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Q13490 (BIRC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Baculoviral IAP repeat-containing protein 2

EC=6.3.2.-
Alternative name(s):
C-IAP1
IAP homolog B
Inhibitor of apoptosis protein 2
Short name=IAP-2
Short name=hIAP-2
Short name=hIAP2
RING finger protein 48
TNFR2-TRAF-signaling complex protein 2
Gene names
Name:BIRC2
Synonyms:API1, IAP2, MIHB, RNF48
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length618 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, 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. Ref.8 Ref.9 Ref.14 Ref.17 Ref.19 Ref.21

Enzyme regulation

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. Ref.18 Ref.24

Subunit structure

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. Ref.8 Ref.17 Ref.18 Ref.19 Ref.23

Subcellular location

Cytoplasm. Nucleus. 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. Ref.8 Ref.17

Tissue specificity

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.

Domain

The BIR domains mediate nuclear localization. Ref.24

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. Ref.24

Post-translational modification

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

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
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Ligase
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNIK/NF-kappaB signaling

Traceable author statement Ref.15. Source: UniProtKB

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

cell surface receptor signaling pathway

Traceable author statement Ref.1. Source: ProtInc

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

necroptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from direct assay PubMed 21525013. Source: UniProtKB

placenta development

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of protein K48-linked ubiquitination

Inferred from direct assay Ref.19. Source: UniProtKB

positive regulation of protein K63-linked ubiquitination

Inferred from direct assay Ref.19. Source: UniProtKB

positive regulation of protein monoubiquitination

Inferred from direct assay Ref.19. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 11907583. Source: UniProtKB

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

protein polyubiquitination

Inferred from direct assay PubMed 11907583. Source: UniProtKB

regulation of RIG-I signaling pathway

Traceable author statement Ref.13. Source: UniProtKB

regulation of cell cycle

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of cell differentiation

Traceable author statement Ref.10. Source: UniProtKB

regulation of cell proliferation

Traceable author statement Ref.10. Source: UniProtKB

regulation of cysteine-type endopeptidase activity

Traceable author statement Ref.15. Source: UniProtKB

regulation of inflammatory response

Traceable author statement Ref.16. Source: UniProtKB

regulation of necroptotic process

Inferred from mutant phenotype PubMed 21737330. Source: UniProtKB

regulation of nucleotide-binding oligomerization domain containing signaling pathway

Traceable author statement Ref.13. Source: UniProtKB

regulation of toll-like receptor signaling pathway

Traceable author statement Ref.13. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCD40 receptor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

XY body

Inferred from electronic annotation. Source: Ensembl

cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

membrane raft

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functiontranscription coactivator activity

Inferred from mutant phenotype Ref.17. Source: UniProtKB

ubiquitin-protein ligase activity

Inferred from direct assay PubMed 11907583Ref.19. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.23PubMed 20447407. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13490-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13490-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 618618Baculoviral IAP repeat-containing protein 2
PRO_0000122347

Regions

Repeat46 – 11368BIR 1
Repeat184 – 25067BIR 2
Repeat269 – 33668BIR 3
Domain453 – 54391CARD
Zinc finger571 – 60636RING-type

Sites

Metal binding3061Zinc
Metal binding3091Zinc
Metal binding3261Zinc
Metal binding3331Zinc

Natural variations

Alternative sequence1 – 4949Missing in isoform 2.
VSP_045314
Natural variant4531M → I.
Corresponds to variant rs34749508 [ dbSNP | Ensembl ].
VAR_049535
Natural variant4531M → V. Ref.4
VAR_025016
Natural variant5061A → V. Ref.4
Corresponds to variant rs34510872 [ dbSNP | Ensembl ].
VAR_025017
Natural variant5491P → S. Ref.4
Corresponds to variant rs35494784 [ dbSNP | Ensembl ].
VAR_025018

Experimental info

Sequence conflict1571S → P in AAC50372. Ref.2
Sequence conflict3081C → G in AAC50372. Ref.2
Sequence conflict4141Q → L in AAC50372. Ref.2
Sequence conflict5141L → W in AAC50372. Ref.2

Secondary structure

................................................................................. 618
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: C1778D328063586D

