Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O15392 (BIRC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Baculoviral IAP repeat-containing protein 5
Alternative name(s):
Apoptosis inhibitor 4
Apoptosis inhibitor survivin
Gene names
Name:BIRC5
Synonyms:API4, IAP4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.16 Ref.18 Ref.23 Ref.28 Ref.33 Ref.34 Ref.37

Subunit structure

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. Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.33 Ref.34 Ref.36 Ref.37 Ref.40

Subcellular location

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. Ref.3 Ref.18 Ref.19 Ref.21 Ref.23 Ref.33 Ref.34

Tissue specificity

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. Ref.2 Ref.4 Ref.5

Developmental stage

Expression is cell cycle-dependent and peaks at mitosis. Ref.33

Induction

Up-regulated by COMP. Ref.31

Domain

The BIR repeat is necessary and sufficient for LAMTOR5 binding.

Post-translational modification

Ubiquitination is required for centrosomal targeting.

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.

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. Ref.34

Sequence similarities

Belongs to the IAP family.

Contains 1 BIR repeat.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
Cell division
Chromosome partition
Mitosis
Transcription
Transcription regulation
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Kinetochore
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMetal-binding
Zinc
   Molecular functionProtease inhibitor
Repressor
Thiol protease inhibitor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Inferred from direct assay Ref.16. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from mutant phenotype PubMed 12805209. Source: UniProtKB

chromosome segregation

Inferred from electronic annotation. Source: UniProtKB-KW

cytokinesis

Inferred from mutant phenotype PubMed 12805209. Source: UniProtKB

establishment of chromosome localization

Inferred from mutant phenotype PubMed 12805209. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of apoptotic process

Inferred from direct assay Ref.2Ref.18Ref.1Ref.16. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay Ref.18. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.34. Source: UniProtKB

positive regulation of cell proliferation

Traceable author statement Ref.22. Source: UniProtKB

positive regulation of exit from mitosis

Inferred from mutant phenotype PubMed 12805209. Source: UniProtKB

positive regulation of mitotic cell cycle

Inferred from mutant phenotype Ref.28. Source: UniProtKB

protein complex localization

Inferred from mutant phenotype Ref.25. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.35. Source: UniProtKB

spindle checkpoint

Inferred from mutant phenotype PubMed 12805209. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentriole

Inferred from direct assay Ref.16. Source: UniProtKB

chromosome passenger complex

Inferred from physical interaction PubMed 15260989Ref.33. Source: UniProtKB

chromosome, centromeric region

Inferred from direct assay Ref.23PubMed 11516652Ref.28. Source: UniProtKB

condensed chromosome kinetochore

Inferred from direct assay Ref.21. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: LIFEdb

cytoplasmic microtubule

Inferred from direct assay Ref.16. Source: UniProtKB

cytosol

Inferred from direct assay Ref.33Ref.18. Source: UniProtKB

interphase microtubule organizing center

Inferred from direct assay Ref.16. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

midbody

Inferred from direct assay Ref.21Ref.17Ref.28Ref.16. Source: UniProtKB

nuclear chromosome

Inferred from direct assay Ref.23. Source: UniProtKB

nucleus

Inferred from direct assay Ref.21Ref.34. Source: UniProtKB

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle microtubule

Inferred from direct assay Ref.17Ref.16. Source: UniProtKB

   Molecular_functionRan GTPase binding

Inferred from physical interaction Ref.33. Source: UniProtKB

chaperone binding

Inferred from physical interaction PubMed 18086682. Source: UniProtKB

cobalt ion binding

Non-traceable author statement Ref.38. Source: UniProtKB

cofactor binding

Inferred from direct assay Ref.18. Source: UniProtKB

cysteine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from mutant phenotype Ref.16. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.23. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.28. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule binding

Inferred from direct assay Ref.16. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.19Ref.21Ref.25Ref.34Ref.37Ref.17PubMed 11516652Ref.18PubMed 15628841Ref.28. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay Ref.28. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.39Ref.38. Source: UniProtKB

tubulin binding

Inferred from direct assay Ref.16. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.39. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15392-1)

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.
Isoform 2 (identifier: O15392-2)

Also known as: 2B; Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     74-74: I → IGPGTVAYACNTSTLGGRGGRITR
Isoform 3 (identifier: O15392-3)

Also known as: DeltaEx3;

The sequence of this isoform differs from the canonical sequence as follows:
     74-142: IEEHKKHSSG...RAIEQLAAMD → MQRKPTIRRK...SLPVGPLAMS
Isoform 4 (identifier: O15392-4)

