Reviewed, UniProtKB/Swiss-Prot O15392 (BIRC5_HUMAN)

Names and origin

Protein names

Recommended name:
    Baculoviral IAP repeat-containing protein 5
Alternative name(s):
    Apoptosis inhibitor survivin
    Apoptosis inhibitor 4

Gene names

Name:	BIRC5
Synonyms:	API4, IAP4

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	142 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. 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 play a role in neoplasia. May counteract a default induction of apoptosis in G2/M phase. Inhibitor of caspase-3 and caspase-7. 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.21 Ref.26 Ref.30
Subunit structure	Monomer or homodimer. Exist as a homodimer in the apo state and as a monomer in the CPC-bound state. When phosphorylated, interacts with HBXIP; the resulting complex binds pro-caspase-9, as well as active caspase-9, but much less efficiently. Component of the CPC at least composed of BIRC5/survivin, CDCA8/borealin, INCENP and AURKB/Aurora-B. 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. Ref.18 Ref.21 Ref.26 Ref.30 Ref.19 Ref.20 Ref.23 Ref.24 Ref.25 Ref.27 Ref.34
Subcellular location	Cytoplasm. Nucleus. Centromere. Cytoplasm › cytoskeleton › spindle. Note: Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalizes with AURKB at mitotic chromosomes. Ref.18 Ref.21 Ref.30 Ref.19 Ref.3
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.30
Induction	Up-regulated by COMP. Ref.29
Domain	The BIR repeat is necessary and sufficient for HBXIP binding.
Post-translational modification	Ubiquitination is required for centrosomal targeting. In vitro phosphorylation at Thr-117 by AURKB/STK12 prevents interaction with INCENP and localization to mitotic chromosomes.
Sequence similarities	Belongs to the IAP family. Contains 1 BIR repeat.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Cell division Chromosome partition Mitosis
Cellular component	Centromere Chromosomal protein Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Protease inhibitor Thiol protease inhibitor
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Inferred from direct assay. Source: UniProtKB anti-apoptosis Inferred from direct assay. Source: UniProtKB apoptosis Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW chromosome segregation Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Inferred from mutant phenotype. Source: UniProtKB establishment of chromosome localization Inferred from mutant phenotype. Source: UniProtKB mitosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of caspase activity Inferred from direct assay. Source: UniProtKB positive regulation of exit from mitosis Inferred from mutant phenotype. Source: UniProtKB positive regulation of mitotic cell cycle Inferred from mutant phenotype. Source: UniProtKB protein complex localization Ref.23 Inferred from mutant phenotype. Source: UniProtKB spindle checkpoint Inferred from mutant phenotype. Source: UniProtKB
Cellular component	centriole Inferred from direct assay. Source: UniProtKB chromosome passenger complex Ref.30 Inferred from physical interaction. Source: UniProtKB chromosome, centromeric region Ref.3 Ref.21 Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from direct assay. Source: UniProtKB cytoplasmic microtubule Inferred from direct assay. Source: UniProtKB cytosol Ref.30 Inferred from direct assay. Source: UniProtKB interphase microtubule organizing center Inferred from direct assay. Source: UniProtKB midbody Ref.3 Inferred from direct assay. Source: MGI nuclear chromosome Ref.21 Inferred from direct assay. Source: UniProtKB spindle Inferred from electronic annotation. Source: UniProtKB-SubCell spindle microtubule Inferred from direct assay. Source: UniProtKB
Molecular function	Ran GTPase binding Ref.30 Inferred from physical interaction. Source: UniProtKB caspase inhibitor activity Inferred from mutant phenotype. Source: UniProtKB chaperone binding Inferred from physical interaction. Source: UniProtKB cobalt ion binding Non-traceable author statement. Source: UniProtKB cofactor binding Inferred from direct assay. Source: UniProtKB cysteine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Ref.26 Inferred from physical interaction. Source: IntAct microtubule binding Inferred from direct assay. Source: UniProtKB protein heterodimerization activity Inferred from direct assay. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-518838,EBI-518838
AURKB	Q96GD4	1	EBI-518823,EBI-624291
AURKB	Q96GD4	2	EBI-518838,EBI-624291
AURKB	Q96GD4	2	EBI-518842,EBI-624291
BIRC5	O15392-1	2	EBI-518842,EBI-518838
BIRC5	O15392-2	2	EBI-518838,EBI-518842
Birc6	O88738	1	EBI-518823,EBI-912068	From a different organism.
CASP9	P55211	1	EBI-518823,EBI-516799
CDC2	P06493	1	EBI-518823,EBI-444308
CDCA8	Q53HL2	2	EBI-518823,EBI-979174
CDCA8	Q53HL2	2	EBI-518838,EBI-979174
CDCA8	Q53HL2	2	EBI-518842,EBI-979174
PPP1CC	P36873-1	1	EBI-518823,EBI-356289
USF2	Q15853	1	EBI-518823,EBI-1055994

