TPX2_HUMAN
ID TPX2_HUMAN Reviewed; 747 AA.
AC Q9ULW0; Q96RR5; Q9H1R4; Q9NRA3; Q9UFN9; Q9UL00; Q9Y2M1;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Targeting protein for Xklp2;
DE AltName: Full=Differentially expressed in cancerous and non-cancerous lung cells 2;
DE Short=DIL-2;
DE AltName: Full=Hepatocellular carcinoma-associated antigen 519;
DE AltName: Full=Hepatocellular carcinoma-associated antigen 90;
DE AltName: Full=Protein fls353;
DE AltName: Full=Restricted expression proliferation-associated protein 100;
DE Short=p100;
GN Name=TPX2; Synonyms=C20orf1, C20orf2, DIL2, HCA519;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10512675; DOI=10.1006/geno.1999.5939;
RA Manda R., Kohno T., Matsuno Y., Takenoshita S., Kuwano H., Yokota J.;
RT "Identification of genes (SPON2 and C20orf2) differentially expressed
RT between cancerous and noncancerous lung cells by mRNA differential
RT display.";
RL Genomics 61:5-14(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10393424; DOI=10.1159/000015251;
RA Zhang Y., Heidebrecht H.J., Rott A., Schlegelberger B., Parwaresch R.;
RT "Assignment of human proliferation associated p100 gene (C20orf1) to human
RT chromosome band 20q11.2 by in situ hybridization.";
RL Cytogenet. Cell Genet. 84:182-183(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RA Nezu J.;
RT "Fetal gene preferentially expressed in colorectal cancer.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hepatoma;
RX PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
RA Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y.,
RA Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W.,
RA Chen W.-F.;
RT "Large scale identification of human hepatocellular carcinoma-associated
RT antigens by autoantibodies.";
RL J. Immunol. 169:1102-1109(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-747 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-747 (ISOFORM 1).
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 [10]
RP CHARACTERIZATION.
RX PubMed=9207457;
RA Heidebrecht H.J., Buck F., Steinmann J., Sprenger R., Wacker H.H.,
RA Parwaresch R.;
RT "p100: a novel proliferation-associated nuclear protein specifically
RT restricted to cell cycle phases S, G2, and M.";
RL Blood 90:226-233(1997).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-369 AND SER-738, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [14]
RP FUNCTION, INTERACTION WITH AURKA, AND SUBCELLULAR LOCATION.
RX PubMed=18663142; DOI=10.1083/jcb.200802005;
RA Bird A.W., Hyman A.A.;
RT "Building a spindle of the correct length in human cells requires the
RT interaction between TPX2 and Aurora A.";
RL J. Cell Biol. 182:289-300(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486 AND SER-738, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59; THR-72; SER-310; THR-338;
RP SER-486 AND SER-738, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19208764; DOI=10.1242/jcs.037259;
RA Moss D.K., Wilde A., Lane J.D.;
RT "Dynamic release of nuclear RanGTP triggers TPX2-dependent microtubule
RT assembly during the apoptotic execution phase.";
RL J. Cell Sci. 122:644-655(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-305, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72; SER-292; SER-293; SER-486
RP AND SER-738, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP INTERACTION WITH HNRNPU.
RX PubMed=21242313; DOI=10.1242/jcs.063347;
RA Ma N., Matsunaga S., Morimoto A., Sakashita G., Urano T., Uchiyama S.,
RA Fukui K.;
RT "The nuclear scaffold protein SAF-A is required for kinetochore-microtubule
RT attachment and contributes to the targeting of Aurora-A to mitotic
RT spindles.";
RL J. Cell Sci. 124:394-404(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-738, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59; THR-72; SER-121; SER-125;
RP THR-147; SER-257; SER-310; SER-359; THR-369; SER-486; THR-499 AND SER-738,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-641, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [26]
RP FUNCTION, AND INTERACTION WITH IMPORTIN-ALPHA.
RX PubMed=26165940; DOI=10.1016/j.cell.2015.06.014;
RA Wei J.H., Zhang Z.C., Wynn R.M., Seemann J.;
RT "GM130 regulates Golgi-derived spindle assembly by activating TPX2 and
RT capturing microtubules.";
RL Cell 162:287-299(2015).
RN [27]
RP INTERACTION WITH HNRNPU.
RX PubMed=25986610; DOI=10.1128/mcb.01312-14;
RA Douglas P., Ye R., Morrice N., Britton S., Trinkle-Mulcahy L.,
RA Lees-Miller S.P.;
RT "Phosphorylation of SAF-A/hnRNP-U serine 59 by polo-like kinase 1 is
RT required for mitosis.";
RL Mol. Cell. Biol. 35:2699-2713(2015).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-477; LYS-500; LYS-641 AND
RP LYS-740, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-43 IN COMPLEX WITH AURKA, AND
RP SUBUNIT.
