTYE INIPKEMRDT LTDYQDFYRV QHGNRNVKWH HGLASAVISA SFRPGCKKEL
670 680 690 700 710 720
IATMYQTVIL LLFNKCETWT VAEIVEHTKI LEIEVVKNVL ALLGGRDKPK VLQRVEGGGS
730 740 750 760 770 780
EKKEGTVENL KNEKFVVNSK FTEKRCRVRI AQVNIKTAVE ETKEVKEEVN SDRQYKIDAA
790 800 810 820 830
VVRIMKARKQ LNHQTLMTEL LQQLRFPVST ADIKKRLESL IEREYISRDP EEASSYNYVA