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 A2VDM0

Entry ID Method Resolution Chain Position Source
AF-A2VDM0-F1 Predicted AlphaFoldDB

22 variants for A2VDM0

Variant ID(s) Position Change Description Diseaes Association Provenance
rs476075998 6 D>A No EVA
rs444731606 6 D>E No EVA
rs440090214 8 D>E No EVA
rs481099275 8 D>H No EVA
rs460280047 9 T>K No EVA
rs476990435 11 E>V No EVA
rs445770296 15 C>S No EVA
rs462604093 20 L>F No EVA
rs448375422 26 Q>H No EVA
rs467743165 28 S>R No EVA
rs380216384 32 R>* No EVA
rs522672506 32 R>Q No EVA
rs436422246 43 P>T No EVA
rs446889256 77 K>I No EVA
rs383011888 100 D>N No EVA
rs432468534 101 N>D No EVA
rs452683053 112 L>P No EVA
rs446804111 152 E>* No EVA
rs476010862 156 L>V No EVA
rs438274805 161 I>M No EVA
rs455270941 163 E>V No EVA
rs386114827 170 C>S No EVA

No associated diseases with A2VDM0

2 regional properties for A2VDM0

Type Name Position InterPro Accession
binding_site Cytochrome c oxidase, subunit I, copper-binding site 275 - 329 IPR023615
domain Cytochrome c oxidase-like, subunit I domain 38 - 556 IPR023616

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Colocalizes with lysosomal marker LAMP2 following homooligomerization and subsequent activation
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

5 GO annotations of biological process

Name Definition
cytoplasmic pattern recognition receptor signaling pathway The series of molecular signals initiated by a ligand binding to a cytoplasmic pattern recognition receptor (PRR). PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species.
I-kappaB kinase/NF-kappaB signaling The process in which a signal is passed on to downstream components within the cell through the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription.
innate immune response Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens.
positive regulation of I-kappaB kinase/NF-kappaB signaling Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling.
protein homooligomerization The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q96CG3 TIFA TRAF-interacting protein with FHA domain-containing protein A Homo sapiens (Human) PR
Q793I8 Tifa TRAF-interacting protein with FHA domain-containing protein A Mus musculus (Mouse) PR
Q5XIB9 Tifa TRAF-interacting protein with FHA domain-containing protein A Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MSSFEDADTE EMVTCLQMTL YHPGHQRSGI FRSIKFFNRE KLPTSEVVKF GRNSHTCNYI
70 80 90 100 110 120
FQDKQVSRVQ FSLQVFKKFN SSVVSFEIKN MSKKTSLLVD NKELGYLNKM DLPDKCMIRF
130 140 150 160 170 180
GDYQFLVEKE DGESLEFFEI QFSLSKKPLL QENNWLSQEP IPECGSYSSC LTQNNSPMEV
GENEW