Skip Header

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

O15392

- BIRC5_HUMAN

UniProt

O15392 - BIRC5_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 5

Gene

BIRC5

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. chaperone binding Source: UniProtKB
  2. cobalt ion binding Source: UniProtKB
  3. cofactor binding Source: UniProtKB
  4. cysteine-type endopeptidase inhibitor activity Source: UniProtKB-KW
  5. cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  6. enzyme binding Source: UniProtKB
  7. identical protein binding Source: IntAct
  8. metal ion binding Source: UniProtKB-KW
  9. microtubule binding Source: UniProtKB
  10. protein heterodimerization activity Source: UniProtKB
  11. protein homodimerization activity Source: UniProtKB
  12. Ran GTPase binding Source: UniProtKB
  13. tubulin binding Source: UniProtKB
  14. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell division Source: UniProtKB
  3. chromosome segregation Source: UniProtKB-KW
  4. cytokinesis Source: UniProtKB
  5. establishment of chromosome localization Source: UniProtKB
  6. G2/M transition of mitotic cell cycle Source: UniProtKB
  7. mitotic cell cycle Source: Reactome
  8. mitotic nuclear division Source: UniProtKB-KW
  9. negative regulation of apoptotic process Source: UniProtKB
  10. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  11. negative regulation of transcription, DNA-templated Source: UniProtKB
  12. positive regulation of cell proliferation Source: UniProtKB
  13. positive regulation of exit from mitosis Source: UniProtKB
  14. positive regulation of mitotic cell cycle Source: UniProtKB
  15. protein complex localization Source: UniProtKB
  16. protein phosphorylation Source: UniProtKB
  17. spindle checkpoint Source: UniProtKB
  18. 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

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.
SignaLinkiO15392.

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
ProteomesiUP000005640: 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

  1. centriole Source: UniProtKB
  2. chromosome, centromeric region Source: UniProtKB
  3. chromosome passenger complex Source: UniProtKB
  4. condensed chromosome kinetochore Source: UniProtKB
  5. cytoplasm Source: LIFEdb
  6. cytoplasmic microtubule Source: UniProtKB
  7. cytosol Source: UniProtKB
  8. interphase microtubule organizing center Source: UniProtKB
  9. microtubule Source: UniProtKB-KW
  10. midbody Source: UniProtKB
  11. nuclear chromosome Source: UniProtKB
  12. nucleus Source: UniProtKB
  13. 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.

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 CDK12 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. Phosphorylation at Thr-48 by CK2 is critical for its mitotic and anti-apoptotic activities.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

MaxQBiO15392.
PaxDbiO15392.
PRIDEiO15392.

PTM databases

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

BgeeiO15392.
CleanExiHS_BIRC5.
ExpressionAtlasiO15392. baseline and differential.
GenevestigatoriO15392.

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

Protein-protein interaction databases

BioGridi106829. 35 interactions.
DIPiDIP-34662N.
IntActiO15392. 16 interactions.
MINTiMINT-147138.
STRINGi9606.ENSP00000301633.

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:
PDBe
RCSB PDB
PDBj
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

eggNOGiNOG271140.
GeneTreeiENSGT00510000047537.
HOVERGENiHBG050690.
InParanoidiO15392.
KOiK08731.
OMAiEYEMSEN.

Family and domain databases

Gene3Di1.10.1170.10. 1 hit.
InterProiIPR001370. BIR.
[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. Align

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. 1 PublicationCurated
Sequence conflicti128 – 1281A → V in CAG46540. 1 PublicationCurated

