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Protein

Baculoviral IAP repeat-containing protein 2

Gene

Birc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. 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. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle.1 Publication

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.1 Publication

Enzyme regulationi

The CARD domain inhibits the activation of E3 ubiquitin ligase activity by preventing RING domain dimerization and E2 ubiquitin donor binding and activation. The CARD domain-mediated autoinhibition of the E3 ubiquitin-protein ligase activity suppresses cell proliferation and migration. USP19 regulates the stability of BIRC2/c-IAP1 by preventing its ubiquitination (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi299ZincPROSITE-ProRule annotation1
Metal bindingi302ZincPROSITE-ProRule annotation1
Metal bindingi319ZincPROSITE-ProRule annotation1
Metal bindingi326ZincPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri565 – 600RING-typePROSITE-ProRule annotationAdd BLAST36

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Transferase

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-111465. Apoptotic cleavage of cellular proteins.
R-MMU-5213460. RIPK1-mediated regulated necrosis.
R-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5675482. Regulation of necroptotic cell death.
R-MMU-5676594. TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
R-MMU-5689880. Ub-specific processing proteases.

Protein family/group databases

MEROPSiI32.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Baculoviral IAP repeat-containing protein 2 (EC:2.3.2.271 Publication)
Alternative name(s):
Cellular inhibitor of apoptosis 1
Short name:
C-IAP11 Publication
Inhibitor of apoptosis protein 21 Publication
Short name:
mIAP21 Publication
RING-type E3 ubiquitin transferase BIRC2Curated
Gene namesi
Name:Birc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1197009. Birc2.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Agents that induce either the extrinsic or intrinsic apoptotic pathways promote its redistribution from the nuclear compartment to the cytoplasmic compartment. Associated with the midbody in telophase cells, and found diffusely in the nucleus of interphase cells (By similarity).By similarity

GO - Cellular componenti

  • CD40 receptor complex Source: BHF-UCL
  • cytoplasm Source: MGI
  • cytoplasmic side of plasma membrane Source: BHF-UCL
  • membrane raft Source: Ensembl
  • nucleus Source: UniProtKB
  • protein complex Source: Ensembl
  • XY body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001223481 – 612Baculoviral IAP repeat-containing protein 2Add BLAST612

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei143Omega-N-methylarginineCombined sources1
Modified residuei153PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ62210.
MaxQBiQ62210.
PaxDbiQ62210.
PRIDEiQ62210.

PTM databases

iPTMnetiQ62210.
PhosphoSitePlusiQ62210.

Expressioni

Tissue specificityi

Expressed in heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis.

Gene expression databases

BgeeiENSMUSG00000057367.
CleanExiMM_BIRC2.
MM_BIRC3.
ExpressionAtlasiQ62210. baseline and differential.
GenevisibleiQ62210. MM.

Interactioni

Subunit structurei

Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with CASP9. Interacts (via BIR domains) with TRAF2; the interaction is required for IKBKE ubiquitination. Interacts with E2F1, RIPK1, RIPK2, RIPK3, RIPK4, BIRC5/survivin and USP19 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198148. 5 interactors.
IntActiQ62210. 3 interactors.
MINTiMINT-2839737.
STRINGi10090.ENSMUSP00000091422.

Structurei

3D structure databases

ProteinModelPortaliQ62210.
SMRiQ62210.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati46 – 113BIR 1Add BLAST68
Repeati177 – 243BIR 2Add BLAST67
Repeati262 – 329BIR 3Add BLAST68
Domaini447 – 537CARDPROSITE-ProRule annotationAdd BLAST91

Domaini

The BIR domains mediate nuclear localization.By similarity
The CARD domain is necessary to stabilize the protein and inhibit the activation of E3 ubiquitin-protein ligase activity of BIRC2/c-IAP1 by preventing RING domain dimerization and E2 ubiquitin donor binding and activation.By similarity

Sequence similaritiesi

Belongs to the IAP family.Curated
Contains 3 BIR repeats.PROSITE-ProRule annotation
Contains 1 CARD domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri565 – 600RING-typePROSITE-ProRule annotationAdd BLAST36

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00500000044782.
HOGENOMiHOG000232059.
HOVERGENiHBG004848.
InParanoidiQ62210.
KOiK16060.
OMAiPIEKHKQ.
OrthoDBiEOG091G0CXH.
PhylomeDBiQ62210.
TreeFamiTF105356.

