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O08863 (BIRC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Baculoviral IAP repeat-containing protein 3

EC=6.3.2.-
Alternative name(s):
Inhibitor of apoptosis protein 1
Short name=IAP-1
Short name=mIAP-1
Short name=mIAP1
Gene names
Name:Birc3
Synonyms:Birc2, Iap1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length600 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, IKBKE, TRAF1, and BCL10. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Ref.3

Enzyme regulation

USP19 regulates the stability of BIRC3/c-IAP2 by preventing its ubiquitination By similarity.

Subunit structure

Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. The BIR motifs region interacts with TNF receptor associated factors 1 and 2 (TRAF1 and TRAF2) to form a heteromeric complex, which is then recruited to the tumor necrosis factor receptor 2 (TNFR2). Interaction with TRAF2 is required for ubiquitination of IKBKE, degradation of NFKBIA and activation of NF-kappa-B. Interacts with RIP1, RIP2, RIP3, RIP4 and USP19 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Post-translational modification

Auto-ubiquitinated and degraded by the proteasome in apoptotic cells By similarity.

Sequence similarities

Belongs to the IAP family.

Contains 3 BIR repeats.

Contains 1 CARD domain.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processApoptosis
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

necroptotic process

Inferred from direct assay PubMed 21052097. Source: UniProtKB

negative regulation of necroptotic process

Inferred from mutant phenotype PubMed 21052097. Source: UniProtKB

negative regulation of phosphorylation

Inferred from mutant phenotype PubMed 21052097. Source: UniProtKB

negative regulation of reactive oxygen species metabolic process

Inferred from mutant phenotype PubMed 21052097. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

regulation of apoptotic process

Inferred from electronic annotation. Source: InterPro

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionubiquitin-protein ligase activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Traf2P394297EBI-642236,EBI-520016

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 600600Baculoviral IAP repeat-containing protein 3
PRO_0000122350

Regions

Repeat27 – 9468BIR 1
Repeat167 – 23367BIR 2
Repeat253 – 32068BIR 3
Domain436 – 52590CARD
Zinc finger553 – 58836RING-type

Sites

Metal binding2901Zinc By similarity
Metal binding2931Zinc By similarity
Metal binding3101Zinc By similarity
Metal binding3171Zinc By similarity

Experimental info

Sequence conflict3981W → R in AAC53531. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08863 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 2EC9C7B567721382

FASTA60067,228
        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        600 
EEQLRKLQEE RMCKVCMDRE VSIVFIPCGH LVVCKDCAPS LRKCPICRGT IKGTVRTFLS 

« Hide

References

« Hide 'large scale' references
[1]"Genomic characterization of the mouse inhibitor of apoptosis protein 1 and 2 genes."
Liston P., Lefebvre C., Fong W.G., Xuan J.Y., Korneluk R.G.
Genomics 46:495-503(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"c-IAP1 and c-IAP2 are critical mediators of tumor necrosis factor alpha (TNFalpha)-induced NF-kappaB activation."
Varfolomeev E., Goncharov T., Fedorova A.V., Dynek J.N., Zobel K., Deshayes K., Fairbrother W.J., Vucic D.
J. Biol. Chem. 283:24295-24299(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U88908 mRNA. Translation: AAC53531.1.
CT030639 Genomic DNA. No translation available.
RefSeqNP_031490.2. NM_007464.3.
UniGeneMm.2026.

3D structure databases

ProteinModelPortalO08863.
SMRO08863. Positions 24-600.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198147. 14 interactions.
DIPDIP-43742N.
IntActO08863. 3 interactions.
MINTMINT-1581324.

Protein family/group databases

MEROPSI32.003.

PTM databases

PhosphoSiteO08863.

Proteomic databases

PaxDbO08863.
PRIDEO08863.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID11796.
KEGGmmu:11796.

Organism-specific databases

CTD330.
MGIMGI:1197007. Birc3.

Phylogenomic databases

eggNOGNOG243347.
HOGENOMHOG000232059.
HOVERGENHBG004848.
InParanoidO08863.
KOK16060.

Gene expression databases

ArrayExpressO08863.
BgeeO08863.
CleanExMM_BIRC2.
MM_BIRC3.
GenevestigatorO08863.

Family and domain databases

Gene3D1.10.1170.10. 4 hits.
1.10.533.10. 1 hit.
InterProIPR001370. BIR.
IPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR001841. Znf_RING.
[Graphical view]
PfamPF00653. BIR. 3 hits.
PF00619. CARD. 1 hit.
[Graphical view]
SMARTSM00238. BIR. 3 hits.
SM00114. CARD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS01282. BIR_REPEAT_1. 3 hits.
PS50143. BIR_REPEAT_2. 3 hits.
PS50209. CARD. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279629.
PROO08863.
SOURCESearch...

Entry information

Entry nameBIRC3_MOUSE
AccessionPrimary (citable) accession number: O08863
Secondary accession number(s): E9QLX3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot