Targeting protein for Xklp2 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q9ULW0 (TPX2_HUMAN)

Last modified May 26, 2009. Version 89. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Targeting protein for Xklp2
Alternative name(s):
    Restricted expression proliferation-associated protein 100
      Short name=p100
    Differentially expressed in cancerous and non-cancerous lung cells 2
      Short name=DIL-2
    Protein fls353
    Hepatocellular carcinoma-associated antigen 519

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

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Protein attributes

Sequence length	747 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Subcellular location	Nucleus. Spindle. 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.
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.18

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Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell proliferation Ref.1 Traceable author statement. Source: ProtInc mitosis Ref.9 Traceable author statement. Source: ProtInc
Cellular component	nucleus Ref.9 Traceable author statement. Source: ProtInc spindle Ref.9 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Ref.1 Traceable author statement. Source: ProtInc GTP binding Ref.1 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
AURKA	O14965	1	EBI-1037322,EBI-448680
CRK	P46108	1	EBI-1037322,EBI-886
GRB2	P62993	1	EBI-1037322,EBI-401755
NCK1	P16333	1	EBI-1037322,EBI-389883
PIK3R1	P27986	1	EBI-1037322,EBI-79464

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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

Phosphothreonine Ref.13

Modified residue

Phosphothreonine Ref.18

Modified residue

Phosphothreonine Ref.13 Ref.18

Modified residue

121

Phosphoserine Ref.13 Ref.15 Ref.17 Ref.18

Modified residue

125

Phosphoserine Ref.13 Ref.15 Ref.17 Ref.18

Modified residue

147

Phosphothreonine Ref.13

Modified residue

185

Phosphoserine Ref.17

Modified residue

186

Phosphoserine Ref.13

Modified residue

257

Phosphoserine Ref.18

Modified residue

293

Phosphoserine Ref.11 Ref.13 Ref.17

Modified residue

310

Phosphoserine Ref.18

Modified residue

338

Phosphothreonine Ref.13 Ref.18

Modified residue

359

Phosphoserine Ref.13

Modified residue

369

Phosphothreonine Ref.12 Ref.13

Modified residue

374

Phosphothreonine Ref.13

Modified residue

486

Phosphoserine Ref.12 Ref.13 Ref.14 Ref.17 Ref.18

Modified residue

542

Phosphoserine Ref.13

Modified residue

634

Phosphoserine Ref.16

Modified residue

652

Phosphoserine Ref.13

Modified residue

654

Phosphoserine Ref.13

Modified residue

738

Phosphoserine Ref.10 Ref.12 Ref.13 Ref.17 Ref.18

Natural variations

Natural variant

464

T → N in a colorectal cancer sample; somatic mutation. Ref.19

VAR_036269

Experimental info

Sequence conflict

182

K → N in BAA76931. Ref.3

Sequence conflict

273

K → E in BAA85893. Ref.1

Sequence conflict

712

V → VTGSMSTDEHKHASVLFYLY LTLYQTGSKV Ref.5

Secondary structure

747

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9ULW0-1 [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: E028E0BB50BBCA0F
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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

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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. 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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder 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: Epithelium.
[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: Epithelium.
[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: Epithelium.
[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: Epithelium.
[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: Epithelium.
[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.
[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.
[17]	"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.
[18]	"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.
[19]	"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. Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-464.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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.

UniGene

Hs.244580
Hs.708960

3D structure databases

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

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9ULW0. 5 interactions.

PTM databases

PhosphoSite

Q9ULW0.

Proteomic databases

PRIDE

Q9ULW0.

Genome annotation databases

Ensembl

ENSG00000088325. Homo sapiens. [Contig view]

GeneID

22974.

KEGG

hsa:22974.

Organism-specific databases

GeneCards

GC20P029790.

H-InvDB

HIX0015714.

HGNC

HGNC:1249. TPX2.

HPA

HPA005487.

MIM

605917. gene.

PharmGKB

PA25638.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9ULW0.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_a_pathway. Aurora A signaling.

Gene expression databases

ArrayExpress

Q9ULW0.

Bgee

Q9ULW0.

CleanEx

HS_TPX2.

GermOnline

ENSG00000088325. Homo sapiens.

Family and domain databases

InterPro

IPR015128. Aurora-A_bd.
IPR009675. TPX2.
[Graphical view]

Pfam

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

ProtoNet

Search...

Other Resources

NextBio

43781.

SOURCE

Search...

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Entry information

Entry name

TPX2_HUMAN

Accession

Primary (citable) accession number: Q9ULW0
Secondary accession number(s): Q9H1R4

Q9Y2M1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	February 21, 2001
Last modified:	May 26, 2009
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents