TPX2_PONAB
ID TPX2_PONAB Reviewed; 739 AA.
AC Q5RAF2;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Targeting protein for Xklp2;
GN Name=TPX2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR859065; CAH91258.1; -; mRNA.
DR RefSeq; NP_001125744.1; NM_001132272.2.
DR AlphaFoldDB; Q5RAF2; -.
DR SMR; Q5RAF2; -.
DR STRING; 9601.ENSPPYP00000012165; -.
DR GeneID; 100172669; -.
DR KEGG; pon:100172669; -.
DR CTD; 22974; -.
DR eggNOG; ENOG502QVQS; Eukaryota.
DR InParanoid; Q5RAF2; -.
DR Proteomes; UP000001595; Unplaced.
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: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:0032147; P:activation of protein kinase activity; IEA:InterPro.
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; 1.
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..739
FT /note="Targeting protein for Xklp2"
FT /id="PRO_0000393113"
FT REGION 110..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..367
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 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2APB8"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 304
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 368
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 374
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2APB8"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 498
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT CROSSLNK 640
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
FT CROSSLNK 732
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULW0"
SQ SEQUENCE 739 AA; 84749 MW; 25EB18EA660687A3 CRC64;
MSQVKSSYSY DAPSDFINFS SLDDEGDTQN IDSWFEEKAN LENKLLGKSG TGGLFQGKTP
LRKANLQQAI VTPLKPVDNT YYKEAEKENL VEQSIPSNAC SSLEVEAAIS RKTPAQPQRR
SLRLSAQKDL KQKEKHNVKM KAKRCATPVI IDEILPSKKM KVSNKKKPEE EGSAHRDTSE
KNASSPEKAK GRHTVPCMPP AKQKVLKSTE EQELEKSMKM QQEVVEMRKK NEEFKKLALA
GIGQPVKKSV SQVTKSIDFH FRTDERIKQH PKNQEEYKEV NFTSELRKHP SSPARVTKGC
TVVKPFNLSQ GKKRTFDETV STYVPLAQQV EDFHKRTPNR YHLRSKKDDI NLLPSKSSVT
KIGRDPQTPV LQTKYRARPV TCKSTAELEA EELEKLQQYK FKARELDPRI LEGGPILPKK
PPVKPPTEPI GFDLEIEKRI QERESKKKSE DEHFEFHSRP CPTKILEDVV GVPEKKVLPI
TVPKSPAFAL KNRIRMPTEE DEEEDEPVVI KAQPVPHYGV PFKPQIPEAR TVEICPFSFD
SRDKERQLQK EKKIKELQKG EVPKFKALPL PHFDTINLPE KKVKNVTQIE PFCLETDRGG
ALKAQTWKHQ LEEELRQQKE AACFKARPNT VISQEPFVPK KEKKSVAVQE PFQLATEKRA
KERQELEKRM AEVEAQKAQQ LEEARQQEEE QKKEELARLR RELVHKANPI RKYQGLEIKS
SDQPLTVPVS PKFSTRFHC
