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Protein

Targeting protein for Xklp2

Gene

TPX2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).3 Publications

GO - Molecular functioni

  • ATP binding Source: ProtInc
  • GTP binding Source: ProtInc
  • importin-alpha family protein binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • activation of protein kinase activity Source: UniProtKB
  • apoptotic process Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • cell proliferation Source: ProtInc
  • G2/M transition of mitotic cell cycle Source: Reactome
  • mitotic nuclear division Source: ProtInc
  • mitotic spindle assembly Source: UniProtKB
  • regulation of mitotic spindle organization Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
Targeting protein for Xklp2
Alternative name(s):
Differentially expressed in cancerous and non-cancerous lung cells 2
Short name:
DIL-2
Hepatocellular carcinoma-associated antigen 519
Hepatocellular carcinoma-associated antigen 90
Protein fls353
Restricted expression proliferation-associated protein 100
Short name:
p100
Gene namesi
Name:TPX2
Synonyms:C20orf1, C20orf2, DIL2, HCA519
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:1249. TPX2.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasmcytoskeletonspindle 2 Publications
  • Cytoplasmcytoskeletonspindle pole 2 Publications

  • 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.1 Publication

GO - Cellular componenti

  • axon hillock Source: Ensembl
  • cytosol Source: Reactome
  • microtubule Source: UniProtKB-KW
  • microtubule cytoskeleton Source: LIFEdb
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
  • spindle Source: UniProtKB
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25638.

Chemistry

ChEMBLiCHEMBL5389.

Polymorphism and mutation databases

BioMutaiTPX2.
DMDMi13124096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 747747Targeting protein for Xklp2PRO_0000065581Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591PhosphothreonineCombined sources
Modified residuei72 – 721PhosphothreonineCombined sources
Modified residuei121 – 1211PhosphoserineCombined sources
Modified residuei125 – 1251PhosphoserineCombined sources
Modified residuei128 – 1281N6-acetyllysineBy similarity
Modified residuei147 – 1471PhosphothreonineCombined sources
Modified residuei257 – 2571PhosphoserineCombined sources
Modified residuei292 – 2921PhosphoserineCombined sources
Modified residuei293 – 2931PhosphoserineCombined sources
Modified residuei305 – 3051N6-acetyllysineCombined sources
Modified residuei310 – 3101PhosphoserineCombined sources
Modified residuei338 – 3381PhosphothreonineCombined sources
Modified residuei359 – 3591PhosphoserineCombined sources
Modified residuei369 – 3691PhosphothreonineCombined sources
Modified residuei375 – 3751N6-acetyllysineBy similarity
Modified residuei486 – 4861PhosphoserineCombined sources
Modified residuei499 – 4991PhosphothreonineCombined sources
Cross-linki641 – 641Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei738 – 7381PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9ULW0.
MaxQBiQ9ULW0.
PaxDbiQ9ULW0.
PeptideAtlasiQ9ULW0.
PRIDEiQ9ULW0.

PTM databases

iPTMnetiQ9ULW0.
PhosphoSiteiQ9ULW0.

Expressioni

Tissue specificityi

Expressed in lung carcinoma cell lines but not in normal lung tissues.

Developmental stagei

Exclusively expressed in proliferating cells from the transition G1/S until the end of cytokinesis.

Gene expression databases

BgeeiQ9ULW0.
CleanExiHS_TPX2.
ExpressionAtlasiQ9ULW0. baseline and differential.
GenevisibleiQ9ULW0. HS.

Organism-specific databases

HPAiHPA005487.

Interactioni

Subunit structurei

Interacts with AURKA (PubMed:14580337, PubMed:18662907, PubMed:18663142). Interacts with importin-alpha; leading to inactivate TPX2 (PubMed:26165940).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AURKAO149652EBI-1037322,EBI-448680
GRB2P629932EBI-1037322,EBI-401755
NCK1P163334EBI-1037322,EBI-389883
PIK3R1P279862EBI-1037322,EBI-79464

GO - Molecular functioni

  • importin-alpha family protein binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116624. 41 interactions.
DIPiDIP-36727N.
DIP-46212N.
IntActiQ9ULW0. 16 interactions.
MINTiMINT-4720346.
STRINGi9606.ENSP00000300403.

Structurei

Secondary structure

1
747
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 335Combined sources
Helixi34 – 407Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OL5X-ray2.50B1-43[»]
3E5AX-ray2.30B1-43[»]
3HA6X-ray2.36B1-43[»]
4C3PX-ray2.69B/E1-43[»]
ProteinModelPortaliQ9ULW0.
SMRiQ9ULW0. Positions 6-42.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ULW0.

Family & Domainsi

Sequence similaritiesi

Belongs to the TPX2 family.Curated

Phylogenomic databases

eggNOGiENOG410IIEY. Eukaryota.
ENOG4110SQ6. LUCA.
GeneTreeiENSGT00390000009842.
HOGENOMiHOG000231739.
HOVERGENiHBG057334.
InParanoidiQ9ULW0.
KOiK16812.
OMAiGLFQGKT.
OrthoDBiEOG7W9RTQ.
PhylomeDBiQ9ULW0.
TreeFamiTF328997.

Family and domain databases

InterProiIPR015128. Aurora-A-bd.
IPR027329. TPX2_C.
IPR027330. TPX2_central_dom.
IPR009675. TPX2_fam.
[Graphical view]
PANTHERiPTHR14326. PTHR14326. 1 hit.
PfamiPF09041. Aurora-A_bind. 1 hit.
PF06886. TPX2. 1 hit.
PF12214. TPX2_importin. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ULW0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSQVKSSYSY DAPSDFINFS SLDDEGDTQN IDSWFEEKAN LENKLLGKNG
60 70 80 90 100
TGGLFQGKTP LRKANLQQAI VTPLKPVDNT YYKEAEKENL VEQSIPSNAC
110 120 130 140 150
SSLEVEAAIS RKTPAQPQRR SLRLSAQKDL EQKEKHHVKM KAKRCATPVI
160 170 180 190 200
IDEILPSKKM KVSNNKKKPE EEGSAHQDTA EKNASSPEKA KGRHTVPCMP
210 220 230 240 250
PAKQKFLKST EEQELEKSMK MQQEVVEMRK KNEEFKKLAL AGIGQPVKKS
260 270 280 290 300
VSQVTKSVDF HFRTDERIKQ HPKNQEEYKE VNFTSELRKH PSSPARVTKG
310 320 330 340 350
CTIVKPFNLS QGKKRTFDET VSTYVPLAQQ VEDFHKRTPN RYHLRSKKDD
360 370 380 390 400
INLLPSKSSV TKICRDPQTP VLQTKHRARA VTCKSTAELE AEELEKLQQY
410 420 430 440 450
KFKARELDPR ILEGGPILPK KPPVKPPTEP IGFDLEIEKR IQERESKKKT
460 470 480 490 500
EDEHFEFHSR PCPTKILEDV VGVPEKKVLP ITVPKSPAFA LKNRIRMPTK
510 520 530 540 550
EDEEEDEPVV IKAQPVPHYG VPFKPQIPEA RTVEICPFSF DSRDKERQLQ
560 570 580 590 600
KEKKIKELQK GEVPKFKALP LPHFDTINLP EKKVKNVTQI EPFCLETDRR
610 620 630 640 650
GALKAQTWKH QLEEELRQQK EAACFKARPN TVISQEPFVP KKEKKSVAEG
660 670 680 690 700
LSGSLVQEPF QLATEKRAKE RQELEKRMAE VEAQKAQQLE EARLQEEEQK
710 720 730 740
KEELARLRRE LVHKANPIRK YQGLEIKSSD QPLTVPVSPK FSTRFHC
Length:747
Mass (Da):85,653
Last modified:February 21, 2001 - v2
Checksum:iE028E0BB50BBCA0F
GO
Isoform 2 (identifier: Q9ULW0-2) [UniParc]FASTAAdd to basket

Also known as: HCA90

The sequence of this isoform differs from the canonical sequence as follows:
     351-351: I → IKTGSCSVTQAGVQWRDHGSLQCPTPGLKQSSCLSLP

Note: No experimental confirmation available.
Show »
Length:783
Mass (Da):89,393
Checksum:i10C8E4122A53BF9E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821K → N in BAA76931 (Ref. 3) Curated
Sequence conflicti273 – 2731K → E in BAA85893 (PubMed:10512675).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti464 – 4641T → N in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036269

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei351 – 3511I → IKTGSCSVTQAGVQWRDHGS LQCPTPGLKQSSCLSLP in isoform 2. 1 PublicationVSP_057355

