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Q13075

- BIRC1_HUMAN

UniProt

Q13075 - BIRC1_HUMAN

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Protein

Baculoviral IAP repeat-containing protein 1

Gene
NAIP, BIRC1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Anti-apoptotic protein which acts by inhibiting the activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in pathological conditions. Prevents motor-neuron apoptosis induced by a variety of signals. Possible role in the prevention of spinal muscular atrophy that seems to be caused by inappropriate persistence of motor-neuron apoptosis: mutated or deleted forms of NAIP have been found in individuals with severe spinal muscular atrophy.6 Publications
Acts as a sensor component of the NLRC4 inflammasome that specifically recognizes and binds needle protein CprI from pathogenic bacteria C.violaceum. Association of pathogenic bacteria proteins drives in turn drive assembly and activation of the NLRC4 inflammasome, promoting caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria such as C.violaceum and L.pneumophila.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi315 – 3151Zinc
Metal bindingi318 – 3181Zinc
Metal bindingi335 – 3351Zinc
Metal bindingi342 – 3421Zinc
Binding sitei476 – 4761ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. nucleoside-triphosphatase activity Source: InterPro
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. inflammatory response Source: UniProtKB-KW
  2. innate immune response Source: UniProtKB-KW
  3. negative regulation of apoptotic process Source: UniProtKB
  4. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  5. negative regulation of neuron apoptotic process Source: UniProtKB
  6. nervous system development Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Thiol protease inhibitor

Keywords - Biological processi

Apoptosis, Immunity, Inflammatory response, Innate immunity

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ13075.

Protein family/group databases

MEROPSiI32.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Baculoviral IAP repeat-containing protein 1
Alternative name(s):
Neuronal apoptosis inhibitory protein
Gene namesi
Name:NAIP
Synonyms:BIRC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:7634. NAIP.

Subcellular locationi

GO - Cellular componenti

  1. basolateral plasma membrane Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi476 – 4761K → T: Prevents the proper cleavage of pro-CASP9, but does not inhibit the cleavage of pro-CASP3 by CASP9. 1 Publication

Organism-specific databases

Orphaneti83330. Proximal spinal muscular atrophy type 1.
83418. Proximal spinal muscular atrophy type 2.
83419. Proximal spinal muscular atrophy type 3.
PharmGKBiPA162396805.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14031403Baculoviral IAP repeat-containing protein 1PRO_0000122341Add
BLAST

Proteomic databases

PaxDbiQ13075.
PRIDEiQ13075.

PTM databases

PhosphoSiteiQ13075.

Expressioni

Tissue specificityi

Expressed in motor neurons, but not in sensory neurons. Found in liver and placenta, and to a lesser extent in spinal cord.

Gene expression databases

ArrayExpressiQ13075.
BgeeiQ13075.
CleanExiHS_NAIP.
GenevestigatoriQ13075.

Organism-specific databases

HPAiHPA042438.

Interactioni

Subunit structurei

Interacts (via NACHT domain) with APAF1 (via CARD and NACHT domains). Interacts with C.violaceum needle protein CprI.2 Publications

Protein-protein interaction databases

BioGridi110752. 8 interactions.
DIPiDIP-59150N.
IntActiQ13075. 2 interactions.
STRINGi9606.ENSP00000194097.

Structurei

Secondary structure

1
1403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi159 – 1646
Helixi165 – 1684
Helixi171 – 1733
Helixi178 – 1836
Beta strandi186 – 1883
Beta strandi195 – 1973
Turni198 – 2003
Beta strandi203 – 2064
Helixi213 – 2208
Helixi225 – 2317

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VM5X-ray1.80A141-244[»]
ProteinModelPortaliQ13075.
SMRiQ13075. Positions 60-129, 140-244, 278-345, 451-929, 1072-1113, 1155-1370.

Miscellaneous databases

EvolutionaryTraceiQ13075.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati60 – 12768BIR 1Add
BLAST
Repeati159 – 22769BIR 2Add
BLAST
Repeati278 – 34568BIR 3Add
BLAST
Domaini464 – 758295NACHTAdd
BLAST

Domaini

Both the BIR and NACHT domains are essential for effective inhibition of pro-CASP9 cleavage. BIR3 domain binds to procaspase-9 and the NACHT domain interacts with the NACHT domain of APAF1 forming a bridge between pro-CASP9 and APAF1.1 Publication

Sequence similaritiesi

Contains 3 BIR repeats.
Contains 1 NACHT domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG291696.
HOGENOMiHOG000236326.
HOVERGENiHBG050689.
InParanoidiQ13075.
KOiK12807.
OMAiDISRHIP.
PhylomeDBiQ13075.
TreeFamiTF105356.

