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Targeting protein for Xklp2 (Differentially expressed in cancerous and non-cancerous lung cells 2) (DIL-2) (Hepatocellular carcinoma-associated antigen 519) (Hepatocellular carcinoma-associated antigen 90) (Protein fls353) (Restricted expression proliferation-associated protein 100) (p100)

 TPX2_HUMAN              Reviewed;         747 AA.
Q9ULW0; Q96RR5; Q9H1R4; Q9NRA3; Q9UFN9; Q9UL00; Q9Y2M1;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
21-FEB-2001, sequence version 2.
22-NOV-2017, entry version 171.
RecName: Full=Targeting protein for Xklp2;
AltName: Full=Differentially expressed in cancerous and non-cancerous lung cells 2;
Short=DIL-2;
AltName: Full=Hepatocellular carcinoma-associated antigen 519;
AltName: Full=Hepatocellular carcinoma-associated antigen 90;
AltName: Full=Protein fls353;
AltName: Full=Restricted expression proliferation-associated protein 100;
Short=p100;
Name=TPX2; Synonyms=C20orf1, C20orf2, DIL2, HCA519;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10512675; DOI=10.1006/geno.1999.5939;
Manda R., Kohno T., Matsuno Y., Takenoshita S., Kuwano H., Yokota J.;
"Identification of genes (SPON2 and C20orf2) differentially expressed
between cancerous and noncancerous lung cells by mRNA differential
display.";
Genomics 61:5-14(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10393424;
Zhang Y., Heidebrecht H.J., Rott A., Schlegelberger B., Parwaresch R.;
"Assignment of human proliferation associated p100 gene (C20orf1) to
human chromosome band 20q11.2 by in situ hybridization.";
Cytogenet. Cell Genet. 84:182-183(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Nezu J.;
"Fetal gene preferentially expressed in colorectal cancer.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Hepatoma;
PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y.,
Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W.,
Chen W.-F.;
"Large scale identification of human hepatocellular carcinoma-
associated antigens by autoantibodies.";
J. Immunol. 169:1102-1109(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Lung;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-747 (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 42-747 (ISOFORM 1).
PubMed=10871281; DOI=10.1083/jcb.149.7.1405;
Wittmann T., Wilm M., Karsenti E., Vernos I.;
"TPX2, a novel Xenopus MAP involved in spindle pole organization.";
J. Cell Biol. 149:1405-1418(2000).
[10]
CHARACTERIZATION.
PubMed=9207457;
Heidebrecht H.J., Buck F., Steinmann J., Sprenger R., Wacker H.H.,
Parwaresch R.;
"p100: a novel proliferation-associated nuclear protein specifically
restricted to cell cycle phases S, G2, and M.";
Blood 90:226-233(1997).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-369 AND SER-738, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[14]
FUNCTION, INTERACTION WITH AURKA, AND SUBCELLULAR LOCATION.
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486 AND SER-738, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59; THR-72; SER-310;
THR-338; SER-486 AND SER-738, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19208764; DOI=10.1242/jcs.037259;
Moss D.K., Wilde A., Lane J.D.;
"Dynamic release of nuclear RanGTP triggers TPX2-dependent microtubule
assembly during the apoptotic execution phase.";
J. Cell Sci. 122:644-655(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-305, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72; SER-292; SER-293;
SER-486 AND SER-738, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
INTERACTION WITH HNRNPU.
PubMed=21242313; DOI=10.1242/jcs.063347;
Ma N., Matsunaga S., Morimoto A., Sakashita G., Urano T., Uchiyama S.,
Fukui K.;
"The nuclear scaffold protein SAF-A is required for kinetochore-
microtubule attachment and contributes to the targeting of Aurora-A to
mitotic spindles.";
J. Cell Sci. 124:394-404(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-738, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59; THR-72; SER-121;
SER-125; THR-147; SER-257; SER-310; SER-359; THR-369; SER-486; THR-499
AND SER-738, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-641, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[26]
FUNCTION, AND INTERACTION WITH IMPORTIN-ALPHA.
PubMed=26165940; DOI=10.1016/j.cell.2015.06.014;
Wei J.H., Zhang Z.C., Wynn R.M., Seemann J.;
"GM130 regulates Golgi-derived spindle assembly by activating TPX2 and
capturing microtubules.";
Cell 162:287-299(2015).
[27]
INTERACTION WITH HNRNPU.
PubMed=25986610; DOI=10.1128/MCB.01312-14;
Douglas P., Ye R., Morrice N., Britton S., Trinkle-Mulcahy L.,
Lees-Miller S.P.;
"Phosphorylation of SAF-A/hnRNP-U serine 59 by polo-like kinase 1 is
required for mitosis.";
Mol. Cell. Biol. 35:2699-2713(2015).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-477; LYS-500; LYS-641 AND
LYS-740, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[29]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-43 IN COMPLEX WITH AURKA,
AND SUBUNIT.
PubMed=14580337; DOI=10.1016/S1097-2765(03)00392-7;
Bayliss R., Sardon T., Vernos I., Conti E.;
"Structural basis of Aurora-A activation by TPX2 at the mitotic
spindle.";
Mol. Cell 12:851-862(2003).
[30]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-43 IN COMPLEX WITH AURKA,
AND SUBUNIT.
PubMed=18662907; DOI=10.1110/ps.036590.108;
Zhao B., Smallwood A., Yang J., Koretke K., Nurse K., Calamari A.,
Kirkpatrick R.B., Lai Z.;
"Modulation of kinase-inhibitor interactions by auxiliary protein
binding: crystallography studies on Aurora A interactions with VX-680
and with TPX2.";
Protein Sci. 17:1791-1797(2008).
[31]
VARIANT [LARGE SCALE ANALYSIS] ASN-464.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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 (PubMed:18663142, PubMed:19208764). Activates
AURKA by promoting its autophosphorylation at 'Thr-288' and
protects this residue against dephosphorylation (PubMed:18663142,
PubMed:19208764). TPX2 is inactivated upon binding to importin-
alpha (PubMed:26165940). 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 (PubMed:26165940). {ECO:0000269|PubMed:18663142,
ECO:0000269|PubMed:19208764, ECO:0000269|PubMed:26165940}.
-!- SUBUNIT: Interacts with AURKA (PubMed:14580337, PubMed:18662907,
PubMed:18663142). Interacts with importin-alpha; leading to
inactivate TPX2 (PubMed:26165940). Interacts with HNRNPU; this
interaction recruits HNRNPU to spindle microtubules (MTs)
(PubMed:21242313, PubMed:25986610). {ECO:0000269|PubMed:14580337,
ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:18663142,
ECO:0000269|PubMed:21242313, ECO:0000269|PubMed:25986610,
ECO:0000269|PubMed:26165940}.
-!- INTERACTION:
O14965:AURKA; NbExp=7; IntAct=EBI-1037322, EBI-448680;
P62993:GRB2; NbExp=2; IntAct=EBI-1037322, EBI-401755;
O75330:HMMR; NbExp=5; IntAct=EBI-1037322, EBI-2556203;
P16333:NCK1; NbExp=4; IntAct=EBI-1037322, EBI-389883;
P27986:PIK3R1; NbExp=2; IntAct=EBI-1037322, EBI-79464;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19208764}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18663142,
ECO:0000269|PubMed:19208764}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000269|PubMed:18663142, ECO:0000269|PubMed:19208764}.
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:0000269|PubMed:19208764}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9ULW0-1; Sequence=Displayed;
Name=2; Synonyms=HCA90;
IsoId=Q9ULW0-2; Sequence=VSP_057355;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in lung carcinoma cell lines but not
in normal lung tissues.
-!- DEVELOPMENTAL STAGE: Exclusively expressed in proliferating cells
from the transition G1/S until the end of cytokinesis.
-!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
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EMBL; AB027467; BAA85893.1; -; mRNA.
EMBL; AF098158; AAF03248.1; -; mRNA.
EMBL; AB024704; BAA76931.1; -; mRNA.
EMBL; AF146731; AAD33965.1; -; mRNA.
EMBL; AF287265; AAK83033.1; -; mRNA.
EMBL; AL160175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW76418.1; -; Genomic_DNA.
EMBL; CH471077; EAW76422.1; -; Genomic_DNA.
EMBL; BC004136; AAH04136.1; -; mRNA.
EMBL; BC020207; AAH20207.1; -; mRNA.
EMBL; AL117534; CAB55982.1; -; mRNA.
EMBL; AF244547; AAF81695.1; -; mRNA.
CCDS; CCDS13190.1; -. [Q9ULW0-1]
PIR; T17292; T17292.
RefSeq; NP_036244.2; NM_012112.4. [Q9ULW0-1]
RefSeq; XP_011526999.1; XM_011528697.2. [Q9ULW0-1]
RefSeq; XP_011527001.1; XM_011528699.2. [Q9ULW0-1]
UniGene; Hs.244580; -.
PDB; 1OL5; X-ray; 2.50 A; B=1-43.
