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Q13489

- BIRC3_HUMAN

UniProt

Q13489 - BIRC3_HUMAN

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Protein

Baculoviral IAP repeat-containing protein 3

Gene

BIRC3

Organism
Homo sapiens (Human)
Status
Reviewed - 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, 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 CASP8.2 Publications

Enzyme regulationi

USP19 regulates the stability of BIRC3/c-IAP2 by preventing its ubiquitination.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi292 – 2921ZincPROSITE-ProRule annotation
Metal bindingi295 – 2951ZincPROSITE-ProRule annotation
Metal bindingi312 – 3121ZincPROSITE-ProRule annotation
Metal bindingi319 – 3191ZincPROSITE-ProRule annotation
Sitei442 – 4432Breakpoint for translocation to form BIRC3-MALT1

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri557 – 59236RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. ubiquitin-protein transferase activity Source: UniProtKB
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell surface receptor signaling pathway Source: ProtInc
  3. innate immune response Source: Reactome
  4. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  5. necroptotic process Source: Ensembl
  6. negative regulation of apoptotic process Source: ProtInc
  7. negative regulation of necroptotic process Source: Ensembl
  8. negative regulation of phosphorylation Source: Ensembl
  9. negative regulation of reactive oxygen species metabolic process Source: Ensembl
  10. NIK/NF-kappaB signaling Source: UniProtKB
  11. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  12. positive regulation of protein ubiquitination Source: UniProtKB
  13. protein heterooligomerization Source: Ensembl
  14. protein ubiquitination Source: GOC
  15. regulation of apoptotic process Source: UniProtKB
  16. regulation of cysteine-type endopeptidase activity Source: UniProtKB
  17. regulation of inflammatory response Source: UniProtKB
  18. regulation of innate immune response Source: UniProtKB
  19. regulation of necroptotic process Source: UniProtKB
  20. regulation of nucleotide-binding oligomerization domain containing signaling pathway Source: UniProtKB
  21. regulation of RIG-I signaling pathway Source: UniProtKB
  22. regulation of toll-like receptor signaling pathway Source: UniProtKB
  23. spermatogenesis Source: Ensembl
  24. toll-like receptor 3 signaling pathway Source: Reactome
  25. toll-like receptor 4 signaling pathway Source: Reactome
  26. toll-like receptor signaling pathway Source: Reactome
  27. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinkiQ13489.

Protein family/group databases

MEROPSiI32.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Baculoviral IAP repeat-containing protein 3 (EC:6.3.2.-)
Alternative name(s):
Apoptosis inhibitor 2
Short name:
API2
C-IAP2
IAP homolog C
Inhibitor of apoptosis protein 1
Short name:
IAP-1
Short name:
hIAP-1
Short name:
hIAP1
RING finger protein 49
TNFR2-TRAF-signaling complex protein 1
Gene namesi
Name:BIRC3
Synonyms:API2, IAP1, MIHC, RNF49
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:591. BIRC3.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. membrane raft Source: Ensembl
  4. nucleus Source: UniProtKB
  5. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving BIRC3 is recurrent in low-grade mucosa-associated lymphoid tissue (MALT lymphoma). Translocation t(11;18)(q21;q21) with MALT1. This translocation is found in approximately 50% of cytogenetically abnormal low-grade MALT lymphoma.

Organism-specific databases

Orphaneti52417. MALT lymphoma.
PharmGKBiPA25360.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 604604Baculoviral IAP repeat-containing protein 3PRO_0000122349Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ13489.
PaxDbiQ13489.
PRIDEiQ13489.

PTM databases

PhosphoSiteiQ13489.

Miscellaneous databases

PMAP-CutDBQ13489.

Expressioni

Tissue specificityi

Highly expressed in fetal lung, and kidney. In the adult, expression is mainly seen in lymphoid tissues, including spleen, thymus and peripheral blood lymphocytes.

Gene expression databases

BgeeiQ13489.
CleanExiHS_BIRC3.
ExpressionAtlasiQ13489. baseline and differential.
GenevestigatoriQ13489.

Organism-specific databases

HPAiHPA002317.

Interactioni

Subunit structurei

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 USP19.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP9P552112EBI-517709,EBI-516799
RIPK1Q135463EBI-517709,EBI-358507
RIPK2O433533EBI-517709,EBI-358522
RIPK3Q9Y5723EBI-517709,EBI-298250
RIPK4P570783EBI-517709,EBI-4422308
TRAF1Q130772EBI-517709,EBI-359224
TRAF2Q129337EBI-517709,EBI-355744

Protein-protein interaction databases

BioGridi106827. 69 interactions.
DIPiDIP-33720N.
IntActiQ13489. 36 interactions.
MINTiMINT-216139.
STRINGi9606.ENSP00000263464.

