Q62210
Gene name |
Birc2 |
Protein name |
Baculoviral IAP repeat-containing protein 2 |
Names |
Cellular inhibitor of apoptosis 1, C-IAP1, Inhibitor of apoptosis protein 2, mIAP2, RING-type E3 ubiquitin transferase BIRC2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:11797 |
EC number |
2.3.2.27: Aminoacyltransferases |
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
565-600 (RING domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Target domain |
565-600 (RING domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

1 structures for Q62210
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q62210-F1 | Predicted | AlphaFoldDB |
4 variants for Q62210
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
rs50329106 | 159 | A>S | No | Ensembl | |
rs264773669 | 431 | A>T | No | Ensembl | |
rs51247281 | 447 | M>L | No | Ensembl | |
rs234547296 | 588 | E>K | No | Ensembl |
No associated diseases with Q62210
Functions
Description | ||
---|---|---|
EC Number | 2.3.2.27 | Aminoacyltransferases |
Subcellular Localization |
|
|
PANTHER Family | ||
PANTHER Subfamily | ||
PANTHER Protein Class | ||
PANTHER Pathway Category | No pathway information available |
7 GO annotations of cellular component
Name | Definition |
---|---|
CD40 receptor complex | A protein complex that contains at least CD40 (a cell surface receptor of the tumour necrosis factor receptor (TNFR) superfamily), and other signaling molecules. |
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
cytoplasmic side of plasma membrane | The leaflet the plasma membrane that faces the cytoplasm and any proteins embedded or anchored in it or attached to its surface. |
membrane raft | Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. |
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. |
XY body | A structure found in a male mammalian spermatocyte containing an unpaired X chromosome that has become densely heterochromatic, silenced and localized at the nuclear periphery. |
12 GO annotations of molecular function
Name | Definition |
---|---|
chaperone binding | Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. |
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. |
FBXO family protein binding | Binding to a member of the FBXO protein family. Members of this family have an F-box protein motif of approximately 50 amino acids that functions as a site of protein-protein interaction. |
identical protein binding | Binding to an identical protein or proteins. |
protein N-terminus binding | Binding to a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue. |
protein-containing complex binding | Binding to a macromolecular complex. |
transcription coactivator activity | A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator. |
transferase activity | Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2. |
ubiquitin binding | Binding to ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation. |
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: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues. |
ubiquitin-protein transferase activity | Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages. |
zinc ion binding | Binding to a zinc ion (Zn). |
22 GO annotations of biological process
Name | Definition |
---|---|
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 ripoptosome assembly involved in necroptotic process | Any process that stops, prevents or reduces the frequency, rate or extent of ripoptosome assembly involved in a necroptotic process. |
placenta development | The process whose specific outcome is the progression of the placenta over time, from its formation to the mature structure. The placenta is an organ of metabolic interchange between fetus and mother, partly of embryonic origin and partly of maternal origin. |
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. |
positive regulation of protein K48-linked ubiquitination | Any process that activates or increases the frequency, rate or extent of protein K48-linked ubiquitination. |
positive regulation of protein K63-linked ubiquitination | Any process that activates or increases the frequency, rate or extent of protein K63-linked ubiquitination. |
positive regulation of protein monoubiquitination | Any process that activates or increases the frequency, rate or extent of protein monoubiquitination. |
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. |
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 polyubiquitination | Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain. |
regulation of apoptotic process | Any process that modulates the occurrence or rate of cell death by apoptotic process. |
regulation of cell cycle | Any process that modulates the rate or extent of progression through the cell cycle. |
regulation of necroptotic process | Any process that modulates 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. |
regulation of NIK/NF-kappaB signaling | Any process that modulates the frequency, rate or extent of NIK/NF-kappaB signaling. |
regulation of reactive oxygen species metabolic process | Any process that modulates the frequency, rate or extent of reactive oxygen species metabolic process. |
response to cAMP | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus. |
response to ethanol | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ethanol stimulus. |
response to hypoxia | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. |
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 |
Q13489 | BIRC3 | Baculoviral IAP repeat-containing protein 3 | Homo sapiens (Human) | 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 |
O08863 | Birc3 | Baculoviral IAP repeat-containing protein 3 | Mus musculus (Mouse) | SS |
O62640 | PIAP | Putative inhibitor of apoptosis | Sus scrofa (Pig) | SS |
10 | 20 | 30 | 40 | 50 | 60 |
MDKTVSQRLG | QGTLHQKLKR | IMEKSTILSN | WTKESEEKMK | FDFSCELYRM | STYSAFPRGV |
70 | 80 | 90 | 100 | 110 | 120 |
PVSERSLARA | GFYYTGVNDK | VKCFCCGLML | DNWKQGDSPV | EKHRQFYPSC | SFVQTLLSAS |
130 | 140 | 150 | 160 | 170 | 180 |
LQSPSKNMSP | VKSRFAHSSP | LERGGIHSNL | CSSPLNSRAV | EDFSSRMDPC | SYAMSTEEAR |
190 | 200 | 210 | 220 | 230 | 240 |
FLTYSMWPLS | FLSPAELARA | GFYYIGPGDR | VACFACGGKL | SNWEPKDDAM | SEHRRHFPHC |
250 | 260 | 270 | 280 | 290 | 300 |
PFLENTSETQ | RFSISNLSMQ | THSARLRTFL | YWPPSVPVQP | EQLASAGFYY | VDRNDDVKCF |
310 | 320 | 330 | 340 | 350 | 360 |
CCDGGLRCWE | PGDDPWIEHA | KWFPRCEFLI | RMKGQEFVDE | IQARYPHLLE | QLLSTSDTPG |
370 | 380 | 390 | 400 | 410 | 420 |
EENADPTETV | VHFGPGESSE | DVVMMSTPVV | KAALEMGFSR | SLVRQTVQRQ | ILATGENYRT |
430 | 440 | 450 | 460 | 470 | 480 |
VNDIVSVLLN | AEDERREEEK | ERQTEEMASG | DLSLIRKNRM | ALFQQLTHVL | PILDNLLEAS |
490 | 500 | 510 | 520 | 530 | 540 |
VITKQEHDII | RQKTQIPLQA | RELIDTVLVK | GNAAANIFKN | SLKEIDSTLY | ENLFVEKNMK |
550 | 560 | 570 | 580 | 590 | 600 |
YIPTEDVSGL | SLEEQLRRLQ | EERTCKVCMD | REVSIVFIPC | GHLVVCQECA | PSLRKCPICR |
610 | |||||
GTIKGTVRTF | LS |