Q9ULW0 · TPX2_HUMAN
- ProteinTargeting protein for Xklp2
- GeneTPX2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids747 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 (PubMed:18663142, PubMed:19208764, PubMed:37728657).
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 activate AURKA kinase and stimulate local microtubule nucleation (PubMed:26165940).
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 activate AURKA kinase and stimulate local microtubule nucleation (PubMed:26165940).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | axon hillock | |
Cellular Component | cytosol | |
Cellular Component | intercellular bridge | |
Cellular Component | microtubule | |
Cellular Component | microtubule cytoskeleton | |
Cellular Component | mitotic spindle | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | spindle | |
Cellular Component | spindle pole | |
Molecular Function | importin-alpha family protein binding | |
Molecular Function | molecular adaptor activity | |
Molecular Function | protein kinase binding | |
Biological Process | activation of protein kinase activity | |
Biological Process | apoptotic process | |
Biological Process | cell division | |
Biological Process | microtubule nucleation | |
Biological Process | mitotic cell cycle | |
Biological Process | mitotic spindle assembly | |
Biological Process | negative regulation of microtubule depolymerization | |
Biological Process | regulation of mitotic spindle organization |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTargeting protein for Xklp2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9ULW0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_036269 | 464 | in a colorectal cancer sample; somatic mutation | |||
Sequence: T → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 786 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000065581 | 1-747 | UniProt | Targeting protein for Xklp2 | |||
Sequence: MSQVKSSYSYDAPSDFINFSSLDDEGDTQNIDSWFEEKANLENKLLGKNGTGGLFQGKTPLRKANLQQAIVTPLKPVDNTYYKEAEKENLVEQSIPSNACSSLEVEAAISRKTPAQPQRRSLRLSAQKDLEQKEKHHVKMKAKRCATPVIIDEILPSKKMKVSNNKKKPEEEGSAHQDTAEKNASSPEKAKGRHTVPCMPPAKQKFLKSTEEQELEKSMKMQQEVVEMRKKNEEFKKLALAGIGQPVKKSVSQVTKSVDFHFRTDERIKQHPKNQEEYKEVNFTSELRKHPSSPARVTKGCTIVKPFNLSQGKKRTFDETVSTYVPLAQQVEDFHKRTPNRYHLRSKKDDINLLPSKSSVTKICRDPQTPVLQTKHRARAVTCKSTAELEAEELEKLQQYKFKARELDPRILEGGPILPKKPPVKPPTEPIGFDLEIEKRIQERESKKKTEDEHFEFHSRPCPTKILEDVVGVPEKKVLPITVPKSPAFALKNRIRMPTKEDEEEDEPVVIKAQPVPHYGVPFKPQIPEARTVEICPFSFDSRDKERQLQKEKKIKELQKGEVPKFKALPLPHFDTINLPEKKVKNVTQIEPFCLETDRRGALKAQTWKHQLEEELRQQKEAACFKARPNTVISQEPFVPKKEKKSVAEGLSGSLVQEPFQLATEKRAKERQELEKRMAEVEAQKAQQLEEARLQEEEQKKEELARLRRELVHKANPIRKYQGLEIKSSDQPLTVPVSPKFSTRFHC | |||||||
Modified residue | 59 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 59 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 72 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 72 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 80 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 121 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 121 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 125 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 125 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 128 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 147 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 147 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 179 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 186 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 209 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 257 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 285 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 292 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 292 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 293 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 293 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 305 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 310 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 310 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 323 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 338 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 338 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 359 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 369 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 369 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 374 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 375 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 385 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 477 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 486 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 486 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 499 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 499 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 500 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 519 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 539 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 542 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 634 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 641 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 646 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 652 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 654 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 734 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 738 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 738 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 740 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
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.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with AURKA (PubMed:14580337, PubMed:18662907, PubMed:18663142).
Interacts with importin-alpha; leading to inactivate TPX2 (PubMed:26165940).
Interacts with HNRNPU; this interaction recruits HNRNPU to spindle microtubules (MTs) (PubMed:21242313, PubMed:25986610).
Interacts with BCL2L10 (By similarity).
Interacts with KIF11 (PubMed:37728657).
Interacts with importin-alpha; leading to inactivate TPX2 (PubMed:26165940).