Structurei

Secondary structure

1
604
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 347
Helixi35 – 384
Helixi47 – 526
Beta strandi55 – 573
Beta strandi64 – 663
Turni67 – 693
Helixi82 – 898
Turni94 – 974
Helixi250 – 2523
Helixi255 – 2606
Helixi261 – 2644
Helixi273 – 2786
Beta strandi281 – 2855
Turni286 – 2883
Beta strandi289 – 2924
Turni293 – 2953
Beta strandi298 – 3014
Helixi308 – 3158
Helixi320 – 33415
Helixi544 – 55512
Turni558 – 5603
Beta strandi561 – 5644
Beta strandi567 – 5704
Beta strandi575 – 5773
Turni579 – 5813
Helixi582 – 5843
Beta strandi589 – 5913
Beta strandi597 – 6004

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UVLX-ray1.91A/B244-337[»]
3EB5X-ray2.00A536-604[»]
3EB6X-ray3.40A536-604[»]
3M0AX-ray2.61D26-99[»]
3M0DX-ray2.80D26-99[»]
ProteinModelPortaliQ13489.
SMRiQ13489. Positions 26-98, 165-235, 244-604.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13489.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati29 – 9668BIR 1Add
BLAST
Repeati169 – 23567BIR 2Add
BLAST
Repeati255 – 32268BIR 3Add
BLAST
Domaini439 – 52991CARDPROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri557 – 59236RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG243347.
GeneTreeiENSGT00500000044782.
HOGENOMiHOG000232059.
HOVERGENiHBG004848.
InParanoidiQ13489.
KOiK16060.
OMAiENSGYFS.
OrthoDBiEOG78H3TF.
PhylomeDBiQ13489.
TreeFamiTF105356.

Family and domain databases

Gene3Di1.10.1170.10. 4 hits.
1.10.533.10. 1 hit.
InterProiIPR001370. BIR.
IPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR001841. Znf_RING.
[Graphical view]
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.

Q13489-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIVENSIFL SNLMKSANTF ELKYDLSCEL YRMSTYSTFP AGVPVSERSL
60 70 80 90 100
ARAGFYYTGV NDKVKCFCCG LMLDNWKRGD SPTEKHKKLY PSCRFVQSLN
110 120 130 140 150
SVNNLEATSQ PTFPSSVTNS THSLLPGTEN SGYFRGSYSN SPSNPVNSRA
160 170 180 190 200
NQDFSALMRS SYHCAMNNEN ARLLTFQTWP LTFLSPTDLA KAGFYYIGPG
210 220 230 240 250
DRVACFACGG KLSNWEPKDN AMSEHLRHFP KCPFIENQLQ DTSRYTVSNL
260 270 280 290 300
SMQTHAARFK TFFNWPSSVL VNPEQLASAG FYYVGNSDDV KCFCCDGGLR
310 320 330 340 350
CWESGDDPWV QHAKWFPRCE YLIRIKGQEF IRQVQASYPH LLEQLLSTSD
360 370 380 390 400
SPGDENAESS IIHFEPGEDH SEDAIMMNTP VINAAVEMGF SRSLVKQTVQ
410 420 430 440 450
RKILATGENY RLVNDLVLDL LNAEDEIREE ERERATEEKE SNDLLLIRKN
460 470 480 490 500
RMALFQHLTC VIPILDSLLT AGIINEQEHD VIKQKTQTSL QARELIDTIL
510 520 530 540 550
VKGNIAATVF RNSLQEAEAV LYEHLFVQQD IKYIPTEDVS DLPVEEQLRR
560 570 580 590 600
LQEERTCKVC MDKEVSIVFI PCGHLVVCKD CAPSLRKCPI CRSTIKGTVR

TFLS
Length:604
Mass (Da):68,372
Last modified:November 1, 1997 - v2
Checksum:i8581A00BA9AAB4A7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181N → Y in AAC83232. (PubMed:10233894)Curated
Sequence conflicti119 – 1191N → H in AAC50371. (PubMed:8552191)Curated
Sequence conflicti153 – 1531D → E in AAC50371. (PubMed:8552191)Curated
Sequence conflicti163 – 1631H → P in AAC50371. (PubMed:8552191)Curated
Sequence conflicti165 – 1651A → P in AAC50371. (PubMed:8552191)Curated
Sequence conflicti191 – 1911K → R in AAC50371. (PubMed:8552191)Curated
Sequence conflicti364 – 3641F → L in AAC50371. (PubMed:8552191)Curated
Sequence conflicti552 – 5521Q → P in AAC50371. (PubMed:8552191)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti260 – 2601K → R.1 Publication
Corresponds to variant rs2276113 [ dbSNP | Ensembl ].
VAR_021069
Natural varianti386 – 3861V → M.
Corresponds to variant rs12222256 [ dbSNP | Ensembl ].
VAR_049536
Natural varianti401 – 4011R → K.1 Publication
Corresponds to variant rs17881197 [ dbSNP | Ensembl ].
VAR_021070

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L49432 mRNA. Translation: AAC41943.1.
U45878 mRNA. Translation: AAC50371.1.
U37546 mRNA. Translation: AAC50507.1.
AF070674 mRNA. Translation: AAC83232.1.
AY764389 Genomic DNA. Translation: AAU88144.1.
BC037420 mRNA. Translation: AAH37420.1.
AF178945 Genomic DNA. Translation: AAG09369.1.
CCDSiCCDS8315.1.
PIRiS68449.
RefSeqiNP_001156.1. NM_001165.4.
NP_892007.1. NM_182962.2.
UniGeneiHs.127799.

Genome annotation databases

EnsembliENST00000263464; ENSP00000263464; ENSG00000023445.
ENST00000532808; ENSP00000432907; ENSG00000023445.
ENST00000615299; ENSP00000481903; ENSG00000023445.
GeneIDi330.
KEGGihsa:330.
UCSCiuc001pgx.3. human.

Polymorphism databases

DMDMi2497236.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L49432 mRNA. Translation: AAC41943.1 .
U45878 mRNA. Translation: AAC50371.1 .
U37546 mRNA. Translation: AAC50507.1 .
AF070674 mRNA. Translation: AAC83232.1 .
AY764389 Genomic DNA. Translation: AAU88144.1 .
BC037420 mRNA. Translation: AAH37420.1 .
AF178945 Genomic DNA. Translation: AAG09369.1 .
CCDSi CCDS8315.1.
PIRi S68449.
RefSeqi NP_001156.1. NM_001165.4.
NP_892007.1. NM_182962.2.
UniGenei Hs.127799.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2UVL X-ray 1.91 A/B 244-337 [» ]
3EB5 X-ray 2.00 A 536-604 [» ]
3EB6 X-ray 3.40 A 536-604 [» ]
3M0A X-ray 2.61 D 26-99 [» ]
3M0D X-ray 2.80 D 26-99 [» ]
ProteinModelPortali Q13489.
SMRi Q13489. Positions 26-98, 165-235, 244-604.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106827. 69 interactions.
DIPi DIP-33720N.
IntActi Q13489. 36 interactions.
MINTi MINT-216139.
STRINGi 9606.ENSP00000263464.

Chemistry

BindingDBi Q13489.
ChEMBLi CHEMBL3038465.

Protein family/group databases

MEROPSi I32.003.

PTM databases

PhosphoSitei Q13489.

Polymorphism databases

DMDMi 2497236.

Proteomic databases

MaxQBi Q13489.
PaxDbi Q13489.
PRIDEi Q13489.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263464 ; ENSP00000263464 ; ENSG00000023445 .
ENST00000532808 ; ENSP00000432907 ; ENSG00000023445 .
ENST00000615299 ; ENSP00000481903 ; ENSG00000023445 .
GeneIDi 330.
KEGGi hsa:330.
UCSCi uc001pgx.3. human.

Organism-specific databases

CTDi 330.
GeneCardsi GC11P102188.
HGNCi HGNC:591. BIRC3.
HPAi HPA002317.
MIMi 601721. gene.
neXtProti NX_Q13489.
Orphaneti 52417. MALT lymphoma.
PharmGKBi PA25360.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG243347.
GeneTreei ENSGT00500000044782.
HOGENOMi HOG000232059.
HOVERGENi HBG004848.
InParanoidi Q13489.
KOi K16060.
OMAi ENSGYFS.
OrthoDBi EOG78H3TF.
PhylomeDBi Q13489.
TreeFami TF105356.

Enzyme and pathway databases

Reactomei REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinki Q13489.