Family and domain databases

Gene3Di1.10.1170.10. 3 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR001370. BIR.
IPR007111. NACHT_NTPase.
IPR028789. Naip.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR10044:SF94. PTHR10044:SF94. 1 hit.
PfamiPF00653. BIR. 3 hits.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00238. BIR. 3 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS01282. BIR_REPEAT_1. 3 hits.
PS50143. BIR_REPEAT_2. 3 hits.
PS50837. NACHT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13075-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MATQQKASDE RISQFDHNLL PELSALLGLD AVQLAKELEE EEQKERAKMQ     50
KGYNSQMRSE AKRLKTFVTY EPYSSWIPQE MAAAGFYFTG VKSGIQCFCC 100
SLILFGAGLT RLPIEDHKRF HPDCGFLLNK DVGNIAKYDI RVKNLKSRLR 150
GGKMRYQEEE ARLASFRNWP FYVQGISPCV LSEAGFVFTG KQDTVQCFSC 200
GGCLGNWEEG DDPWKEHAKW FPKCEFLRSK KSSEEITQYI QSYKGFVDIT 250
GEHFVNSWVQ RELPMASAYC NDSIFAYEEL RLDSFKDWPR ESAVGVAALA 300
KAGLFYTGIK DIVQCFSCGG CLEKWQEGDD PLDDHTRCFP NCPFLQNMKS 350
SAEVTPDLQS RGELCELLET TSESNLEDSI AVGPIVPEMA QGEAQWFQEA 400
KNLNEQLRAA YTSASFRHMS LLDISSDLAT DHLLGCDLSI ASKHISKPVQ 450
EPLVLPEVFG NLNSVMCVEG EAGSGKTVLL KKIAFLWASG CCPLLNRFQL 500
VFYLSLSSTR PDEGLASIIC DQLLEKEGSV TEMCVRNIIQ QLKNQVLFLL 550
DDYKEICSIP QVIGKLIQKN HLSRTCLLIA VRTNRARDIR RYLETILEIK 600
AFPFYNTVCI LRKLFSHNMT RLRKFMVYFG KNQSLQKIQK TPLFVAAICA 650
HWFQYPFDPS FDDVAVFKSY MERLSLRNKA TAEILKATVS SCGELALKGF 700
FSCCFEFNDD DLAEAGVDED EDLTMCLMSK FTAQRLRPFY RFLSPAFQEF 750
LAGMRLIELL DSDRQEHQDL GLYHLKQINS PMMTVSAYNN FLNYVSSLPS 800
TKAGPKIVSH LLHLVDNKES LENISENDDY LKHQPEISLQ MQLLRGLWQI 850
CPQAYFSMVS EHLLVLALKT AYQSNTVAAC SPFVLQFLQG RTLTLGALNL 900
QYFFDHPESL SLLRSIHFPI RGNKTSPRAH FSVLETCFDK SQVPTIDQDY 950
ASAFEPMNEW ERNLAEKEDN VKSYMDMQRR ASPDLSTGYW KLSPKQYKIP 1000
CLEVDVNDID VVGQDMLEIL MTVFSASQRI ELHLNHSRGF IESIRPALEL 1050
SKASVTKCSI SKLELSAAEQ ELLLTLPSLE SLEVSGTIQS QDQIFPNLDK 1100
FLCLKELSVD LEGNINVFSV IPEEFPNFHH MEKLLIQISA EYDPSKLVKL 1150
IQNSPNLHVF HLKCNFFSDF GSLMTMLVSC KKLTEIKFSD SFFQAVPFVA 1200
SLPNFISLKI LNLEGQQFPD EETSEKFAYI LGSLSNLEEL ILPTGDGIYR 1250
VAKLIIQQCQ QLHCLRVLSF FKTLNDDSVV EIAKVAISGG FQKLENLKLS 1300
INHKITEEGY RNFFQALDNM PNLQELDISR HFTECIKAQA TTVKSLSQCV 1350
LRLPRLIRLN MLSWLLDADD IALLNVMKER HPQSKYLTIL QKWILPFSPI 1400
IQK 1403
Length:1,403
Mass (Da):159,582
Last modified:May 30, 2006 - v3
Checksum:iC1CE163D55900C6D
GO
Isoform 2 (identifier: Q13075-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MATQQKASDE...GYNSQMRSEA → MPLHIGDFVW...IRLELWINLR
     62-223: Missing.