RX PubMed=14580337; DOI=10.1016/s1097-2765(03)00392-7;
RA Bayliss R., Sardon T., Vernos I., Conti E.;
RT "Structural basis of Aurora-A activation by TPX2 at the mitotic spindle.";
RL Mol. Cell 12:851-862(2003).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-43 IN COMPLEX WITH AURKA, AND
RP SUBUNIT.
RX PubMed=18662907; DOI=10.1110/ps.036590.108;
RA Zhao B., Smallwood A., Yang J., Koretke K., Nurse K., Calamari A.,
RA Kirkpatrick R.B., Lai Z.;
RT "Modulation of kinase-inhibitor interactions by auxiliary protein binding:
RT crystallography studies on Aurora A interactions with VX-680 and with
RT TPX2.";
RL Protein Sci. 17:1791-1797(2008).
RN [31]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-464.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 (PubMed:18663142, PubMed:19208764). Activates AURKA by
CC promoting its autophosphorylation at 'Thr-288' and protects this
CC residue against dephosphorylation (PubMed:18663142, PubMed:19208764).
CC TPX2 is inactivated upon binding to importin-alpha (PubMed:26165940).
CC At the onset of mitosis, GOLGA2 interacts with importin-alpha,
CC liberating TPX2 from importin-alpha, allowing TPX2 to activates AURKA
CC kinase and stimulates local microtubule nucleation (PubMed:26165940).
CC {ECO:0000269|PubMed:18663142, ECO:0000269|PubMed:19208764,
CC ECO:0000269|PubMed:26165940}.
CC -!- SUBUNIT: Interacts with AURKA (PubMed:14580337, PubMed:18662907,
CC PubMed:18663142). Interacts with importin-alpha; leading to inactivate
CC TPX2 (PubMed:26165940). Interacts with HNRNPU; this interaction
CC recruits HNRNPU to spindle microtubules (MTs) (PubMed:21242313,
CC PubMed:25986610). Interacts with BCL2L10 (By similarity).
CC {ECO:0000250|UniProtKB:A2APB8, ECO:0000269|PubMed:14580337,
CC ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:18663142,
CC ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:25986610,
CC ECO:0000269|PubMed:26165940}.
CC -!- INTERACTION:
CC Q9ULW0; O14965: AURKA; NbExp=8; IntAct=EBI-1037322, EBI-448680;
CC Q9ULW0; P27797: CALR; NbExp=3; IntAct=EBI-1037322, EBI-1049597;
CC Q9ULW0; P12830: CDH1; NbExp=3; IntAct=EBI-1037322, EBI-727477;
CC Q9ULW0; Q15078: CDK5R1; NbExp=3; IntAct=EBI-1037322, EBI-746189;
CC Q9ULW0; P36957: DLST; NbExp=3; IntAct=EBI-1037322, EBI-351007;
CC Q9ULW0; Q08379: GOLGA2; NbExp=6; IntAct=EBI-1037322, EBI-618309;
CC Q9ULW0; P62993: GRB2; NbExp=2; IntAct=EBI-1037322, EBI-401755;
CC Q9ULW0; O75330: HMMR; NbExp=5; IntAct=EBI-1037322, EBI-2556203;
CC Q9ULW0; O00629: KPNA4; NbExp=3; IntAct=EBI-1037322, EBI-396343;
CC Q9ULW0; P16333: NCK1; NbExp=4; IntAct=EBI-1037322, EBI-389883;
CC Q9ULW0; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-1037322, EBI-1055945;
CC Q9ULW0; P27986: PIK3R1; NbExp=2; IntAct=EBI-1037322, EBI-79464;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19208764}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:18663142,
CC ECO:0000269|PubMed:19208764}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:18663142, ECO:0000269|PubMed:19208764}. Note=During
CC mitosis it is strictly associated with the spindle pole and with the
CC mitotic spindle, whereas during S and G2, it is diffusely distributed
CC throughout the nucleus. Is released from the nucleus in apoptotic cells
CC and is detected on apoptotic microtubules.
CC {ECO:0000269|PubMed:19208764}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULW0-1; Sequence=Displayed;
CC Name=2; Synonyms=HCA90;
CC IsoId=Q9ULW0-2; Sequence=VSP_057355;
CC -!- TISSUE SPECIFICITY: Expressed in lung carcinoma cell lines but not in
CC normal lung tissues.
CC -!- DEVELOPMENTAL STAGE: Exclusively expressed in proliferating cells from
CC the transition G1/S until the end of cytokinesis.
CC -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
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DR EMBL; AB027467; BAA85893.1; -; mRNA.
DR EMBL; AF098158; AAF03248.1; -; mRNA.
DR EMBL; AB024704; BAA76931.1; -; mRNA.
DR EMBL; AF146731; AAD33965.1; -; mRNA.
DR EMBL; AF287265; AAK83033.1; -; mRNA.
DR EMBL; AL160175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76418.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76422.1; -; Genomic_DNA.
DR EMBL; BC004136; AAH04136.1; -; mRNA.
DR EMBL; BC020207; AAH20207.1; -; mRNA.
DR EMBL; AL117534; CAB55982.1; -; mRNA.
DR EMBL; AF244547; AAF81695.1; -; mRNA.
DR CCDS; CCDS13190.1; -. [Q9ULW0-1]
DR PIR; T17292; T17292.
DR RefSeq; NP_036244.2; NM_012112.4. [Q9ULW0-1]
DR RefSeq; XP_011526999.1; XM_011528697.2. [Q9ULW0-1]
DR RefSeq; XP_011527001.1; XM_011528699.2. [Q9ULW0-1]
DR PDB; 1OL5; X-ray; 2.50 A; B=1-43.
DR PDB; 3E5A; X-ray; 2.30 A; B=1-43.
DR PDB; 3HA6; X-ray; 2.36 A; B=1-43.
DR PDB; 4C3P; X-ray; 2.69 A; B/E=1-43.
DR PDB; 5LXM; X-ray; 2.08 A; D=6-43.
DR PDB; 6BJC; EM; 3.30 A; P/T=1-747.
DR PDB; 6VPG; X-ray; 2.64 A; A=7-21.
DR PDB; 6VPH; X-ray; 2.14 A; A=7-21.
DR PDB; 6VPI; X-ray; 2.00 A; A=7-21.
DR PDB; 6VPJ; X-ray; 2.10 A; A=7-21.
DR PDB; 6VPL; X-ray; 1.86 A; A/B=7-21.
DR PDB; 6VPM; X-ray; 1.58 A; A/B=7-21.
DR PDB; 6XKA; X-ray; 2.65 A; A=7-21.
DR PDBsum; 1OL5; -.
DR PDBsum; 3E5A; -.
DR PDBsum; 3HA6; -.
DR PDBsum; 4C3P; -.
DR PDBsum; 5LXM; -.
DR PDBsum; 6BJC; -.
DR PDBsum; 6VPG; -.
DR PDBsum; 6VPH; -.
DR PDBsum; 6VPI; -.
DR PDBsum; 6VPJ; -.
DR PDBsum; 6VPL; -.
DR PDBsum; 6VPM; -.
DR PDBsum; 6XKA; -.
DR AlphaFoldDB; Q9ULW0; -.
DR SMR; Q9ULW0; -.
DR BioGRID; 116624; 157.
DR CORUM; Q9ULW0; -.
DR DIP; DIP-36727N; -.
DR DIP; DIP-46212N; -.
DR IntAct; Q9ULW0; 41.
DR MINT; Q9ULW0; -.
DR STRING; 9606.ENSP00000300403; -.
DR BindingDB; Q9ULW0; -.
DR ChEMBL; CHEMBL5389; -.
DR GlyGen; Q9ULW0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9ULW0; -.
DR PhosphoSitePlus; Q9ULW0; -.
DR SwissPalm; Q9ULW0; -.
DR BioMuta; TPX2; -.
DR DMDM; 13124096; -.
DR CPTAC; CPTAC-1016; -.
DR EPD; Q9ULW0; -.
DR jPOST; Q9ULW0; -.
DR MassIVE; Q9ULW0; -.
DR MaxQB; Q9ULW0; -.
DR PaxDb; Q9ULW0; -.
DR PeptideAtlas; Q9ULW0; -.
DR PRIDE; Q9ULW0; -.
DR ProteomicsDB; 78016; -.
DR ProteomicsDB; 85139; -. [Q9ULW0-1]
DR Antibodypedia; 1228; 649 antibodies from 38 providers.
DR DNASU; 22974; -.
DR Ensembl; ENST00000300403.11; ENSP00000300403.6; ENSG00000088325.16. [Q9ULW0-1]
DR Ensembl; ENST00000340513.4; ENSP00000341145.4; ENSG00000088325.16. [Q9ULW0-2]
DR GeneID; 22974; -.
DR KEGG; hsa:22974; -.
DR MANE-Select; ENST00000300403.11; ENSP00000300403.6; NM_012112.5; NP_036244.2.