FASTA61869,900
        10         20         30         40         50         60 
MHKTASQRLF PGPSYQNIKS IMEDSTILSD WTNSNKQKMK YDFSCELYRM STYSTFPAGV 

        70         80         90        100        110        120 
PVSERSLARA GFYYTGVNDK VKCFCCGLML DNWKLGDSPI QKHKQLYPSC SFIQNLVSAS 

       130        140        150        160        170        180 
LGSTSKNTSP MRNSFAHSLS PTLEHSSLFS GSYSSLSPNP LNSRAVEDIS SSRTNPYSYA 

       190        200        210        220        230        240 
MSTEEARFLT YHMWPLTFLS PSELARAGFY YIGPGDRVAC FACGGKLSNW EPKDDAMSEH 

       250        260        270        280        290        300 
RRHFPNCPFL ENSLETLRFS ISNLSMQTHA ARMRTFMYWP SSVPVQPEQL ASAGFYYVGR 

       310        320        330        340        350        360 
NDDVKCFCCD GGLRCWESGD DPWVEHAKWF PRCEFLIRMK GQEFVDEIQG RYPHLLEQLL 

       370        380        390        400        410        420 
STSDTTGEEN ADPPIIHFGP GESSSEDAVM MNTPVVKSAL EMGFNRDLVK QTVQSKILTT 

       430        440        450        460        470        480 
GENYKTVNDI VSALLNAEDE KREEEKEKQA EEMASDDLSL IRKNRMALFQ QLTCVLPILD 

       490        500        510        520        530        540 
NLLKANVINK QEHDIIKQKT QIPLQARELI DTILVKGNAA ANIFKNCLKE IDSTLYKNLF 

       550        560        570        580        590        600 
VDKNMKYIPT EDVSGLSLEE QLRRLQEERT CKVCMDKEVS VVFIPCGHLV VCQECAPSLR 

       610 
KCPICRGIIK GTVRTFLS 

« Hide

Isoform 2 [UniParc].

Checksum: B678A4C2069F0A22
Show »

FASTA56964,098

References

« Hide 'large scale' references
[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] (ISOFORM 1).
[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] (ISOFORM 1).
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] (ISOFORM 1).
Tissue: Fetal liver.
[4]NIEHS SNPs program
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-453; VAL-506 AND SER-549.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Thymus.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 1).
Tissue: Testis and Uterus.
[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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BIRC5/SURVIVIN.
[9]"c-IAP1 cooperates with Myc by acting as a ubiquitin ligase for Mad1."
Xu L., Zhu J., Hu X., Zhu H., Kim H.T., LaBaer J., Goldberg A., Yuan J.
Mol. Cell 28:914-922(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE UBIQUITINATION OF MXD1/MAD1.
[10]"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.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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.
[14]"Systematic in vivo RNAi analysis identifies IAPs as NEDD8-E3 ligases."
Broemer M., Tenev T., Rigbolt K.T., Hempel S., Blagoev B., Silke J., Ditzel M., Meier P.
Mol. Cell 40:810-822(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE OF THE NEDD8 CONJUGATION PATHWAY.
[15]"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.
[16]"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.
[17]"Cellular inhibitor of apoptosis protein-1 (cIAP1) can regulate E2F1 transcription factor-mediated control of cyclin transcription."
Cartier J., Berthelet J., Marivin A., Gemble S., Edmond V., Plenchette S., Lagrange B., Hammann A., Dupoux A., Delva L., Eymin B., Solary E., Dubrez L.
J. Biol. Chem. 286:26406-26417(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH E2F1 AND TRAF2, SUBCELLULAR LOCATION.
[18]"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.
[19]"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.
[20]"IAPs: guardians of RIPK1."
Darding M., Meier P.
Cell Death Differ. 19:58-66(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[21]"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.
[22]"Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat."
Hinds M.G., Norton R.S., Vaux D.L., Day C.L.
Nat. Struct. Biol. 6:648-651(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 266-363.
[23]"The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9."
Kulathila R., Vash B., Sage D., Cornell-Kennon S., Wright K., Koehn J., Stams T., Clark K., Price A.
Acta Crystallogr. D 65:58-66(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 260-352 IN COMPLEXES WITH ZINC IONS; DIABLO AND CASP9 PEPTIDES, SUBUNIT.
[24]"CARD-mediated autoinhibition of cIAP1's E3 ligase activity suppresses cell proliferation and migration."
Lopez J., John S.W., Tenev T., Rautureau G.J., Hinds M.G., Francalanci F., Wilson R., Broemer M., Santoro M.M., Day C.L., Meier P.
Mol. Cell 42:569-583(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 435-562, DOMAIN CARD, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L49431 mRNA. Translation: AAC41942.1.
U45879 mRNA. Translation: AAC50372.1.
U37547 mRNA. Translation: AAC50508.1.
AK303197 mRNA. Translation: BAG64288.1.
AP000942 Genomic DNA. No translation available.
DQ068066 Genomic DNA. Translation: AAY46158.1.
BC016174 mRNA. Translation: AAH16174.1.
BC028578 mRNA. Translation: AAH28578.1.
PIRS68450.
RefSeqNP_001157.1. NM_001166.4.
NP_001243092.1. NM_001256163.1.
NP_001243095.1. NM_001256166.1.
UniGeneHs.696238.
Hs.731943.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QBHNMR-A266-363[»]
2L9MNMR-A435-562[»]
3D9TX-ray1.50A/B260-352[»]
3D9UX-ray2.30A260-352[»]
3M1DX-ray2.00A/B40-119[»]
3MUPX-ray2.60A/B/C/D251-363[»]
3OZ1X-ray3.00A/B/C/D251-363[»]
3T6PX-ray1.90A265-618[»]
3UW4X-ray1.79A266-343[»]
4EB9X-ray2.60A/B/C/D251-363[»]
4HY4X-ray1.25A/B260-352[»]
4HY5X-ray1.75A/B260-352[»]
4LGEX-ray1.55A/B260-352[»]
4LGUX-ray2.00A/B260-352[»]
4MTIX-ray2.15A/B260-352[»]
4MU7X-ray1.79A/B260-352[»]
ProteinModelPortalQ13490.
SMRQ13490. Positions 41-616.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106826. 92 interactions.
IntActQ13490. 55 interactions.
MINTMINT-216174.
STRING9606.ENSP00000227758.