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: AKETNNKKKEFEETAEKVRRAIEQLAAMD → ERALLAE

Isoform 5 (identifier: O15392-5)

Also known as: SI;

The sequence of this isoform differs from the canonical sequence as follows:
     105-142: DRERAKNKIAKETNNKKKEFEETAEKVRRAIEQLAAMD → 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: IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAEKVRRAIEQLAAMD → 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: IEEHKKHSSGCAFLSVKKQFEELTLGEFLKLDRERAKNKIAKETNNKKKEFEETAEKVRRAIEQLAAMD → M

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 142

142

Baculoviral IAP repeat-containing protein 5

PRO_0000122356

Regions

Repeat

18 – 88

71

BIR

Sites

Metal binding

57

1

Zinc

Metal binding

60

1

Zinc

Metal binding

77

1

Zinc

Metal binding

84

1

Zinc

Amino acid modifications

Modified residue

34

1

Phosphothreonine; by CDC2 Ref.17 Ref.28 Ref.31

Modified residue

117

1

Phosphothreonine; by STK12 Ref.19

Natural variations

Alternative sequence

74 – 142

69

IEEHK…LAAMD → MQRKPTIRRKNLRKLRRKCA VPSSSWLPWIEASGRSCLVP EWLHHFQGLFPGATSLPVGP LAMS in isoform 3.

VSP_020338

Alternative sequence

74 – 142

69

IEEHK…LAAMD → MRELC in isoform 6.

VSP_020339

Alternative sequence

74 – 142

69

IEEHK…LAAMD → M in isoform 7.

VSP_020340

Alternative sequence

74

1

I → IGPGTVAYACNTSTLGGRGG RITR in isoform 2.

VSP_002454

Alternative sequence

105 – 142

38

DRERA…LAAMD → VRETLPPPRSFIR in isoform 5.

VSP_020341

Alternative sequence

114 – 142

29

AKETN…LAAMD → ERALLAE in isoform 4.

VSP_020342

Natural variant

129

1

E → K: dbSNP rs2071214. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.15

VAR_021071

Experimental info

Mutagenesis

23

1

K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-62, R-78 and R-79. Ref.21

Mutagenesis

34

1

T → A: Loss of HBXIP binding. Ref.18

Mutagenesis

34

1

T → E: Higher affinity for HBXIP binding. Ref.18

Mutagenesis

62

1

K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-78 and R-79. Ref.21

Mutagenesis

65

1

E → A: Almost abolishes RAN-binding. Does not disrupt binding to AURKB or CDCA8. Disrupts mitotic spindle assembly. Does not disrupt nuclear export. Ref.30

Mutagenesis

70

1

D → A: No change. Loss of interaction with AURKB; when associated A-71. Ref.22

Mutagenesis

71

1

D → A: No change. Loss of interaction with AURKB; when associated with A-70. Ref.22

Mutagenesis

78

1

K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-79. Ref.21

Mutagenesis

79

1

K → R: Increases ubiquitination and blocks dissociation from centromeres; when associated with R-23; R-62 and R-78. Ref.21

Mutagenesis

84

1

C → A: Loss of cytoprotection.

