TPX2B_XENLA
ID TPX2B_XENLA Reviewed; 715 AA.
AC Q6DDV8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Targeting protein for Xklp2-B;
GN Name=tpx2-b;
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 [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SUBUNIT: Associates with microtubules. Interacts with aurka and plk1.
CC Interacts with kif15 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250}. Note=Localizes during metaphase on spindle microtubules,
CC with a strong enrichment at spindle poles. Localizes to the minus ends
CC of spindle pole and aster microtubules in a dynein- and dynactin-
CC dependent manner (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated during mitosis. Hyperphosphorylated upon assembly
CC of microtubules (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
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DR EMBL; BC077396; AAH77396.1; -; mRNA.
DR RefSeq; NP_001086751.1; NM_001093282.1.
DR AlphaFoldDB; Q6DDV8; -.
DR DNASU; 446586; -.
DR GeneID; 446586; -.
DR KEGG; xla:446586; -.
DR CTD; 446586; -.
DR Xenbase; XB-GENE-6255926; tpx2.S.
DR OrthoDB; 1390734at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 446586; 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; 1.
DR Pfam; PF12214; TPX2_importin; 2.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..715
FT /note="Targeting protein for Xklp2-B"
FT /id="PRO_0000393115"
FT REGION 36..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..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..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 204
FT /note="Phosphoserine; by plk1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 715 AA; 82010 MW; 1BA4194FB09FD164 CRC64;
MADAQDTYSY DAPSIFNFSS FHDDHNADSW FDQLTNAENI PPDQKPLSET SVNAEQNCKV
EPGKITPSKE EVSKSTTHVC DVKSQTKRSA RRMSKKHRQK ILLKMKETHL EKETAQSEYP
PCKKLKGSST KDRQAPVIRG QPTSSHHGTT SPKPKAQLTM PATPTVLKRR NILAKSKSSE
EQELEKMQAL QKEMLENLKK NEHSMKVAIS GAGQPVKNFI PVTKPVDFHF KTDDRLKRNA
NPPEGDGYKE VDFASVLRKP PTSPVQVTKG GHTVPKPFNL SKGKRKHEEA SDFVSTAEQV
VAFYRRTPAR YHLRSRQKEM EGPSPVKMLK PKLTNPKTPL LQTKQRHRPT TCKSAAELEA
EELDMIHQYK FKAQELDTRI LEGGPVLPKK PSVKEPTKAI GFDLEIEKRI QQREKKDEVE
EEAFSFHSRP CPSKILADVV GVPQKKLLPV TVPQSPAFAL KNRVRIPAQE EKEEEVPVIK
ATRMPHYGVP FKPKLVEQKQ VEACPFSFCE RDKERQLQKE KRLDELRKEE VPKFKAQRLP
QFDHISLPEK KVKMPTQQEP FQLEIDKRGA TKLQRWQHQI KEELKQQKEM VVFKARPNTV
VHQEPFVPKK ESRSLTDSLS GSMIQEGFEL ATAKRAKERQ EFEKCLAEME AQKSLLEEET
RKQREEEERE EINQLRQELV HKAQPIRKFK AVEVKASDVP LTVPASPNFS DRFKC