SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q13490

- BIRC2_HUMAN

UniProt

Q13490 - BIRC2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Baculoviral IAP repeat-containing protein 2
Gene
BIRC2, API1, IAP2, MIHB, RNF48
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, 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.6 Publications

Enzyme regulationi

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi306 – 3061Zinc
Metal bindingi309 – 3091Zinc
Metal bindingi326 – 3261Zinc
Metal bindingi333 – 3331Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri571 – 60636RING-type
Add
BLAST

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. protein N-terminus binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. transcription coactivator activity Source: UniProtKB
  5. ubiquitin-protein transferase activity Source: UniProtKB
  6. zinc ion binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  2. NIK/NF-kappaB signaling Source: UniProtKB
  3. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  4. apoptotic process Source: Reactome
  5. cell surface receptor signaling pathway Source: ProtInc
  6. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  7. innate immune response Source: Reactome
  8. necroptotic process Source: Ensembl
  9. negative regulation of apoptotic process Source: UniProtKB
  10. placenta development Source: Ensembl
  11. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  12. positive regulation of protein K48-linked ubiquitination Source: UniProtKB
  13. positive regulation of protein K63-linked ubiquitination Source: UniProtKB
  14. positive regulation of protein monoubiquitination Source: UniProtKB
  15. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  16. protein heterooligomerization Source: Ensembl
  17. protein polyubiquitination Source: UniProtKB
  18. regulation of RIG-I signaling pathway Source: UniProtKB
  19. regulation of apoptotic process Source: UniProtKB
  20. regulation of cell cycle Source: UniProtKB
  21. regulation of cell differentiation Source: UniProtKB
  22. regulation of cell proliferation Source: UniProtKB
  23. regulation of cysteine-type endopeptidase activity Source: UniProtKB
  24. regulation of inflammatory response Source: UniProtKB
  25. regulation of innate immune response Source: UniProtKB
  26. regulation of necroptotic process Source: UniProtKB
  27. regulation of nucleotide-binding oligomerization domain containing signaling pathway Source: UniProtKB
  28. regulation of toll-like receptor signaling pathway Source: UniProtKB
  29. regulation of transcription, DNA-templated Source: UniProtKB-KW
  30. response to cAMP Source: Ensembl
  31. response to ethanol Source: Ensembl
  32. response to hypoxia Source: Ensembl
  33. toll-like receptor 3 signaling pathway Source: Reactome
  34. toll-like receptor 4 signaling pathway Source: Reactome
  35. toll-like receptor signaling pathway Source: Reactome
  36. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Ligase

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinkiQ13490.

Protein family/group databases

MEROPSiI32.002.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:BIRC2
Synonyms:API1, IAP2, MIHB, RNF48
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:590. BIRC2.

Subcellular locationi

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.2 Publications

GO - Cellular componenti

  1. CD40 receptor complex Source: BHF-UCL
  2. XY body Source: Ensembl
  3. cytoplasmic side of plasma membrane Source: BHF-UCL
  4. cytosol Source: Reactome
  5. membrane raft Source: Ensembl
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25359.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 618618Baculoviral IAP repeat-containing protein 2
PRO_0000122347Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ13490.
PaxDbiQ13490.
PRIDEiQ13490.

PTM databases

PhosphoSiteiQ13490.

Miscellaneous databases

PMAP-CutDBQ13490.

Expressioni

Tissue specificityi

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.

Gene expression databases

ArrayExpressiQ13490.
BgeeiQ13490.
CleanExiHS_BIRC2.
GenevestigatoriQ13490.

Organism-specific databases

HPAiCAB020661.
HPA005513.

Interactioni

Subunit structurei

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 USP19.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP7P552102EBI-514538,EBI-523958
CASP9P552113EBI-514538,EBI-516799
DIABLOQ9NR285EBI-514538,EBI-517508
OTUB1Q96FW13EBI-514538,EBI-1058491
RAC1P630002EBI-514538,EBI-413628
RIPK1Q135463EBI-514538,EBI-358507
RIPK2O433533EBI-514538,EBI-358522
RIPK3Q9Y5723EBI-514538,EBI-298250
RIPK4P570783EBI-514538,EBI-4422308
TNFRSF12AQ9NP842EBI-514538,EBI-2851995
TRAF2Q129339EBI-514538,EBI-355744

Protein-protein interaction databases

BioGridi106826. 94 interactions.
IntActiQ13490. 55 interactions.
MINTiMINT-216174.
STRINGi9606.ENSP00000227758.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 519
Helixi52 – 554
Helixi64 – 696
Beta strandi72 – 743
Beta strandi81 – 833
Turni84 – 863
Helixi99 – 1068
Helixi111 – 1177
Helixi264 – 2663
Helixi269 – 2746
Turni275 – 2784
Beta strandi279 – 2824
Beta strandi283 – 2853
Helixi287 – 2926
Beta strandi295 – 2973
Beta strandi304 – 3063
Turni307 – 3093
Beta strandi312 – 3143
Helixi322 – 3298
Helixi334 – 3407
Helixi342 – 3487
Helixi355 – 3617
Helixi389 – 3913
Helixi394 – 4018
Helixi406 – 42015
Helixi427 – 45024
Turni451 – 4533
Helixi456 – 4638
Helixi465 – 4717
Helixi476 – 4849
Beta strandi485 – 4873
Helixi490 – 4978
Helixi502 – 51615
Helixi518 – 53114
Helixi533 – 5408
Helixi553 – 5553
Helixi558 – 5669
Turni572 – 5743
Beta strandi575 – 5784
Beta strandi581 – 5844
Beta strandi589 – 5913
Turni593 – 5953
Helixi596 – 5983
Turni603 – 6053
Beta strandi611 – 6144

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4KMNX-ray1.52A260-357[»]
4LGEX-ray1.55A/B260-352[»]
4LGUX-ray2.00A/B260-352[»]
4MTIX-ray2.15A/B260-352[»]
4MU7X-ray1.79A/B260-352[»]
ProteinModelPortaliQ13490.
SMRiQ13490. Positions 41-118, 180-250, 260-616.

Miscellaneous databases

EvolutionaryTraceiQ13490.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati46 – 11368BIR 1
Add
BLAST
Repeati184 – 25067BIR 2
Add
BLAST
Repeati269 – 33668BIR 3
Add
BLAST
Domaini453 – 54391CARD
Add
BLAST

Domaini

The BIR domains mediate nuclear localization.1 Publication
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.1 Publication

Sequence similaritiesi

Belongs to the IAP family.
Contains 3 BIR repeats.
Contains 1 CARD domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG243347.
HOGENOMiHOG000232059.
HOVERGENiHBG004848.
InParanoidiQ13490.
KOiK16060.
OMAiTYHMWPL.
OrthoDBiEOG78H3TF.
PhylomeDBiQ13490.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13490-1) [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

MHKTASQRLF PGPSYQNIKS IMEDSTILSD WTNSNKQKMK YDFSCELYRM    50
STYSTFPAGV PVSERSLARA GFYYTGVNDK VKCFCCGLML DNWKLGDSPI 100
QKHKQLYPSC SFIQNLVSAS LGSTSKNTSP MRNSFAHSLS PTLEHSSLFS 150
GSYSSLSPNP LNSRAVEDIS SSRTNPYSYA MSTEEARFLT YHMWPLTFLS 200
PSELARAGFY YIGPGDRVAC FACGGKLSNW EPKDDAMSEH RRHFPNCPFL 250
ENSLETLRFS ISNLSMQTHA ARMRTFMYWP SSVPVQPEQL ASAGFYYVGR 300
NDDVKCFCCD GGLRCWESGD DPWVEHAKWF PRCEFLIRMK GQEFVDEIQG 350
RYPHLLEQLL STSDTTGEEN ADPPIIHFGP GESSSEDAVM MNTPVVKSAL 400
EMGFNRDLVK QTVQSKILTT GENYKTVNDI VSALLNAEDE KREEEKEKQA 450
EEMASDDLSL IRKNRMALFQ QLTCVLPILD NLLKANVINK QEHDIIKQKT 500
QIPLQARELI DTILVKGNAA ANIFKNCLKE IDSTLYKNLF VDKNMKYIPT 550
EDVSGLSLEE QLRRLQEERT CKVCMDKEVS VVFIPCGHLV VCQECAPSLR 600
KCPICRGIIK GTVRTFLS 618
Length:618
Mass (Da):69,900
Last modified:November 1, 1997 - v2
Checksum:iC1778D328063586D
GO
Isoform 2 (identifier: Q13490-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:569
Mass (Da):64,098
Checksum:iB678A4C2069F0A22
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti453 – 4531M → I.
Corresponds to variant rs34749508 [ dbSNP | Ensembl ].
VAR_049535
Natural varianti453 – 4531M → V.1 Publication
VAR_025016
Natural varianti506 – 5061A → V.1 Publication
Corresponds to variant rs34510872 [ dbSNP | Ensembl ].
VAR_025017
Natural varianti549 – 5491P → S.1 Publication
Corresponds to variant rs35494784 [ dbSNP | Ensembl ].
VAR_025018

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4949Missing in isoform 2.
VSP_045314Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571S → P in AAC50372. 1 Publication
Sequence conflicti308 – 3081C → G in AAC50372. 1 Publication
Sequence conflicti414 – 4141Q → L in AAC50372. 1 Publication
Sequence conflicti514 – 5141L → W in AAC50372. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS58169.1. [Q13490-2]
CCDS8316.1. [Q13490-1]
PIRiS68450.
RefSeqiNP_001157.1. NM_001166.4. [Q13490-1]
NP_001243092.1. NM_001256163.1. [Q13490-1]
NP_001243095.1. NM_001256166.1. [Q13490-2]
UniGeneiHs.696238.
Hs.731943.

