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Protein

Baculoviral IAP repeat-containing protein 2

Gene

BIRC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.4 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)DescriptionActionsGraphical viewLength
Metal bindingi306Zinc1
Metal bindingi309Zinc1
Metal bindingi326Zinc1
Metal bindingi333Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri571 – 606RING-typePROSITE-ProRule annotationAdd BLAST36

GO - Molecular functioni

  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: GO_Central
  • FBXO family protein binding Source: ParkinsonsUK-UCL
  • protein N-terminus binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • transferase activity Source: Reactome
  • ubiquitin binding Source: ParkinsonsUK-UCL
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cell surface receptor signaling pathway Source: ProtInc
  • cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  • I-kappaB kinase/NF-kappaB signaling Source: Reactome
  • inhibition of cysteine-type endopeptidase activity involved in apoptotic process Source: GO_Central
  • necroptotic process Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of ripoptosome assembly involved in necroptotic process Source: Ensembl
  • NIK/NF-kappaB signaling Source: UniProtKB
  • placenta development Source: Ensembl
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of protein K48-linked ubiquitination Source: UniProtKB
  • positive regulation of protein K63-linked ubiquitination Source: UniProtKB
  • positive regulation of protein monoubiquitination Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein heterooligomerization Source: Ensembl
  • protein polyubiquitination Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
  • regulation of cell cycle Source: UniProtKB
  • regulation of cell differentiation Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • regulation of cysteine-type endopeptidase activity Source: UniProtKB
  • regulation of inflammatory response Source: UniProtKB
  • regulation of innate immune response Source: UniProtKB
  • regulation of necroptotic process Source: UniProtKB
  • regulation of necrotic cell death Source: Reactome
  • regulation of nucleotide-binding oligomerization domain containing signaling pathway Source: UniProtKB
  • regulation of reactive oxygen species metabolic process Source: Ensembl
  • regulation of RIG-I signaling pathway Source: UniProtKB
  • regulation of toll-like receptor signaling pathway Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • regulation of tumor necrosis factor-mediated signaling pathway Source: Reactome
  • response to cAMP Source: Ensembl
  • response to ethanol Source: Ensembl
  • response to hypoxia Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
  • TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  • tumor necrosis factor-mediated signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Transferase

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000023445-MONOMER.
ZFISH:ENSG00000110330-MONOMER.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-5213460. RIPK1-mediated regulated necrosis.
R-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5675482. Regulation of necroptotic cell death.
R-HSA-5676594. TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-937041. IKK complex recruitment mediated by RIP1.
SignaLinkiQ13490.
SIGNORiQ13490.

Protein family/group databases

MEROPSiI32.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Baculoviral IAP repeat-containing protein 2 (EC:2.3.2.274 Publications)
Alternative name(s):
Cellular inhibitor of apoptosis 1
Short name:
C-IAP11 Publication
IAP homolog B
Inhibitor of apoptosis protein 2
Short name:
hIAP-2
Short name:
hIAP2
RING finger protein 48
RING-type E3 ubiquitin transferase BIRC2Curated
TNFR2-TRAF-signaling complex protein 2
Gene namesi
Name:BIRC2
Synonyms:API1, MIHB, RNF48
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: 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.

GO - Cellular componenti

  • CD40 receptor complex Source: BHF-UCL
  • cytoplasm Source: ParkinsonsUK-UCL
  • cytoplasmic side of plasma membrane Source: BHF-UCL
  • cytosol Source: Reactome
  • membrane raft Source: Ensembl
  • nucleus Source: UniProtKB
  • protein complex Source: Ensembl
  • XY body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi329.
OpenTargetsiENSG00000110330.
PharmGKBiPA25359.

Chemistry databases

ChEMBLiCHEMBL5462.
GuidetoPHARMACOLOGYi2791.

Polymorphism and mutation databases

BioMutaiBIRC2.
DMDMi2497238.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001223471 – 618Baculoviral IAP repeat-containing protein 2Add BLAST618

Post-translational modificationi

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

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ13490.
MaxQBiQ13490.
PaxDbiQ13490.
PeptideAtlasiQ13490.
PRIDEiQ13490.

PTM databases

iPTMnetiQ13490.
PhosphoSitePlusiQ13490.

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

BgeeiENSG00000110330.
CleanExiHS_BIRC2.
ExpressionAtlasiQ13490. baseline and differential.
GenevisibleiQ13490. HS.

