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Protein

Targeting protein for Xklp2

Gene

Tpx2

Organism
Mus musculus (Mouse)
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. Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation. TPX2 is inactivated upon binding to importin-alpha. 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.By similarity1 Publication

GO - Molecular functioni

  • 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
  • mitotic spindle assembly Source: UniProtKB
  • regulation of mitotic spindle organization Source: UniProtKB
  • spindle assembly Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Targeting protein for Xklp2
Gene namesi
Name:Tpx2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1919369. Tpx2.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasmcytoskeletonspindle By similarity
  • Cytoplasmcytoskeletonspindle pole By similarity

  • 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.By similarity

GO - Cellular componenti

  • aster Source: MGI
  • axon hillock Source: MGI
  • cytoplasm Source: UniProtKB-KW
  • microtubule Source: UniProtKB-KW
  • microtubule cytoskeleton Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • spindle Source: UniProtKB
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 114YSFD → ASAA: Abolishes interaction with AURKA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 745745Targeting protein for Xklp2PRO_0000393112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721PhosphothreonineCombined sources
Modified residuei128 – 1281N6-acetyllysineCombined sources
Modified residuei294 – 2941PhosphoserineBy similarity
Modified residuei307 – 3071N6-acetyllysineBy similarity
Modified residuei312 – 3121PhosphoserineBy similarity
Modified residuei340 – 3401PhosphothreonineBy similarity
Modified residuei369 – 3691PhosphothreonineBy similarity
Modified residuei375 – 3751N6-acetyllysineCombined sources
Modified residuei486 – 4861PhosphoserineCombined sources
Cross-linki640 – 640Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei737 – 7371PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiA2APB8.
MaxQBiA2APB8.
PaxDbiA2APB8.
PRIDEiA2APB8.

PTM databases

iPTMnetiA2APB8.
PhosphoSiteiA2APB8.

Expressioni

Gene expression databases

BgeeiA2APB8.
GenevisibleiA2APB8. MM.

Interactioni

Subunit structurei

Interacts with AURKA (PubMed:18663142). Interacts with importin-alpha; leading to inactivate TPX2 (By similarity).By similarity1 Publication

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi215163. 53 interactions.
IntActiA2APB8. 51 interactions.
STRINGi10090.ENSMUSP00000028969.

Structurei

3D structure databases

ProteinModelPortaliA2APB8.
SMRiA2APB8. Positions 6-42.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TPX2 family.Curated

Phylogenomic databases

eggNOGiENOG410IIEY. Eukaryota.
ENOG4110SQ6. LUCA.
GeneTreeiENSGT00390000009842.
HOGENOMiHOG000231739.
HOVERGENiHBG057334.
InParanoidiA2APB8.
KOiK16812.
OMAiGLFQGKT.
OrthoDBiEOG7W9RTQ.
PhylomeDBiA2APB8.
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]

Sequencei

Sequence statusi: Complete.

A2APB8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQVPTTYSF DAPTDFINFS SLDAEEDTEN IDSWFDEKAN LENKFLRQRG
60 70 80 90 100
IGEPFQGKNS LRKAKLQQGF VTPLKAVDNT YHKETEKENL QKQSIPSNDC
110 120 130 140 150
SSLDAKRAVS GNTPVQPQRR SIRLSAQKDL EQKEKNHVAS VEMKAKRCVA
160 170 180 190 200
PATDCPPQKR MKVSHKKKLE EEEEGSAPAT SRKNERETLE KAKGKHTVPG
210 220 230 240 250
VPPAREKVLK STEEQEIEKR LRMQQEVVEL RRKNEEFKKL ALAGPGQPVK
260 270 280 290 300
KSTSQVTKTV DFHFLTDERI KQHPKNQEEY KEVNFMSELR KHSSTPARGT
310 320 330 340 350
RGCTIIKPFN LSKGKKRTFD EAASTYVPIA QQVEAFHKRT PNRYHLRNKK
360 370 380 390 400
DESLLPSKSV NKIARDPQTP ILQTKYRTRA VTCKSTAEQE AEELEKLQQY
410 420 430 440 450
KFKARELDPR IFESGPILPK RAPVKPPTQP VGFDLEIEKR IHERESKKKT
460 470 480 490 500
EDEQFEFHSR PCPTKILEDV VGVPEKKVIP ATVPKSPVFA LKNRIRVPIK
510 520 530 540 550
DEEEEKPVVI KAQPVPHYGV PYKPHIAEAR NVEVCPFSFD TRDKERQLQK
560 570 580 590 600
EKKIKEMQKG EVPKFKALPV PHFDTINLPE KKVKNVTQAE PFSLETDKRG
610 620 630 640 650
AYKAEMWKHQ LEEEQKQQKD AACFKARPNT VIFQEPFVPK KEKKSLAENP
660 670 680 690 700
SGSLVQEPFQ LATERRAKER QELEKKMAEV EAWKLQQLEE VRQQEEEQQK
710 720 730 740
EELARLRKEL VHKANPIRKY AAVEVKSSEL PLTVPVSPKF STRFQ
Length:745
Mass (Da):85,894
Last modified:February 20, 2007 - v1
Checksum:i4E60692BC52DAE34
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651H → D in AAH60619 (PubMed:15489334).Curated
Sequence conflicti453 – 4531E → K in BAE32280 (PubMed:16141072).Curated
Sequence conflicti509 – 5091V → L in BAE32280 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK153957 mRNA. Translation: BAE32280.1.
AL833801 Genomic DNA. Translation: CAM23677.1.
CH466551 Genomic DNA. Translation: EDL05994.1.
BC060619 mRNA. Translation: AAH60619.1.
CCDSiCCDS16900.1.
RefSeqiNP_001135447.1. NM_001141975.1.
NP_001135448.1. NM_001141976.1.
NP_001135449.1. NM_001141977.1.
NP_001135450.1. NM_001141978.1.
NP_082385.3. NM_028109.4.
XP_006500276.1. XM_006500213.1.
XP_006500277.1. XM_006500214.1.
XP_006500278.1. XM_006500215.1.
UniGeneiMm.407737.