Show »
Length:1,241
Mass (Da):141,329
Checksum:i51648FB32357B99A
GO

Sequence cautioni

The sequence AAC62261.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti535 – 5351V → M.5 Publications
VAR_026477

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6161MATQQ…MRSEA → MPLHIGDFVWDSKVHSLQSS LNIFSLLPTKGRTEHLFFSH ILSFHWPAFSSIRLELWINL R in isoform 2. VSP_047196Add
BLAST
Alternative sequencei62 – 223162Missing in isoform 2. VSP_047197Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti386 – 3872VP → ST in AAA64504. 1 Publication
Sequence conflicti553 – 5531Y → H in AAA64504. 1 Publication
Sequence conflicti567 – 5682IQ → FK in BAD92360. 1 Publication
Sequence conflicti919 – 9191P → S in BAD92360. 1 Publication
Sequence conflicti1066 – 10661S → T in BAD92360. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U19251 mRNA. Translation: AAC52045.1.
U80017 Genomic DNA. Translation: AAC52047.1.
AC005031 Genomic DNA. Translation: AAC62261.1. Sequence problems.
AC044797 Genomic DNA. No translation available.
BC136273 mRNA. Translation: AAI36274.1.
AB048534 mRNA. Translation: BAB87181.1.
AH003063 mRNA. Translation: AAA64504.1.
AB209123 mRNA. Translation: BAD92360.1.
CCDSiCCDS4009.1. [Q13075-1]
CCDS43327.1. [Q13075-2]
RefSeqiNP_004527.2. NM_004536.2. [Q13075-1]
NP_075043.1. NM_022892.1. [Q13075-2]
UniGeneiHs.654500.
Hs.710305.

Genome annotation databases

EnsembliENST00000194097; ENSP00000443944; ENSG00000249437. [Q13075-1]
ENST00000503719; ENSP00000424913; ENSG00000249437. [Q13075-2]
ENST00000517649; ENSP00000428657; ENSG00000249437. [Q13075-1]
ENST00000523981; ENSP00000428363; ENSG00000249437. [Q13075-2]
ENST00000576435; ENSP00000458196; ENSG00000263062.
ENST00000576583; ENSP00000459350; ENSG00000263062.
GeneIDi4671.
KEGGihsa:4671.
UCSCiuc003jyj.1. human. [Q13075-1]

Polymorphism databases

DMDMi109940027.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U19251 mRNA. Translation: AAC52045.1 .
U80017 Genomic DNA. Translation: AAC52047.1 .
AC005031 Genomic DNA. Translation: AAC62261.1 . Sequence problems.
AC044797 Genomic DNA. No translation available.
BC136273 mRNA. Translation: AAI36274.1 .
AB048534 mRNA. Translation: BAB87181.1 .
AH003063 mRNA. Translation: AAA64504.1 .
AB209123 mRNA. Translation: BAD92360.1 .
CCDSi CCDS4009.1. [Q13075-1 ]
CCDS43327.1. [Q13075-2 ]
RefSeqi NP_004527.2. NM_004536.2. [Q13075-1 ]
NP_075043.1. NM_022892.1. [Q13075-2 ]
UniGenei Hs.654500.
Hs.710305.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2VM5 X-ray 1.80 A 141-244 [» ]
ProteinModelPortali Q13075.
SMRi Q13075. Positions 60-129, 140-244, 278-345, 451-929, 1072-1113, 1155-1370.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110752. 8 interactions.
DIPi DIP-59150N.
IntActi Q13075. 2 interactions.
STRINGi 9606.ENSP00000194097.

Protein family/group databases

MEROPSi I32.001.

PTM databases

PhosphoSitei Q13075.

Polymorphism databases

DMDMi 109940027.

Proteomic databases

PaxDbi Q13075.
PRIDEi Q13075.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000194097 ; ENSP00000443944 ; ENSG00000249437 . [Q13075-1 ]
ENST00000503719 ; ENSP00000424913 ; ENSG00000249437 . [Q13075-2 ]
ENST00000517649 ; ENSP00000428657 ; ENSG00000249437 . [Q13075-1 ]
ENST00000523981 ; ENSP00000428363 ; ENSG00000249437 . [Q13075-2 ]
ENST00000576435 ; ENSP00000458196 ; ENSG00000263062 .
ENST00000576583 ; ENSP00000459350 ; ENSG00000263062 .
GeneIDi 4671.
KEGGi hsa:4671.
UCSCi uc003jyj.1. human. [Q13075-1 ]

Organism-specific databases

CTDi 4671.
GeneCardsi GC05M070267.
H-InvDB HIX0164257.
HGNCi HGNC:7634. NAIP.
HPAi HPA042438.
MIMi 600355. gene.
neXtProti NX_Q13075.
Orphaneti 83330. Proximal spinal muscular atrophy type 1.
83418. Proximal spinal muscular atrophy type 2.
83419. Proximal spinal muscular atrophy type 3.
PharmGKBi PA162396805.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG291696.
HOGENOMi HOG000236326.
HOVERGENi HBG050689.
InParanoidi Q13075.
KOi K12807.
OMAi DISRHIP.
PhylomeDBi Q13075.
TreeFami TF105356.