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. 1 Publication
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:
EMBL
GenBank
DDBJ
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.
UCSCiuc002jvg.3. human. [O15392-1]
uc002jvh.3. human. [O15392-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11755.1. [O15392-1 ]
CCDS32751.1. [O15392-3 ]
CCDS32752.1. [O15392-2 ]
RefSeqi NP_001012270.1. NM_001012270.1. [O15392-3 ]
NP_001012271.1. NM_001012271.1.
NP_001159.2. NM_001168.2.
UniGenei Hs.744872.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E31 X-ray 2.71 A/B 1-142 [» ]
1F3H X-ray 2.58 A/B 1-142 [» ]
1XOX NMR - A/B 1-117 [» ]
2QFA X-ray 1.40 A 1-142 [» ]
2RAW X-ray 2.40 A 1-142 [» ]
2RAX X-ray 3.30 A/E/X 1-120 [» ]
3UEC X-ray 2.18 A 1-142 [» ]
3UED X-ray 2.70 A/C 1-142 [» ]
3UEE X-ray 2.61 A/C 1-142 [» ]
3UEF X-ray 2.45 A/C 1-142 [» ]
3UEG X-ray 2.80 A/B 1-142 [» ]
3UEH X-ray 2.60 A/B 1-142 [» ]
3UEI X-ray 2.70 A/B 1-142 [» ]
3UIG X-ray 2.40 A/B 1-142 [» ]
3UIH X-ray 2.40 A/B 1-142 [» ]
3UII X-ray 2.60 A/B 1-142 [» ]
3UIJ X-ray 2.70 A/B 1-142 [» ]
3UIK X-ray 2.70 A/B 1-142 [» ]
4A0I X-ray 2.60 A/B 1-142 [» ]
4A0J X-ray 2.80 A/B 1-142 [» ]
4A0N X-ray 2.74 A 1-142 [» ]
ProteinModelPortali O15392.
SMRi O15392. Positions 5-142.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106829. 35 interactions.
DIPi DIP-34662N.
IntActi O15392. 16 interactions.
MINTi MINT-147138.
STRINGi 9606.ENSP00000301633.

Chemistry

BindingDBi O15392.
ChEMBLi CHEMBL5989.

Protein family/group databases

MEROPSi I32.005.

PTM databases

PhosphoSitei O15392.

Proteomic databases

MaxQBi O15392.
PaxDbi O15392.
PRIDEi O15392.

Protocols and materials databases

DNASUi 332.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374948 ; ENSP00000364086 ; ENSG00000089685 . [O15392-3 ]
ENST00000590449 ; ENSP00000465868 ; ENSG00000089685 . [O15392-7 ]
ENST00000590925 ; ENSP00000467336 ; ENSG00000089685 . [O15392-4 ]
ENST00000592734 ; ENSP00000466617 ; ENSG00000089685 . [O15392-6 ]
GeneIDi 332.
KEGGi hsa:332.
UCSCi uc002jvg.3. human. [O15392-1 ]
uc002jvh.3. human. [O15392-3 ]

Organism-specific databases

CTDi 332.
GeneCardsi GC17P076210.
HGNCi HGNC:593. BIRC5.
HPAi CAB004270.
HPA002830.
MIMi 603352. gene.
neXtProti NX_O15392.
PharmGKBi PA25362.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271140.
GeneTreei ENSGT00510000047537.
HOVERGENi HBG050690.
InParanoidi O15392.
KOi K08731.
OMAi EYEMSEN.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.
SignaLinki O15392.

Miscellaneous databases

ChiTaRSi BIRC5. human.
EvolutionaryTracei O15392.
GeneWikii Survivin.
GenomeRNAii 332.
NextBioi 1369.
PROi O15392.
SOURCEi Search...

Gene expression databases

Bgeei O15392.
CleanExi HS_BIRC5.
ExpressionAtlasi O15392. baseline and differential.
Genevestigatori O15392.

