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O15392

- BIRC5_HUMAN

UniProt

O15392 - BIRC5_HUMAN

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
  1. 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 binding Source: UniProtKB
    11. protein heterodimerization activity Source: UniProtKB
    12. protein homodimerization activity Source: UniProtKB
    13. Ran GTPase binding Source: UniProtKB
    14. tubulin binding Source: UniProtKB
    15. 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

    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 Source: UniProtKB-SubCell
    14. spindle microtubule Source: UniProtKB

    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

    ArrayExpressiO15392.
    BgeeiO15392.
    CleanExiHS_BIRC5.
    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
    AURKBQ96GD47EBI-518823,EBI-624291
    BECN1Q144573EBI-518823,EBI-949378
    CASP9P552112EBI-518823,EBI-516799
    CDCA8Q53HL214EBI-518823,EBI-979174
    GAS2L3Q86XJ14EBI-518823,EBI-9248152
    INCENPQ9NQS710EBI-518823,EBI-307907
    XPO1O149802EBI-518823,EBI-355867

    Protein-protein interaction databases

    BioGridi106829. 35 interactions.
    DIPiDIP-34662N.
    IntActiO15392. 14 interactions.
    MINTiMINT-147138.
    STRINGi9606.ENSP00000301633.

    Structurei

    Secondary structure

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

    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.
    HOVERGENiHBG050690.
    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

    MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN    50
    EPDLAQCFFC FKELEGWEPD DDPIEEHKKH SSGCAFLSVK KQFEELTLGE 100
    FLKLDRERAK NKIAKETNNK KKEFEETAKK VRRAIEQLAA MD 142
    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. 14 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.
    HOVERGENi HBG050690.
    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

    ArrayExpressi O15392.
    Bgeei O15392.
    CleanExi HS_BIRC5.
    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

    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 54:0-0(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 1, 2014
    This is version 172 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