O08863

SS
Gene name
Birc3
Protein name
Baculoviral IAP repeat-containing protein 3
Names
EC 2.3.2.27 , Cellular inhibitor of apoptosis 2 , C-IAP2 , Inhibitor of apoptosis protein 1 , mIAP1 , RING-type E3 ubiquitin transferase BIRC3
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:11796
EC number
2.3.2.27: Aminoacyltransferases
Protein Class

Descriptions

E3 ligases mediate the covalent attachment of ubiquitin to target proteins thereby enabling ubiquitin dependent signaling. Baculoviral IAP repeat-containing protein 2 (BIRC2) protein is an E3 ligase that modulates diverse biological processes such as cell survival, proliferation, and migration. Full-length BIRC2 fails to associate with E2, but CARD-deleted mutant BIRC2 readily interacts with E2. The CARD inhibits activation of BIRC2’s E3 activity by preventing RING dimerization, E2 binding, and E2 activation. In addition, BIRC2 lacking only the BIR3 domain readily associates with the E2, representing that the CARD and BIR3 domains are both required for inhibition of E3 activity of BIRC2.

Autoinhibitory domains (AIDs)

418-544 (CARD domain) SS

Target domain

553-598 (RING domain)

Relief mechanism

Ligand binding

Assay

251-322 (BIR3 domain) SS

Target domain

553-598 (RING domain)

Relief mechanism

Ligand binding

Assay

Accessory elements

No accessory elements

References

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

7 regional properties for O08863

Type Name Position InterPro Accession
domain CARD domain 436 - 525 IPR001315
repeat BIR repeat 25 - 96 IPR001370-1
repeat BIR repeat 165 - 235 IPR001370-2
repeat BIR repeat 251 - 322 IPR001370-3
domain Zinc finger, RING-type 553 - 588 IPR001841
domain BIRC2/BIRC3, UBA domain 374 - 423 IPR041933
domain BIRC2/3-like, UBA domain 372 - 423 IPR048875

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Cytoplasm
  • Nucleus
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
MVQDSAFLAK LMKSADTFEL KYDFSCELYR LSTYSAFPRG VPVSERSLAR AGFYYTGAND
70 80 90 100 110 120
KVKCFCCGLM LDNWKQGDSP MEKHRKLYPS CNFVQTLNPA NSLEASPRPS LPSTAMSTMP
130 140 150 160 170 180
LSFASSENTG YFSGSYSSFP SDPVNFRANQ DCPALSTSPY HFAMNTEKAR LLTYETWPLS
190 200 210 220 230 240
FLSPAKLAKA GFYYIGPGDR VACFACDGKL SNWERKDDAM SEHQRHFPSC PFLKDLGQSA
250 260 270 280 290 300
SRYTVSNLSM QTHAARIRTF SNWPSSALVH SQELASAGFY YTGHSDDVKC FCCDGGLRCW
310 320 330 340 350 360
ESGDDPWVEH AKWFPRCEYL LRIKGQEFVS QVQAGYPHLL EQLLSTSDSP EDENADAAIV
370 380 390 400 410 420
HFGPGESSED VVMMSTPVVK AALEMGFSRS LVRQTVQWQI LATGENYRTV SDLVIGLLDA
430 440 450 460 470 480
EDEMREEQME QAAEEEESDD LALIRKNKMV LFQHLTCVTP MLYCLLSARA ITEQECNAVK
490 500 510 520 530 540
QKPHTLQAST LIDTVLAKGN TAATSFRNSL REIDPALYRD IFVQQDIRSL PTDDIAALPM
550 560 570 580 590
EEQLRKLQEE RMCKVCMDRE VSIVFIPCGH LVVCKDCAPS LRKCPICRGT IKGTVRTFLS