TACC3_HUMAN
ID TACC3_HUMAN Reviewed; 838 AA.
AC Q9Y6A5; Q2NKK4; Q3KQS5; Q9UMQ1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Transforming acidic coiled-coil-containing protein 3;
DE AltName: Full=ERIC-1;
GN Name=TACC3; Synonyms=ERIC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10366448; DOI=10.1006/geno.1999.5829;
RA Still I.H., Vince P., Cowell J.K.;
RT "The third member of the transforming acidic coiled coil-containing gene
RT family, TACC3, maps in 4p16, close to translocation breakpoints in multiple
RT myeloma, and is upregulated in various cancer cell lines.";
RL Genomics 58:165-170(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS TYR-275; SER-287 AND GLU-514.
RX PubMed=11298601; DOI=10.1046/j.1365-2141.2001.02644.x;
RA McKeveney P.J., Hodges V.M., Mullan R.N., Maxwell P., Simpson D.,
RA Thompson A., Winter P.C., Lappin T.R., Maxwell A.P.;
RT "Characterization and localization of expression of an erythropoietin-
RT induced gene, ERIC-1/TACC3, identified in erythroid precursor cells.";
RL Br. J. Haematol. 112:1016-1024(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-275; SER-287 AND
RP GLU-514.
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH GCN5L2 AND PCAF, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=14767476; DOI=10.1038/sj.onc.1207424;
RA Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.;
RT "The transforming acidic coiled coil proteins interact with nuclear histone
RT acetyltransferases.";
RL Oncogene 23:2559-2563(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-434, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION AT SER-558, AND SUBCELLULAR LOCATION.
RX PubMed=17545617; DOI=10.1158/0008-5472.can-07-0122;
RA LeRoy P.J., Hunter J.J., Hoar K.M., Burke K.E., Shinde V., Ruan J.,
RA Bowman D., Galvin K., Ecsedy J.A.;
RT "Localization of human TACC3 to mitotic spindles is mediated by
RT phosphorylation on Ser558 by Aurora A: a novel pharmacodynamic method for
RT measuring Aurora A activity.";
RL Cancer Res. 67:5362-5370(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-71; SER-317; SER-434
RP AND SER-558, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-71; SER-317 AND
RP SER-402, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP INTERACTION WITH CKAP5D AND CLATHRIN, FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF SER-558.
RX PubMed=21297582; DOI=10.1038/emboj.2011.15;
RA Booth D.G., Hood F.E., Prior I.A., Royle S.J.;
RT "A TACC3/ch-TOG/clathrin complex stabilises kinetochore fibres by inter-
RT microtubule bridging.";
RL EMBO J. 30:906-919(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP INTERACTION WITH CLATHRIN AND CKAP5, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP 566-LEU-LEU-567, AND FUNCTION.
RX PubMed=23918938; DOI=10.1083/jcb.201211127;
RA Hood F.E., Williams S.J., Burgess S.G., Richards M.W., Roth D., Straube A.,
RA Pfuhl M., Bayliss R., Royle S.J.;
RT "Coordination of adjacent domains mediates TACC3-ch-TOG-clathrin assembly
RT and mitotic spindle binding.";
RL J. Cell Biol. 202:463-478(2013).
RN [16]
RP FUNCTION OF THE TACC3/CH-TOG/CLATHRIN COMPLEX.
RX PubMed=23532825; DOI=10.1242/jcs.124834;
RA Cheeseman L.P., Harry E.F., McAinsh A.D., Prior I.A., Royle S.J.;
RT "Specific removal of TACC3-ch-TOG-clathrin at metaphase deregulates
RT kinetochore fiber tension.";
RL J. Cell Sci. 126:2102-2113(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-39; SER-71; SER-177;
RP SER-250; SER-317; SER-434 AND SER-558, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP INTERACTION WITH CKAP5, AND SUBCELLULAR LOCATION.
RX PubMed=25596274; DOI=10.1242/bio.201410843;
RA Gutierrez-Caballero C., Burgess S.G., Bayliss R., Royle S.J.;
RT "TACC3-ch-TOG track the growing tips of microtubules independently of
RT clathrin and Aurora-A phosphorylation.";
RL Biol. Open 4:170-179(2015).