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027467 mRNA. Translation: BAA85893.1.
AF098158 mRNA. Translation: AAF03248.1.
AB024704 mRNA. Translation: BAA76931.1.
AF146731 mRNA. Translation: AAD33965.1.
AF287265 mRNA. Translation: AAK83033.1.
AL160175 Genomic DNA. Translation: CAD38007.1.
CH471077 Genomic DNA. Translation: EAW76418.1.
CH471077 Genomic DNA. Translation: EAW76422.1.
BC004136 mRNA. Translation: AAH04136.1.
BC020207 mRNA. Translation: AAH20207.1.
AL117534 mRNA. Translation: CAB55982.1.
AF244547 mRNA. Translation: AAF81695.1.
CCDSiCCDS13190.1. [Q9ULW0-1]
PIRiT17292.
RefSeqiNP_036244.2. NM_012112.4. [Q9ULW0-1]
XP_011526999.1. XM_011528697.1. [Q9ULW0-1]
XP_011527000.1. XM_011528698.1. [Q9ULW0-1]
XP_011527001.1. XM_011528699.1. [Q9ULW0-1]
UniGeneiHs.244580.

Genome annotation databases

EnsembliENST00000300403; ENSP00000300403; ENSG00000088325. [Q9ULW0-1]
ENST00000340513; ENSP00000341145; ENSG00000088325. [Q9ULW0-2]
GeneIDi22974.
KEGGihsa:22974.
UCSCiuc002wwp.2. human. [Q9ULW0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027467 mRNA. Translation: BAA85893.1.
AF098158 mRNA. Translation: AAF03248.1.
AB024704 mRNA. Translation: BAA76931.1.
AF146731 mRNA. Translation: AAD33965.1.
AF287265 mRNA. Translation: AAK83033.1.
AL160175 Genomic DNA. Translation: CAD38007.1.
CH471077 Genomic DNA. Translation: EAW76418.1.
CH471077 Genomic DNA. Translation: EAW76422.1.
BC004136 mRNA. Translation: AAH04136.1.
BC020207 mRNA. Translation: AAH20207.1.
AL117534 mRNA. Translation: CAB55982.1.
AF244547 mRNA. Translation: AAF81695.1.
CCDSiCCDS13190.1. [Q9ULW0-1]
PIRiT17292.
RefSeqiNP_036244.2. NM_012112.4. [Q9ULW0-1]
XP_011526999.1. XM_011528697.1. [Q9ULW0-1]
XP_011527000.1. XM_011528698.1. [Q9ULW0-1]
XP_011527001.1. XM_011528699.1. [Q9ULW0-1]
UniGeneiHs.244580.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OL5X-ray2.50B1-43[»]
3E5AX-ray2.30B1-43[»]
3HA6X-ray2.36B1-43[»]
4C3PX-ray2.69B/E1-43[»]
ProteinModelPortaliQ9ULW0.
SMRiQ9ULW0. Positions 6-42.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116624. 41 interactions.
DIPiDIP-36727N.
DIP-46212N.
IntActiQ9ULW0. 16 interactions.
MINTiMINT-4720346.
STRINGi9606.ENSP00000300403.

Chemistry

ChEMBLiCHEMBL5389.

PTM databases

iPTMnetiQ9ULW0.
PhosphoSiteiQ9ULW0.

Polymorphism and mutation databases

BioMutaiTPX2.
DMDMi13124096.

Proteomic databases

EPDiQ9ULW0.
MaxQBiQ9ULW0.
PaxDbiQ9ULW0.
PeptideAtlasiQ9ULW0.
PRIDEiQ9ULW0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300403; ENSP00000300403; ENSG00000088325. [Q9ULW0-1]
ENST00000340513; ENSP00000341145; ENSG00000088325. [Q9ULW0-2]
GeneIDi22974.
KEGGihsa:22974.
UCSCiuc002wwp.2. human. [Q9ULW0-1]

Organism-specific databases

CTDi22974.
GeneCardsiTPX2.
HGNCiHGNC:1249. TPX2.
HPAiHPA005487.
MIMi605917. gene.
neXtProtiNX_Q9ULW0.
PharmGKBiPA25638.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIEY. Eukaryota.
ENOG4110SQ6. LUCA.
GeneTreeiENSGT00390000009842.
HOGENOMiHOG000231739.
HOVERGENiHBG057334.
InParanoidiQ9ULW0.
KOiK16812.
OMAiGLFQGKT.
OrthoDBiEOG7W9RTQ.
PhylomeDBiQ9ULW0.
TreeFamiTF328997.