Enzyme and pathway databases

SignaLinki Q13075.

Miscellaneous databases

ChiTaRSi NAIP. human.
EvolutionaryTracei Q13075.
GeneWikii NAIP_(gene).
GenomeRNAii 4671.
NextBioi 18000.
PROi Q13075.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13075.
Bgeei Q13075.
CleanExi HS_NAIP.
Genevestigatori Q13075.

Family and domain databases

Gene3Di 1.10.1170.10. 3 hits.
3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR001370. BIR.
IPR007111. NACHT_NTPase.
IPR028789. Naip.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR10044:SF94. PTHR10044:SF94. 1 hit.
Pfami PF00653. BIR. 3 hits.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
SM00238. BIR. 3 hits.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS01282. BIR_REPEAT_1. 3 hits.
PS50143. BIR_REPEAT_2. 3 hits.
PS50837. NACHT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-535, POSSIBLE ROLE IN THE PROTECTION FROM SPINAL MUSCULAR ATROPHY.
    Tissue: Fetal brain.
  2. "Sequence of a 131-kb region of 5q13.1 containing the spinal muscular atrophy candidate genes SMN and NAIP."
    Chen Q., Baird S.D., Mahadevan M., Besner-Johnston A., Farahani R., Xuan J.-Y., Kang X., Lefebvre C., Ikeda J.-E., Korneluk R.G., MacKenzie A.E.
    Genomics 48:121-127(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, VARIANT MET-535.
    Tissue: Brain.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT MET-535.
  4. "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), VARIANT MET-535.
    Tissue: Testis.
  5. "Functional human NAIP promoter transcription regulatory elements for the NAIP and PsiNAIP genes."
    Xu M., Okada T., Sakai H., Miyamoto N., Yanagisawa Y., MacKenzie A.E., Hadano S., Ikeda J.-E.
    Biochim. Biophys. Acta 1574:35-50(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1160 (ISOFORM 2), VARIANT MET-535.
  6. "A provisional transcript map of the spinal muscular atrophy (SMA) critical region."
    van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C., van Ommen G.J.B., Buys C.H.C.M.
    Eur. J. Hum. Genet. 3:87-95(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 386-623 (ISOFORM 1/2).
    Tissue: Pre-B cell.
  7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 567-1403 (ISOFORM 1/2).
    Tissue: Brain.
  8. "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: FUNCTION.
    Tissue: Liver.
  9. "The neuronal apoptosis inhibitory protein is a direct inhibitor of caspases 3 and 7."
    Maier J.K., Lahoua Z., Gendron N.H., Fetni R., Johnston A., Davoodi J., Rasper D., Roy S., Slack R.S., Nicholson D.W., MacKenzie A.E.
    J. Neurosci. 22:2035-2043(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  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. "Integrity of ATP binding site is essential for effective inhibition of the intrinsic apoptosis pathway by NAIP."
    Karimpour S., Davoodi J., Ghahremani M.H.
    Biochem. Biophys. Res. Commun. 407:158-162(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH APAF1, DOMAIN BIR3 AND NACHT, MUTAGENESIS OF LYS-476.
  12. "The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus."
    Zhao Y., Yang J., Shi J., Gong Y.N., Lu Q., Xu H., Liu L., Shao F.
    Nature 477:596-600(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INFLAMMASOME, INTERACTION WITH C.VIOLACEUM CPRI.
  13. "The human apoptosis inhibitor NAIP induces pyroptosis in macrophages infected with Legionella pneumophila."
    Katagiri N., Shobuike T., Chang B., Kukita A., Miyamoto H.
    Microbes Infect. 14:1123-1132(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INFLAMMASOME.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 141-244 IN COMPLEX WITH ZINC IONS.

Entry informationi

Entry nameiBIRC1_HUMAN
AccessioniPrimary (citable) accession number: Q13075
Secondary accession number(s): B9EG72
, E9PHD1, O75857, Q13730, Q59GI6, Q8TDZ4, Q99796
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2006
Last modified: September 3, 2014
This is version 132 of the entry and version 3 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 5
    Human chromosome 5: 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

Dasty 3

Similar proteinsi