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
BIRC7Q96CA53EBI-514538,EBI-517623
BOLA1Q9Y3E25EBI-514538,EBI-1049556
CASP7P552102EBI-514538,EBI-523958
CASP9P552119EBI-514538,EBI-516799
DIABLOQ9NR285EBI-514538,EBI-517508
EAF2Q96CJ13EBI-514538,EBI-1245604
EXOSC5Q9NQT45EBI-514538,EBI-371876
GCC1Q96CN95EBI-514538,EBI-746252
GFAPP141363EBI-514538,EBI-744302
NMBP089493EBI-514538,EBI-7964376
OTUB1Q96FW13EBI-514538,EBI-1058491
PPM1KQ8N3J55EBI-514538,EBI-3923368
RAC1P630002EBI-514538,EBI-413628
RIPK1Q135463EBI-514538,EBI-358507
RIPK2O433533EBI-514538,EBI-358522
RIPK3Q9Y5723EBI-514538,EBI-298250
RIPK4P570783EBI-514538,EBI-4422308
TNFRSF12AQ9NP842EBI-514538,EBI-2851995
TRAF2Q1293312EBI-514538,EBI-355744
TSGA10Q9BZW74EBI-514538,EBI-744794
WDYHV1Q96HA83EBI-514538,EBI-741158

GO - Molecular functioni

  • FBXO family protein binding Source: ParkinsonsUK-UCL
  • protein N-terminus binding Source: UniProtKB
  • ubiquitin binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi106826. 142 interactors.
DIPiDIP-33485N.
IntActiQ13490. 73 interactors.
MINTiMINT-216174.
STRINGi9606.ENSP00000227758.

Chemistry databases

BindingDBiQ13490.

Structurei

Secondary structure

1618
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 51Combined sources9
Helixi52 – 55Combined sources4
Helixi64 – 69Combined sources6
Beta strandi72 – 74Combined sources3
Beta strandi81 – 83Combined sources3
Turni84 – 86Combined sources3
Helixi99 – 106Combined sources8
Helixi111 – 117Combined sources7
Helixi264 – 266Combined sources3
Helixi269 – 274Combined sources6
Turni275 – 278Combined sources4
Beta strandi279 – 282Combined sources4
Beta strandi283 – 285Combined sources3
Helixi287 – 292Combined sources6
Beta strandi295 – 297Combined sources3
Beta strandi304 – 306Combined sources3
Turni307 – 309Combined sources3
Beta strandi312 – 314Combined sources3
Helixi322 – 329Combined sources8
Helixi334 – 340Combined sources7
Helixi342 – 348Combined sources7
Helixi355 – 361Combined sources7
Helixi389 – 391Combined sources3
Helixi394 – 401Combined sources8
Helixi406 – 420Combined sources15
Helixi427 – 450Combined sources24
Turni451 – 453Combined sources3
Helixi456 – 463Combined sources8
Helixi465 – 471Combined sources7
Helixi476 – 484Combined sources9
Beta strandi485 – 487Combined sources3
Helixi490 – 497Combined sources8
Helixi502 – 516Combined sources15
Helixi518 – 531Combined sources14
Helixi533 – 540Combined sources8
Helixi553 – 555Combined sources3
Helixi558 – 566Combined sources9
Turni572 – 574Combined sources3
Beta strandi575 – 578Combined sources4
Beta strandi581 – 584Combined sources4
Beta strandi589 – 591Combined sources3
Turni593 – 595Combined sources3
Helixi596 – 598Combined sources3
Turni603 – 605Combined sources3
Beta strandi611 – 614Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13490.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati46 – 113BIR 1Add BLAST68
Repeati184 – 250BIR 2Add BLAST67
Repeati269 – 336BIR 3Add BLAST68
Domaini453 – 543CARDPROSITE-ProRule annotationAdd BLAST91

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.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)DescriptionActionsGraphical viewLength
Zinc fingeri571 – 606RING-typePROSITE-ProRule annotationAdd BLAST36

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00500000044782.
HOGENOMiHOG000232059.
HOVERGENiHBG004848.
InParanoidiQ13490.
KOiK16060.
OMAiPIEKHKQ.
OrthoDBiEOG091G0CXH.
PhylomeDBiQ13490.
TreeFamiTF105356.

Family and domain databases

CDDicd00022. BIR. 3 hits.
Gene3Di1.10.1170.10. 4 hits.
1.10.533.10. 1 hit.
InterProiIPR001370. BIR_rpt.
IPR028795. C-IAP1.
IPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR001841. Znf_RING.
[Graphical view]
PANTHERiPTHR10044:SF79. PTHR10044:SF79. 1 hit.
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. AlignAdd to basket