Chemistry

BindingDBQ13490.
ChEMBLCHEMBL5462.

Protein family/group databases

MEROPSI32.002.

PTM databases

PhosphoSiteQ13490.

Polymorphism databases

DMDM2497238.

Proteomic databases

PaxDbQ13490.
PRIDEQ13490.

Protocols and materials databases

DNASU329.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000227758; ENSP00000227758; ENSG00000110330. [Q13490-1]
ENST00000530675; ENSP00000431723; ENSG00000110330. [Q13490-2]
GeneID329.
KEGGhsa:329.
UCSCuc001pgy.4. human. [Q13490-1]

Organism-specific databases

CTD329.
GeneCardsGC11P102252.
HGNCHGNC:590. BIRC2.
HPACAB020661.
HPA005513.
MIM601712. gene.
neXtProtNX_Q13490.
PharmGKBPA25359.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG243347.
HOGENOMHOG000232059.
HOVERGENHBG004848.
InParanoidQ13490.
KOK16060.
OMATYHMWPL.
OrthoDBEOG78H3TF.
PhylomeDBQ13490.
TreeFamTF105356.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
REACT_6900. Immune System.
SignaLinkQ13490.

Gene expression databases

ArrayExpressQ13490.
BgeeQ13490.
CleanExHS_BIRC2.
GenevestigatorQ13490.

Family and domain databases

Gene3D1.10.1170.10. 4 hits.
1.10.533.10. 1 hit.
InterProIPR001370. BIR.
IPR028795. C-IAP1.
IPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR001841. Znf_RING.
[Graphical view]
PANTHERPTHR10044:SF79. PTHR10044:SF79. 1 hit.
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

EvolutionaryTraceQ13490.
GeneWikiBIRC2.
GenomeRNAi329.
NextBio1355.
PMAP-CutDBQ13490.
PROQ13490.
SOURCESearch...

Entry information

Entry nameBIRC2_HUMAN
AccessionPrimary (citable) accession number: Q13490
Secondary accession number(s): B4E026, Q16516, Q4TTG0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM