Search Results

Overview

Uniprot IDQ96GX5
Protein NameSerine/threonine-protein kinase greatwall
Gene NameMASTL
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
266 DTTPYSSKLLKSCLE
358 SANAIETKGFNKKDL
362 IETKGFNKKDLELAL
363 ETKGFNKKDLELALS
391 SCVNLAKKCFSGEVS
456 LVDSSPCKKIIQNKK
457 VDSSPCKKIIQNKKT
497 DLKLSVHKSQQNDCA

Function

Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance (PubMed:19680222). Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively (PubMed:38123684). ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high (PubMed:20818157). Following DNA damage, it is also involved in checkpoint recovery by being inhibited. Phosphorylates histone protein in vitro; however such activity is unsure in vivo. May be involved in megakaryocyte differentiation

Protein Sequence

10 MDPTAGSKKE 20 PGGGAATEEG 30 VNRIAVPKPP 40 SIEEFSIVKP 50 ISRGAFGKVY 60 LGQKGGKLYA 70 VKVVKKADMI 80 NKNMTHQVQA 90 ERDALALSKS 100 PFIVHLYYSL 110 QSANNVYLVM 120 EYLIGGDVKS 130 LLHIYGYFDE 140 EMAVKYISEV 150 ALALDYLHRH 160 GIIHRDLKPD 170 NMLISNEGHI 180 KLTDFGLSKV 190 TLNRDINMMD 200 ILTTPSMAKP 210 RQDYSRTPGQ 220 VLSLISSLGF 230 NTPIAEKNQD 240 PANILSACLS 250 ETSQLSQGLV 260 CPMSVDQKDT 270 TPYSSKLLKS 280 CLETVASNPG 290 MPVKCLTSNL 300 LQSRKRLATS 310 SASSQSHTFI 320 SSVESECHSS 330 PKWEKDCQES 340 DEALGPTMMS 350 WNAVEKLCAK 360 SANAIETKGF 370 NKKDLELALS 380 PIHNSSALPT 390 TGRSCVNLAK 400 KCFSGEVSWE 410 AVELDVNNIN 420 MDTDTSQLGF 430 HQSNQWAVDS 440 GGISEEHLGK 450 RSLKRNFELV 460 DSSPCKKIIQ 470 NKKTCVEYKH 480 NEMTNCYTNQ 490 NTGLTVEVQD 500 LKLSVHKSQQ 510 NDCANKENIV 520 NSFTDKQQTP 530 EKLPIPMIAK 540 NLMCELDEDC 550 EKNSKRDYLS 560 SSFLCSDDDR 570 ASKNISMNSD 580 SSFPGISIME 590 SPLESQPLDS 600 DRSIKESSFE 610 ESNIEDPLIV 620 TPDCQEKTSP 630 KGVENPAVQE 640 SNQKMLGPPL 650 EVLKTLASKR 660 NAVAFRSFNS 670 HINASNNSEP 680 SRMNMTSLDA 690 MDISCAYSGS 700 YPMAITPTQK 710 RRSCMPHQQT 720 PNQIKSGTPY 730 RTPKSVRRGV 740 APVDDGRILG 750 TPDYLAPELL 760 LGRAHGPAVD 770 WWALGVCLFE 780 FLTGIPPFND 790 ETPQQVFQNI 800 LKRDIPWPEG 810 EEKLSDNAQS 820 AVEILLTIDD 830 TKRAGMKELK 840 RHPLFSDVDW 850 ENLQHQTMPF 860 IPQPDDETDT 870 SYFEARNTAQ HLTVSGFSL

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005813 centrosome
Cellular Component GO:0032154 cleavage furrow
Cellular Component GO:0015630 microtubule cytoskeleton
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016301 kinase activity
Molecular Function GO:0051721 protein phosphatase 2A binding
Molecular Function GO:0106310 protein serine kinase activity
Molecular Function GO:0004674 protein serine/threonine kinase activity
Molecular Function GO:0044325 transmembrane transporter binding
Biological Process GO:0051301 cell division
Biological Process GO:0006974 DNA damage response
Biological Process GO:0000086 G2/M transition of mitotic cell cycle
Biological Process GO:0035556 intracellular signal transduction
Biological Process GO:0051726 regulation of cell cycle
Biological Process GO:0007346 regulation of mitotic cell cycle

Reference

[1] 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.

[2] 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.