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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. 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.8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571Zinc
Metal bindingi60 – 601Zinc
Metal bindingi77 – 771Zinc
Metal bindingi84 – 841Zinc

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
  • identical protein binding Source: IntAct
  • 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

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

  • Cytoplasm
  • Nucleus
  • Chromosome
  • Chromosomecentromere
  • Cytoplasmcytoskeletonspindle
  • Chromosomecentromerekinetochore
  • Midbody

  • Note: Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody. Colocalizes with AURKB at mitotic chromosomes. Acetylation at Lys-129 directs its localization to the nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1-mediated nuclear export.

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-62; R-78 and R-79. 1 Publication
Mutagenesisi34 – 341T → A: Loss of LAMTOR5 binding. 1 Publication
Mutagenesisi34 – 341T → E: Higher affinity for LAMTOR5 binding. 1 Publication
Mutagenesisi48 – 481T → A or E: Localizes normally during mitosis but cannot support cell proliferation. Increased affinity for CDCA8/borealin. 1 Publication
Mutagenesisi62 – 621K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-78 and R-79. 1 Publication
Mutagenesisi65 – 651E → A: Almost abolishes RAN-binding. Does not disrupt binding to AURKB or CDCA8. Disrupts mitotic spindle assembly. Does not disrupt nuclear export. 1 Publication
Mutagenesisi70 – 701D → A: No change. Loss of interaction with AURKB; when associated with A-71. 1 Publication
Mutagenesisi71 – 711D → A: No change. Loss of interaction with AURKB; when associated with A-70. 1 Publication
Mutagenesisi78 – 781K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-79. 1 Publication
Mutagenesisi79 – 791K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-78. 1 Publication
Mutagenesisi84 – 841C → A: Loss of cytoprotection.
Mutagenesisi117 – 1171T → A: Prevents phosphorylation by AURKB. Still able to localize correctly but prevents interaction with INCENP. 1 Publication
Mutagenesisi117 – 1171T → E: Mimics phosphorylation. Disrupts subcellular localization during mitosis and prevents interaction with INCENP. 1 Publication
Mutagenesisi129 – 1291K → A or Q: Mimics acetylation. Localization primarily within the nucleus. 1 Publication
Mutagenesisi129 – 1291K → R: Loss of acetylation. Localization primarily within the cytoplasm. 1 Publication

Organism-specific databases

PharmGKBiPA25362.

Chemistry

ChEMBLiCHEMBL5989.
GuidetoPHARMACOLOGYi2795.

Polymorphism and mutation databases

BioMutaiBIRC5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 142142Baculoviral IAP repeat-containing protein 5PRO_0000122356Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231N6-acetyllysine1 Publication
Modified residuei34 – 341Phosphothreonine; by CDK1 and CDK15Combined sources2 Publications
Modified residuei48 – 481Phosphothreonine; by CK2; in vitro1 Publication
Modified residuei90 – 901N6-acetyllysine1 Publication
Modified residuei110 – 1101N6-acetyllysine1 Publication
Modified residuei112 – 1121N6-acetyllysine1 Publication
Modified residuei115 – 1151N6-acetyllysine1 Publication
Modified residuei117 – 1171Phosphothreonine; by AURKB1 Publication
Modified residuei121 – 1211N6-acetyllysine1 Publication
Modified residuei129 – 1291N6-acetyllysine1 Publication

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).4 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.
PhosphoSiteiO15392.

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 and AURKC. Interacts with JTB. Interacts with CDCA8 and INCENP; interaction is direct. 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
  • identical protein binding Source: IntAct
  • 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 interactions.
DIPiDIP-34662N.
IntActiO15392. 16 interactions.
MINTiMINT-147138.

Chemistry

BindingDBiO15392.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 103Combined sources
Helixi11 – 133Combined sources
Helixi15 – 206Combined sources
Beta strandi31 – 333Combined sources
Helixi35 – 406Combined sources
Beta strandi43 – 453Combined sources
Beta strandi49 – 513Combined sources
Beta strandi55 – 573Combined sources
Turni58 – 603Combined sources
Beta strandi63 – 653Combined sources
Helixi73 – 808Combined sources
Turni81 – 833Combined sources
Helixi85 – 884Combined sources
Helixi93 – 953Combined sources
Helixi98 – 13942Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 5-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15392.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati18 – 8871BIRAdd
BLAST

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

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 582CF → WV in AAW22624 (PubMed:16329164).Curated
Sequence conflicti58 – 581F → L in BAD97148 (Ref. 11) Curated
Sequence conflicti128 – 1281A → V in CAG46540 (Ref. 9) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291K → E Loss of acetylation; localization primarily within the cytoplasm; increased likelihood of existing as monomer; stronger binding to XPO1/CRM1. 2 Publications
Corresponds to variant rs2071214 [ dbSNP | Ensembl ].
VAR_021071

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei74 – 14269IEEHK…LAAMD → MQRKPTIRRKNLRKLRRKCA VPSSSWLPWIEASGRSCLVP EWLHHFQGLFPGATSLPVGP LAMS in isoform 3. 1 PublicationVSP_020338Add
BLAST
Alternative sequencei74 – 14269IEEHK…LAAMD → MRELC in isoform 6. 1 PublicationVSP_020339Add
BLAST
Alternative sequencei74 – 14269IEEHK…LAAMD → M in isoform 7. 1 PublicationVSP_020340Add
BLAST
Alternative sequencei74 – 741I → IGPGTVAYACNTSTLGGRGG RITR in isoform 2. 2 PublicationsVSP_002454
Alternative sequencei105 – 14238DRERA…LAAMD → VRETLPPPRSFIR in isoform 5. 1 PublicationVSP_020341Add
BLAST
Alternative sequencei114 – 14229AKETN…LAAMD → ERALLAE in isoform 4. 1 PublicationVSP_020342Add
BLAST

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
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. Positions 5-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106829. 59 interactions.
DIPiDIP-34662N.
IntActiO15392. 16 interactions.
MINTiMINT-147138.

Chemistry

BindingDBiO15392.
ChEMBLiCHEMBL5989.
GuidetoPHARMACOLOGYi2795.

Protein family/group databases

MEROPSiI32.005.

PTM databases

iPTMnetiO15392.
PhosphoSiteiO15392.

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

Phylogenomic databases

GeneTreeiENSGT00510000047537.
HOGENOMiHOG000172188.
HOVERGENiHBG050690.
InParanoidiO15392.
KOiK08731.

Enzyme and pathway databases

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

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: September 7, 2016
This is version 193 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.