Family and domain databases

Gene3Di 1.10.1170.10. 1 hit.
InterProi IPR001370. BIR.
[Graphical view ]
Pfami PF00653. BIR. 1 hit.
[Graphical view ]
SMARTi SM00238. BIR. 1 hit.
[Graphical view ]
PROSITEi PS50143. BIR_REPEAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma."
    Ambrosini G., Adida C., Altieri D.C.
    Nat. Med. 3:917-921(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  2. "Survivin-deltaEx3 and survivin-2B: two novel splice variants of the apoptosis inhibitor survivin with different antiapoptotic properties."
    Mahotka C., Wenzel M., Springer E., Gabbert H.E., Gerharz C.D.
    Cancer Res. 59:6097-6102(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, TISSUE SPECIFICITY.
  3. "Survivin and the inner centromere protein INCENP show similar cell-cycle localization and gene knockout phenotype."
    Uren A.G., Wong L., Pakusch M., Fowler K.J., Burrows F.J., Vaux D.L., Choo K.H.
    Curr. Biol. 10:1319-1328(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  4. "Identification of a novel splice variant of the human anti-apoptosis gene survivin."
    Badran A., Yoshida A., Ishikawa K., Goi T., Yamaguchi A., Ueda T., Inuzuka M.
    Biochem. Biophys. Res. Commun. 314:902-907(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY.
    Tissue: Myeloid leukemia cell.
  5. "Molecular cloning and bioinformatics analysis of a novel spliced variant of survivin from human breast cancer cells."
    Zheng W., Ma X., Wei D., Wang T., Ma Y., Yang S.
    DNA Seq. 16:321-328(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY.
    Tissue: Mammary cancer.
  6. "An isoform of survivin (survivin-beta) which has 23 amino acids insertion into the BIR domain."
    Kageyama H., Islam A., Takayasu H., Nakagawara A.
    Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Neuroblastoma.
  7. "Survivin 2 alpha: a novel survivin splice variant expressed in human malignancies."
    Caldas H., Honsey L.E., Altura R.A.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
  8. "Identification of a novel survivin splicing variant 3alpha in acute myeloid leukemia."
    Vietri M.T., Cioffi M., Sessa M., Sica V., Molinari A.M.
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
    Tissue: Myeloid leukemia cell.
  9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  10. "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] (ISOFORM 1).
  11. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  12. NIEHS SNPs program
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  13. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-129.
  14. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  15. "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: Lung, Mammary gland and Muscle.
  16. "Control of apoptosis and mitotic spindle checkpoint by survivin."
    Li F., Ambrosini G., Chu E.Y., Plescia J., Tognin S., Marchisio P.C., Altieri D.C.
    Nature 396:580-584(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. Cited for: PHOSPHORYLATION AT THR-34.
  18. "HBXIP functions as a cofactor of survivin in apoptosis suppression."
    Marusawa H., Matsuzawa S., Welsh K., Zou H., Armstrong R., Tamm I., Reed J.C.
    EMBO J. 22:2729-2740(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS SUPPRESSION, INTERACTION WITH LAMTOR5/HBXIP, MUTAGENESIS OF THR-34, SUBCELLULAR LOCATION.
  19. "Aurora-B phosphorylation in vitro identifies a residue of survivin that is essential for its localization and binding to inner centromere protein (INCENP) in vivo."
    Wheatley S.P., Henzing A.J., Dodson H., Khaled W., Earnshaw W.C.
    J. Biol. Chem. 279:5655-5660(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INCENP, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-117, MUTAGENESIS OF THR-117.
  20. "Borealin: a novel chromosomal passenger required for stability of the bipolar mitotic spindle."
    Gassmann R., Carvalho A., Henzing A.J., Ruchaud S., Hudson D.F., Honda R., Nigg E.A., Gerloff D.L., Earnshaw W.C.
    J. Cell Biol. 166:179-191(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDCA8.
  21. "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: SUBCELLULAR LOCATION, INTERACTION WITH BIRC2/C-IAP1.
  22. "Survivin: a protein with dual roles in mitosis and apoptosis."
    Wheatley S.P., McNeish I.A.
    Int. Rev. Cytol. 247:35-88(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  23. "Chromosome alignment and segregation regulated by ubiquitination of survivin."
    Vong Q.P., Cao K., Li H.Y., Iglesias P.A., Zheng Y.
    Science 310:1499-1504(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH USP9X, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF LYS-23; LYS-62; LYS-78 AND LYS-79.
  24. "Survivin mutant (Surv-DD70, 71AA) disrupts the interaction of Survivin with Aurora B and causes multinucleation in HeLa cells."
    Cao L., Yan X., Wu Y., Hu H., Li Q., Zhou T., Jiang S., Yu L.
    Biochem. Biophys. Res. Commun. 346:400-407(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-70; ASP-71 AND 70-ASP--ASP-71.
