INCEA_XENLA
ID INCEA_XENLA Reviewed; 873 AA.
AC O13024; Q4V878; Q7ZXJ9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Inner centromere protein A;
DE Short=XL-INCENP;
DE Short=xINC;
DE Short=xIncenp;
DE AltName: Full=Mitotic phosphoprotein 130;
GN Name=incenp-a;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9115395; DOI=10.1016/s0960-9822(06)00157-6;
RA Stukenberg P.T., Lustig K.D., McGarry T.J., King R.W., Kuang J.,
RA Kirschner M.W.;
RT "Systematic identification of mitotic phosphoproteins.";
RL Curr. Biol. 7:338-348(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION, INTERACTION WITH AURKB, AND DOMAIN.
RX PubMed=10996078; DOI=10.1016/s0960-9822(00)00673-4;
RA Adams R.R., Wheatleya S.P., Gouldsworthy A.M., Kandels-Lewis S.E.,
RA Carmena M., Smythe C., Gerloff D.L., Earnshaw W.C.;
RT "INCENP binds the Aurora-related kinase AIRK2 and is required to target it
RT to chromosomes, the central spindle and cleavage furrow.";
RL Curr. Biol. 10:1075-1078(2000).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH AURKB AND BIRC5.1, AND SUBCELLULAR
RP LOCATION.
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 [5]
RP FUNCTION, INTERACTION WITH AURKB AND BIRC5.1, AND IDENTIFICATION IN A
RP COMPLEX WITH AURKB AND BIRC5.1.
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 [6]
RP INTERACTION WITH MTUS1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12919681; DOI=10.1016/s1534-5807(03)00229-6;
RA Ohi R., Coughlin M.L., Lane W.S., Mitchison T.J.;
RT "An inner centromere protein that stimulates the microtubule depolymerizing
RT activity of a KinI kinesin.";
RL Dev. Cell 5:309-321(2003).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH BIRC5.1; CDCA9 AND AURKB, AND
RP IDENTIFICATION IN A COMPLEX WITH CDCA8.
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 [8]
RP IDENTIFICATION IN A COMPLEX WITH AURKB AND BIRC5.1.
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 [9]
RP FUNCTION, INTERACTION WITH BIRC5.1; BIRC5.2; CDCA8 AND CDCA9, AND
RP IDENTIFICATION IN A COMPLEX WITH AURKB; CDCA8; CDCA9; BIRC5.1 AND BIRC5.2.
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 798-840 IN COMPLEX WITH AURKB-A,
RP PHOSPHORYLATION AT SER-849 AND SER-850, DOMAIN, AND MUTAGENESIS OF PHE-837.
RX PubMed=15866179; DOI=10.1016/j.molcel.2005.03.031;
RA Sessa F., Mapelli M., Ciferri C., Tarricone C., Areces L.B.,
RA Schneider T.R., Stukenberg P.T., Musacchio A.;
RT "Mechanism of Aurora B activation by INCENP and inhibition by hesperadin.";
RL Mol. Cell 18:379-391(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. Acts as a scaffold
CC regulating CPC localization and activity. The C-terminus associates
CC with aurkb/aurora-B, the N-terminus associated with cdca8/borealin
CC and/or cdca9/dasra-A tethers the CPC to the inner centromere, and the
CC microtubule binding activity within the central SAH domain directs
CC aurkb/aurora-B toward substrates near microtubules. Activates aurkb.
CC {ECO:0000250|UniProtKB:P53352, ECO:0000269|PubMed:12221116,
CC ECO:0000269|PubMed:17199039}.
CC -!- SUBUNIT: Component of the CPC composed of survivin/birc5, incenp,
CC cdca8/borealin and/or cdca9/dasra-A, and aurkb/aurora-B. Interacts (via
CC C-terminus) with aurkb (via N-terminus and kinase domain). Interacts
CC (via N-terminus) with birc5.1, birc5.2, cdca8 and cdca9. Interacts with
CC mtus1. {ECO:0000269|PubMed:10996078, ECO:0000269|PubMed:12221116,
CC ECO:0000269|PubMed:12464631, ECO:0000269|PubMed:12919681,
CC ECO:0000269|PubMed:15260989, ECO:0000269|PubMed:15866179,
CC ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:17199039, ECO:0000305}.
CC -!- INTERACTION:
CC O13024; Q6DE08: aurkb-a; NbExp=2; IntAct=EBI-1042275, EBI-1042262;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NQS7}.
CC Chromosome {ECO:0000269|PubMed:12464631}. Chromosome, centromere
CC {ECO:0000269|PubMed:10996078}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:10996078}. Midbody {ECO:0000250|UniProtKB:Q9NQS7}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9NQS7}.
CC Note=Localizes on chromosome arms and inner centromeres from prophase
CC through metaphase and then transferring to the spindle midzone and
CC midbody from anaphase through cytokinesis (PubMed:10996078).
CC Colocalizes to the equatorial cell cortex at anaphase
CC (PubMed:10996078). Colocalizes with AURKB at mitotic chromosomes
CC (PubMed:10996078). {ECO:0000269|PubMed:10996078}.
CC -!- DOMAIN: The IN box mediates interaction with aurkb/aurora-B.
CC {ECO:0000269|PubMed:15866179}.
CC -!- DOMAIN: The SAH (single alpha-helix) region is characterized by a high
CC content of charged residues which are predicted to stabilize the alpha-
CC helical structure by ionic bonds. It can refold after extension
CC suggesting an in vivo force-dependent function. The isolated SAH domain
CC is monomeric. {ECO:0000250|UniProtKB:P53352}.
CC -!- SIMILARITY: Belongs to the INCENP family. {ECO:0000305}.
CC -!- CAUTION: Originally predicted to contain a coiled coil domain but shown
CC to contain a stable SAH domain instead. {ECO:0000250|UniProtKB:P53352}.
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DR EMBL; U95094; AAC60120.1; -; mRNA.
DR EMBL; BC044958; AAH44958.1; -; mRNA.
DR EMBL; BC097506; AAH97506.1; -; mRNA.
DR RefSeq; NP_001081890.1; NM_001088421.1.
DR PDB; 2BFX; X-ray; 1.80 A; C/D=798-840.
DR PDB; 2BFY; X-ray; 1.80 A; C/D=798-840.
DR PDB; 2VGO; X-ray; 1.70 A; C/D=797-840.
DR PDB; 2VGP; X-ray; 1.70 A; C/D=798-840.
DR PDB; 2VRX; X-ray; 1.86 A; C/D=798-840.
DR PDB; 3ZTX; X-ray; 1.95 A; C/D=797-840.
DR PDB; 4B8L; X-ray; 3.00 A; D=797-840.
DR PDB; 4B8M; X-ray; 1.85 A; C/D=797-840.
DR PDB; 4C2V; X-ray; 1.49 A; C/D=797-840.
DR PDB; 4C2W; X-ray; 1.70 A; C/D=797-847.
DR PDB; 5EYK; X-ray; 1.93 A; C/D=790-847.
DR PDB; 5K3Y; X-ray; 1.60 A; C/D=790-847.
DR PDBsum; 2BFX; -.
DR PDBsum; 2BFY; -.
DR PDBsum; 2VGO; -.
DR PDBsum; 2VGP; -.
DR PDBsum; 2VRX; -.
DR PDBsum; 3ZTX; -.
DR PDBsum; 4B8L; -.
DR PDBsum; 4B8M; -.
DR PDBsum; 4C2V; -.
DR PDBsum; 4C2W; -.
DR PDBsum; 5EYK; -.
DR PDBsum; 5K3Y; -.
DR AlphaFoldDB; O13024; -.
DR SMR; O13024; -.
DR BioGRID; 99440; 9.
DR IntAct; O13024; 2.
DR iPTMnet; O13024; -.
DR PRIDE; O13024; -.
DR DNASU; 398105; -.
DR GeneID; 398105; -.
DR KEGG; xla:398105; -.
DR CTD; 398105; -.
DR Xenbase; XB-GENE-6251940; incenp.L.
DR OrthoDB; 671886at2759; -.