Family and domain databases

CDDicd00022. BIR. 3 hits.
Gene3Di1.10.1170.10. 4 hits.
1.10.533.10. 1 hit.
InterProiIPR001370. BIR_rpt.
IPR028795. C-IAP1.
IPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR001841. Znf_RING.
[Graphical view]
PANTHERiPTHR10044:SF132. PTHR10044:SF132. 1 hit.
PfamiPF00653. BIR. 3 hits.
PF00619. CARD. 1 hit.
[Graphical view]
SMARTiSM00238. BIR. 3 hits.
SM00114. CARD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS01282. BIR_REPEAT_1. 3 hits.
PS50143. BIR_REPEAT_2. 3 hits.
PS50209. CARD. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q62210-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKTVSQRLG QGTLHQKLKR IMEKSTILSN WTKESEEKMK FDFSCELYRM
60 70 80 90 100
STYSAFPRGV PVSERSLARA GFYYTGVNDK VKCFCCGLML DNWKQGDSPV
110 120 130 140 150
EKHRQFYPSC SFVQTLLSAS LQSPSKNMSP VKSRFAHSSP LERGGIHSNL
160 170 180 190 200
CSSPLNSRAV EDFSSRMDPC SYAMSTEEAR FLTYSMWPLS FLSPAELARA
210 220 230 240 250
GFYYIGPGDR VACFACGGKL SNWEPKDDAM SEHRRHFPHC PFLENTSETQ
260 270 280 290 300
RFSISNLSMQ THSARLRTFL YWPPSVPVQP EQLASAGFYY VDRNDDVKCF
310 320 330 340 350
CCDGGLRCWE PGDDPWIEHA KWFPRCEFLI RMKGQEFVDE IQARYPHLLE
360 370 380 390 400
QLLSTSDTPG EENADPTETV VHFGPGESSE DVVMMSTPVV KAALEMGFSR
410 420 430 440 450
SLVRQTVQRQ ILATGENYRT VNDIVSVLLN AEDERREEEK ERQTEEMASG
460 470 480 490 500
DLSLIRKNRM ALFQQLTHVL PILDNLLEAS VITKQEHDII RQKTQIPLQA
510 520 530 540 550
RELIDTVLVK GNAAANIFKN SLKEIDSTLY ENLFVEKNMK YIPTEDVSGL
560 570 580 590 600
SLEEQLRRLQ EERTCKVCMD REVSIVFIPC GHLVVCQECA PSLRKCPICR
610
GTIKGTVRTF LS
Length:612
Mass (Da):69,676
Last modified:November 1, 1996 - v1
Checksum:iE08969D93C6C610D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti380E → K in AAC53532 (PubMed:9441758).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L49433 mRNA. Translation: AAC42078.1.
U88909 mRNA. Translation: AAC53532.1.
BC145985 mRNA. Translation: AAI45986.1.
CCDSiCCDS22811.1.
RefSeqiNP_001278432.1. NM_001291503.1.
NP_031491.2. NM_007465.3.
XP_017168599.1. XM_017313110.1.
UniGeneiMm.335659.
Mm.400826.

Genome annotation databases

EnsembliENSMUST00000074246; ENSMUSP00000091422; ENSMUSG00000057367.
ENSMUST00000190341; ENSMUSP00000140049; ENSMUSG00000057367.
GeneIDi11797.
KEGGimmu:11797.
UCSCiuc009ocz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L49433 mRNA. Translation: AAC42078.1.
U88909 mRNA. Translation: AAC53532.1.
BC145985 mRNA. Translation: AAI45986.1.
CCDSiCCDS22811.1.
RefSeqiNP_001278432.1. NM_001291503.1.
NP_031491.2. NM_007465.3.
XP_017168599.1. XM_017313110.1.
UniGeneiMm.335659.
Mm.400826.

3D structure databases

ProteinModelPortaliQ62210.
SMRiQ62210.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198148. 5 interactors.
IntActiQ62210. 3 interactors.
MINTiMINT-2839737.
STRINGi10090.ENSMUSP00000091422.

Protein family/group databases

MEROPSiI32.002.

PTM databases

iPTMnetiQ62210.
PhosphoSitePlusiQ62210.

Proteomic databases

EPDiQ62210.
MaxQBiQ62210.
PaxDbiQ62210.
PRIDEiQ62210.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000074246; ENSMUSP00000091422; ENSMUSG00000057367.
ENSMUST00000190341; ENSMUSP00000140049; ENSMUSG00000057367.
GeneIDi11797.
KEGGimmu:11797.
UCSCiuc009ocz.2. mouse.

Organism-specific databases

CTDi329.
MGIiMGI:1197009. Birc2.

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00500000044782.
HOGENOMiHOG000232059.
HOVERGENiHBG004848.
InParanoidiQ62210.
KOiK16060.
OMAiPIEKHKQ.
OrthoDBiEOG091G0CXH.
PhylomeDBiQ62210.
TreeFamiTF105356.

Enzyme and pathway databases

ReactomeiR-MMU-111465. Apoptotic cleavage of cellular proteins.
R-MMU-5213460. RIPK1-mediated regulated necrosis.
R-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5675482. Regulation of necroptotic cell death.
R-MMU-5676594. TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
R-MMU-5689880. Ub-specific processing proteases.

Miscellaneous databases

ChiTaRSiBirc2. mouse.
PROiQ62210.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000057367.
CleanExiMM_BIRC2.
MM_BIRC3.
ExpressionAtlasiQ62210. baseline and differential.
GenevisibleiQ62210. MM.

Family and domain databases

CDDicd00022. BIR. 3 hits.
Gene3Di1.10.1170.10. 4 hits.
1.10.533.10. 1 hit.
InterProiIPR001370. BIR_rpt.
IPR028795. C-IAP1.
IPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR001841. Znf_RING.
[Graphical view]
PANTHERiPTHR10044:SF132. PTHR10044:SF132. 1 hit.
PfamiPF00653. BIR. 3 hits.
PF00619. CARD. 1 hit.
[Graphical view]
SMARTiSM00238. BIR. 3 hits.
SM00114. CARD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS01282. BIR_REPEAT_1. 3 hits.
PS50143. BIR_REPEAT_2. 3 hits.
PS50209. CARD. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBIRC2_MOUSE
AccessioniPrimary (citable) accession number: Q62210
Secondary accession number(s): A6H6S7, O08864
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.