Interacts with HNRNPU; this interaction recruits HNRNPU to spindle microtubules (MTs) (PubMed:21242313, PubMed:25986610).
Interacts with BCL2L10 (By similarity).
Interacts with KIF11 (PubMed:37728657).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9ULW0 | AURKA O14965 | 10 | EBI-1037322, EBI-448680 | |
BINARY | Q9ULW0 | CALR P27797 | 3 | EBI-1037322, EBI-1049597 | |
BINARY | Q9ULW0 | CDH1 P12830 | 3 | EBI-1037322, EBI-727477 | |
BINARY | Q9ULW0 | CDK5R1 Q15078 | 3 | EBI-1037322, EBI-746189 | |
BINARY | Q9ULW0 | DLST P36957 | 3 | EBI-1037322, EBI-351007 | |
BINARY | Q9ULW0 | GOLGA2 Q08379 | 6 | EBI-1037322, EBI-618309 | |
BINARY | Q9ULW0 | GRB2 P62993 | 2 | EBI-1037322, EBI-401755 | |
BINARY | Q9ULW0 | HMMR O75330 | 5 | EBI-1037322, EBI-2556203 | |
BINARY | Q9ULW0 | NCK1 P16333 | 4 | EBI-1037322, EBI-389883 | |
BINARY | Q9ULW0 | NEK7 Q8TDX7 | 3 | EBI-1037322, EBI-1055945 | |
BINARY | Q9ULW0 | PIK3R1 P27986 | 2 | EBI-1037322, EBI-79464 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 110-143 | Disordered | ||||
Sequence: SRKTPAQPQRRSLRLSAQKDLEQKEKHHVKMKAK | ||||||
Region | 156-202 | Disordered | ||||
Sequence: PSKKMKVSNNKKKPEEEGSAHQDTAEKNASSPEKAKGRHTVPCMPPA | ||||||
Compositional bias | 159-189 | Basic and acidic residues | ||||
Sequence: KMKVSNNKKKPEEEGSAHQDTAEKNASSPEK |
Sequence similarities
Belongs to the TPX2 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9ULW0-1
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.
- Name1
- Length747
- Mass (Da)85,653
- Last updated2001-02-21 v2
- ChecksumE028E0BB50BBCA0F
Q9ULW0-2
- Name2
- SynonymsHCA90
- Differences from canonical
- 351-351: I → IKTGSCSVTQAGVQWRDHGSLQCPTPGLKQSSCLSLP
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 159-189 | Basic and acidic residues | ||||
Sequence: KMKVSNNKKKPEEEGSAHQDTAEKNASSPEK | ||||||
Sequence conflict | 182 | in Ref. 3; BAA76931 | ||||
Sequence: K → N | ||||||
Sequence conflict | 273 | in Ref. 1; BAA85893 | ||||
Sequence: K → E | ||||||
Alternative sequence | VSP_057355 | 351 | in isoform 2 | |||
Sequence: I → IKTGSCSVTQAGVQWRDHGSLQCPTPGLKQSSCLSLP |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB027467 EMBL· GenBank· DDBJ | BAA85893.1 EMBL· GenBank· DDBJ | mRNA | ||
AF098158 EMBL· GenBank· DDBJ | AAF03248.1 EMBL· GenBank· DDBJ | mRNA | ||
AB024704 EMBL· GenBank· DDBJ | BAA76931.1 EMBL· GenBank· DDBJ | mRNA | ||
AF146731 EMBL· GenBank· DDBJ | AAD33965.1 EMBL· GenBank· DDBJ | mRNA | ||
AF287265 EMBL· GenBank· DDBJ | AAK83033.1 EMBL· GenBank· DDBJ | mRNA | ||
AL160175 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471077 EMBL· GenBank· DDBJ | EAW76418.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471077 EMBL· GenBank· DDBJ | EAW76422.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004136 EMBL· GenBank· DDBJ | AAH04136.1 EMBL· GenBank· DDBJ | mRNA | ||
BC020207 EMBL· GenBank· DDBJ | AAH20207.1 EMBL· GenBank· DDBJ | mRNA | ||
AL117534 EMBL· GenBank· DDBJ | CAB55982.1 EMBL· GenBank· DDBJ | mRNA | ||
AF244547 EMBL· GenBank· DDBJ | AAF81695.1 EMBL· GenBank· DDBJ | mRNA |