BI51A_XENLA
ID BI51A_XENLA Reviewed; 160 AA.
AC Q8JGN5; Q4V7U0; Q50L40; Q8JG75;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Baculoviral IAP repeat-containing protein 5.1-A;
DE AltName: Full=Bir1-A protein {ECO:0000312|EMBL:AAH73047.1};
DE Short=Survivin/XBIR1 {ECO:0000303|PubMed:12464631};
DE Short=XBIR1 {ECO:0000303|PubMed:12464631};
DE AltName: Full=Survivin1-a;
DE Short=XSurvivin1 {ECO:0000303|PubMed:15853809};
DE Short=XSurvivin1A {ECO:0000312|EMBL:BAD98265.1};
DE Short=Xsvv1 {ECO:0000303|PubMed:15853809};
DE Short=xSurvivin {ECO:0000303|PubMed:12221116};
GN Name=birc5.1-a;
GN Synonyms=bir1-A {ECO:0000312|EMBL:AAH73047.1},
GN svv1 {ECO:0000303|PubMed:15853809};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM44085.1}
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A COMPLEX WITH AURKB AND
RP INCENP, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte {ECO:0000269|PubMed:12464631};
RX PubMed=12464631; DOI=10.1101/gad.249202;
RA Losada A., Hirano M., Hirano T.;
RT "Cohesin release is required for sister chromatid resolution, but not for
RT condensin-mediated compaction, at the onset of mitosis.";
RL Genes Dev. 16:3004-3016(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAM76714.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH INCENP, PUTATIVE
RP INTERACTION WITH AURKB, AND IDENTIFICATION IN A COMPLEX WITH AURKB AND
RP INCENP.
RC TISSUE=Gastrula {ECO:0000269|PubMed:12221116};
RX PubMed=12221116; DOI=10.1091/mbc.e02-02-0092;
RA Bolton M.A., Lan W., Powers S.E., McCleland M.L., Kuang J.,
RA Stukenberg P.T.;
RT "Aurora B kinase exists in a complex with survivin and INCENP and its
RT kinase activity is stimulated by survivin binding and phosphorylation.";
RL Mol. Biol. Cell 13:3064-3077(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAD98265.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND LACK OF ANTI-APOPTOTIC FUNCTION.
RC TISSUE=Oocyte {ECO:0000269|PubMed:15853809};
RX PubMed=15853809; DOI=10.1111/j.1742-4658.2005.04648.x;
RA Tsuchiya Y., Murai S., Yamashita S.;
RT "Apoptosis-inhibiting activities of BIR family proteins in Xenopus egg
RT extracts.";
RL FEBS J. 272:2237-2250(2005).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, AND MUTAGENESIS OF THR-43.
RX PubMed=16888809; DOI=10.1002/jcb.21065;
RA Canovas P.M., Guadagno T.M.;
RT "Functional analysis of Survivin in spindle assembly in Xenopus egg
RT extracts.";
RL J. Cell. Biochem. 100:217-229(2007).
RN [5] {ECO:0000312|EMBL:AAH73047.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg {ECO:0000312|EMBL:AAH97720.1}, and
RC Ovary {ECO:0000312|EMBL:AAH73047.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP IDENTIFICATION IN A COMPLEX WITH AURKB; CDCA9 AND INCENP.
RX PubMed=15260989; DOI=10.1016/j.cell.2004.06.026;
RA Sampath S.C., Ohi R., Leismann O., Salic A., Pozniakovski A., Funabiki H.;
RT "The chromosomal passenger complex is required for chromatin-induced
RT microtubule stabilization and spindle assembly.";
RL Cell 118:187-202(2004).
RN [7] {ECO:0000305}
RP INTERACTION WITH USP9X, IDENTIFICATION IN A COMPLEX WITH USP9X; NPLOC4 AND
RP UFD1, AND IDENTIFICATION IN A COMPLEX WITH AURKB AND INCENP.
RX PubMed=16322459; DOI=10.1126/science.1120160;
RA Vong Q.P., Cao K., Li H.Y., Iglesias P.A., Zheng Y.;
RT "Chromosome alignment and segregation regulated by ubiquitination of
RT survivin.";
RL Science 310:1499-1504(2005).
RN [8] {ECO:0000305}
RP INTERACTION WITH INCENP, AND IDENTIFICATION IN A COMPLEX WITH AURKB;
RP BIRC5.2; CDCA8; CDCA9 AND INCENP.
RX PubMed=17199039; DOI=10.1016/j.devcel.2006.11.001;
RA Kelly A.E., Sampath S.C., Maniar T.A., Woo E.M., Chait B.T., Funabiki H.;
RT "Chromosomal enrichment and activation of the aurora B pathway are coupled
RT to spatially regulate spindle assembly.";
RL Dev. Cell 12:31-43(2007).
RN [9] {ECO:0000305}
RP INDUCTION.
RX PubMed=18378691; DOI=10.1128/mcb.00169-08;
RA Yamamoto T.M., Lewellyn A.L., Maller J.L.;
RT "Regulation of the Aurora B chromosome passenger protein complex during
RT oocyte maturation in Xenopus laevis.";
RL Mol. Cell. Biol. 28:4196-4203(2008).
RN [10] {ECO:0000305}
RP INTERACTION WITH RAN.
RX PubMed=18591255; DOI=10.1128/mcb.02039-07;
RA Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.;
RT "A survivin-ran complex regulates spindle formation in tumor cells.";
RL Mol. Cell. Biol. 28:5299-5311(2008).
