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Targeting protein for Xklp2

 TPX2_MOUSE              Reviewed;         745 AA.
A2APB8; Q3U500; Q6P9S6;
23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
22-NOV-2017, entry version 87.
RecName: Full=Targeting protein for Xklp2;
Name=Tpx2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72 AND SER-486, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
FUNCTION, INTERACTION WITH AURKA, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 8-TYR--ASP-11.
PubMed=18663142; DOI=10.1083/jcb.200802005;
Bird A.W., Hyman A.A.;
"Building a spindle of the correct length in human cells requires the
interaction between TPX2 and Aurora A.";
J. Cell Biol. 182:289-300(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486 AND SER-737, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128 AND LYS-375, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Spindle assembly factor required for normal assembly of
mitotic spindles. Required for normal assembly of microtubules
during apoptosis. Required for chromatin and/or kinetochore
dependent microtubule nucleation. Mediates AURKA localization to
spindle microtubules. Activates AURKA by promoting its
autophosphorylation at 'Thr-288' and protects this residue against
dephosphorylation. TPX2 is inactivated upon binding to importin-
alpha. At the onset of mitosis, GOLGA2 interacts with importin-
alpha, liberating TPX2 from importin-alpha, allowing TPX2 to
activates AURKA kinase and stimulates local microtubule
nucleation. {ECO:0000250|UniProtKB:Q9ULW0,
ECO:0000269|PubMed:18663142}.
-!- SUBUNIT: Interacts with AURKA (PubMed:18663142). Interacts with
importin-alpha; leading to inactivate TPX2 (By similarity).
Interacts with HNRNPU; this interaction recruits HNRNPU to spindle
microtubules (MTs) (By similarity). {ECO:0000250|UniProtKB:Q9ULW0,
ECO:0000269|PubMed:18663142}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULW0}.
Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9ULW0}.
Cytoplasm, cytoskeleton, spindle pole
{ECO:0000250|UniProtKB:Q9ULW0}. Note=During mitosis it is strictly
associated with the spindle pole and with the mitotic spindle,
whereas during S and G2, it is diffusely distributed throughout
the nucleus. Is released from the nucleus in apoptotic cells and
is detected on apoptotic microtubules.
{ECO:0000250|UniProtKB:Q9ULW0}.
-!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK153957; BAE32280.1; -; mRNA.
EMBL; AL833801; CAM23677.1; -; Genomic_DNA.
EMBL; CH466551; EDL05994.1; -; Genomic_DNA.
EMBL; BC060619; AAH60619.1; -; mRNA.
CCDS; CCDS16900.1; -.
RefSeq; NP_001135447.1; NM_001141975.1.
RefSeq; NP_001135448.1; NM_001141976.1.
RefSeq; NP_001135449.1; NM_001141977.1.
RefSeq; NP_001135450.1; NM_001141978.1.
RefSeq; NP_082385.3; NM_028109.4.
RefSeq; XP_006500276.1; XM_006500213.2.
RefSeq; XP_006500277.1; XM_006500214.2.
RefSeq; XP_006500278.1; XM_006500215.2.
UniGene; Mm.407737; -.
ProteinModelPortal; A2APB8; -.
SMR; A2APB8; -.
BioGrid; 215163; 53.
IntAct; A2APB8; 51.
STRING; 10090.ENSMUSP00000028969; -.
iPTMnet; A2APB8; -.
PhosphoSitePlus; A2APB8; -.
EPD; A2APB8; -.
MaxQB; A2APB8; -.
PaxDb; A2APB8; -.
PeptideAtlas; A2APB8; -.
PRIDE; A2APB8; -.
Ensembl; ENSMUST00000028969; ENSMUSP00000028969; ENSMUSG00000027469.
Ensembl; ENSMUST00000109816; ENSMUSP00000105441; ENSMUSG00000027469.
Ensembl; ENSMUST00000164120; ENSMUSP00000128888; ENSMUSG00000027469.
Ensembl; ENSMUST00000178997; ENSMUSP00000136457; ENSMUSG00000027469.
GeneID; 72119; -.
KEGG; mmu:72119; -.
UCSC; uc008ngo.2; mouse.
CTD; 22974; -.
MGI; MGI:1919369; Tpx2.
eggNOG; ENOG410IIEY; Eukaryota.
eggNOG; ENOG4110SQ6; LUCA.
GeneTree; ENSGT00390000009842; -.
HOGENOM; HOG000231739; -.
HOVERGEN; HBG057334; -.
InParanoid; A2APB8; -.
KO; K16812; -.
OMA; SRPCPTK; -.
OrthoDB; EOG091G0MIV; -.
PhylomeDB; A2APB8; -.
TreeFam; TF328997; -.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-8854518; AURKA Activation by TPX2.
ChiTaRS; Tpx2; mouse.
PRO; PR:A2APB8; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027469; -.
Genevisible; A2APB8; MM.
GO; GO:0005818; C:aster; ISO:MGI.
GO; GO:0043203; C:axon hillock; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
GO; GO:0072686; C:mitotic spindle; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0061676; F:importin-alpha family protein binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
GO; GO:0051225; P:spindle assembly; ISO:MGI.
InterPro; IPR015128; Aurora-A-bd.
InterPro; IPR027329; TPX2_C.
InterPro; IPR027330; TPX2_central_dom.
InterPro; IPR009675; TPX2_fam.
PANTHER; PTHR14326; PTHR14326; 1.
Pfam; PF09041; Aurora-A_bind; 1.
Pfam; PF06886; TPX2; 1.
Pfam; PF12214; TPX2_importin; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Cell cycle; Cell division; Complete proteome;
Cytoplasm; Cytoskeleton; Isopeptide bond; Microtubule; Mitosis;
Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 745 Targeting protein for Xklp2.
/FTId=PRO_0000393112.
MOD_RES 72 72 Phosphothreonine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ULW0}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ULW0}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ULW0}.
MOD_RES 307 307 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9ULW0}.
MOD_RES 312 312 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ULW0}.
MOD_RES 340 340 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9ULW0}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ULW0}.
MOD_RES 369 369 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9ULW0}.
MOD_RES 375 375 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 737 737 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CROSSLNK 477 477 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9ULW0}.
CROSSLNK 500 500 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9ULW0}.
CROSSLNK 640 640 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9ULW0}.
CROSSLNK 739 739 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9ULW0}.
MUTAGEN 8 11 YSFD->ASAA: Abolishes interaction with
AURKA. {ECO:0000269|PubMed:18663142}.
CONFLICT 165 165 H -> D (in Ref. 4; AAH60619).
{ECO:0000305}.
CONFLICT 453 453 E -> K (in Ref. 1; BAE32280).
{ECO:0000305}.
CONFLICT 509 509 V -> L (in Ref. 1; BAE32280).
{ECO:0000305}.
SEQUENCE 745 AA; 85894 MW; 4E60692BC52DAE34 CRC64;
MSQVPTTYSF DAPTDFINFS SLDAEEDTEN IDSWFDEKAN LENKFLRQRG IGEPFQGKNS
LRKAKLQQGF VTPLKAVDNT YHKETEKENL QKQSIPSNDC SSLDAKRAVS GNTPVQPQRR
SIRLSAQKDL EQKEKNHVAS VEMKAKRCVA PATDCPPQKR MKVSHKKKLE EEEEGSAPAT
SRKNERETLE KAKGKHTVPG VPPAREKVLK STEEQEIEKR LRMQQEVVEL RRKNEEFKKL
ALAGPGQPVK KSTSQVTKTV DFHFLTDERI KQHPKNQEEY KEVNFMSELR KHSSTPARGT
RGCTIIKPFN LSKGKKRTFD EAASTYVPIA QQVEAFHKRT PNRYHLRNKK DESLLPSKSV
NKIARDPQTP ILQTKYRTRA VTCKSTAEQE AEELEKLQQY KFKARELDPR IFESGPILPK
RAPVKPPTQP VGFDLEIEKR IHERESKKKT EDEQFEFHSR PCPTKILEDV VGVPEKKVIP
ATVPKSPVFA LKNRIRVPIK DEEEEKPVVI KAQPVPHYGV PYKPHIAEAR NVEVCPFSFD
TRDKERQLQK EKKIKEMQKG EVPKFKALPV PHFDTINLPE KKVKNVTQAE PFSLETDKRG
AYKAEMWKHQ LEEEQKQQKD AACFKARPNT VIFQEPFVPK KEKKSLAENP SGSLVQEPFQ
LATERRAKER QELEKKMAEV EAWKLQQLEE VRQQEEEQQK EELARLRKEL VHKANPIRKY
AAVEVKSSEL PLTVPVSPKF STRFQ


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