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Protein

Baculoviral IAP repeat-containing protein 5

Gene

BIRC5

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

Functioni

Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.9 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi57Zinc1
Metal bindingi60Zinc1
Metal bindingi77Zinc1
Metal bindingi84Zinc1

GO - Molecular functioni

  • chaperone binding Source: UniProtKB
  • cobalt ion binding Source: UniProtKB
  • cofactor binding Source: UniProtKB
  • cysteine-type endopeptidase inhibitor activity Source: UniProtKB-KW
  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • microtubule binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • Ran GTPase binding Source: UniProtKB
  • tubulin binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: GO_Central
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell division Source: UniProtKB
  • cytokinesis Source: UniProtKB
  • establishment of chromosome localization Source: UniProtKB
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • inhibition of cysteine-type endopeptidase activity involved in apoptotic process Source: GO_Central
  • mitotic nuclear division Source: UniProtKB
  • mitotic spindle assembly Source: GO_Central
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of exit from mitosis Source: UniProtKB
  • positive regulation of mitotic cell cycle Source: UniProtKB
  • protein complex localization Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • protein sumoylation Source: Reactome
  • regulation of apoptotic process Source: Reactome
  • regulation of signal transduction Source: GO_Central
  • sister chromatid cohesion Source: Reactome
  • spindle checkpoint Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Repressor, Thiol protease inhibitor

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Chromosome partition, Mitosis, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000089685-MONOMER.
ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6803205. TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
R-HSA-68877. Mitotic Prometaphase.
SignaLinkiO15392.
SIGNORiO15392.

Protein family/group databases

MEROPSiI32.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Baculoviral IAP repeat-containing protein 5
Alternative name(s):
Apoptosis inhibitor 4
Apoptosis inhibitor survivin
Gene namesi
Name:BIRC5
Synonyms:API4, IAP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:593. BIRC5.

Subcellular locationi

GO - Cellular componenti

  • centriole Source: UniProtKB
  • chromosome, centromeric region Source: UniProtKB
  • chromosome passenger complex Source: UniProtKB
  • condensed chromosome kinetochore Source: UniProtKB
  • cytoplasm Source: LIFEdb
  • cytoplasmic microtubule Source: UniProtKB
  • cytosol Source: UniProtKB
  • interphase microtubule organizing center Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • midbody Source: UniProtKB
  • nuclear chromosome Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • spindle Source: UniProtKB-SubCell
  • spindle microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi18R → A: Disruts interaction with histone H3pT3, no effect on interaction with INCENP. 1 Publication1
Mutagenesisi23K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-62; R-78 and R-79. 1 Publication1
Mutagenesisi25W → A: Disruts interaction with histone H3pT3, no effect on interaction with INCENP. 1 Publication1
Mutagenesisi33C → R: Disruts interaction with histone H3pT3, no effect on interaction with INCENP. 1 Publication1
Mutagenesisi34T → A: Loss of LAMTOR5 binding. 1 Publication1
Mutagenesisi34T → E: Higher affinity for LAMTOR5 binding. 1 Publication1
Mutagenesisi48T → A or E: Localizes normally during mitosis but cannot support cell proliferation. Increased affinity for CDCA8/borealin. 1 Publication1
Mutagenesisi57C → A: Disruts interaction with histone H3pT3, no effect on interaction with INCENP. 1 Publication1
Mutagenesisi62K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-78 and R-79. 1 Publication1
Mutagenesisi65E → A: Almost abolishes RAN-binding. Does not disrupt binding to AURKB or CDCA8. Disrupts mitotic spindle assembly. Does not disrupt nuclear export. 1 Publication1
Mutagenesisi67W → A: Disruts interaction with histone H3pT3, no effect on interaction with INCENP. 1 Publication1
Mutagenesisi70D → A: No change. Loss of interaction with AURKB; when associated with A-71. 1 Publication1
Mutagenesisi71D → A: No change. Loss of interaction with AURKB; when associated with A-70. 1 Publication1
Mutagenesisi78K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-79. 1 Publication1
Mutagenesisi79K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-78. 1 Publication1
Mutagenesisi84C → A: Loss of cytoprotection. 1
Mutagenesisi117T → A: Prevents phosphorylation by AURKB. Still able to localize correctly but prevents interaction with INCENP. 1 Publication1
Mutagenesisi117T → E: Mimics phosphorylation. Disrupts subcellular localization during mitosis and prevents interaction with INCENP. 1 Publication1
Mutagenesisi129K → A or Q: Mimics acetylation. Localization primarily within the nucleus. 1 Publication1
Mutagenesisi129K → R: Loss of acetylation. Localization primarily within the cytoplasm. 1 Publication1

