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Protein Page:
BIRC2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
BIRC2 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 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. Interacts with DIABLO/SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity. Interacts with CASP9. Interacts (via BIR domains) with TRAF2. Interacts with E2F1, RIPK1, RIPK2, RIPK3, RIPK4, BIRC5/survivin and USP19. Present in many fetal and adult tissues. Mainly expressed in adult skeletal muscle, thymus, testis, ovary, and pancreas, low or absent in brain and peripheral blood leukocytes. 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. Belongs to the IAP family. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin conjugating system; EC 6.3.2.-; Ligase; Ubiquitin ligase
Chromosomal Location of Human Ortholog: 11q22
Cellular Component: XY body; internal side of plasma membrane; nucleus; cytosol; lipid raft
Molecular Function: protein binding; zinc ion binding; transcription coactivator activity; ubiquitin-protein ligase activity; protein N-terminus binding; ligase activity
Biological Process: proteasomal ubiquitin-dependent protein catabolic process; regulation of toll-like receptor signaling pathway; response to cAMP; protein polyubiquitination; regulation of cell cycle; apoptosis; protein heterooligomerization; toll-like receptor 3 signaling pathway; regulation of apoptosis; cell surface receptor linked signal transduction; regulation of transcription, DNA-dependent; regulation of cell differentiation; toll-like receptor 4 signaling pathway; placenta development; cell structure disassembly during apoptosis; positive regulation of I-kappaB kinase/NF-kappaB cascade; transcription, DNA-dependent; MyD88-independent toll-like receptor signaling pathway; regulation of cell proliferation; regulation of innate immune response; response to ethanol; regulation of inflammatory response; response to hypoxia; toll-like receptor signaling pathway; innate immune response; negative regulation of apoptosis
Reference #:  Q13490 (UniProtKB)
Alt. Names/Synonyms: API1; apoptosis inhibitor 1; baculoviral IAP repeat-containing 2; Baculoviral IAP repeat-containing protein 2; BIRC2; C-IAP1; cIAP1; hIAP-2; hIAP2; IAP homolog B; IAP-2; IAP2; Inhibitor of apoptosis protein 2; MIHB; NFR2-TRAF signalling complex protein; RING finger protein 48; RNF48; TNFR2-TRAF-signaling complex protein 2
Gene Symbols: BIRC2
Molecular weight: 69,900 Da
Basal Isoelectric point: 6.27  Predict pI for various phosphorylation states
CST Pathways:  Apoptosis Regulation  |  Death Receptor Signaling  |  Inhibition of Apoptosis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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BIRC2

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K19-ub GPSYQNIkSIMEDST
0 1 K36-ub SDWTNSNkQKMkYDF
0 1 K40-ub NSNkQKMkYDFSCEL
0 1 K82 TGVNDKVKCFCCGLM
0 1 K94 GLMLDNWKLGDsPIQ
0 2 S98-p DNWKLGDsPIQKHKQ
0 1 S123 LVSASLGSTSkNTSP
0 4 K126-ub ASLGSTSkNTSPMRN
0 1 S129 GSTSkNTSPMRNSFA
0 3 S140-p NSFAHSLsPTLEHSs
0 2 - gap
0 1 S147-p sPTLEHSsLFSGSYS
0 2 S157-p SGSYSSLsPNPLNSR
0 2 N159 SYSSLsPNPLNSRAV
0 4 Y177-p SSSRTNPySYAMSTE
0 2 K226-ub ACFACGGkLSNWEPk
0 4 K233-ub kLSNWEPkDDAMSEH
0 1 K305-ub VGRNDDVkCFCCDGG
0 1 K340-ub CEFLIRMkGQEFVDE
0 1 K410-ub GFNRDLVkQTVQSkI
0 1 K416-ub VkQTVQSkILTTGEN
0 2 K425-ub LTTGENYkTVNDIVS
0 4 K441-ub LLNAEDEkREEEkEk
0 5 K446-ub DEkREEEkEkQAEEM
0 4 K448-ub kREEEkEkQAEEMAS
0 1 K537-ub EIDSTLYkNLFVDKN
0 1 K546-ub LFVDKNMkYIPTEDV
  mouse

 
K19 GTLHQKLKRIMEKST
E36 SNWTKESEEKMKFDF
K40 KESEEKMKFDFSCEL
K82-ub TGVNDKVkCFCCGLM
K94-ub GLMLDNWkQGDSPVE
S98 DNWkQGDSPVEKHRQ
S123-p LLSASLQsPSKNMsP
K126 ASLQsPSKNMsPVKS
S129-p QsPSKNMsPVKSRFA
S139 KSRFAHSSPLErGGI
R143-m1 AHSSPLErGGIHSNL
- gap
C151 GGIHSNLCSsPLNSR
S153-p IHSNLCSsPLNSRAV
C170 FSSRMDPCSYAMSTE
K219 ACFACGGKLSNWEPK
K226 KLSNWEPKDDAMSEH
K298 VDRNDDVKCFCCDGG
K333 CEFLIRMKGQEFVDE
R404 GFSRSLVRQTVQRQI
Q410 VRQTVQRQILATGEN
R419 LATGENYRTVNDIVS
R435 LLNAEDERREEEKER
K440 DERREEEKERQTEEM
R442 RREEEKERQTEEMAS
E531 EIDSTLYENLFVEKN
K540 LFVEKNMKYIPTEDV
  rat

 
- gap
K15 SNWTKENKEKMKYDF
K19 KENKEKMKYDFSCEL
K61 TGVNDKVKCFCCGLM
K73 GLMLDNWKQGDSPTE
S77 DNWKQGDSPTEKHRQ
S102 LLSGGLQSAAKNTSP
K105 GGLQSAAKNTSPAKS
S108 QSAAKNTSPAKSRFA
L118 KSRFAHSLPLEQGGI
Q122 AHSLPLEQGGIHSSL
- gap
P130 GGIHSSLPSNPLNSR
N132 IHSSLPSNPLNSRAV
C149 FSLRMNPCSYAMSTE
K198 ACFACGGKLSNWEPN
N205 KLSNWEPNDDPLSEH
K277 VDHNDDVKCFCCDGG
K312 CEFLIRMKGQEFVDE
R381 GFSRSLVRQTVQRQI
Q387 VRQTVQRQILATGEN
R396 LATGENYRTVSDIVS
R412 LLNAEDERREEEKER
K417 DERREEEKERQSEET
R419 RREEEKERQSEETAS
E508 EVDSTLYEHLFVEKT
K517 LFVEKTMKYIPTEDV
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