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 A4IHK8

Entry ID Method Resolution Chain Position Source
AF-A4IHK8-F1 Predicted AlphaFoldDB

No variants for A4IHK8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4IHK8

No associated diseases with A4IHK8

1 regional properties for A4IHK8

Type Name Position InterPro Accession
domain Potentiating neddylation domain 85 - 277 IPR005176

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane
  • Cytoplasm
  • Nucleus
  • Cytoplasm, perinuclear region
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
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.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
ubiquitin ligase complex A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex.

3 GO annotations of molecular function

Name Definition
cullin family protein binding Binding to a member of the cullin family, hydrophobic proteins that act as scaffolds for ubiquitin ligases (E3).
ubiquitin conjugating enzyme binding Binding to a ubiquitin conjugating enzyme, any of the E2 proteins.
ubiquitin-like protein binding Binding to a small conjugating protein such as ubiquitin or a ubiquitin-like protein.

6 GO annotations of biological process

Name Definition
negative regulation of protein neddylation Any process that stops, prevents or reduces the frequency, rate or extent of protein neddylation.
positive regulation of protein neddylation Any process that activates or increases the frequency, rate or extent of protein neddylation.
positive regulation of ubiquitin-protein transferase activity Any process that activates, maintains or increases the rate of ubiquitin transferase activity.
protein neddylation Covalent attachment of the ubiquitin-like protein NEDD8 (RUB1) to another protein.
regulation of cell cycle process Any process that modulates a cellular process that is involved in the progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events.
regulation of protein neddylation Any process that modulates the frequency, rate or extent of protein neddylation.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5E9V1 DCUN1D3 DCN1-like protein 3 Bos taurus (Bovine) PR
Q8IWE4 DCUN1D3 DCN1-like protein 3 Homo sapiens (Human) PR
Q8K0V2 Dcun1d3 DCN1-like protein 3 Mus musculus (Mouse) PR
Q4V8B2 Dcun1d3 DCN1-like protein 3 Rattus norvegicus (Rat) PR
Q9U3C8 dcn-1 Defective in cullin neddylation protein 1 Caenorhabditis elegans PR
10 20 30 40 50 60
MGQCVTKCKN PSSTLGSKNG ERESSKPHKR SSSHKDEHLS ICGKASREIL VNGTKKGDVS
70 80 90 100 110 120
LEASQPLAAG GDTKKKEQGT GAELSSVQRI EELFWRYKDE REDAILEEGM ERFCNDLYVD
130 140 150 160 170 180
PTEFRVLVLA WKFQAATMCK FTRREFFEGC KAINADGIEG ICARFPSLLN EAKQEDKFKD
190 200 210 220 230 240
LYRFTFQFGL DSEEGQRSLH REIAIALWKL VFTQNKPLIL DQWLDFLTEN PSGIKGISRD
250 260 270 280 290 300
TWNMFLNFTQ VIGPDLSNYS EDEAWPSLFD TFVEWEMERR KNEEETKCIP CSGTDDQSTE
GQT