Organism-specific databases

DisGeNETi332.
OpenTargetsiENSG00000089685.
PharmGKBiPA25362.

Chemistry databases

ChEMBLiCHEMBL5989.
GuidetoPHARMACOLOGYi2795.

Polymorphism and mutation databases

BioMutaiBIRC5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001223561 – 142Baculoviral IAP repeat-containing protein 5Add BLAST142

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei20Phosphoserine; by AURKC1 Publication1
Modified residuei23N6-acetyllysine1 Publication1
Modified residuei34Phosphothreonine; by CDK1 and CDK15Combined sources2 Publications1
Modified residuei48Phosphothreonine; by CK2; in vitro1 Publication1
Modified residuei90N6-acetyllysine1 Publication1
Modified residuei110N6-acetyllysine1 Publication1
Modified residuei112N6-acetyllysine1 Publication1
Modified residuei115N6-acetyllysine1 Publication1
Modified residuei117Phosphothreonine; by AURKB1 Publication1
Modified residuei121N6-acetyllysine1 Publication1
Modified residuei129N6-acetyllysine1 Publication1

Post-translational modificationi

Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting.2 Publications
In vitro phosphorylation at Thr-117 by AURKB prevents interaction with INCENP and localization to mitotic chromosomes (PubMed:14610074). Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities (PubMed:21252625). Phosphorylation at Thr-34 by CDK15 is critical for its anti-apoptotic activity (PubMed:24866247). Phosphorylation at Ser-20 by AURKC is critical for regulation of proper chromosome alignment and segregation, and possibly cytokinesis.5 Publications
Acetylation at Lys-129 by CBP results in its homodimerization, while deacetylation promotes the formation of monomers which heterodimerize with XPO1/CRM1 which facilitates its nuclear export. The acetylated form represses STAT3 transactivation. The dynamic equilibrium between its acetylation and deacetylation at Lys-129 determines its interaction with XPO1/CRM1, its subsequent subcellular localization, and its ability to inhibit STAT3 transactivation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO15392.
MaxQBiO15392.
PeptideAtlasiO15392.
PRIDEiO15392.

PTM databases

iPTMnetiO15392.
PhosphoSitePlusiO15392.

Expressioni

Tissue specificityi

Expressed only in fetal kidney and liver, and to lesser extent, lung and brain. Abundantly expressed in adenocarcinoma (lung, pancreas, colon, breast, and prostate) and in high-grade lymphomas. Also expressed in various renal cell carcinoma cell lines.3 Publications

Developmental stagei

Expression is cell cycle-dependent and peaks at mitosis.1 Publication

Inductioni

Up-regulated by COMP.1 Publication

Gene expression databases

BgeeiENSG00000089685.
CleanExiHS_BIRC5.
ExpressionAtlasiO15392. baseline and differential.
GenevisibleiO15392. HS.

Organism-specific databases

HPAiCAB004270.
HPA002830.

