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Q6NUF4 (TPX2A_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Targeting protein for Xklp2-A
Gene names
Name:tpx2-a
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraMesobatrachiaPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length716 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Spindle assembly factor. Required for normal assembly of mitotic spindles. Mediates the binding kif15 and aurka to spindle microtubules. Required for targeting kif15 to microtubule minus ends. Activates aurka by promoting its autophosphorylation and protects the phosphorylated residue against dephosphorylation By similarity. Ref.1 Ref.4

Subunit structure

Associates with microtubules. Interacts with aurka and plk1. Interacts with kif15. Ref.3 Ref.4

Subcellular location

Nucleus. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonspindle pole. Note: Localizes during metaphase on spindle microtubules, with a strong enrichment at spindle poles. Localizes to the minus ends of spindle pole and aster microtubules in a dynein- and dynactin-dependent manner. Ref.1 Ref.3

Developmental stage

Detected in mitotic eggs (at protein level). Ref.3

Post-translational modification

Phosphorylated during mitosis. Hyperphosphorylated upon assembly of microtubules. Ref.1 Ref.4

Sequence similarities

Belongs to the TPX2 family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
Nucleus
   PTMPhosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 716716Targeting protein for Xklp2-A
PRO_0000393114

Amino acid modifications

Modified residue2041Phosphoserine; by plk1 Ref.4

Experimental info

Mutagenesis2041S → A: Decreases activation of aurka. Ref.4
Mutagenesis2041S → D: Increases activation of aurka. Ref.4
Sequence conflict611E → Q in AAF81694. Ref.1
Sequence conflict4731Missing in AAF81694. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6NUF4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F402B114123E839C

FASTA71682,512
        10         20         30         40         50         60 
MEDTQDTYSY DAPSIFNFSS FHEDHNADSW FDQVTNAENI PPDQRRLSET SVNTEQNSKV 

        70         80         90        100        110        120 
EPVQTTPSKD DVSNSATHVC DVKSQSKRSS RRMSKKHRQK LLVKMKDTHL EKETAPPEYP 

       130        140        150        160        170        180 
PCKKLKGSSS KGRHAPVIKS QSTSSHHSMT SPKPKAQLTM PSTPTVLKRR NVLVKAKNSE 

       190        200        210        220        230        240 
EQELEKMQEL QKEMLENLKK NEHSMKVAIT GAGQPVKTFI PVTKPVDFHF KTDDRLKRTA 

       250        260        270        280        290        300 
NQPEGDGYKA VDFASELRKH PPSPVQVTKG GHTVPKPFNL SKGKRKHEEA SDYVSTAEQV 

       310        320        330        340        350        360 
IAFYKRTPAR YHLRSRQREM EGPSPVKMIK TKLTNPKTPL LQTKGRHRPV TCKSAAELEA 

       370        380        390        400        410        420 
EELEMINQYK FKAQELDTRI LEGGPVLLKK PLVKEPTKAI GFDLEIEKRI QQREKKEEIE 

       430        440        450        460        470        480 
EETFTFHSRP CPSKMLTDVV GVPLKKLLPV TVPQSPAFAL KNRVRIPAQE EKQEEMVPVI 

       490        500        510        520        530        540 
KATRMPHYGV PFKPKLVEQR QVDVCPFSFC DRDKERQLQK EKRLDELRKD EVPKFKAQPL 

       550        560        570        580        590        600 
PQFDNIRLPE KKVKMPTQQE PFDLEIEKRG ASKLQRWQQQ IQEELKQQKE MVVFKARPNT 

       610        620        630        640        650        660 
VVHQEPFVPK KENRSLTESL SGSIVQEGFE LATAKRAKER QEFDKCLAET EAQKSLLEEE 

       670        680        690        700        710 
IRKRREEEEK EEISQLRQEL VHKAKPIRKY RAVEVKASDV PLTVPRSPNF SDRFKC 

« Hide

References

« Hide 'large scale' references
[1]"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], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, PHOSPHORYLATION.
Tissue: Egg.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[3]"Localization of the kinesin-like protein Xklp2 to spindle poles requires a leucine zipper, a microtubule-associated protein, and dynein."
Wittmann T., Boleti H., Antony C., Karsenti E., Vernos I.
J. Cell Biol. 143:673-685(1998) [PubMed: 9813089] [Abstract]
Cited for: INTERACTION WITH KIF15, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
[4]"Phosphorylation of TPX2 by Plx1 enhances activation of Aurora A."
Eckerdt F., Pascreau G., Phistry M., Lewellyn A.L., DePaoli-Roach A.A., Maller J.L.
Cell Cycle 8:2413-2419(2009) [PubMed: 19556869] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-204, MUTAGENESIS OF SER-204, INTERACTION WITH PLK1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF244546 mRNA. Translation: AAF81694.1.
BC068637 mRNA. Translation: AAH68637.1.
RefSeqNP_001082006.1. NM_001088537.1.
UniGeneXl.658.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KNDX-ray2.15B270-350[»]
ProteinModelPortalQ6NUF4.
SMRQ6NUF4. Positions 7-39.
ModBaseSearch...

Protein-protein interaction databases

IntActQ6NUF4. 4 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID398174.
KEGGxla:398174.

Organism-specific databases

CTD398174.
XenbaseXB-GENE-6251919. tpx2.

Phylogenomic databases

HOVERGENHBG057334.

Family and domain databases

InterProIPR015128. Aurora-A-bd.
IPR022021. TPX2_importin.
IPR009675. Xklp2_targeting_prot.
[Graphical view]
PfamPF09041. Aurora-A_bind. 1 hit.
PF06886. TPX2. 1 hit.
PF12214. TPX2_importin. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTPX2A_XENLA
AccessionPrimary (citable) accession number: Q6NUF4
Secondary accession number(s): Q9I8N0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: July 5, 2004
Last modified: October 19, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families