Miscellaneous databases

ChiTaRSi BIRC3. human.
EvolutionaryTracei Q13489.
GeneWikii Baculoviral_IAP_repeat-containing_protein_3.
GenomeRNAii 330.
NextBioi 1359.
PMAP-CutDB Q13489.
PROi Q13489.
SOURCEi Search...

Gene expression databases

Bgeei Q13489.
CleanExi HS_BIRC3.
ExpressionAtlasi Q13489. baseline and differential.
Genevestigatori Q13489.

Family and domain databases

Gene3Di 1.10.1170.10. 4 hits.
1.10.533.10. 1 hit.
InterProi IPR001370. BIR.
IPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR001841. Znf_RING.
[Graphical view ]
Pfami PF00653. BIR. 3 hits.
PF00619. CARD. 1 hit.
[Graphical view ]
SMARTi SM00238. BIR. 3 hits.
SM00114. CARD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
PROSITEi PS01282. BIR_REPEAT_1. 3 hits.
PS50143. BIR_REPEAT_2. 3 hits.
PS50209. CARD. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins."
    Rothe M., Pan M.-G., Henzel W.J., Ayres T.M., Goeddel D.V.
    Cell 83:1243-1252(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes."
    Liston P., Roy N., Tamai K., Lefebvre C., Baird S., Cherton-Horvat G., Farahani R., McLean M., Ikeda J., Mackenzie A., Korneluk R.G.
    Nature 379:349-353(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors."
    Uren A.G., Pakusch M., Hawkins C.J., Puls K.L., Vaux D.L.
    Proc. Natl. Acad. Sci. U.S.A. 93:4974-4978(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal liver.
  4. "Vascular endothelial genes that are responsive to tumor necrosis factor-alpha in vitro are expressed in atherosclerotic lesions, including inhibitor of apoptosis protein-1, stannin, and two novel genes."
    Horrevoets A.J.G., Fontijn R.D., van Zonneveld A.J., de Vries C.J.M., ten Cate J.W., Pannekoek H.
    Blood 93:3418-3431(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. NIEHS SNPs program
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-260 AND LYS-401.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lymph.
  7. "Structure of the MLT gene and molecular characterization of the genomic breakpoint junctions in the t(11;18)(q21;q21) of marginal zone B-cell lymphomas of MALT type."
    Baens M., Steyls A., Dierlamm J., De Wolf-Peeters C., Marynen P.
    Genes Chromosomes Cancer 29:281-291(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-441.
  8. "cIAP1 Localizes to the nuclear compartment and modulates the cell cycle."
    Samuel T., Okada K., Hyer M., Welsh K., Zapata J.M., Reed J.C.
    Cancer Res. 65:210-218(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "IAPs: more than just inhibitors of apoptosis proteins."
    Dubrez-Daloz L., Dupoux A., Cartier J.
    Cell Cycle 7:1036-1046(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  10. "To fight or die - inhibitor of apoptosis proteins at the crossroad of innate immunity and death."
    Lopez J., Meier P.
    Curr. Opin. Cell Biol. 22:872-881(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  11. "IAPs: from caspase inhibitors to modulators of NF-kappaB, inflammation and cancer."
    Gyrd-Hansen M., Meier P.
    Nat. Rev. Cancer 10:561-574(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  12. "Inhibitor of apoptosis (IAP) proteins in regulation of inflammation and innate immunity."
    Damgaard R.B., Gyrd-Hansen M.
    Discov. Med. 11:221-231(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  13. "The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2."
    Mei Y., Hahn A.A., Hu S., Yang X.
    J. Biol. Chem. 286:35380-35387(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH USP19.
  14. "cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4)."
    Bertrand M.J., Lippens S., Staes A., Gilbert B., Roelandt R., De Medts J., Gevaert K., Declercq W., Vandenabeele P.
    PLoS ONE 6:E22356-E22356(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE UBIQUITINATION OF RIPK1; RIPK2; RIPK3 AND RIPK4, INTERACTION WITH RIPK1; RIPK2; RIPK3 AND RIPK4.
  15. Cited for: REVIEW ON FUNCTION.
  16. "IKKepsilon-mediated tumorigenesis requires K63-linked polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase complex."
    Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.
    Cell Rep. 3:724-733(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IKBKE UBIQUITINATION.

Entry informationi

Entry nameiBIRC3_HUMAN
AccessioniPrimary (citable) accession number: Q13489
Secondary accession number(s): Q16628, Q9HC27, Q9UP46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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