RN [11] {ECO:0000305}
RP REVIEW.
RX PubMed=16344111; DOI=10.1016/s0074-7696(05)47002-3;
RA Wheatley S.P., McNeish I.A.;
RT "Survivin: a protein with dual roles in mitosis and apoptosis.";
RL Int. Rev. Cytol. 247:35-88(2005).
CC -!- FUNCTION: Component of the chromosomal passenger complex (CPC), a
CC complex that acts as a key regulator of mitosis. The CPC complex has
CC essential functions at the centromere in ensuring correct chromosome
CC alignment and segregation and is required for chromatin-induced
CC microtubule stabilization and spindle assembly. Stimulates the mitotic
CC kinase activity of aurkb/aurora-B in the CPC. Does not appear to
CC exhibit anti-apoptotic activity. {ECO:0000269|PubMed:12221116,
CC ECO:0000269|PubMed:15853809, ECO:0000269|PubMed:16888809}.
CC -!- SUBUNIT: Component of the CPC at least composed of survivin/birc5,
CC incenp, cdca8/borealin and/or cdca9/dasra-A, and aurkb/aurora-B.
CC Interacts directly with incenp (via N-terminus), and may weakly
CC interact with aurkb (via N-terminus) to stabilize the complex.
CC Interacts with GTP-bound ran in both the S and M phases of the cell
CC cycle. Also found in a complex with ubiquitin-mediated signaling
CC proteins including at least usp9x/xFAM, nploc4/npl4 and ufd1.
CC {ECO:0000269|PubMed:12221116, ECO:0000269|PubMed:12464631,
CC ECO:0000269|PubMed:15260989, ECO:0000269|PubMed:16322459,
CC ECO:0000269|PubMed:17199039, ECO:0000269|PubMed:18591255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15392}. Nucleus
CC {ECO:0000269|PubMed:12464631}. Chromosome
CC {ECO:0000269|PubMed:12464631}. Chromosome, centromere
CC {ECO:0000269|PubMed:12464631}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:12464631}. Note=Localizes on chromosome arms and
CC inner centromeres from prophase through metaphase and then transferring
CC to the spindle midzone and midbody from anaphase through cytokinesis.
CC {ECO:0000250|UniProtKB:O15392, ECO:0000269|PubMed:12464631}.
CC -!- DEVELOPMENTAL STAGE: Expressed maternally.
CC {ECO:0000269|PubMed:12464631}.
CC -!- INDUCTION: By progesterone. {ECO:0000269|PubMed:18378691}.
CC -!- DOMAIN: C-terminus is required for spindle assembly.
CC {ECO:0000269|PubMed:16888809}.
CC -!- PTM: Ubiquitination is required for centrosome-targeting.
CC {ECO:0000250|UniProtKB:O15392}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH97720.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY100639; AAM44085.1; -; mRNA.
DR EMBL; AY115553; AAM76714.1; -; mRNA.
DR EMBL; AB197247; BAD98265.1; -; mRNA.
DR EMBL; BC073047; AAH73047.1; -; mRNA.
DR EMBL; BC097720; AAH97720.1; ALT_INIT; mRNA.
DR RefSeq; NP_001081100.1; NM_001087631.1.
DR RefSeq; NP_001082294.1; NM_001088825.1.
DR AlphaFoldDB; Q8JGN5; -.
DR SMR; Q8JGN5; -.
DR BioGRID; 98984; 5.
DR MEROPS; I32.005; -.
DR iPTMnet; Q8JGN5; -.
DR DNASU; 394382; -.
DR GeneID; 394382; -.
DR GeneID; 398389; -.
DR KEGG; xla:394382; -.
DR CTD; 394382; -.
DR Xenbase; XB-GENE-6254428; birc5.S.
DR OrthoDB; 1404665at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 394382; Expressed in egg cell and 11 other tissues.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0032133; C:chromosome passenger complex; IPI:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
DR CDD; cd00022; BIR; 1.
DR InterPro; IPR001370; BIR_rpt.
DR Pfam; PF00653; BIR; 1.
DR SMART; SM00238; BIR; 1.
DR PROSITE; PS50143; BIR_REPEAT_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Cytoplasm; Cytoskeleton; Metal-binding; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..160
FT /note="Baculoviral IAP repeat-containing protein 5.1-A"
FT /id="PRO_0000382461"
FT REPEAT 27..97
FT /note="BIR"
FT /evidence="ECO:0000255"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15392,
FT ECO:0000255|PROSITE-ProRule:PRU00029"
FT MOD_RES 43
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250"
FT MUTAGEN 43
FT /note="T->A: Inhibits spindle assembly."
FT /evidence="ECO:0000269|PubMed:16888809"
FT MUTAGEN 43
FT /note="T->E: Mimics phosphorylation but still inhibits
FT spindle assembly."
FT /evidence="ECO:0000269|PubMed:16888809"
FT CONFLICT 27
FT /note="R -> C (in Ref. 3; BAD98265)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="H -> Q (in Ref. 2; AAM76714)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 160 AA; 18686 MW; 9AC32E02119DC609 CRC64;
MYSAKNRFVQ AVQRLQDFKN MYDYDARLAT FADWPFTENC KCTPESMAKA GFVHCPTENE
PDVACCFFCL KELEGWEPDD DPWTEHSKRS ANCGFLSLTK CVNDLTMEGF LRLEGDRIKS
FYRKFSTVVL QYVEEEMTAA TKRLLEYFSN QHHCSIDLDH
