UniProt ID | TPX2_MOUSE | |
---|---|---|
UniProt AC | A2APB8 | |
Protein Name | Targeting protein for Xklp2 | |
Gene Name | Tpx2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 745 | |
Subcellular Localization | Nucleus . Cytoplasm, cytoskeleton, spindle . Cytoplasm, cytoskeleton, spindle pole . 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 nucl | |
Protein Description | 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.. | |
Protein Sequence | MSQVPTTYSFDAPTDFINFSSLDAEEDTENIDSWFDEKANLENKFLRQRGIGEPFQGKNSLRKAKLQQGFVTPLKAVDNTYHKETEKENLQKQSIPSNDCSSLDAKRAVSGNTPVQPQRRSIRLSAQKDLEQKEKNHVASVEMKAKRCVAPATDCPPQKRMKVSHKKKLEEEEEGSAPATSRKNERETLEKAKGKHTVPGVPPAREKVLKSTEEQEIEKRLRMQQEVVELRRKNEEFKKLALAGPGQPVKKSTSQVTKTVDFHFLTDERIKQHPKNQEEYKEVNFMSELRKHSSTPARGTRGCTIIKPFNLSKGKKRTFDEAASTYVPIAQQVEAFHKRTPNRYHLRNKKDESLLPSKSVNKIARDPQTPILQTKYRTRAVTCKSTAEQEAEELEKLQQYKFKARELDPRIFESGPILPKRAPVKPPTQPVGFDLEIEKRIHERESKKKTEDEQFEFHSRPCPTKILEDVVGVPEKKVIPATVPKSPVFALKNRIRVPIKDEEEEKPVVIKAQPVPHYGVPYKPHIAEARNVEVCPFSFDTRDKERQLQKEKKIKEMQKGEVPKFKALPVPHFDTINLPEKKVKNVTQAEPFSLETDKRGAYKAEMWKHQLEEEQKQQKDAACFKARPNTVIFQEPFVPKKEKKSLAENPSGSLVQEPFQLATERRAKERQELEKKMAEVEAWKLQQLEEVRQQEEEQQKEELARLRKELVHKANPIRKYAAVEVKSSELPLTVPVSPKFSTRFQ | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
44 | Ubiquitination | EKANLENKFLRQRGI HHHHHHHHHHHHCCC | 36.08 | - | |
60 | Phosphorylation | EPFQGKNSLRKAKLQ CCCCCCHHHHHHHCC | 32.79 | 25266776 | |
72 | Phosphorylation | KLQQGFVTPLKAVDN HCCCCCCCCHHHHCC | 22.20 | 26824392 | |
75 | Acetylation | QGFVTPLKAVDNTYH CCCCCCHHHHCCCCC | 47.79 | 23806337 | |
101 | Phosphorylation | SIPSNDCSSLDAKRA CCCCCCCCCHHHHHH | 36.48 | 25266776 | |
102 | Phosphorylation | IPSNDCSSLDAKRAV CCCCCCCCHHHHHHH | 36.28 | 25266776 | |
110 | Phosphorylation | LDAKRAVSGNTPVQP HHHHHHHCCCCCCCC | 25.91 | 24453211 | |
113 | Phosphorylation | KRAVSGNTPVQPQRR HHHHCCCCCCCCCHH | 28.50 | 26824392 | |
121 | Phosphorylation | PVQPQRRSIRLSAQK CCCCCHHHHHHHHHH | 17.78 | 21659605 | |
125 | Phosphorylation | QRRSIRLSAQKDLEQ CHHHHHHHHHHHHHH | 20.85 | 21743459 | |
128 | Acetylation | SIRLSAQKDLEQKEK HHHHHHHHHHHHHHH | 65.09 | 23806337 | |
140 | Phosphorylation | KEKNHVASVEMKAKR HHHHCCEEHHHHHHH | 19.95 | 28066266 | |
188 | Phosphorylation | SRKNERETLEKAKGK CCHHHHHHHHHHCCC | 46.57 | 28507225 | |
291 | Acetylation | NFMSELRKHSSTPAR HHHHHHHHCCCCCCC | 61.54 | 19847687 | |
294 | Phosphorylation | SELRKHSSTPARGTR HHHHHCCCCCCCCCC | 37.82 | - | |
307 | Acetylation | TRGCTIIKPFNLSKG CCCCEEEECCCCCCC | 39.44 | 23806337 | |
312 | Phosphorylation | IIKPFNLSKGKKRTF EEECCCCCCCCCCCH | 40.23 | 26745281 | |
326 | Phosphorylation | FDEAASTYVPIAQQV HHHHHHHHHCHHHHH | 11.18 | 23984901 | |
340 | Phosphorylation | VEAFHKRTPNRYHLR HHHHHHHCCCCCCCC | 29.71 | 23984901 | |
353 | Phosphorylation | LRNKKDESLLPSKSV CCCCCCCCCCCCCCH | 45.39 | 28066266 | |
357 | Phosphorylation | KDESLLPSKSVNKIA CCCCCCCCCCHHHHH | 37.22 | 28066266 | |
359 | Phosphorylation | ESLLPSKSVNKIARD CCCCCCCCHHHHHCC | 34.95 | 28066266 | |
369 | Phosphorylation | KIARDPQTPILQTKY HHHCCCCCCCCCCCC | 20.06 | 26824392 | |
374 | Phosphorylation | PQTPILQTKYRTRAV CCCCCCCCCCCCCEE | 26.97 | 22817900 | |
375 | Acetylation | QTPILQTKYRTRAVT CCCCCCCCCCCCEEC | 21.55 | 23806337 | |
414 | Phosphorylation | LDPRIFESGPILPKR CCHHHHCCCCCCCCC | 38.84 | 25159016 | |
465 | Acetylation | HSRPCPTKILEDVVG HCCCCCCHHHHHHCC | 30.36 | 22826441 | |
482 | Phosphorylation | EKKVIPATVPKSPVF CCCEECCCCCCCCCE | 31.80 | 25159016 | |
486 | Phosphorylation | IPATVPKSPVFALKN ECCCCCCCCCEEECC | 21.89 | 26824392 | |
523 | Acetylation | PHYGVPYKPHIAEAR CCCCCCCCCCCCCCC | 24.85 | 23806337 | |
645 | Phosphorylation | VPKKEKKSLAENPSG CCHHHHHCCCCCCCC | 43.83 | 26824392 | |
651 | Phosphorylation | KSLAENPSGSLVQEP HCCCCCCCCCCCCHH | 53.23 | 26643407 | |
653 | Phosphorylation | LAENPSGSLVQEPFQ CCCCCCCCCCCHHHH | 29.70 | 25777480 | |
727 | Phosphorylation | YAAVEVKSSELPLTV EEEEEEECCCCCCEE | 33.93 | 25619855 | |
733 | Phosphorylation | KSSELPLTVPVSPKF ECCCCCCEEECCCCC | 22.33 | 25619855 | |
737 | Phosphorylation | LPLTVPVSPKFSTRF CCCEEECCCCCCCCC | 19.12 | 27087446 | |
741 | Phosphorylation | VPVSPKFSTRFQ--- EECCCCCCCCCC--- | 25.46 | 23984901 | |
742 | Phosphorylation | PVSPKFSTRFQ---- ECCCCCCCCCC---- | 38.34 | 23984901 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
369 | T | Phosphorylation | Kinase | MAPK1 | P63085 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TPX2_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of TPX2_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737, AND MASSSPECTROMETRY. |