Interactioni

Subunit structurei

Monomer or homodimer. Exists as a homodimer in the apo state and as a monomer in the CPC-bound state. The monomer protects cells against apoptosis more efficiently than the dimer. Only the dimeric form is capable of enhancing tubulin stability in cells. When phosphorylated, interacts with LAMTOR5/HBXIP; the resulting complex binds pro-CASP9, as well as active CASP9, but much less efficiently. Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB or AURKC; in the complex forms a triple-helix bundle-based subcomplex with INCENP and CDCA8 (PubMed:17956729). Interacts with JTB. Interacts (via BIR domain) with histone H3 phosphorylated at 'Thr-3' (H3pT3). Interacts with EVI5. Interacts with GTP-bound RAN in both the S and M phases of the cell cycle. Interacts with USP9X. Interacts with tubulin. Interacts with BIRC2/c-IAP1. The acetylated form at Lys-129 interacts with STAT3. The monomeric form deacetylated at Lys-129 interacts with XPO1/CRM1. The monomeric form interacts with XIAP/BIRC4. Both the dimeric and monomeric form can interact with DIABLO/SMAC. Interacts with BIRC6/bruce.16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-518823,EBI-518823
AURKBQ96GD47EBI-518823,EBI-624291
BECN1Q144573EBI-518823,EBI-949378
CASP9P552112EBI-518823,EBI-516799
CDCA8Q53HL214EBI-518823,EBI-979174
DIABLOQ9NR282EBI-518823,EBI-517508
GAS2L3Q86XJ14EBI-518823,EBI-9248152
INCENPQ9NQS710EBI-518823,EBI-307907
RANP628267EBI-518823,EBI-286642
XPO1O149802EBI-518823,EBI-355867

GO - Molecular functioni

  • chaperone binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • microtubule binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • Ran GTPase binding Source: UniProtKB
  • tubulin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106829. 59 interactors.
DIPiDIP-34662N.
IntActiO15392. 17 interactors.
MINTiMINT-147138.

Chemistry databases

BindingDBiO15392.

Structurei

Secondary structure

1142
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni8 – 10Combined sources3
Helixi11 – 13Combined sources3
Helixi15 – 20Combined sources6
Beta strandi31 – 33Combined sources3
Helixi35 – 40Combined sources6
Beta strandi43 – 45Combined sources3
Beta strandi49 – 51Combined sources3
Beta strandi55 – 57Combined sources3
Turni58 – 60Combined sources3
Beta strandi63 – 65Combined sources3
Helixi73 – 80Combined sources8
Turni81 – 83Combined sources3
Helixi85 – 88Combined sources4
Helixi93 – 95Combined sources3
Helixi98 – 139Combined sources42

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E31X-ray2.71A/B1-142[»]
1F3HX-ray2.58A/B1-142[»]
1XOXNMR-A/B1-117[»]
2QFAX-ray1.40A1-142[»]
2RAWX-ray2.40A1-142[»]
2RAXX-ray3.30A/E/X1-120[»]
3UECX-ray2.18A1-142[»]
3UEDX-ray2.70A/C1-142[»]
3UEEX-ray2.61A/C1-142[»]
3UEFX-ray2.45A/C1-142[»]
3UEGX-ray2.80A/B1-142[»]
3UEHX-ray2.60A/B1-142[»]
3UEIX-ray2.70A/B1-142[»]
3UIGX-ray2.40A/B1-142[»]
3UIHX-ray2.40A/B1-142[»]
3UIIX-ray2.60A/B1-142[»]
3UIJX-ray2.70A/B1-142[»]
3UIKX-ray2.70A/B1-142[»]
4A0IX-ray2.60A/B1-142[»]
4A0JX-ray2.80A/B1-142[»]
4A0NX-ray2.74A1-142[»]
ProteinModelPortaliO15392.
SMRiO15392.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15392.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati18 – 88BIRAdd BLAST71

Domaini

The BIR repeat is necessary and sufficient for LAMTOR5 binding.

Sequence similaritiesi

Belongs to the IAP family.Curated
Contains 1 BIR repeat.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00510000047537.
HOGENOMiHOG000172188.
HOVERGENiHBG050690.
InParanoidiO15392.
KOiK08731.