CC -!- FUNCTION: Plays a role in the microtubule-dependent coupling of the
CC nucleus and the centrosome. Involved in the processes that regulate
CC centrosome-mediated interkinetic nuclear migration (INM) of neural
CC progenitors (By similarity). Acts as component of the TACC3/ch-
CC TOG/clathrin complex proposed to contribute to stabilization of
CC kinetochore fibers of the mitotic spindle by acting as inter-
CC microtubule bridge. The TACC3/ch-TOG/clathrin complex is required for
CC the maintenance of kinetochore fiber tension (PubMed:21297582,
CC PubMed:23532825). May be involved in the control of cell growth and
CC differentiation. May contribute to cancer (PubMed:14767476).
CC {ECO:0000250|UniProtKB:Q9JJ11, ECO:0000269|PubMed:14767476,
CC ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:23532825}.
CC -!- SUBUNIT: Interacts with microtubules. Interacts with CKAP5
CC independently of clathrin. Interacts with CKAP5 and clathrin forming
CC the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules
CC bridges; TACC3 (phosphorylated at Ser-558 by AURKA) and CLTC are
CC proposed to form a composite microtubule interaction surface
CC (PubMed:21297582, PubMed:23918938, PubMed:25596274). Interacts with
CC CCDC100/CEP120. The coiled coil C-terminal region interacts with AH
CC receptor nuclear translocator protein (ARNT) and ARNT2 (By similarity).
CC Interacts with GCN5L2 and PCAF (PubMed:14767476).
CC {ECO:0000250|UniProtKB:Q9JJ11, ECO:0000269|PubMed:14767476,
CC ECO:0000269|PubMed:21297582, ECO:0000269|PubMed:23918938,
CC ECO:0000269|PubMed:25596274}.
CC -!- INTERACTION:
CC Q9Y6A5; Q99819: ARHGDIG; NbExp=3; IntAct=EBI-2554984, EBI-10295284;
CC Q9Y6A5; Q9BZE9: ASPSCR1; NbExp=3; IntAct=EBI-2554984, EBI-1993677;
CC Q9Y6A5; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-2554984, EBI-745073;
CC Q9Y6A5; Q00994: BEX3; NbExp=3; IntAct=EBI-2554984, EBI-741753;
CC Q9Y6A5; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-2554984, EBI-739879;
CC Q9Y6A5; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-2554984, EBI-10175300;
CC Q9Y6A5; Q86Y33-5: CDC20B; NbExp=3; IntAct=EBI-2554984, EBI-11983537;
CC Q9Y6A5; Q96Q77: CIB3; NbExp=9; IntAct=EBI-2554984, EBI-10292696;
CC Q9Y6A5; Q14008: CKAP5; NbExp=7; IntAct=EBI-2554984, EBI-310585;
CC Q9Y6A5; P09496: CLTA; NbExp=3; IntAct=EBI-2554984, EBI-1171169;
CC Q9Y6A5; Q99988: GDF15; NbExp=3; IntAct=EBI-2554984, EBI-2116863;
CC Q9Y6A5; Q96DY2-2: IQCD; NbExp=3; IntAct=EBI-2554984, EBI-23670573;
CC Q9Y6A5; Q2M2Z5: KIZ; NbExp=6; IntAct=EBI-2554984, EBI-2554344;
CC Q9Y6A5; Q07866-2: KLC1; NbExp=3; IntAct=EBI-2554984, EBI-11979975;
CC Q9Y6A5; Q2WGJ6: KLHL38; NbExp=4; IntAct=EBI-2554984, EBI-6426443;
CC Q9Y6A5; Q9GZM8: NDEL1; NbExp=3; IntAct=EBI-2554984, EBI-928842;
CC Q9Y6A5; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-2554984, EBI-741048;
CC Q9Y6A5; Q5VTR2: RNF20; NbExp=3; IntAct=EBI-2554984, EBI-2372238;
CC Q9Y6A5; Q7Z614: SNX20; NbExp=3; IntAct=EBI-2554984, EBI-744896;
CC Q9Y6A5; Q8TC71: SPATA18; NbExp=3; IntAct=EBI-2554984, EBI-11334239;
CC Q9Y6A5; Q9NU19: TBC1D22B; NbExp=7; IntAct=EBI-2554984, EBI-8787464;
CC Q9Y6A5; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-2554984, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:17545617}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:17545617, ECO:0000269|PubMed:21297582,
CC ECO:0000269|PubMed:23918938}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q9PTG8}. Note=In complex with CKAP5 localized to
CC microtubule plus-ends in mitosis and interphase. In complex with CKAP5
CC and clathrin localized to inter-microtubule bridges in mitotic
CC spindles. {ECO:0000269|PubMed:25596274}.
CC -!- INDUCTION: Up-regulated in various cancer cell lines.