DR EvolutionaryTrace; O13024; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0032133; C:chromosome passenger complex; IPI:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005721; C:pericentric heterochromatin; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:InterPro.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IEA:InterPro.
DR GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
DR InterPro; IPR039130; INCENP.
DR InterPro; IPR022006; INCENP_N.
DR InterPro; IPR005635; Inner_centromere_prot_ARK-bd.
DR PANTHER; PTHR13142; PTHR13142; 1.
DR Pfam; PF03941; INCENP_ARK-bind; 1.
DR Pfam; PF12178; INCENP_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Cytoplasm; Cytoskeleton; Kinetochore; Microtubule;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..873
FT /note="Inner centromere protein A"
FT /id="PRO_0000278829"
FT REGION 50..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..707
FT /note="SAH"
FT /evidence="ECO:0000250|UniProtKB:P53352"
FT REGION 566..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..856
FT /note="IN box"
FT /evidence="ECO:0000305|PubMed:10996078"
FT COMPBIAS 68..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..449
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 849
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15866179"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15866179"
FT MUTAGEN 837
FT /note="F->A: Disrupts interaction with aurkb-a."
FT /evidence="ECO:0000269|PubMed:15866179"
FT CONFLICT 140
FT /note="T -> K (in Ref. 2; AAH97506)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="R -> C (in Ref. 2; AAH97506)"
FT /evidence="ECO:0000305"
FT CONFLICT 495..496
FT /note="Missing (in Ref. 2; AAH44958)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="M -> K (in Ref. 2; AAH44958)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="A -> T (in Ref. 2; AAH97506)"
FT /evidence="ECO:0000305"
FT HELIX 800..802
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 804..816
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 821..824
FT /evidence="ECO:0007829|PDB:4C2V"
FT TURN 825..827
FT /evidence="ECO:0007829|PDB:4C2V"
FT HELIX 833..836
FT /evidence="ECO:0007829|PDB:4C2V"
SQ SEQUENCE 873 AA; 101199 MW; EA3C7581315131FB CRC64;
MNDAECLSHL LQVCARKTEE FVRTLDSKHM VWLLEIEEEA RKMFSSDFNA EPELMPKTPS
QKRRRKKRTS ILPDENRDPS GRRISRRQSN ASWSSSVRRL SVRNQNKAND DSIQEEPAQL
KRMTRARAQA SIKSTPVLET ALPESPSQIC QKNAQVKISE QERRSAEQKL IESDFELKTV
PEITKDNVSE TVNSAVPAVP VTPENKSRAA GKLKIAASST PEQKAEMVDL TCESPRPANE
QQLNLSNQSA TPTGSKSDRR SVRRSLVVRK SSSRRASLAS QFSLASKRES MTREAVRKSI
RQSISQKKAA MEISSTSSQR SYQSSIEMVD DEITIKIRPE TVPSETVSEE APAAESPRRS
LRSRAFKKIA ISNLPDSEEP PRKVTRQMVA GNAEPTPETT EDAQNIRRKS YKRAVDELSD
DERPSEEERS PPRKKTPSPP CPPSKIVRPP PHMKSFLHTV QKNQLLMMTP GSIGKNIIMK
SFIKRNTPLK TDPKTEEKER QRLDALRKKE EAELQRKQKI EEGKKRKQEE LKVRREERLR
KVLQARERVE QLEEEKKKKI EQKFAQIDEK SEKVREDRMA EEKAKKKMTA KKQEEVECRR
KQEEEARRLK VKQMEEEERR HQELLQKKRE EEELERQKKI AEAKRLAEQE RERQLLAEKE
RLRAEREKER IEKEKALQLQ RELERAAQEK EQQRREAEER KKREQQERLE QERLRKEQEA
KRLQEEEQRK AKEQAAVAAS APVMNVTVDM QNSPACESYE MTPKSCKVPS VKVNEDNYGM
DLNSDDSTDD ESQPRKPIPA WASGNLLTQA IRQQYYKPID VDRMYGTIDS PKLEELFNKS
KPRYFKRTSS AVWHSPPLSS NRHHLAVGYG LKY
