Inhibitor of apoptosis protein 1
HIAP-1
HIAP1
C-IAP2
TNFR2-TRAF-signaling complex protein 1
IAP homolog C
Apoptosis inhibitor 2
API2
RING finger protein 49

Gene name

	Name:	BIRC3
	Synonyms:	API2, IAP1, MIHC, RNF49

From

Homo sapiens (Human)

[TaxID: 9606]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0092-8674(95)90149-3; PubMed=8548810 [NCBI, ExPASy, EBI, Israel, Japan] Rothe M., Pan M.-G., Henzel W.J., Ayres T.M., Goeddel D.V.; "The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins."; Cell 83:1243-1252(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1038/379349a0; PubMed=8552191 [NCBI, ExPASy, EBI, Israel, Japan] Liston P., Roy N., Tamai K., Lefebvre C., Baird S., Cherton-Horvat G., Farahani R., McLean M., Ikeda J., Mackenzie A., Korneluk R.G.; "Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes."; Nature 379:349-353(1996).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Fetal liver; DOI=10.1073/pnas.93.10.4974; PubMed=8643514 [NCBI, ExPASy, EBI, Israel, Japan] Uren A.G., Pakusch M., Hawkins C.J., Puls K.L., Vaux D.L.; "Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors."; Proc. Natl. Acad. Sci. U.S.A. 93:4974-4978(1996).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=10233894 [NCBI, ExPASy, EBI, Israel, Japan] Horrevoets A.J.G., Fontijn R.D., van Zonneveld A.J., de Vries C.J.M., ten Cate J.W., Pannekoek H.; "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."; Blood 93:3418-3431(1999).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-260 AND LYS-401. NIEHS SNPs program; Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lymph; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-441. DOI=10.1002/1098-2264(2000)9999:9999<::AID-GCC1036>3.0.CO;2-I; PubMed=11066071 [NCBI, ExPASy, EBI, Israel, Japan] Baens M., Steyls A., Dierlamm J., De Wolf-Peeters C., Marynen P.; "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."; Genes Chromosomes Cancer 29:281-291(2000).

Comments

FUNCTION: Apoptotic suppressor. The BIR motifs region interacts with TNF receptor associated factors 1 and 2 (TRAF1 and TRAF2) to form an heteromeric complex, which is then recruited to the tumor necrosis factor receptor 2 (TNFR2).
SUBUNIT: Interacts with SMAC and with PRSS25; these interactions inhibit apoptotic suppressor activity.
INTERACTION:
Q9NR28:DIABLO; NbExp=1; IntAct=EBI-517709, EBI-517508;
Q12933:TRAF2; NbExp=2; IntAct=EBI-517709, EBI-355744;
SUBCELLULAR LOCATION: Cytoplasm (Potential).
TISSUE SPECIFICITY: Highly expressed in fetal lung, and kidney. In the adult, expression is mainly seen in lymphoid tissues, including spleen, thymus and peripheral blood lymphocytes.
DISEASE: 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.
SIMILARITY: Belongs to the IAP family.
SIMILARITY: Contains 3 BIR repeats.
SIMILARITY: Contains 1 CARD domain.
SIMILARITY: Contains 1 RING-type zinc finger.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/BIRC3ID239.html";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/birc3/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L49432; AAC41943.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U45878; AAC50371.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U37546; AAC50507.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF070674; AAC83232.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY764389; AAU88144.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC037420; AAH37420.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF178945; AAG09369.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00013409; -.

PIR

S68449; S68449.

RefSeq

NP_001156.1; -.
NP_892007.1; -.

UniGene

Hs.127799

3D structure databases

PDB

2UVL; X-ray; 1.91 A; A/B=244-337.	[ExPASy / RCSB / EBI]
3EB5; X-ray; 2.00 A; A=536-604.	[ExPASy / RCSB / EBI]
3EB6; X-ray; 3.40 A; A=536-604.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2UVL; -.
3EB5; -.
3EB6; -.

ModBase

Q13489.

Protein-protein interaction databases

IntAct

Q13489; 4.

Protein family/group databases

MEROPS

I32.003; -.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_pathway; Caspase cascade in apoptosis.
ceramidepathway; Ceramide signaling pathway.
hivnefpathway; HIV-1 Nef: Negative effector of Fas and TNF-alpha.
p75ntrpathway; p75(NTR)-mediated signaling.
tnfpathway; TNF receptor signaling pathway.

Organism-specific databases

GC11P101693; -.

HIX0026135; -.

HGNC:591; BIRC3.

HPA002317; -.

601721; gene. [NCBI / EBI]

PharmGKB

PA25360; -.

Gene expression databases

Q13489; -.

Q13489; -.

HS_BIRC3; -.

ENSG00000023445; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004842;	Molecular function: ubiquitin-protein ligase activity (inferred from direct assay from UniProtKB).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006916;	Biological process: anti-apoptosis (traceable author statement from ProtInc).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0007166;	Biological process: cell surface receptor linked signal transduction (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR001315; CARD.
IPR011029; DEATH-like.
IPR001370; Prot_inh_I32_IAP.
IPR018957; Znf_C3HC4_RING-type.
IPR001841; Znf_RING.
IPR017907; Znf_RING_CS.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.533.10; DEATH_like; 1.

Pfam

PF00653; BIR; 3.
PF00619; CARD; 1.
PF00097; zf-C3HC4; 1.
Pfam graphical view of domain structure.

SMART

SM00238; BIR; 3.
SM00114; CARD; 1.
SM00184; RING; 1.
SMART graphical view of domain structure.

PROSITE

PS01282; BIR_REPEAT_1; 3.
PS50143; BIR_REPEAT_2; 3.
PS50209; CARD; 1.
PS00518; ZF_RING_1; FALSE_NEG.
PS50089; ZF_RING_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q13489; -.

Genome annotation databases

Ensembl

ENSG00000023445; Homo sapiens. [Contig view]

GeneID

330; -.

KEGG

hsa:330; -.

Phylogenomic databases

HOGENOM

Q13489; -.

HOVERGEN

Q13489; -.

OMA

Q13489; FFNWPSS.

Other

1359; -.

Q13489; -.

BIRC3; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Apoptosis; Chromosomal rearrangement; Cytoplasm; Metal-binding; Polymorphism; Repeat; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 604`	`604`	`Baculoviral IAP repeat-containing protein 3.`	`PRO_0000122349`
`REPEAT`	`29 96`	`68`	`BIR 1.`
`REPEAT`	`169 235`	`67`	`BIR 2.`
`REPEAT`	`255 322`	`68`	`BIR 3.`
`DOMAIN`	`439 529`	`91`	`CARD.`
`ZN_FING`	`557 592`	`36`	`RING-type.`
`METAL`	`292 292`		`Zinc (By similarity).`
`METAL`	`295 295`		`Zinc (By similarity).`
`METAL`	`312 312`		`Zinc (By similarity).`
`METAL`	`319 319`		`Zinc (By similarity).`
`SITE`	`442 443`	`2`	`Breakpoint for translocation to form BIRC3-MALT1.`
`VARIANT`	`260 260`	`1`	`K -> R (in dbSNP:rs2276113 [NCBI]).`	`VAR_021069 [3D]`
`VARIANT`	`386 386`	`1`	`V -> M (in dbSNP:rs12222256 [NCBI]).`	`VAR_049536`
`VARIANT`	`401 401`	`1`	`R -> K (in dbSNP:rs17881197 [NCBI]).`	`VAR_021070`
`CONFLICT`	`18 18`		`N -> Y (in Ref. 4; AAC83232).`
`CONFLICT`	`119 119`		`N -> H (in Ref. 2; AAC50371).`
`CONFLICT`	`153 153`		`D -> E (in Ref. 2; AAC50371).`
`CONFLICT`	`163 163`		`H -> P (in Ref. 2).`
`CONFLICT`	`165 165`		`A -> P (in Ref. 2).`
`CONFLICT`	`191 191`		`K -> R (in Ref. 2; AAC50371).`
`CONFLICT`	`364 364`		`F -> L (in Ref. 2; AAC50371).`
`CONFLICT`	`552 552`		`Q -> P (in Ref. 2; AAC50371).`
`HELIX`	`250 252`	`3`
`HELIX`	`255 260`	`6`
`HELIX`	`261 264`	`4`
`HELIX`	`273 278`	`6`
`STRAND`	`281 285`	`5`
`TURN`	`286 288`	`3`
`STRAND`	`289 292`	`4`
`TURN`	`293 295`	`3`
`STRAND`	`298 301`	`4`
`HELIX`	`308 315`	`8`
`HELIX`	`320 334`	`15`

Sequence information

Length: 604 AA [This is the length of the unprocessed precursor]

Molecular weight: 68372 Da [This is the MW of the unprocessed precursor]

CRC64: 8581A00BA9AAB4A7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNIVENSIFL SNLMKSANTF ELKYDLSCEL YRMSTYSTFP AGVPVSERSL ARAGFYYTGV 

        70         80         90        100        110        120 
NDKVKCFCCG LMLDNWKRGD SPTEKHKKLY PSCRFVQSLN SVNNLEATSQ PTFPSSVTNS 

       130        140        150        160        170        180 
THSLLPGTEN SGYFRGSYSN SPSNPVNSRA NQDFSALMRS SYHCAMNNEN ARLLTFQTWP 

       190        200        210        220        230        240 
LTFLSPTDLA KAGFYYIGPG DRVACFACGG KLSNWEPKDN AMSEHLRHFP KCPFIENQLQ 

       250        260        270        280        290        300 
DTSRYTVSNL SMQTHAARFK TFFNWPSSVL VNPEQLASAG FYYVGNSDDV KCFCCDGGLR 

       310        320        330        340        350        360 
CWESGDDPWV QHAKWFPRCE YLIRIKGQEF IRQVQASYPH LLEQLLSTSD SPGDENAESS 

       370        380        390        400        410        420 
IIHFEPGEDH SEDAIMMNTP VINAAVEMGF SRSLVKQTVQ RKILATGENY RLVNDLVLDL 

       430        440        450        460        470        480 
LNAEDEIREE ERERATEEKE SNDLLLIRKN RMALFQHLTC VIPILDSLLT AGIINEQEHD 

       490        500        510        520        530        540 
VIKQKTQTSL QARELIDTIL VKGNIAATVF RNSLQEAEAV LYEHLFVQQD IKYIPTEDVS 

       550        560        570        580        590        600 
DLPVEEQLRR LQEERTCKVC MDKEVSIVFI PCGHLVVCKD CAPSLRKCPI CRSTIKGTVR 


TFLS

Q13489 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools