Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

553-598 (RING domain)

Relief mechanism

Ligand binding

Assay

Target domain

553-598 (RING domain)

Relief mechanism

Ligand binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for O08863

Entry ID Method Resolution Chain Position Source
AF-O08863-F1 Predicted AlphaFoldDB

No variants for O08863

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O08863

No associated diseases with O08863

2 regional properties for O08863

Type Name Position InterPro Accession
repeat Leucine-rich repeat 551 - 572 IPR001611
domain NB-ARC 150 - 388 IPR002182

Functions

Description
EC Number 3.6.4.13 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Nucleus
  • Cytoplasm
  • Can translocate to the cytoplasm in the presence of MX1
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.

4 GO annotations of molecular function

Name Definition
cysteine-type endopeptidase inhibitor activity involved in apoptotic process Binds to and stops, prevents or reduces the activity of a cysteine-type endopeptidase involved in the apoptotic process.
metal ion binding Binding to a metal ion.
protein-containing complex binding Binding to a macromolecular complex.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond

11 GO annotations of biological process

Name Definition
apoptotic process A programmed cell death process which begins when a cell receives an internal (e.g. DNA damage) or external signal (e.g. an extracellular death ligand), and proceeds through a series of biochemical events (signaling pathway phase) which trigger an execution phase. The execution phase is the last step of an apoptotic process, and is typically characterized by rounding-up of the cell, retraction of pseudopodes, reduction of cellular volume (pyknosis), chromatin condensation, nuclear fragmentation (karyorrhexis), plasma membrane blebbing and fragmentation of the cell into apoptotic bodies. When the execution phase is completed, the cell has died.
cellular response to tumor necrosis factor 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 tumor necrosis factor stimulus.
necroptotic process A programmed necrotic cell death process which begins when a cell receives a signal (e.g. a ligand binding to a death receptor or to a Toll-like receptor), and proceeds through a series of biochemical events (signaling pathways), characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3) and by critical dependence on mixed lineage kinase domain-like (MLKL), and which typically lead to common morphological features of necrotic cell death. The process ends when the cell has died. The process is divided into a signaling phase, and an execution phase, which is triggered by the former.
negative regulation of apoptotic process Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
negative regulation of necroptotic process Any process that decreases the rate, frequency or extent of a necroptotic process, a necrotic cell death process that results from the activation of endogenous cellular processes, such as signaling involving death domain receptors or Toll-like receptors.
negative regulation of phosphorylation Any process that stops, prevents or decreases the rate of addition of phosphate groups to a molecule.
negative regulation of reactive oxygen species metabolic process Any process that stops, prevents or reduces the frequency, rate or extent of reactive oxygen species metabolic process.
positive regulation of protein polyubiquitination Any process that activates or increases the frequency, rate or extent of protein polyubiquitination.
positive regulation of protein ubiquitination Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein.
regulation of cell cycle Any process that modulates the rate or extent of progression through the cell cycle.
regulation of non-canonical NF-kappaB signal transduction Any process that modulates the frequency, rate or extent of NIK/NF-kappaB signaling.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q90660 ITA Inhibitor of apoptosis protein Gallus gallus (Chicken) SS
A1E2V0 BIRC3 Baculoviral IAP repeat-containing protein 3 Canis lupus familiaris (Dog) (Canis familiaris) SS
Q96P09 BIRC8 Baculoviral IAP repeat-containing protein 8 Homo sapiens (Human) PR
Q13490 BIRC2 Baculoviral IAP repeat-containing protein 2 Homo sapiens (Human) EV
Q13489 BIRC3 Baculoviral IAP repeat-containing protein 3 Homo sapiens (Human) SS
Q62210 Birc2 Baculoviral IAP repeat-containing protein 2 Mus musculus (Mouse) SS
O62640 PIAP Putative inhibitor of apoptosis Sus scrofa (Pig) SS
10 20 30 40 50 60
MAEQDVENDL LDYDEEEEPQ APQESTPAPP KKDIKGSYVS IHSSGFRDFL LKPELLRAIV
70 80 90 100 110 120
DCGFEHPSEV QHECIPQAIL GMDVLCQAKS GMGKTAVFVL ATLQQIEPVN GQVTVLVMCH
130 140 150 160 170 180
TRELAFQISK EYERFSKYMP SVKVSVFFGG LSIKKDEEVL KKNCPHVVVG TPGRILALVR
190 200 210 220 230 240
NRSFSLKNVK HFVLDECDKM LEQLDMRRDV QEIFRLTPHE KQCMMFSATL SKDIRPVCRK
250 260 270 280 290 300
FMQDPMEVFV DDETKLTLHG LQQYYVKLKD SEKNRKLFDL LDVLEFNQVI IFVKSVQRCM
310 320 330 340 350 360
ALAQLLVEQN FPAIAIHRGM AQEERLSRYQ QFKDFQRRIL VATNLFGRGM DIERVNIVFN
370 380 390 400 410 420
YDMPEDSDTY LHRVARAGRF GTKGLAITFV SDENDAKILN DVQDRFEVNV AELPEEIDIS
TYIEQSR