Family and domain databases

CDDicd00022. BIR. 1 hit.
Gene3Di1.10.1170.10. 1 hit.
InterProiIPR001370. BIR_rpt.
[Graphical view]
PfamiPF00653. BIR. 1 hit.
[Graphical view]
SMARTiSM00238. BIR. 1 hit.
[Graphical view]
PROSITEiPS50143. BIR_REPEAT_2. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15392-1) [UniParc]FASTAAdd to basket
Also known as: Alpha

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
MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN
60 70 80 90 100
EPDLAQCFFC FKELEGWEPD DDPIEEHKKH SSGCAFLSVK KQFEELTLGE
110 120 130 140
FLKLDRERAK NKIAKETNNK KKEFEETAKK VRRAIEQLAA MD
Length:142
Mass (Da):16,389
Last modified:March 21, 2012 - v3
Checksum:i9E7CADCDF2822286
GO
Isoform 2 (identifier: O15392-2) [UniParc]FASTAAdd to basket
Also known as: 2B, Beta

The sequence of this isoform differs from the canonical sequence as follows:
     74-74: I → IGPGTVAYACNTSTLGGRGGRITR

Show »
Length:165
Mass (Da):18,636
Checksum:iD1E961E51ADDD01E
GO
Isoform 3 (identifier: O15392-3) [UniParc]FASTAAdd to basket
Also known as: DeltaEx3

The sequence of this isoform differs from the canonical sequence as follows:
     74-142: IEEHKKHSSG...RAIEQLAAMD → MQRKPTIRRK...SLPVGPLAMS

Show »
Length:137
Mass (Da):15,622
Checksum:i38C82D22E46BFF7C
GO
Isoform 4 (identifier: O15392-4) [UniParc]FASTAAdd to basket
Also known as: 3B

The sequence of this isoform differs from the canonical sequence as follows:
     114-142: AKETNNKKKEFEETAKKVRRAIEQLAAMD → ERALLAE

Show »
Length:120
Mass (Da):13,812
Checksum:i3904E8C8AF6945F7
GO
Isoform 5 (identifier: O15392-5) [UniParc]FASTAAdd to basket
Also known as: SI

The sequence of this isoform differs from the canonical sequence as follows:
     105-142: DRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD → VRETLPPPRSFIR

Show »
Length:117
Mass (Da):13,467
Checksum:i82FC6A9B55F06876
GO
Isoform 6 (identifier: O15392-6) [UniParc]FASTAAdd to basket
Also known as: 3 alpha

The sequence of this isoform differs from the canonical sequence as follows:
     74-142: IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD → MRELC

Show »
Length:78
Mass (Da):8,991
Checksum:iD06E2937DCAC8283
GO
Isoform 7 (identifier: O15392-7) [UniParc]FASTAAdd to basket
Also known as: 2 alpha

The sequence of this isoform differs from the canonical sequence as follows:
     74-142: IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD → M

Show »
Length:74
Mass (Da):8,490
Checksum:i8CAC8283CD371FD9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti57 – 58CF → WV in AAW22624 (PubMed:16329164).Curated2
Sequence conflicti58F → L in BAD97148 (Ref. 11) Curated1
Sequence conflicti128A → V in CAG46540 (Ref. 9) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021071129K → E Loss of acetylation; localization primarily within the cytoplasm; increased likelihood of existing as monomer; stronger binding to XPO1/CRM1. 2 PublicationsCorresponds to variant rs2071214dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_02033874 – 142IEEHK…LAAMD → MQRKPTIRRKNLRKLRRKCA VPSSSWLPWIEASGRSCLVP EWLHHFQGLFPGATSLPVGP LAMS in isoform 3. 1 PublicationAdd BLAST69
Alternative sequenceiVSP_02033974 – 142IEEHK…LAAMD → MRELC in isoform 6. 1 PublicationAdd BLAST69
Alternative sequenceiVSP_02034074 – 142IEEHK…LAAMD → M in isoform 7. 1 PublicationAdd BLAST69
Alternative sequenceiVSP_00245474I → IGPGTVAYACNTSTLGGRGG RITR in isoform 2. 2 Publications1
Alternative sequenceiVSP_020341105 – 142DRERA…LAAMD → VRETLPPPRSFIR in isoform 5. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_020342114 – 142AKETN…LAAMD → ERALLAE in isoform 4. 1 PublicationAdd BLAST29

