Search Results

Overview

Uniprot IDQ9ULW0
Protein NameTargeting protein for Xklp2
Gene NameTPX2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
128 SLRLSAQKDLEQKEK
158 IDEILPSKKMKVSNN
159 DEILPSKKMKVSNNK
203 VPCMPPAKQKFLKST
208 PAKQKFLKSTEEQEL
237 KKNEEFKKLALAGIG
248 AGIGQPVKKSVSQVT
249 GIGQPVKKSVSQVTK
305 TKGCTIVKPFNLSQG
314 FNLSQGKKRTFDETV
347 NRYHLRSKKDDINLL
348 RYHLRSKKDDINLLP
357 DINLLPSKSSVTKIC
362 PSKSSVTKICRDPQT
375 QTPVLQTKHRARAVT
401 LEKLQQYKFKARELD
44 EKANLENKLLGKNGT
476 DVVGVPEKKVLPITV
477 VVGVPEKKVLPITVP
48 LENKLLGKNGTGGLF
485 VLPITVPKSPAFALK
492 KSPAFALKNRIRMPT
560 KKIKELQKGEVPKFK
565 LQKGEVPKFKALPLP
567 KGEVPKFKALPLPHF
58 TGGLFQGKTPLRKAN
582 DTINLPEKKVKNVTQ
583 TINLPEKKVKNVTQI
604 TDRRGALKAQTWKHQ
626 QKEAACFKARPNTVI
63 QGKTPLRKANLQQAI
641 SQEPFVPKKEKKSVA
714 LRRELVHKANPIRKY
720 HKANPIRKYQGLEIK
740 LTVPVSPKFSTRFHC

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)

Protein Sequence

10 MSQVKSSYSY 20 DAPSDFINFS 30 SLDDEGDTQN 40 IDSWFEEKAN 50 LENKLLGKNG 60 TGGLFQGKTP 70 LRKANLQQAI 80 VTPLKPVDNT 90 YYKEAEKENL 100 VEQSIPSNAC 110 SSLEVEAAIS 120 RKTPAQPQRR 130 SLRLSAQKDL 140 EQKEKHHVKM 150 KAKRCATPVI 160 IDEILPSKKM 170 KVSNNKKKPE 180 EEGSAHQDTA 190 EKNASSPEKA 200 KGRHTVPCMP 210 PAKQKFLKST 220 EEQELEKSMK 230 MQQEVVEMRK 240 KNEEFKKLAL 250 AGIGQPVKKS 260 VSQVTKSVDF 270 HFRTDERIKQ 280 HPKNQEEYKE 290 VNFTSELRKH 300 PSSPARVTKG 310 CTIVKPFNLS 320 QGKKRTFDET 330 VSTYVPLAQQ 340 VEDFHKRTPN 350 RYHLRSKKDD 360 INLLPSKSSV 370 TKICRDPQTP 380 VLQTKHRARA 390 VTCKSTAELE 400 AEELEKLQQY 410 KFKARELDPR 420 ILEGGPILPK 430 KPPVKPPTEP 440 IGFDLEIEKR 450 IQERESKKKT 460 EDEHFEFHSR 470 PCPTKILEDV 480 VGVPEKKVLP 490 ITVPKSPAFA 500 LKNRIRMPTK 510 EDEEEDEPVV 520 IKAQPVPHYG 530 VPFKPQIPEA 540 RTVEICPFSF 550 DSRDKERQLQ 560 KEKKIKELQK 570 GEVPKFKALP 580 LPHFDTINLP 590 EKKVKNVTQI 600 EPFCLETDRR 610 GALKAQTWKH 620 QLEEELRQQK 630 EAACFKARPN 640 TVISQEPFVP 650 KKEKKSVAEG 660 LSGSLVQEPF 670 QLATEKRAKE 680 RQELEKRMAE 690 VEAQKAQQLE 700 EARLQEEEQK 710 KEELARLRRE 720 LVHKANPIRK 730 YQGLEIKSSD 740 QPLTVPVSPK FSTRFHC

Gene Ontology

Classification GO ID Description
Cellular Component GO:0043203 axon hillock
Cellular Component GO:0005829 cytosol
Cellular Component GO:0045171 intercellular bridge
Cellular Component GO:0005874 microtubule
Cellular Component GO:0015630 microtubule cytoskeleton
Cellular Component GO:0072686 mitotic spindle
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005819 spindle
Cellular Component GO:0000922 spindle pole
Molecular Function GO:0061676 importin-alpha family protein binding
Molecular Function GO:0060090 molecular adaptor activity
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:0043539 protein serine/threonine kinase activator activity
Biological Process GO:0032147 activation of protein kinase activity
Biological Process GO:0006915 apoptotic process
Biological Process GO:0051301 cell division
Biological Process GO:0007020 microtubule nucleation
Biological Process GO:0000278 mitotic cell cycle
Biological Process GO:0090307 mitotic spindle assembly
Biological Process GO:0007026 negative regulation of microtubule depolymerization
Biological Process GO:0060236 regulation of mitotic spindle organization

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[4] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[5] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.