TPX2_BOVIN
ID TPX2_BOVIN Reviewed; 704 AA.
AC A6H6Z7;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Targeting protein for Xklp2;
GN Name=TPX2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Spindle assembly factor required for normal assembly of
CC mitotic spindles. Required for normal assembly of microtubules during
CC apoptosis. Required for chromatin and/or kinetochore dependent
CC microtubule nucleation. Mediates AURKA localization to spindle
CC microtubules. Activates AURKA by promoting its autophosphorylation at
CC 'Thr-288' and protects this residue against dephosphorylation. TPX2 is
CC inactivated upon binding to importin-alpha. At the onset of mitosis,
CC GOLGA2 interacts with importin-alpha, liberating TPX2 from importin-
CC alpha, allowing TPX2 to activates AURKA kinase and stimulates local
CC microtubule nucleation. {ECO:0000250|UniProtKB:Q9ULW0}.
CC -!- SUBUNIT: Interacts with AURKA (By similarity). Interacts with importin-
CC alpha; leading to inactivate TPX2 (By similarity). Interacts with
CC HNRNPU; this interaction recruits HNRNPU to spindle microtubules (MTs)
CC (By similarity). Interacts with BCL2L10 (By similarity).
CC {ECO:0000250|UniProtKB:A2APB8, ECO:0000250|UniProtKB:Q9ULW0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULW0}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9ULW0}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9ULW0}.
CC Note=During mitosis it is strictly associated with the spindle pole and
CC with the mitotic spindle, whereas during S and G2, it is diffusely
CC distributed throughout the nucleus. Is released from the nucleus in
CC apoptotic cells and is detected on apoptotic microtubules.
CC {ECO:0000250|UniProtKB:Q9ULW0}.
CC -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
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DR EMBL; BC146057; AAI46058.1; -; mRNA.
DR RefSeq; NP_001092368.1; NM_001098898.1.
DR AlphaFoldDB; A6H6Z7; -.
DR SMR; A6H6Z7; -.
DR STRING; 9913.ENSBTAP00000049473; -.
DR PaxDb; A6H6Z7; -.
DR PRIDE; A6H6Z7; -.
DR GeneID; 507226; -.
DR KEGG; bta:507226; -.
DR CTD; 22974; -.
DR eggNOG; ENOG502QVQS; Eukaryota.
DR InParanoid; A6H6Z7; -.
DR OrthoDB; 1390734at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005880; C:nuclear microtubule; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0061676; F:importin-alpha family protein binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..704
FT /note="Targeting protein for Xklp2"
FT /id="PRO_0000393111"
FT REGION 92..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2APB8"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 296
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 332
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2APB8"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 456
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT CROSSLNK 434
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT CROSSLNK 457
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT CROSSLNK 598
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT CROSSLNK 697
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
SQ SEQUENCE 704 AA; 81593 MW; 22E09662012A5F00 CRC64;
MSQVTTSYSY DAPTDFINFS SLTDEEDMQH IDSWFDEKAN LENKFTGKDG TGGLYQGKTP
LRKANLHRDV TPLRPVDNTY NKQAEKENLV EESIPSNECP SMKVKETTSR NNPVQPQRRS
LRLSAKKNLE QKEKQHVKMK AKRCGTPVII NEFPPSKKMK VQKILKSTEE QELEKRMKMQ
QEVVEMRKRN EEFKKFALAG AGQPVKKSVS QVTKAVDFHF RTDERVKQHP KNQEEYKEVN
FTSELRKHPP SPARVTKGCT IVMPFNLSQG KKRTFDETAS TYVPLAQQVE AFHKRTPTRY
HLRNRKDDIM PLPSKSVVRI CRDPQTPVLQ TKHRTRPVTC KSAADLEAEE LEKQQQYKFK
AQELDPRILE GGPILPKKPP VKPPTQPVGF DLEIEKRIQE RESKKKLEEE HYEFHSRPCP
TKILEDVVGV PEKKELPITV PKSPAFALKN RIRMPTKEDK EEEEPVMIRA QPVPYFGMPF
KPQIPVGRTV EVCPFSFDSR DKERQLQKEK KIKELQKGEV PKFKAHPLPH FDTINLPEKK
VKNTTQVEPF CLETDRRGAL KAQTWKHQLD EELKQQKEAA CFKARPNTVI SQEPFVPKRE
KKSVIEGLSG SLVQEPFQLA TEKRAKERQE LEKRMAEVEA LKAQQLEEAR QQEEEQQKEE
LARLRKELVH KANPIRRYQG VEVKSSDQPL TVPVSPKFST RFHC