Enzyme and pathway databases

ReactomeiR-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-8854518. AURKA Activation by TPX2.

Miscellaneous databases

ChiTaRSiTPX2. human.
EvolutionaryTraceiQ9ULW0.
GeneWikiiTPX2.
GenomeRNAii22974.
PROiQ9ULW0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ULW0.
CleanExiHS_TPX2.
ExpressionAtlasiQ9ULW0. baseline and differential.
GenevisibleiQ9ULW0. HS.

Family and domain databases

InterProiIPR015128. Aurora-A-bd.
IPR027329. TPX2_C.
IPR027330. TPX2_central_dom.
IPR009675. TPX2_fam.
[Graphical view]
PANTHERiPTHR14326. PTHR14326. 1 hit.
PfamiPF09041. Aurora-A_bind. 1 hit.
PF06886. TPX2. 1 hit.
PF12214. TPX2_importin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display."
    Manda R., Kohno T., Matsuno Y., Takenoshita S., Kuwano H., Yokota J.
    Genomics 61:5-14(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Assignment of human proliferation associated p100 gene (C20orf1) to human chromosome band 20q11.2 by in situ hybridization."
    Zhang Y., Heidebrecht H.J., Rott A., Schlegelberger B., Parwaresch R.
    Cytogenet. Cell Genet. 84:182-183(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Fetal gene preferentially expressed in colorectal cancer."
    Nezu J.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  4. "Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies."
    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.
    J. Immunol. 169:1102-1109(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Tissue: Hepatoma.
  5. "The DNA sequence and comparative analysis of human chromosome 20."
    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.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain and Lung.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-747 (ISOFORM 1).
    Tissue: Testis.
  9. "TPX2, a novel Xenopus MAP involved in spindle pole organization."
    Wittmann T., Wilm M., Karsenti E., Vernos I.
    J. Cell Biol. 149:1405-1418(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-747 (ISOFORM 1).
  10. "p100: a novel proliferation-associated nuclear protein specifically restricted to cell cycle phases S, G2, and M."
    Heidebrecht H.J., Buck F., Steinmann J., Sprenger R., Wacker H.H., Parwaresch R.
    Blood 90:226-233(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-369 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Building a spindle of the correct length in human cells requires the interaction between TPX2 and Aurora A."
    Bird A.W., Hyman A.A.
    J. Cell Biol. 182:289-300(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AURKA, SUBCELLULAR LOCATION.
  15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59; THR-72; SER-310; THR-338; SER-486 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Dynamic release of nuclear RanGTP triggers TPX2-dependent microtubule assembly during the apoptotic execution phase."
    Moss D.K., Wilde A., Lane J.D.
    J. Cell Sci. 122:644-655(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72; SER-292; SER-293; SER-486 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  24. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "GM130 regulates Golgi-derived spindle assembly by activating TPX2 and capturing microtubules."
    Wei J.H., Zhang Z.C., Wynn R.M., Seemann J.
    Cell 162:287-299(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IMPORTIN-ALPHA.
  26. "Structural basis of Aurora-A activation by TPX2 at the mitotic spindle."
    Bayliss R., Sardon T., Vernos I., Conti E.
    Mol. Cell 12:851-862(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-43 IN COMPLEX WITH AURKA, SUBUNIT.
  27. "Modulation of kinase-inhibitor interactions by auxiliary protein binding: crystallography studies on Aurora A interactions with VX-680 and with TPX2."
    Zhao B., Smallwood A., Yang J., Koretke K., Nurse K., Calamari A., Kirkpatrick R.B., Lai Z.
    Protein Sci. 17:1791-1797(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-43 IN COMPLEX WITH AURKA, SUBUNIT.
  28. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-464.

Entry informationi

Entry nameiTPX2_HUMAN
AccessioniPrimary (citable) accession number: Q9ULW0
Secondary accession number(s): Q96RR5
, Q9H1R4, Q9NRA3, Q9UFN9, Q9UL00, Q9Y2M1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: July 6, 2016
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.