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75285 Genomic DNA. Translation: AAC51660.1.
AF077350 mRNA. Translation: AAD34226.1.
AB154416 mRNA. Translation: BAD11155.1.
AY830084 mRNA. Translation: AAW22624.1.
AB028869 mRNA. Translation: BAA93676.1.
AY927772 mRNA. Translation: AAY15202.1.
DQ227257 mRNA. Translation: ABB76601.1.
DQ310375 mRNA. Translation: ABC42341.1.
DQ310376 mRNA. Translation: ABC42342.1.
DQ310377 mRNA. Translation: ABC42343.1.
DQ310378 mRNA. Translation: ABC42344.1.
DQ310379 mRNA. Translation: ABC42345.1.
CR541740 mRNA. Translation: CAG46540.1.
AK223428 mRNA. Translation: BAD97148.1.
AK311917 mRNA. Translation: BAG34858.1.
AY795969 Genomic DNA. Translation: AAV40840.1.
AC087645 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89514.1.
BC008718 mRNA. Translation: AAH08718.1.
BC034148 mRNA. Translation: AAH34148.1.
BC065497 mRNA. Translation: AAH65497.1.
CCDSiCCDS11755.1. [O15392-1]
CCDS32751.1. [O15392-3]
CCDS32752.1. [O15392-2]
RefSeqiNP_001012270.1. NM_001012270.1. [O15392-3]
NP_001012271.1. NM_001012271.1.
NP_001159.2. NM_001168.2.
UniGeneiHs.744872.

Genome annotation databases

EnsembliENST00000374948; ENSP00000364086; ENSG00000089685. [O15392-3]
ENST00000590449; ENSP00000465868; ENSG00000089685. [O15392-7]
ENST00000590925; ENSP00000467336; ENSG00000089685. [O15392-4]
ENST00000592734; ENSP00000466617; ENSG00000089685. [O15392-6]
GeneIDi332.
KEGGihsa:332.
UCSCiuc002jvh.4. human. [O15392-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U75285 Genomic DNA. Translation: AAC51660.1.
AF077350 mRNA. Translation: AAD34226.1.
AB154416 mRNA. Translation: BAD11155.1.
AY830084 mRNA. Translation: AAW22624.1.
AB028869 mRNA. Translation: BAA93676.1.
AY927772 mRNA. Translation: AAY15202.1.
DQ227257 mRNA. Translation: ABB76601.1.
DQ310375 mRNA. Translation: ABC42341.1.
DQ310376 mRNA. Translation: ABC42342.1.
DQ310377 mRNA. Translation: ABC42343.1.
DQ310378 mRNA. Translation: ABC42344.1.
DQ310379 mRNA. Translation: ABC42345.1.
CR541740 mRNA. Translation: CAG46540.1.
AK223428 mRNA. Translation: BAD97148.1.
AK311917 mRNA. Translation: BAG34858.1.
AY795969 Genomic DNA. Translation: AAV40840.1.
AC087645 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89514.1.
BC008718 mRNA. Translation: AAH08718.1.
BC034148 mRNA. Translation: AAH34148.1.
BC065497 mRNA. Translation: AAH65497.1.
CCDSiCCDS11755.1. [O15392-1]
CCDS32751.1. [O15392-3]
CCDS32752.1. [O15392-2]
RefSeqiNP_001012270.1. NM_001012270.1. [O15392-3]
NP_001012271.1. NM_001012271.1.
NP_001159.2. NM_001168.2.
UniGeneiHs.744872.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E31X-ray2.71A/B1-142[»]
1F3HX-ray2.58A/B1-142[»]
1XOXNMR-A/B1-117[»]
2QFAX-ray1.40A1-142[»]
2RAWX-ray2.40A1-142[»]
2RAXX-ray3.30A/E/X1-120[»]
3UECX-ray2.18A1-142[»]
3UEDX-ray2.70A/C1-142[»]
3UEEX-ray2.61A/C1-142[»]
3UEFX-ray2.45A/C1-142[»]
3UEGX-ray2.80A/B1-142[»]
3UEHX-ray2.60A/B1-142[»]
3UEIX-ray2.70A/B1-142[»]
3UIGX-ray2.40A/B1-142[»]
3UIHX-ray2.40A/B1-142[»]
3UIIX-ray2.60A/B1-142[»]
3UIJX-ray2.70A/B1-142[»]
3UIKX-ray2.70A/B1-142[»]
4A0IX-ray2.60A/B1-142[»]
4A0JX-ray2.80A/B1-142[»]
4A0NX-ray2.74A1-142[»]
ProteinModelPortaliO15392.
SMRiO15392.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106829. 59 interactors.
DIPiDIP-34662N.
IntActiO15392. 17 interactors.
MINTiMINT-147138.