Mutagenesis

117

1

T → A: Prevents phosphorylation by STK12/AURKB. Still able to localize correctly but prevents interaction with INCENP. Ref.19

Mutagenesis

117

1

T → E: Mimics phosphorylation. Disrupts subcellular localization during mitosis and prevents interaction with INCENP. Ref.19

Sequence conflict

57 – 58

2

CF → WV in AAW22624. Ref.5

Sequence conflict

58

1

F → L in BAD97148. Ref.11

Sequence conflict

128

1

A → V in CAG46540. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

142

Helix Strand Turn

Details...

Turn

8 – 10

3

Helix

11 – 13

3

Helix

15 – 20

6

Helix

35 – 40

6

Beta strand

43 – 45

3

Beta strand

55 – 57

3

Turn

58 – 60

3

Helix

73 – 80

8

Helix

85 – 88

4

Helix

93 – 95

3

Helix

98 – 139

42

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified October 23, 2007. Version 2. Checksum: 9E7CADCDF28F9486	FASTA	142	16,390
	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 KKEFEETAEK VRRAIEQLAA MD
	Isoform 2 (2B) (Beta). Checksum: D1E961E51AD0661E	FASTA	165	18,637
	10 20 30 40 50 60 MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN EPDLAQCFFC 70 80 90 100 110 120 FKELEGWEPD DDPIGPGTVA YACNTSTLGG RGGRITREEH KKHSSGCAFL SVKKQFEELT 130 140 150 160 LGEFLKLDRE RAKNKIAKET NNKKKEFEET AEKVRRAIEQ LAAMD
	Isoform 3 (DeltaEx3). Checksum: 38C82D22E46BFF7C	FASTA	137	15,622
	10 20 30 40 50 60 MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN EPDLAQCFFC 70 80 90 100 110 120 FKELEGWEPD DDPMQRKPTI RRKNLRKLRR KCAVPSSSWL PWIEASGRSC LVPEWLHHFQ 130 GLFPGATSLP VGPLAMS
	Isoform 4 (3B). Checksum: 3904E8C8AF6945F7	FASTA	120	13,812
	10 20 30 40 50 60 MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN EPDLAQCFFC 70 80 90 100 110 120 FKELEGWEPD DDPIEEHKKH SSGCAFLSVK KQFEELTLGE FLKLDRERAK NKIERALLAE
	Isoform 5 (SI). Checksum: 82FC6A9B55F06876	FASTA	117	13,467
	10 20 30 40 50 60 MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN EPDLAQCFFC 70 80 90 100 110 FKELEGWEPD DDPIEEHKKH SSGCAFLSVK KQFEELTLGE FLKLVRETLP PPRSFIR
	Isoform 6 (3 alpha). Checksum: D06E2937DCAC8283	FASTA	78	8,991
	10 20 30 40 50 60 MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN EPDLAQCFFC 70 FKELEGWEPD DDPMRELC
	Isoform 7 (2 alpha). Checksum: 8CAC8283CD371FD9	FASTA	74	8,490
	10 20 30 40 50 60 MGAPTLPPAW QPFLKDHRIS TFKNWPFLEG CACTPERMAE AGFIHCPTEN EPDLAQCFFC 70 FKELEGWEPD DDPM