Genome annotation databases

EnsembliENSMUST00000028969; ENSMUSP00000028969; ENSMUSG00000027469.
ENSMUST00000109816; ENSMUSP00000105441; ENSMUSG00000027469.
ENSMUST00000164120; ENSMUSP00000128888; ENSMUSG00000027469.
ENSMUST00000178997; ENSMUSP00000136457; ENSMUSG00000027469.
GeneIDi72119.
KEGGimmu:72119.
UCSCiuc008ngo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK153957 mRNA. Translation: BAE32280.1.
AL833801 Genomic DNA. Translation: CAM23677.1.
CH466551 Genomic DNA. Translation: EDL05994.1.
BC060619 mRNA. Translation: AAH60619.1.
CCDSiCCDS16900.1.
RefSeqiNP_001135447.1. NM_001141975.1.
NP_001135448.1. NM_001141976.1.
NP_001135449.1. NM_001141977.1.
NP_001135450.1. NM_001141978.1.
NP_082385.3. NM_028109.4.
XP_006500276.1. XM_006500213.1.
XP_006500277.1. XM_006500214.1.
XP_006500278.1. XM_006500215.1.
UniGeneiMm.407737.

3D structure databases

ProteinModelPortaliA2APB8.
SMRiA2APB8. Positions 6-42.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215163. 53 interactions.
IntActiA2APB8. 51 interactions.
STRINGi10090.ENSMUSP00000028969.

PTM databases

iPTMnetiA2APB8.
PhosphoSiteiA2APB8.

Proteomic databases

EPDiA2APB8.
MaxQBiA2APB8.
PaxDbiA2APB8.
PRIDEiA2APB8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028969; ENSMUSP00000028969; ENSMUSG00000027469.
ENSMUST00000109816; ENSMUSP00000105441; ENSMUSG00000027469.
ENSMUST00000164120; ENSMUSP00000128888; ENSMUSG00000027469.
ENSMUST00000178997; ENSMUSP00000136457; ENSMUSG00000027469.
GeneIDi72119.
KEGGimmu:72119.
UCSCiuc008ngo.2. mouse.

Organism-specific databases

CTDi22974.
MGIiMGI:1919369. Tpx2.

Phylogenomic databases

eggNOGiENOG410IIEY. Eukaryota.
ENOG4110SQ6. LUCA.
GeneTreeiENSGT00390000009842.
HOGENOMiHOG000231739.
HOVERGENiHBG057334.
InParanoidiA2APB8.
KOiK16812.
OMAiGLFQGKT.
OrthoDBiEOG7W9RTQ.
PhylomeDBiA2APB8.
TreeFamiTF328997.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiTpx2. mouse.
PROiA2APB8.
SOURCEiSearch...

Gene expression databases

BgeeiA2APB8.
GenevisibleiA2APB8. MM.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72 AND SER-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "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, MUTAGENESIS OF 8-TYR--ASP-11.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486 AND SER-737, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung, Spleen and Testis.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128 AND LYS-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTPX2_MOUSE
AccessioniPrimary (citable) accession number: A2APB8
Secondary accession number(s): Q3U500, Q6P9S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: February 20, 2007
Last modified: June 8, 2016
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.