Chemistry databases

BindingDBiO15392.
ChEMBLiCHEMBL5989.
GuidetoPHARMACOLOGYi2795.

Protein family/group databases

MEROPSiI32.005.

PTM databases

iPTMnetiO15392.
PhosphoSitePlusiO15392.

Polymorphism and mutation databases

BioMutaiBIRC5.

Proteomic databases

EPDiO15392.
MaxQBiO15392.
PeptideAtlasiO15392.
PRIDEiO15392.

Protocols and materials databases

DNASUi332.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374948; ENSP00000364086; ENSG00000089685. [O15392-3]
ENST00000590449; ENSP00000465868; ENSG00000089685. [O15392-7]
ENST00000590925; ENSP00000467336; ENSG00000089685. [O15392-4]
ENST00000592734; ENSP00000466617; ENSG00000089685. [O15392-6]
GeneIDi332.
KEGGihsa:332.
UCSCiuc002jvh.4. human. [O15392-1]

Organism-specific databases

CTDi332.
DisGeNETi332.
GeneCardsiBIRC5.
HGNCiHGNC:593. BIRC5.
HPAiCAB004270.
HPA002830.
MIMi603352. gene.
neXtProtiNX_O15392.
OpenTargetsiENSG00000089685.
PharmGKBiPA25362.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00510000047537.
HOGENOMiHOG000172188.
HOVERGENiHBG050690.
InParanoidiO15392.
KOiK08731.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000089685-MONOMER.
ReactomeiR-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6803205. TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
R-HSA-68877. Mitotic Prometaphase.
SignaLinkiO15392.
SIGNORiO15392.

Miscellaneous databases

ChiTaRSiBIRC5. human.
EvolutionaryTraceiO15392.
GeneWikiiSurvivin.
GenomeRNAii332.
PROiO15392.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000089685.
CleanExiHS_BIRC5.
ExpressionAtlasiO15392. baseline and differential.
GenevisibleiO15392. HS.

Family and domain databases

CDDicd00022. BIR. 1 hit.
Gene3Di1.10.1170.10. 1 hit.
InterProiIPR001370. BIR_rpt.
[Graphical view]
PfamiPF00653. BIR. 1 hit.
[Graphical view]
SMARTiSM00238. BIR. 1 hit.
[Graphical view]
PROSITEiPS50143. BIR_REPEAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBIRC5_HUMAN
AccessioniPrimary (citable) accession number: O15392
Secondary accession number(s): A2SUH6
, B2R4R1, Q2I3N8, Q4VGX0, Q53F61, Q5MGC6, Q6FHL2, Q75SP2, Q9P2W8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: March 21, 2012
Last modified: November 30, 2016
This is version 196 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 17
    Human chromosome 17: 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.