References

	« Hide 'large scale' referencesShow '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: 9256286] [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: 10626797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, TISSUE SPECIFICITY, VARIANT LYS-129.
[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: 11084331] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANT LYS-129.
[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: 14741722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, VARIANT LYS-129. 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: 16329164] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), VARIANT LYS-129, 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), VARIANT LYS-129. 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), VARIANT LYS-129.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LYS-129.
[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), VARIANT LYS-129.
[12]	NIEHS SNPs program Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-129.
[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: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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. , 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], VARIANT LYS-129.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LYS-129. 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: 9859993] [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: 11069302] [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: 12773388] [Abstract] Cited for: FUNCTION IN APOPTOSIS SUPPRESSION, INTERACTION WITH 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: 14610074] [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: 15249581] [Abstract] Cited for: INTERACTION WITH CDCA8.
[21]	"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: 16322459] [Abstract] Cited for: FUNCTION, INTERACTION WITH USP9X, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF LYS-23; LYS-62; LYS-78 AND LYS-79.
[22]	"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: 16762323] [Abstract] Cited for: MUTAGENESIS OF ASP-70; ASP-71 AND 70-ASP--ASP-71.
[23]	"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: 16239925] [Abstract] Cited for: INTERACTION WITH CDCA8.
[24]	"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: 16427043] [Abstract] Cited for: INTERACTION WITH CDCA8.
[25]	"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: 16764853] [Abstract] Cited for: INTERACTION WITH EVI5.
[26]	"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: 16291752] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDCA8.
[27]	"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: 16436504] [Abstract] Cited for: INTERACTION WITH CDCA8.
[28]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, MASS SPECTROMETRY. Tissue: Epithelium.
[29]	"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: 17993464] [Abstract] Cited for: INDUCTION.
[30]	"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: 18591255] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAN; AURKB AND CDCA8, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLU-65.
[31]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, MASS SPECTROMETRY.
[32]	"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: 10949039] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF ISOFORM 1.
[33]	"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: 10876248] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF ISOFORM 1.
[34]	"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: 17956729] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC IONS, SUBUNIT, INTERACTION WITH CDCA8 AND INCENP.
[35]	"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: 19530738] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.
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.

IPI

IPI00006210.
IPI00218095.
IPI00735946.
IPI00784873.
IPI00784916.
IPI00784964.
IPI00785191.

RefSeq

NP_001012270.1.
NP_001012271.1.
NP_001159.2.

UniGene

Hs.514527

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O15392. 16 interactions.

STRING

O15392.

Protein family/group databases

MEROPS

I32.005.

PTM databases

PhosphoSite

O15392.

Proteomic databases

PRIDE

O15392.

Genome annotation databases

Ensembl

ENST00000350051; ENSP00000324180; ENSG00000089685; Homo sapiens. [Genome view]

GeneID

332.

KEGG

hsa:332.

NMPDR

fig|9606.3.peg.14485.

UCSC

uc002jvc.2. human.
uc002jvf.1. human.
uc002jvg.1. human.
uc002jvh.1. human.

Organism-specific databases

CTD

332.

GeneCards

GC17P073722.

H-InvDB

HIX0037877.

HGNC

HGNC:593. BIRC5.

HPA

CAB004270.
HPA002830.

MIM

603352. gene.

PharmGKB

PA25362.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O15392.

OMA

SCTPERM.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_a_pathway. Aurora A signaling.
aurora_b_pathway. Aurora B signaling.
foxm1pathway. FOXM1 transcription factor network.

Reactome

REACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpress

O15392.

Bgee

O15392.

CleanEx

HS_BIRC5.

Genevestigator

O15392.

GermOnline

ENSG00000089685. Homo sapiens.

Family and domain databases

InterPro

IPR001370. Prot_inh_I32_IAP.
[Graphical view]

Pfam

PF00653. BIR. 1 hit.
[Graphical view]

SMART

SM00238. BIR. 1 hit.
[Graphical view]

PROSITE

PS01282. BIR_REPEAT_1. False negative.
PS50143. BIR_REPEAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

1369.

SOURCE

Search...

Entry information

Entry name

BIRC5_HUMAN

Accession

Primary (citable) accession number: O15392
Secondary accession number(s): B2R4R1 , Q2I3N8, Q4VGX0, Q53F61, Q5MGC6, Q6FHL2, Q75SP2, Q9P2W8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	October 23, 2007
Last modified:	January 19, 2010
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.