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

        10         20         30         40         50
MHKTASQRLF PGPSYQNIKS IMEDSTILSD WTNSNKQKMK YDFSCELYRM
60 70 80 90 100
STYSTFPAGV PVSERSLARA GFYYTGVNDK VKCFCCGLML DNWKLGDSPI
110 120 130 140 150
QKHKQLYPSC SFIQNLVSAS LGSTSKNTSP MRNSFAHSLS PTLEHSSLFS
160 170 180 190 200
GSYSSLSPNP LNSRAVEDIS SSRTNPYSYA MSTEEARFLT YHMWPLTFLS
210 220 230 240 250
PSELARAGFY YIGPGDRVAC FACGGKLSNW EPKDDAMSEH RRHFPNCPFL
260 270 280 290 300
ENSLETLRFS ISNLSMQTHA ARMRTFMYWP SSVPVQPEQL ASAGFYYVGR
310 320 330 340 350
NDDVKCFCCD GGLRCWESGD DPWVEHAKWF PRCEFLIRMK GQEFVDEIQG
360 370 380 390 400
RYPHLLEQLL STSDTTGEEN ADPPIIHFGP GESSSEDAVM MNTPVVKSAL
410 420 430 440 450
EMGFNRDLVK QTVQSKILTT GENYKTVNDI VSALLNAEDE KREEEKEKQA
460 470 480 490 500
EEMASDDLSL IRKNRMALFQ QLTCVLPILD NLLKANVINK QEHDIIKQKT
510 520 530 540 550
QIPLQARELI DTILVKGNAA ANIFKNCLKE IDSTLYKNLF VDKNMKYIPT
560 570 580 590 600
EDVSGLSLEE QLRRLQEERT CKVCMDKEVS VVFIPCGHLV VCQECAPSLR
610
KCPICRGIIK GTVRTFLS
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti157S → P in AAC50372 (PubMed:8552191).Curated1
Sequence conflicti308C → G in AAC50372 (PubMed:8552191).Curated1
Sequence conflicti414Q → L in AAC50372 (PubMed:8552191).Curated1
Sequence conflicti514L → W in AAC50372 (PubMed:8552191).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_049535453M → I.Corresponds to variant rs34749508dbSNPEnsembl.1
Natural variantiVAR_025016453M → V.1 PublicationCorresponds to variant rs370745983dbSNPEnsembl.1
Natural variantiVAR_025017506A → V.1 PublicationCorresponds to variant rs34510872dbSNPEnsembl.1
Natural variantiVAR_025018549P → S.1 PublicationCorresponds to variant rs35494784dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0453141 – 49Missing in isoform 2. 1 PublicationAdd BLAST49

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
ENST00000613397; ENSP00000477613; ENSG00000110330. [Q13490-1]
GeneIDi329.
KEGGihsa:329.
UCSCiuc001pgy.5. human. [Q13490-1]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106826. 142 interactors.
DIPiDIP-33485N.
IntActiQ13490. 73 interactors.
MINTiMINT-216174.
STRINGi9606.ENSP00000227758.

Chemistry databases

BindingDBiQ13490.
ChEMBLiCHEMBL5462.
GuidetoPHARMACOLOGYi2791.

Protein family/group databases

MEROPSiI32.002.

PTM databases

iPTMnetiQ13490.
PhosphoSitePlusiQ13490.

Polymorphism and mutation databases

BioMutaiBIRC2.
DMDMi2497238.

Proteomic databases

EPDiQ13490.
MaxQBiQ13490.
PaxDbiQ13490.
PeptideAtlasiQ13490.
PRIDEiQ13490.

Protocols and materials databases

DNASUi329.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000227758; ENSP00000227758; ENSG00000110330. [Q13490-1]
ENST00000530675; ENSP00000431723; ENSG00000110330. [Q13490-2]
ENST00000613397; ENSP00000477613; ENSG00000110330. [Q13490-1]
GeneIDi329.
KEGGihsa:329.
UCSCiuc001pgy.5. human. [Q13490-1]

Organism-specific databases

CTDi329.
DisGeNETi329.
GeneCardsiBIRC2.
HGNCiHGNC:590. BIRC2.
HPAiCAB020661.
HPA005513.
MIMi601712. gene.
neXtProtiNX_Q13490.
OpenTargetsiENSG00000110330.
PharmGKBiPA25359.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1101. Eukaryota.
ENOG410YPNM. LUCA.
GeneTreeiENSGT00500000044782.
HOGENOMiHOG000232059.
HOVERGENiHBG004848.
InParanoidiQ13490.
KOiK16060.
OMAiPIEKHKQ.
OrthoDBiEOG091G0CXH.
PhylomeDBiQ13490.
TreeFamiTF105356.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000023445-MONOMER.
ZFISH:ENSG00000110330-MONOMER.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-5213460. RIPK1-mediated regulated necrosis.
R-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5675482. Regulation of necroptotic cell death.
R-HSA-5676594. TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-937041. IKK complex recruitment mediated by RIP1.
SignaLinkiQ13490.
SIGNORiQ13490.

Miscellaneous databases

ChiTaRSiBIRC2. human.
EvolutionaryTraceiQ13490.
GeneWikiiBIRC2.
GenomeRNAii329.
PMAP-CutDBQ13490.
PROiQ13490.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110330.
CleanExiHS_BIRC2.
ExpressionAtlasiQ13490. baseline and differential.
GenevisibleiQ13490. HS.

Family and domain databases

CDDicd00022. BIR. 3 hits.
Gene3Di1.10.1170.10. 4 hits.
1.10.533.10. 1 hit.
InterProiIPR001370. BIR_rpt.
IPR028795. C-IAP1.
IPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR001841. Znf_RING.
[Graphical view]
PANTHERiPTHR10044:SF79. PTHR10044:SF79. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 177 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.