DR UCSC; uc002wwp.2; human. [Q9ULW0-1]
DR CTD; 22974; -.
DR DisGeNET; 22974; -.
DR GeneCards; TPX2; -.
DR HGNC; HGNC:1249; TPX2.
DR HPA; ENSG00000088325; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MIM; 605917; gene.
DR neXtProt; NX_Q9ULW0; -.
DR OpenTargets; ENSG00000088325; -.
DR PharmGKB; PA25638; -.
DR VEuPathDB; HostDB:ENSG00000088325; -.
DR eggNOG; ENOG502QVQS; Eukaryota.
DR GeneTree; ENSGT00390000009842; -.
DR HOGENOM; CLU_022592_0_0_1; -.
DR InParanoid; Q9ULW0; -.
DR OMA; GRHTVSC; -.
DR PhylomeDB; Q9ULW0; -.
DR TreeFam; TF328997; -.
DR PathwayCommons; Q9ULW0; -.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; Q9ULW0; -.
DR SIGNOR; Q9ULW0; -.
DR BioGRID-ORCS; 22974; 710 hits in 1091 CRISPR screens.
DR ChiTaRS; TPX2; human.
DR EvolutionaryTrace; Q9ULW0; -.
DR GeneWiki; TPX2; -.
DR GenomeRNAi; 22974; -.
DR Pharos; Q9ULW0; Tbio.
DR PRO; PR:Q9ULW0; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9ULW0; protein.
DR Bgee; ENSG00000088325; Expressed in ventricular zone and 129 other tissues.
DR ExpressionAtlas; Q9ULW0; baseline and differential.
DR Genevisible; Q9ULW0; HS.
DR GO; GO:0043203; C:axon hillock; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:LIFEdb.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005880; C:nuclear microtubule; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
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; IDA: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:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007020; P:microtubule nucleation; IDA:CACAO.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0090307; P:mitotic spindle assembly; IDA:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:CACAO.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cell cycle;
KW Cell division; Cytoplasm; Cytoskeleton; Isopeptide bond; Microtubule;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..747
FT /note="Targeting protein for Xklp2"
FT /id="PRO_0000065581"
FT REGION 110..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2APB8"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 338
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 369
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:A2APB8"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 499
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 477
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 500
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 641
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 740
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 351
FT /note="I -> IKTGSCSVTQAGVQWRDHGSLQCPTPGLKQSSCLSLP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:12097419"
FT /id="VSP_057355"
FT VARIANT 464
FT /note="T -> N (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036269"
FT CONFLICT 182
FT /note="K -> N (in Ref. 3; BAA76931)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="K -> E (in Ref. 1; BAA85893)"
FT /evidence="ECO:0000305"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:5LXM"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:5LXM"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:5LXM"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:6BJC"
SQ SEQUENCE 747 AA; 85653 MW; E028E0BB50BBCA0F CRC64;
MSQVKSSYSY DAPSDFINFS SLDDEGDTQN IDSWFEEKAN LENKLLGKNG TGGLFQGKTP
LRKANLQQAI VTPLKPVDNT YYKEAEKENL VEQSIPSNAC SSLEVEAAIS RKTPAQPQRR
SLRLSAQKDL EQKEKHHVKM KAKRCATPVI IDEILPSKKM KVSNNKKKPE EEGSAHQDTA
EKNASSPEKA KGRHTVPCMP PAKQKFLKST EEQELEKSMK MQQEVVEMRK KNEEFKKLAL
AGIGQPVKKS VSQVTKSVDF HFRTDERIKQ HPKNQEEYKE VNFTSELRKH PSSPARVTKG
CTIVKPFNLS QGKKRTFDET VSTYVPLAQQ VEDFHKRTPN RYHLRSKKDD INLLPSKSSV
TKICRDPQTP VLQTKHRARA VTCKSTAELE AEELEKLQQY KFKARELDPR ILEGGPILPK
KPPVKPPTEP IGFDLEIEKR IQERESKKKT EDEHFEFHSR PCPTKILEDV VGVPEKKVLP
ITVPKSPAFA LKNRIRMPTK EDEEEDEPVV IKAQPVPHYG VPFKPQIPEA RTVEICPFSF
DSRDKERQLQ KEKKIKELQK GEVPKFKALP LPHFDTINLP EKKVKNVTQI EPFCLETDRR
GALKAQTWKH QLEEELRQQK EAACFKARPN TVISQEPFVP KKEKKSVAEG LSGSLVQEPF
QLATEKRAKE RQELEKRMAE VEAQKAQQLE EARLQEEEQK KEELARLRRE LVHKANPIRK
YQGLEIKSSD QPLTVPVSPK FSTRFHC