Genome annotation databases

EnsembliENST00000227758; ENSP00000227758; ENSG00000110330. [Q13490-1]
ENST00000530675; ENSP00000431723; ENSG00000110330. [Q13490-2]
GeneIDi329.
KEGGihsa:329.
UCSCiuc001pgy.4. human. [Q13490-1]

Polymorphism databases

DMDMi2497238.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS58169.1. [Q13490-2 ]
CCDS8316.1. [Q13490-1 ]
PIRi S68450.
RefSeqi NP_001157.1. NM_001166.4. [Q13490-1 ]
NP_001243092.1. NM_001256163.1. [Q13490-1 ]
NP_001243095.1. NM_001256166.1. [Q13490-2 ]
UniGenei Hs.696238.
Hs.731943.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QBH NMR - A 266-363 [» ]
2L9M NMR - A 435-562 [» ]
3D9T X-ray 1.50 A/B 260-352 [» ]
3D9U X-ray 2.30 A 260-352 [» ]
3M1D X-ray 2.00 A/B 40-119 [» ]
3MUP X-ray 2.60 A/B/C/D 251-363 [» ]
3OZ1 X-ray 3.00 A/B/C/D 251-363 [» ]
3T6P X-ray 1.90 A 265-618 [» ]
3UW4 X-ray 1.79 A 266-343 [» ]
4EB9 X-ray 2.60 A/B/C/D 251-363 [» ]
4HY4 X-ray 1.25 A/B 260-352 [» ]
4HY5 X-ray 1.75 A/B 260-352 [» ]
4KMN X-ray 1.52 A 260-357 [» ]
4LGE X-ray 1.55 A/B 260-352 [» ]
4LGU X-ray 2.00 A/B 260-352 [» ]
4MTI X-ray 2.15 A/B 260-352 [» ]
4MU7 X-ray 1.79 A/B 260-352 [» ]
ProteinModelPortali Q13490.
SMRi Q13490. Positions 41-118, 180-250, 260-616.
ModBasei Search...

Protein-protein interaction databases

BioGridi 106826. 94 interactions.
IntActi Q13490. 55 interactions.
MINTi MINT-216174.
STRINGi 9606.ENSP00000227758.

Chemistry

BindingDBi Q13490.
ChEMBLi CHEMBL5462.

Protein family/group databases

MEROPSi I32.002.

PTM databases

PhosphoSitei Q13490.

Polymorphism databases

DMDMi 2497238.

Proteomic databases

MaxQBi Q13490.
PaxDbi Q13490.
PRIDEi Q13490.

Protocols and materials databases

DNASUi 329.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000227758 ; ENSP00000227758 ; ENSG00000110330 . [Q13490-1 ]
ENST00000530675 ; ENSP00000431723 ; ENSG00000110330 . [Q13490-2 ]
GeneIDi 329.
KEGGi hsa:329.
UCSCi uc001pgy.4. human. [Q13490-1 ]

Organism-specific databases

CTDi 329.
GeneCardsi GC11P102252.
HGNCi HGNC:590. BIRC2.
HPAi CAB020661.
HPA005513.
MIMi 601712. gene.
neXtProti NX_Q13490.
PharmGKBi PA25359.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG243347.
HOGENOMi HOG000232059.
HOVERGENi HBG004848.
InParanoidi Q13490.
KOi K16060.
OMAi TYHMWPL.
OrthoDBi EOG78H3TF.
PhylomeDBi Q13490.
TreeFami TF105356.

Enzyme and pathway databases

Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
REACT_25374. IKK complex recruitment mediated by RIP1.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinki Q13490.

Miscellaneous databases

EvolutionaryTracei Q13490.
GeneWikii BIRC2.
GenomeRNAii 329.
NextBioi 1355.
PMAP-CutDB Q13490.
PROi Q13490.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13490.
Bgeei Q13490.
CleanExi HS_BIRC2.
Genevestigatori Q13490.

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] (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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiBIRC2_HUMAN
AccessioniPrimary (citable) accession number: Q13490
Secondary accession number(s): B4E026, Q16516, Q4TTG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 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

Dasty 3

Similar proteinsi