Also known as: 3B;

The sequence of this isoform differs from the canonical sequence as follows:
     114-142: AKETNNKKKEFEETAKKVRRAIEQLAAMD → ERALLAE
Isoform 5 (identifier: O15392-5)

Also known as: SI;

The sequence of this isoform differs from the canonical sequence as follows:
     105-142: DRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD → VRETLPPPRSFIR
Isoform 6 (identifier: O15392-6)

Also known as: 3 alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     74-142: IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAKKVRRAIEQLAAMD → MRELC
Isoform 7 (identifier: O15392-7)

Also known as: 2 alpha;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 142142Baculoviral IAP repeat-containing protein 5
PRO_0000122356

Regions

Repeat18 – 8871BIR

Sites

Metal binding571Zinc
Metal binding601Zinc
Metal binding771Zinc
Metal binding841Zinc

Amino acid modifications

Modified residue231N6-acetyllysine Ref.34
Modified residue341Phosphothreonine; by CDK1 Ref.17 Ref.32
Modified residue481Phosphothreonine; by CK2; in vitro Ref.35
Modified residue901N6-acetyllysine Ref.34
Modified residue1101N6-acetyllysine Ref.34
Modified residue1121N6-acetyllysine Ref.34
Modified residue1151N6-acetyllysine Ref.34
Modified residue1171Phosphothreonine; by AURKB Ref.19
Modified residue1211N6-acetyllysine Ref.34
Modified residue1291N6-acetyllysine Ref.34

Natural variations

Alternative sequence74 – 14269IEEHK…LAAMD → MQRKPTIRRKNLRKLRRKCA VPSSSWLPWIEASGRSCLVP EWLHHFQGLFPGATSLPVGP LAMS in isoform 3.
VSP_020338
Alternative sequence74 – 14269IEEHK…LAAMD → MRELC in isoform 6.
VSP_020339
Alternative sequence74 – 14269IEEHK…LAAMD → M in isoform 7.
VSP_020340
Alternative sequence741I → IGPGTVAYACNTSTLGGRGG RITR in isoform 2.
VSP_002454
Alternative sequence105 – 14238DRERA…LAAMD → VRETLPPPRSFIR in isoform 5.
VSP_020341
Alternative sequence114 – 14229AKETN…LAAMD → ERALLAE in isoform 4.
VSP_020342
Natural variant1291K → E Loss of acetylation; localization primarily within the cytoplasm; increased likelihood of existing as monomer; stronger binding to XPO1/CRM1. Ref.13 Ref.34
Corresponds to variant rs2071214 [ dbSNP | Ensembl ].
VAR_021071

Experimental info

Mutagenesis231K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-62; R-78 and R-79. Ref.23
Mutagenesis341T → A: Loss of LAMTOR5 binding. Ref.18
Mutagenesis341T → E: Higher affinity for LAMTOR5 binding. Ref.18
Mutagenesis481T → A or E: Localizes normally during mitosis but cannot support cell proliferation. Increased affinity for CDCA8/borealin. Ref.35
Mutagenesis621K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-78 and R-79. Ref.23
Mutagenesis651E → A: Almost abolishes RAN-binding. Does not disrupt binding to AURKB or CDCA8. Disrupts mitotic spindle assembly. Does not disrupt nuclear export. Ref.33
Mutagenesis701D → A: No change. Loss of interaction with AURKB; when associated with A-71. Ref.24
Mutagenesis711D → A: No change. Loss of interaction with AURKB; when associated with A-70. Ref.24
Mutagenesis781K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-79. Ref.23
Mutagenesis791K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-78. Ref.23
Mutagenesis841C → A: Loss of cytoprotection.
Mutagenesis1171T → A: Prevents phosphorylation by AURKB. Still able to localize correctly but prevents interaction with INCENP. Ref.19
Mutagenesis1171T → E: Mimics phosphorylation. Disrupts subcellular localization during mitosis and prevents interaction with INCENP. Ref.19
Mutagenesis1291K → A or Q: Mimics acetylation. Localization primarily within the nucleus. Ref.34
Mutagenesis1291K → R: Loss of acetylation. Localization primarily within the cytoplasm. Ref.34
Sequence conflict57 – 582CF → WV in AAW22624. Ref.5
Sequence conflict581F → L in BAD97148. Ref.11
Sequence conflict1281A → V in CAG46540. Ref.9

Secondary structure

............................ 142
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified March 21, 2012. Version 3.
Checksum: 9E7CADCDF2822286

FASTA14216,389
        10         20         30         40         50         60 
MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN EPDLAQCFFC 

        70         80         90        100        110        120 
FKELEGWEPD DDPIEEHKKH SSGCAFLSVK KQFEELTLGE FLKLDRERAK NKIAKETNNK 

       130        140 
KKEFEETAKK VRRAIEQLAA MD 

« Hide

Isoform 2 (2B) (Beta) [UniParc].

