ID   TPX2A_XENLA             Reviewed;         716 AA.
AC   Q6NUF4; Q9I8N0;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Targeting protein for Xklp2-A;
GN   Name=tpx2-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], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR
RP   LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION.
RC   TISSUE=Egg;
RX   PubMed=10871281; DOI=10.1083/jcb.149.7.1405;
RA   Wittmann T., Wilm M., Karsenti E., Vernos I.;
RT   "TPX2, a novel Xenopus MAP involved in spindle pole organization.";
RL   J. Cell Biol. 149:1405-1418(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH KIF15, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=9813089; DOI=10.1083/jcb.143.3.673;
RA   Wittmann T., Boleti H., Antony C., Karsenti E., Vernos I.;
RT   "Localization of the kinesin-like protein Xklp2 to spindle poles requires a
RT   leucine zipper, a microtubule-associated protein, and dynein.";
RL   J. Cell Biol. 143:673-685(1998).
RN   [4]
RP   FUNCTION, PHOSPHORYLATION AT SER-204, MUTAGENESIS OF SER-204, AND
RP   INTERACTION WITH PLK1.
RX   PubMed=19556869; DOI=10.4161/cc.8.15.9086;
RA   Eckerdt F., Pascreau G., Phistry M., Lewellyn A.L., DePaoli-Roach A.A.,
RA   Maller J.L.;
RT   "Phosphorylation of TPX2 by Plx1 enhances activation of Aurora A.";
RL   Cell Cycle 8:2413-2419(2009).
CC   -!- FUNCTION: Spindle assembly factor. Required for normal assembly of
CC       mitotic spindles. Mediates the binding kif15 and aurka to spindle
CC       microtubules. Required for targeting kif15 to microtubule minus ends.
CC       Activates aurka by promoting its autophosphorylation and protects the
CC       phosphorylated residue against dephosphorylation (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:10871281,
CC       ECO:0000269|PubMed:19556869}.
CC   -!- SUBUNIT: Associates with microtubules. Interacts with aurka and plk1.
CC       Interacts with kif15. {ECO:0000269|PubMed:19556869,
CC       ECO:0000269|PubMed:9813089}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
CC       Cytoplasm, cytoskeleton, spindle pole. Note=Localizes during metaphase
CC       on spindle microtubules, with a strong enrichment at spindle poles.
CC       Localizes to the minus ends of spindle pole and aster microtubules in a
CC       dynein- and dynactin-dependent manner.
CC   -!- DEVELOPMENTAL STAGE: Detected in mitotic eggs (at protein level).
CC       {ECO:0000269|PubMed:9813089}.
CC   -!- PTM: Phosphorylated during mitosis. Hyperphosphorylated upon assembly
CC       of microtubules. {ECO:0000269|PubMed:10871281,
CC       ECO:0000269|PubMed:19556869}.
CC   -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
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DR   EMBL; AF244546; AAF81694.1; -; mRNA.
DR   EMBL; BC068637; AAH68637.1; -; mRNA.
DR   RefSeq; NP_001082006.1; NM_001088537.1.
DR   RefSeq; XP_018089642.1; XM_018234153.1.
DR   PDB; 3KND; X-ray; 2.15 A; B=270-350.
DR   PDBsum; 3KND; -.
DR   AlphaFoldDB; Q6NUF4; -.
DR   SMR; Q6NUF4; -.
DR   BioGRID; 99509; 3.
DR   IntAct; Q6NUF4; 4.
DR   iPTMnet; Q6NUF4; -.
DR   MaxQB; Q6NUF4; -.
DR   PRIDE; Q6NUF4; -.
DR   GeneID; 398174; -.
DR   KEGG; xla:398174; -.
DR   CTD; 398174; -.
DR   Xenbase; XB-GENE-6251919; tpx2.L.
DR   OMA; HQXGLSG; -.
DR   OrthoDB; 1390734at2759; -.
DR   EvolutionaryTrace; Q6NUF4; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 398174; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0032147; P:activation of protein kinase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0060236; P:regulation of mitotic spindle organization; IEA:InterPro.
DR   InterPro; IPR015128; Aurora-A-bd.
DR   InterPro; IPR027329; TPX2_C.
DR   InterPro; IPR027330; TPX2_central_dom.
DR   InterPro; IPR009675; TPX2_fam.
DR   PANTHER; PTHR14326; PTHR14326; 1.
DR   Pfam; PF09041; Aurora-A_bind; 1.
DR   Pfam; PF06886; TPX2; 2.
DR   Pfam; PF12214; TPX2_importin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..716
FT                   /note="Targeting protein for Xklp2-A"
FT                   /id="PRO_0000393114"
FT   REGION          35..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..103
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..119
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         204
FT                   /note="Phosphoserine; by plk1"
FT                   /evidence="ECO:0000269|PubMed:19556869"
FT   MUTAGEN         204
FT                   /note="S->A: Decreases activation of aurka."
FT                   /evidence="ECO:0000269|PubMed:19556869"
FT   MUTAGEN         204
FT                   /note="S->D: Increases activation of aurka."
FT                   /evidence="ECO:0000269|PubMed:19556869"
FT   CONFLICT        61
FT                   /note="E -> Q (in Ref. 1; AAF81694)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        473
FT                   /note="Missing (in Ref. 1; AAF81694)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   716 AA;  82512 MW;  F402B114123E839C CRC64;
     MEDTQDTYSY DAPSIFNFSS FHEDHNADSW FDQVTNAENI PPDQRRLSET SVNTEQNSKV
     EPVQTTPSKD DVSNSATHVC DVKSQSKRSS RRMSKKHRQK LLVKMKDTHL EKETAPPEYP
     PCKKLKGSSS KGRHAPVIKS QSTSSHHSMT SPKPKAQLTM PSTPTVLKRR NVLVKAKNSE
     EQELEKMQEL QKEMLENLKK NEHSMKVAIT GAGQPVKTFI PVTKPVDFHF KTDDRLKRTA
     NQPEGDGYKA VDFASELRKH PPSPVQVTKG GHTVPKPFNL SKGKRKHEEA SDYVSTAEQV
     IAFYKRTPAR YHLRSRQREM EGPSPVKMIK TKLTNPKTPL LQTKGRHRPV TCKSAAELEA
     EELEMINQYK FKAQELDTRI LEGGPVLLKK PLVKEPTKAI GFDLEIEKRI QQREKKEEIE
     EETFTFHSRP CPSKMLTDVV GVPLKKLLPV TVPQSPAFAL KNRVRIPAQE EKQEEMVPVI
     KATRMPHYGV PFKPKLVEQR QVDVCPFSFC DRDKERQLQK EKRLDELRKD EVPKFKAQPL
     PQFDNIRLPE KKVKMPTQQE PFDLEIEKRG ASKLQRWQQQ IQEELKQQKE MVVFKARPNT
     VVHQEPFVPK KENRSLTESL SGSIVQEGFE LATAKRAKER QEFDKCLAET EAQKSLLEEE
     IRKRREEEEK EEISQLRQEL VHKAKPIRKY RAVEVKASDV PLTVPRSPNF SDRFKC