PDB; 3E5A; X-ray; 2.30 A; B=1-43.
PDB; 3HA6; X-ray; 2.36 A; B=1-43.
PDB; 4C3P; X-ray; 2.69 A; B/E=1-43.
PDB; 5LXM; X-ray; 2.08 A; D=6-43.
PDBsum; 1OL5; -.
PDBsum; 3E5A; -.
PDBsum; 3HA6; -.
PDBsum; 4C3P; -.
PDBsum; 5LXM; -.
ProteinModelPortal; Q9ULW0; -.
SMR; Q9ULW0; -.
BioGrid; 116624; 41.
CORUM; Q9ULW0; -.
DIP; DIP-36727N; -.
DIP; DIP-46212N; -.
IntAct; Q9ULW0; 20.
MINT; MINT-4720346; -.
STRING; 9606.ENSP00000300403; -.
ChEMBL; CHEMBL5389; -.
iPTMnet; Q9ULW0; -.
PhosphoSitePlus; Q9ULW0; -.
BioMuta; TPX2; -.
DMDM; 13124096; -.
EPD; Q9ULW0; -.
PaxDb; Q9ULW0; -.
PeptideAtlas; Q9ULW0; -.
PRIDE; Q9ULW0; -.
Ensembl; ENST00000300403; ENSP00000300403; ENSG00000088325. [Q9ULW0-1]
Ensembl; ENST00000340513; ENSP00000341145; ENSG00000088325. [Q9ULW0-2]
GeneID; 22974; -.
KEGG; hsa:22974; -.
UCSC; uc002wwp.2; human. [Q9ULW0-1]
CTD; 22974; -.
DisGeNET; 22974; -.
EuPathDB; HostDB:ENSG00000088325.15; -.
GeneCards; TPX2; -.
HGNC; HGNC:1249; TPX2.
HPA; HPA005487; -.
MIM; 605917; gene.
neXtProt; NX_Q9ULW0; -.
OpenTargets; ENSG00000088325; -.
PharmGKB; PA25638; -.
eggNOG; ENOG410IIEY; Eukaryota.
eggNOG; ENOG4110SQ6; LUCA.
GeneTree; ENSGT00390000009842; -.
HOGENOM; HOG000231739; -.
HOVERGEN; HBG057334; -.
InParanoid; Q9ULW0; -.
KO; K16812; -.
OMA; SRPCPTK; -.
OrthoDB; EOG091G0MIV; -.
PhylomeDB; Q9ULW0; -.
TreeFam; TF328997; -.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
ChiTaRS; TPX2; human.
EvolutionaryTrace; Q9ULW0; -.
GeneWiki; TPX2; -.
GenomeRNAi; 22974; -.
PRO; PR:Q9ULW0; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000088325; -.
CleanEx; HS_TPX2; -.
ExpressionAtlas; Q9ULW0; baseline and differential.
Genevisible; Q9ULW0; HS.
GO; GO:0043203; C:axon hillock; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:LIFEdb.
GO; GO:0072686; C:mitotic spindle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005819; C:spindle; ISS:UniProtKB.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0005525; F:GTP binding; TAS:ProtInc.
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; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
GO; GO:0090307; P:mitotic spindle assembly; IDA:UniProtKB.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0060236; P:regulation of mitotic spindle organization; ISS:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
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;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
Isopeptide bond; Microtubule; Mitosis; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 747 Targeting protein for Xklp2.
/FTId=PRO_0000065581.
MOD_RES 59 59 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 72 72 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000250|UniProtKB:A2APB8}.
MOD_RES 147 147 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 292 292 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 293 293 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 305 305 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 338 338 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 359 359 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 369 369 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:23186163}.
MOD_RES 375 375 N6-acetyllysine.
{ECO:0000250|UniProtKB:A2APB8}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 499 499 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 477 477 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 500 500 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 641 641 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 740 740 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 351 351 I -> IKTGSCSVTQAGVQWRDHGSLQCPTPGLKQSSCLSL
P (in isoform 2).
{ECO:0000303|PubMed:12097419}.
/FTId=VSP_057355.
VARIANT 464 464 T -> N (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036269.
CONFLICT 182 182 K -> N (in Ref. 3; BAA76931).
{ECO:0000305}.
CONFLICT 273 273 K -> E (in Ref. 1; BAA85893).
{ECO:0000305}.
TURN 19 21 {ECO:0000244|PDB:5LXM}.
HELIX 30 32 {ECO:0000244|PDB:5LXM}.
HELIX 33 41 {ECO:0000244|PDB:5LXM}.
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


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