CC -!- SIMILARITY: Belongs to the TACC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TACC3ID42458ch4p16.html";
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DR EMBL; AF093543; AAD25964.1; -; mRNA.
DR EMBL; AJ243997; CAB53009.1; -; mRNA.
DR EMBL; BC106071; AAI06072.1; -; mRNA.
DR EMBL; BC111771; AAI11772.1; -; mRNA.
DR CCDS; CCDS3352.1; -.
DR RefSeq; NP_006333.1; NM_006342.2.
DR RefSeq; XP_016863142.1; XM_017007653.1.
DR PDB; 5LXN; X-ray; 2.08 A; A/B/C/D/E/F/G/H=758-838.
DR PDB; 5LXO; X-ray; 2.18 A; A/B/C/D/E/F/G/H=758-838.
DR PDB; 5ODS; X-ray; 3.09 A; E/F/G/H=550-567.
DR PDB; 5ODT; X-ray; 2.02 A; B=518-563.
DR PDBsum; 5LXN; -.
DR PDBsum; 5LXO; -.
DR PDBsum; 5ODS; -.
DR PDBsum; 5ODT; -.
DR AlphaFoldDB; Q9Y6A5; -.
DR SMR; Q9Y6A5; -.
DR BioGRID; 115723; 128.
DR CORUM; Q9Y6A5; -.
DR IntAct; Q9Y6A5; 75.
DR MINT; Q9Y6A5; -.
DR STRING; 9606.ENSP00000326550; -.
DR GlyGen; Q9Y6A5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y6A5; -.
DR MetOSite; Q9Y6A5; -.
DR PhosphoSitePlus; Q9Y6A5; -.
DR BioMuta; TACC3; -.
DR DMDM; 13431939; -.
DR EPD; Q9Y6A5; -.
DR jPOST; Q9Y6A5; -.
DR MassIVE; Q9Y6A5; -.
DR MaxQB; Q9Y6A5; -.
DR PaxDb; Q9Y6A5; -.
DR PeptideAtlas; Q9Y6A5; -.
DR PRIDE; Q9Y6A5; -.
DR ProteomicsDB; 86642; -.
DR Antibodypedia; 8499; 416 antibodies from 37 providers.
DR DNASU; 10460; -.
DR Ensembl; ENST00000313288.9; ENSP00000326550.4; ENSG00000013810.21.
DR Ensembl; ENST00000651472.1; ENSP00000498361.1; ENSG00000013810.21.
DR GeneID; 10460; -.
DR KEGG; hsa:10460; -.
DR MANE-Select; ENST00000313288.9; ENSP00000326550.4; NM_006342.3; NP_006333.1.
DR UCSC; uc003gdo.4; human.
DR CTD; 10460; -.
DR DisGeNET; 10460; -.
DR GeneCards; TACC3; -.
DR HGNC; HGNC:11524; TACC3.
DR HPA; ENSG00000013810; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MalaCards; TACC3; -.
DR MIM; 605303; gene.
DR neXtProt; NX_Q9Y6A5; -.
DR OpenTargets; ENSG00000013810; -.
DR Orphanet; 251579; Giant cell glioblastoma.
DR Orphanet; 251576; Gliosarcoma.
DR PharmGKB; PA36301; -.
DR VEuPathDB; HostDB:ENSG00000013810; -.
DR eggNOG; ENOG502QQ1G; Eukaryota.
DR GeneTree; ENSGT00940000158858; -.
DR HOGENOM; CLU_013959_0_0_1; -.
DR InParanoid; Q9Y6A5; -.
DR OMA; MEPAAML; -.
DR OrthoDB; 669540at2759; -.
DR PhylomeDB; Q9Y6A5; -.
DR TreeFam; TF333149; -.
DR PathwayCommons; Q9Y6A5; -.
DR Reactome; R-HSA-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR SignaLink; Q9Y6A5; -.
DR SIGNOR; Q9Y6A5; -.
DR BioGRID-ORCS; 10460; 382 hits in 1094 CRISPR screens.
DR ChiTaRS; TACC3; human.
DR GeneWiki; TACC3; -.
DR GenomeRNAi; 10460; -.
DR Pharos; Q9Y6A5; Tbio.
DR PRO; PR:Q9Y6A5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9Y6A5; protein.
DR Bgee; ENSG00000013810; Expressed in oocyte and 117 other tissues.
DR ExpressionAtlas; Q9Y6A5; baseline and differential.
DR Genevisible; Q9Y6A5; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:1902850; P:microtubule cytoskeleton organization involved in mitosis; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IEA:InterPro.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
DR InterPro; IPR039915; TACC.
DR InterPro; IPR007707; TACC_C.
DR PANTHER; PTHR13924; PTHR13924; 1.
DR Pfam; PF05010; TACC_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Mitosis; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..838
FT /note="Transforming acidic coiled-coil-containing protein
FT 3"
FT /id="PRO_0000179990"
FT REGION 123..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..577
FT /note="Necessary but not sufficient for spindle
FT localization"
FT /evidence="ECO:0000269|PubMed:23918938"
FT REGION 569..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..838
FT /note="Necessary but not sufficient for spindle
FT localization"
FT /evidence="ECO:0000269|PubMed:23918938"
FT COILED 637..837
FT /evidence="ECO:0000255"
FT COMPBIAS 135..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 558
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000269|PubMed:17545617,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT VARIANT 143
FT /note="E -> K (in dbSNP:rs34205238)"
FT /id="VAR_053714"
FT VARIANT 275
FT /note="C -> Y (in dbSNP:rs17132047)"
FT /evidence="ECO:0000269|PubMed:11298601,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_053715"
FT VARIANT 287
FT /note="G -> S (in dbSNP:rs1063743)"
FT /evidence="ECO:0000269|PubMed:11298601,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_053716"
FT VARIANT 514
FT /note="G -> E (in dbSNP:rs17680881)"
FT /evidence="ECO:0000269|PubMed:11298601,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_053717"
FT MUTAGEN 558
FT /note="S->A: Disrupts localization to mitotic spindle and
FT impairs recruitment of clathrin to mitotic spindle."
FT /evidence="ECO:0000269|PubMed:21297582"
FT MUTAGEN 566..567
FT /note="LL->AA: Impairs localization to mitotic spindle."
FT /evidence="ECO:0000269|PubMed:23918938"
FT CONFLICT 342
FT /note="V -> L (in Ref. 2; CAB53009)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="D -> G (in Ref. 2; CAB53009)"
FT /evidence="ECO:0000305"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:5ODT"
FT TURN 531..541
FT /evidence="ECO:0007829|PDB:5ODT"
FT HELIX 546..555
FT /evidence="ECO:0007829|PDB:5ODT"
FT HELIX 759..835
FT /evidence="ECO:0007829|PDB:5LXN"
SQ SEQUENCE 838 AA; 90360 MW; 07F056678096775E CRC64;
MSLQVLNDKN VSNEKNTENC DFLFSPPEVT GRSSVLRVSQ KENVPPKNLA KAMKVTFQTP
LRDPQTHRIL SPSMASKLEA PFTQDDTLGL ENSHPVWTQK ENQQLIKEVD AKTTHGILQK
PVEADTDLLG DASPAFGSGS SSESGPGALA DLDCSSSSQS PGSSENQMVS PGKVSGSPEQ
AVEENLSSYS LDRRVTPASE TLEDPCRTES QHKAETPHGA EEECKAETPH GAEEECRHGG
VCAPAAVATS PPGAIPKEAC GGAPLQGLPG EALGCPAGVG TPVPADGTQT LTCAHTSAPE
STAPTNHLVA GRAMTLSPQE EVAAGQMASS SRSGPVKLEF DVSDGATSKR APPPRRLGER
SGLKPPLRKA AVRQQKAPQE VEEDDGRSGA GEDPPMPASR GSYHLDWDKM DDPNFIPFGG
DTKSGCSEAQ PPESPETRLG QPAAEQLHAG PATEEPGPCL SQQLHSASAE DTPVVQLAAE
TPTAESKERA LNSASTSLPT SCPGSEPVPT HQQGQPALEL KEESFRDPAE VLGTGAEVDY
LEQFGTSSFK ESALRKQSLY LKFDPLLRDS PGRPVPVATE TSSMHGANET PSGRPREAKL
VEFDFLGALD IPVPGPPPGV PAPGGPPLST GPIVDLLQYS QKDLDAVVKA TQEENRELRS
RCEELHGKNL ELGKIMDRFE EVVYQAMEEV QKQKELSKAE IQKVLKEKDQ LTTDLNSMEK
SFSDLFKRFE KQKEVIEGYR KNEESLKKCV EDYLARITQE GQRYQALKAH AEEKLQLANE
EIAQVRSKAQ AEALALQASL RKEQMRIQSL EKTVEQKTKE NEELTRICDD LISKMEKI