Checksum: D1E961E51ADDD01E
Show »

FASTA16518,636
Isoform 3 (DeltaEx3) [UniParc].

Checksum: 38C82D22E46BFF7C
Show »

FASTA13715,622
Isoform 4 (3B) [UniParc].

Checksum: 3904E8C8AF6945F7
Show »

FASTA12013,812
Isoform 5 (SI) [UniParc].

Checksum: 82FC6A9B55F06876
Show »

FASTA11713,467
Isoform 6 (3 alpha) [UniParc].

Checksum: D06E2937DCAC8283
Show »

FASTA788,991
Isoform 7 (2 alpha) [UniParc].

Checksum: 8CAC8283CD371FD9
Show »

FASTA748,490

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Regulation of apoptosis at cell division by p34cdc2 phosphorylation of survivin."
O'Connor D.S., Grossman D., Plescia J., Li F., Zhang H., Villa A., Tognin S., Marchisio P.C., Altieri D.C.
Proc. Natl. Acad. Sci. U.S.A. 97:13103-13107(2000) [PubMed] [Europe PMC] [Abstract]
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]"Survivin monomer plays an essential role in apoptosis regulation."
Pavlyukov M.S., Antipova N.V., Balashova M.V., Vinogradova T.V., Kopantzev E.P., Shakhparonov M.I.
J. Biol. Chem. 286:23296-23307(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH XIAP/BIRC4 AND DIABLO/SMAC.
[38]"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.
[39]"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.
[40]"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.
[41]"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).
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11755.1. [O15392-1]
CCDS32751.1. [O15392-3]
CCDS32752.1. [O15392-2]
RefSeqNP_001012270.1. NM_001012270.1. [O15392-3]
NP_001012271.1. NM_001012271.1.
NP_001159.2. NM_001168.2.
UniGeneHs.744872.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalO15392.
SMRO15392. Positions 5-142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106829. 35 interactions.
DIPDIP-34662N.
IntActO15392. 13 interactions.
MINTMINT-147138.
STRING9606.ENSP00000301633.

Chemistry

BindingDBO15392.
ChEMBLCHEMBL5989.

Protein family/group databases

MEROPSI32.005.

PTM databases

PhosphoSiteO15392.

Proteomic databases

MaxQBO15392.
PaxDbO15392.
PRIDEO15392.

Protocols and materials databases

DNASU332.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374948; ENSP00000364086; ENSG00000089685. [O15392-3]
ENST00000590449; ENSP00000465868; ENSG00000089685. [O15392-7]
ENST00000590925; ENSP00000467336; ENSG00000089685. [O15392-4]
ENST00000592734; ENSP00000466617; ENSG00000089685. [O15392-6]
GeneID332.
KEGGhsa:332.
UCSCuc002jvg.3. human. [O15392-1]
uc002jvh.3. human. [O15392-3]

Organism-specific databases

CTD332.
GeneCardsGC17P076210.
HGNCHGNC:593. BIRC5.
HPACAB004270.
HPA002830.
MIM603352. gene.
neXtProtNX_O15392.
PharmGKBPA25362.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271140.
HOVERGENHBG050690.
KOK08731.
OMAEYEMSEN.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkO15392.

Gene expression databases

ArrayExpressO15392.
BgeeO15392.
CleanExHS_BIRC5.
GenevestigatorO15392.

Family and domain databases

Gene3D1.10.1170.10. 1 hit.
InterProIPR001370. BIR.
[Graphical view]
PfamPF00653. BIR. 1 hit.
[Graphical view]
SMARTSM00238. BIR. 1 hit.
[Graphical view]
PROSITEPS50143. BIR_REPEAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBIRC5. human.
EvolutionaryTraceO15392.
GeneWikiSurvivin.
GenomeRNAi332.
NextBio1369.
PROO15392.
SOURCESearch...

Entry information

Entry nameBIRC5_HUMAN
AccessionPrimary (citable) accession number: O15392
Secondary accession number(s): A2SUH6 expand/collapse secondary AC list , B2R4R1, Q2I3N8, Q4VGX0, Q53F61, Q5MGC6, Q6FHL2, Q75SP2, Q9P2W8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: March 21, 2012
Last modified: July 9, 2014
This is version 170 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM