Q9ULW0 (TPX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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
Protein fls353
Restricted expression proliferation-associated protein 100
Short name=p100

Gene names

Name:	TPX2
Synonyms:	C20orf1, C20orf2, DIL2, HCA519

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	747 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.18 Ref.22
Subunit structure	Interacts with AURKA. Ref.18 Ref.26 Ref.27
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › spindle. Cytoplasm › cytoskeleton › spindle pole. 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. Ref.18 Ref.22
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.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24
Sequence similarities	Belongs to the TPX2 family.

Ontologies

Keywords
Biological process	Apoptosis Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Microtubule Nucleus
Coding sequence diversity	Polymorphism
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	activation of protein kinase activity Inferred from direct assay Ref.26. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Traceable author statement. Source: ProtInc mitosis Traceable author statement. Source: ProtInc regulation of mitotic spindle organization Inferred from sequence or structural similarity Ref.18. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: HPA spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Traceable author statement. Source: ProtInc GTP binding Traceable author statement. Source: ProtInc protein kinase binding Inferred from physical interaction Ref.26Ref.27. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	2	EBI-1037322,EBI-401755
NCK1	P16333	4	EBI-1037322,EBI-389883
PIK3R1	P27986	2	EBI-1037322,EBI-79464

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 747

747

Targeting protein for Xklp2

PRO_0000065581

Amino acid modifications

Modified residue

20

1

Phosphoserine Ref.17

Modified residue

21

1

Phosphoserine Ref.17

Modified residue

28

1

Phosphothreonine Ref.17

Modified residue

33

1

Phosphoserine Ref.17

Modified residue

51

1

Phosphothreonine Ref.13 Ref.17

Modified residue

59

1

Phosphothreonine Ref.20

Modified residue

72

1

Phosphothreonine Ref.13 Ref.17 Ref.20 Ref.24

Modified residue

94

1

Phosphoserine Ref.17

Modified residue

113

1

Phosphothreonine Ref.17

Modified residue

121

1

Phosphoserine Ref.13 Ref.15 Ref.17 Ref.19 Ref.20

Modified residue

125

1

Phosphoserine Ref.13 Ref.15 Ref.17 Ref.19 Ref.20

Modified residue

147

1

Phosphothreonine Ref.13

Modified residue

179

1

Phosphothreonine Ref.17

Modified residue

185

1

Phosphoserine Ref.17 Ref.19

Modified residue

186

1

Phosphoserine Ref.13 Ref.17

Modified residue

209

1

Phosphoserine Ref.17

Modified residue

218

1

Phosphoserine Ref.17

Modified residue

250

1

Phosphoserine Ref.17

Modified residue

257

1

Phosphoserine Ref.20

Modified residue

293

1

Phosphoserine Ref.11 Ref.13 Ref.17 Ref.19

Modified residue

305

1

N6-acetyllysine Ref.25

Modified residue

310

1

Phosphoserine Ref.20

Modified residue

338

1

Phosphothreonine Ref.13 Ref.20

Modified residue

359

1

Phosphoserine Ref.13

Modified residue

369

1

Phosphothreonine Ref.12 Ref.13 Ref.17

Modified residue

374

1

Phosphothreonine Ref.13 Ref.17

Modified residue

486

1

Phosphoserine Ref.12 Ref.13 Ref.14 Ref.17 Ref.19 Ref.20

Modified residue

542

1

Phosphoserine Ref.13

Modified residue

634

1

Phosphoserine Ref.16

Modified residue

652

1

Phosphoserine Ref.13 Ref.17

Modified residue

654

1

Phosphoserine Ref.13

Modified residue

738

1

Phosphoserine Ref.10 Ref.12 Ref.13 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24

Natural variations

Natural variant

464

1

T → N in a colorectal cancer sample; somatic mutation. Ref.28

VAR_036269

Experimental info

Sequence conflict

182

1

K → N in BAA76931. Ref.3

Sequence conflict

273

1

K → E in BAA85893. Ref.1

Secondary structure

1

.

.

.

.

747

Helix Strand Turn

Details...

Helix

31 – 33

3

Helix

34 – 40

7

Sequences

	Sequence		Length	Mass (Da)
	Q9ULW0 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: E028E0BB50BBCA0F	FASTA	747	85,653
	10 20 30 40 50 60 MSQVKSSYSY DAPSDFINFS SLDDEGDTQN IDSWFEEKAN LENKLLGKNG TGGLFQGKTP 70 80 90 100 110 120 LRKANLQQAI VTPLKPVDNT YYKEAEKENL VEQSIPSNAC SSLEVEAAIS RKTPAQPQRR 130 140 150 160 170 180 SLRLSAQKDL EQKEKHHVKM KAKRCATPVI IDEILPSKKM KVSNNKKKPE EEGSAHQDTA 190 200 210 220 230 240 EKNASSPEKA KGRHTVPCMP PAKQKFLKST EEQELEKSMK MQQEVVEMRK KNEEFKKLAL 250 260 270 280 290 300 AGIGQPVKKS VSQVTKSVDF HFRTDERIKQ HPKNQEEYKE VNFTSELRKH PSSPARVTKG 310 320 330 340 350 360 CTIVKPFNLS QGKKRTFDET VSTYVPLAQQ VEDFHKRTPN RYHLRSKKDD INLLPSKSSV 370 380 390 400 410 420 TKICRDPQTP VLQTKHRARA VTCKSTAELE AEELEKLQQY KFKARELDPR ILEGGPILPK 430 440 450 460 470 480 KPPVKPPTEP IGFDLEIEKR IQERESKKKT EDEHFEFHSR PCPTKILEDV VGVPEKKVLP 490 500 510 520 530 540 ITVPKSPAFA LKNRIRMPTK EDEEEDEPVV IKAQPVPHYG VPFKPQIPEA RTVEICPFSF 550 560 570 580 590 600 DSRDKERQLQ KEKKIKELQK GEVPKFKALP LPHFDTINLP EKKVKNVTQI EPFCLETDRR 610 620 630 640 650 660 GALKAQTWKH QLEEELRQQK EAACFKARPN TVISQEPFVP KKEKKSVAEG LSGSLVQEPF 670 680 690 700 710 720 QLATEKRAKE RQELEKRMAE VEAQKAQQLE EARLQEEEQK KEELARLRRE LVHKANPIRK 730 740 YQGLEIKSSD QPLTVPVSPK FSTRFHC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10512675] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 10393424] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Fetal gene preferentially expressed in colorectal cancer." Nezu J. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 12097419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Lung.
[7]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-747. Tissue: Testis.
[8]	"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: 10871281] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 42-747.
[9]	"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: 9207457] [Abstract] Cited for: CHARACTERIZATION.
[10]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, MASS SPECTROMETRY. 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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-369; SER-486 AND SER-738, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51; THR-72; SER-121; SER-125; THR-147; SER-186; SER-293; THR-338; SER-359; THR-369; THR-374; SER-486; SER-542; SER-652; SER-654 AND SER-738, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[14]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-125, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[17]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-21; THR-28; SER-33; THR-51; THR-72; SER-94; THR-113; SER-121; SER-125; THR-179; SER-185; SER-186; SER-209; SER-218; SER-250; SER-293; THR-369; THR-374; SER-486; SER-652 AND SER-738, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: 18663142] [Abstract] Cited for: FUNCTION, INTERACTION WITH AURKA, SUBCELLULAR LOCATION.
[19]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-125; SER-185; SER-293; SER-486 AND SER-738, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59; THR-72; SER-121; SER-125; SER-257; SER-310; THR-338; SER-486 AND SER-738, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[22]	"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: 19208764] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[23]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738, MASS SPECTROMETRY.
[24]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72 AND SER-738, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-305, MASS SPECTROMETRY.
[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: 14580337] [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: 18662907] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-43 IN COMPLEX WITH AURKA, SUBUNIT.
[28]	"The consensus coding sequences of human breast and colorectal cancers." 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. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-464.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB027467 mRNA. Translation: BAA85893.1.
AF098158 mRNA. Translation: AAF03248.1.
AB024704 mRNA. Translation: BAA76931.1.
AF146731 mRNA. Translation: AAD33965.1.
AL160175 Genomic DNA. Translation: CAD38007.1.
BC004136 mRNA. Translation: AAH04136.1.
BC020207 mRNA. Translation: AAH20207.1.
AL117534 mRNA. Translation: CAB55982.1.
AF244547 mRNA. Translation: AAF81695.1.

IPI

IPI00008477.

PIR

T17292.

RefSeq

NP_036244.2. NM_012112.4.

UniGene

Hs.244580.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OL5	X-ray	2.50	B	3-43	[»]
3E5A	X-ray	2.30	B	1-43	[»]
3HA6	X-ray	2.36	B	1-43	[»]

ProteinModelPortal

Q9ULW0.

SMR

Q9ULW0. Positions 6-42.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36727N.

IntAct

Q9ULW0. 7 interactions.

MINT

MINT-4720346.

STRING

Q9ULW0.

PTM databases

PhosphoSite

Q9ULW0.

Polymorphism databases

DMDM

13124096.

Proteomic databases

PRIDE

Q9ULW0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000300403; ENSP00000300403; ENSG00000088325.

GeneID

22974.

KEGG

hsa:22974.

UCSC

uc002wwp.1. human.

Organism-specific databases

CTD

22974.

GeneCards

GC20P030326.

H-InvDB

HIX0015714.

HGNC

HGNC:1249. TPX2.

HPA

HPA005487.

MIM

605917. gene.

neXtProt

NX_Q9ULW0.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000009842.

HOVERGEN

HBG057334.

OrthoDB

EOG434W5K.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_a_pathway. Aurora A signaling.

Gene expression databases

ArrayExpress

Q9ULW0.

Bgee

Q9ULW0.

CleanEx

HS_TPX2.

Genevestigator

Q9ULW0.

GermOnline

ENSG00000088325. Homo sapiens.

Family and domain databases

InterPro

IPR015128. Aurora-A-bd.
IPR022021. TPX2_importin.
IPR009675. Xklp2_targeting_prot.
[Graphical view]

Pfam

PF09041. Aurora-A_bind. 1 hit.
PF06886. TPX2. 1 hit.
PF12214. TPX2_importin. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

43781.

SOURCE

Search...

Entry information

Entry name

TPX2_HUMAN

Accession

Primary (citable) accession number: Q9ULW0
Secondary accession number(s): Q9H1R4 , Q9NRA3, Q9UFN9, Q9UL00, Q9Y2M1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	February 21, 2001
Last modified:	January 25, 2012
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.