  25. "Survivin mediates targeting of the chromosomal passenger complex to the centromere and midbody."
    Vader G., Kauw J.J.W., Medema R.H., Lens S.M.A.
    EMBO Rep. 7:85-92(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDCA8.
  26. "Borealin/Dasra B is a cell cycle-regulated chromosomal passenger protein and its nuclear accumulation is linked to poor prognosis for human gastric cancer."
    Chang J.-L., Chen T.-H., Wang C.-F., Chiang Y.-H., Huang Y.-L., Wong F.-H., Chou C.-K., Chen C.-M.
    Exp. Cell Res. 312:962-973(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDCA8.
  27. "EVI5 protein associates with the INCENP-aurora B kinase-survivin chromosomal passenger complex and is involved in the completion of cytokinesis."
    Faitar S.L., Sossey-Alaoui K., Ranalli T.A., Cowell J.K.
    Exp. Cell Res. 312:2325-2335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EVI5.
  28. "Molecular analysis of survivin isoforms: evidence that alternatively spliced variants do not play a role in mitosis."
    Noton E.A., Colnaghi R., Tate S., Starck C., Carvalho A., Ko Ferrigno P., Wheatley S.P.
    J. Biol. Chem. 281:1286-1295(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDCA8.
  29. "Uncoupling the central spindle-associated function of the chromosomal passenger complex from its role at centromeres."
    Lens S.M.A., Rodriguez J.A., Vader G., Span S.W., Giaccone G., Medema R.H.
    Mol. Biol. Cell 17:1897-1909(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDCA8.
  30. "Final stages of cytokinesis and midbody ring formation are controlled by BRUCE."
    Pohl C., Jentsch S.
    Cell 132:832-845(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BIRC6/BRUCE.
  31. "Cartilage oligomeric matrix protein protects cells against death by elevating members of the IAP family of survival proteins."
    Gagarina V., Carlberg A.L., Pereira-Mouries L., Hall D.J.
    J. Biol. Chem. 283:648-659(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  32. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "A survivin-ran complex regulates spindle formation in tumor cells."
    Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.
    Mol. Cell. Biol. 28:5299-5311(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAN; AURKB AND CDCA8, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLU-65.
  34. "Acetylation directs survivin nuclear localization to repress STAT3 oncogenic activity."
    Wang H., Holloway M.P., Ma L., Cooper Z.A., Riolo M., Samkari A., Elenitoba-Johnson K.S., Chin Y.E., Altura R.A.
    J. Biol. Chem. 285:36129-36137(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAT3 AND XPO1/CRM1, ACETYLATION AT LYS-23; LYS-90; LYS-110; LYS-112; LYS-115; LYS-121 AND LYS-129, MUTAGENESIS OF LYS-129, CHARACTERIZATION OF VARIANT GLU-129.
  35. "Threonine 48 in the BIR domain of survivin is critical to its mitotic and anti-apoptotic activities and can be phosphorylated by CK2 in vitro."
    Barrett R.M., Colnaghi R., Wheatley S.P.
    Cell Cycle 10:538-548(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-48, MUTAGENESIS OF THR-48.
  36. "PAR, a protein involved in the cell cycle, is functionally related to chromosomal passenger proteins."
    Platica M., Ionescu A., Ivan E., Holland J.F., Mandeli J., Platica O.
    Int. J. Oncol. 38:777-785(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JTB.
  37. Cited for: FUNCTION, SUBUNIT, INTERACTION WITH XIAP/BIRC4 AND DIABLO/SMAC.
  38. "CUL9 mediates the functions of the 3M complex and ubiquitylates survivin to maintain genome integrity."
    Li Z., Pei X.H., Yan J., Yan F., Cappell K.M., Whitehurst A.W., Xiong Y.
    Mol. Cell 54:805-819(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  39. "Crystal structure of human survivin reveals a bow tie-shaped dimer with two unusual alpha-helical extensions."
    Chantalat L., Skoufias D.A., Kleman J.P., Jung B., Dideberg O., Margolis R.L.
    Mol. Cell 6:183-189(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF ISOFORM 1.
  40. "Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement."
    Verdecia M.A., Huang H., Dutil E., Kaiser D.A., Hunter T., Noel J.P.
    Nat. Struct. Biol. 7:602-608(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF ISOFORM 1.
  41. "Structure of a Survivin-Borealin-INCENP core complex reveals how chromosomal passengers travel together."
    Jeyaprakash A.A., Klein U.R., Lindner D., Ebert J., Nigg E.A., Conti E.
    Cell 131:271-285(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, INTERACTION WITH CDCA8 AND INCENP.
  42. "Phosphorylation of a borealin dimerization domain is required for proper chromosome segregation."
    Bourhis E., Lingel A., Phung Q., Fairbrother W.J., Cochran A.G.
    Biochemistry 48:6783-6793(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

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: October 29, 2014
This is version 173 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

External Data

Dasty 3