CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019290
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase greatwall 
Protein Synonyms/Alias
 GW; GWL; hGWL; Microtubule-associated serine/threonine-protein kinase-like; MAST-L 
Gene Name
 MASTL 
Gene Synonyms/Alias
 GW; GWL; THC2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MDPTAGSKKEPGGGAubiquitination[1]
9DPTAGSKKEPGGGAAubiquitination[1]
39IEEFSIVKPISRGAFubiquitination[1, 2, 3, 4]
57YLGQKGGKLYAVKVVubiquitination[1]
66YAVKVVKKADMINKNubiquitination[5]
158GIIHRDLKPDNMLISubiquitination[5]
179LTDFGLSKVTLNRDIubiquitination[1, 5, 6, 7]
199LTTPSMAKPRQDYSRubiquitination[1, 5, 7]
269PYSSKLLKSCLETVAubiquitination[1, 7]
284SNPGMPVKCLTSNLLubiquitination[1]
350AVEKLCAKSANAIETubiquitination[1, 7]
358SANAIETKGFNKKDLubiquitination[1]
362IETKGFNKKDLELALubiquitination[1]
363ETKGFNKKDLELALSubiquitination[1]
457VDSSPCKKIIQNKKTubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. 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. 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. 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. 
Sequence Annotation
 DOMAIN 35 835 Protein kinase.
 DOMAIN 836 879 AGC-kinase C-terminal.
 NP_BIND 41 49 ATP (By similarity).
 ACT_SITE 156 156 Proton acceptor (By similarity).
 BINDING 62 62 ATP (By similarity).
 MOD_RES 207 207 Phosphothreonine.
 MOD_RES 222 222 Phosphothreonine.
 MOD_RES 293 293 Phosphoserine.
 MOD_RES 370 370 Phosphoserine.
 MOD_RES 552 552 Phosphoserine.
 MOD_RES 556 556 Phosphoserine.
 MOD_RES 631 631 Phosphoserine.
 MOD_RES 657 657 Phosphoserine.
 MOD_RES 668 668 Phosphoserine.
 MOD_RES 722 722 Phosphothreonine.
 MOD_RES 725 725 Phosphoserine.
 MOD_RES 741 741 Phosphothreonine.
 MOD_RES 875 875 Phosphoserine.
 MOD_RES 878 878 Phosphoserine.  
Keyword
 Alternative splicing; ATP-binding; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Kinase; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 879 AA 
Protein Sequence
MDPTAGSKKE PGGGAATEEG VNRIAVPKPP SIEEFSIVKP ISRGAFGKVY LGQKGGKLYA 60
VKVVKKADMI NKNMTHQVQA ERDALALSKS PFIVHLYYSL QSANNVYLVM EYLIGGDVKS 120
LLHIYGYFDE EMAVKYISEV ALALDYLHRH GIIHRDLKPD NMLISNEGHI KLTDFGLSKV 180
TLNRDINMMD ILTTPSMAKP RQDYSRTPGQ VLSLISSLGF NTPIAEKNQD PANILSACLS 240
ETSQLSQGLV CPMSVDQKDT TPYSSKLLKS CLETVASNPG MPVKCLTSNL LQSRKRLATS 300
SASSQSHTFI SSVESECHSS PKWEKDCQES DEALGPTMMS WNAVEKLCAK SANAIETKGF 360
NKKDLELALS PIHNSSALPT TGRSCVNLAK KCFSGEVSWE AVELDVNNIN MDTDTSQLGF 420
HQSNQWAVDS GGISEEHLGK RSLKRNFELV DSSPCKKIIQ NKKTCVEYKH NEMTNCYTNQ 480
NTGLTVEVQD LKLSVHKSQQ NDCANKENIV NSFTDKQQTP EKLPIPMIAK NLMCELDEDC 540
EKNSKRDYLS SSFLCSDDDR ASKNISMNSD SSFPGISIME SPLESQPLDS DRSIKESSFE 600
ESNIEDPLIV TPDCQEKTSP KGVENPAVQE SNQKMLGPPL EVLKTLASKR NAVAFRSFNS 660
HINASNNSEP SRMNMTSLDA MDISCAYSGS YPMAITPTQK RRSCMPHQQT PNQIKSGTPY 720
RTPKSVRRGV APVDDGRILG TPDYLAPELL LGRAHGPAVD WWALGVCLFE FLTGIPPFND 780
ETPQQVFQNI LKRDIPWPEG EEKLSDNAQS AVEILLTIDD TKRAGMKELK RHPLFSDVDW 840
ENLQHQTMPF IPQPDDETDT SYFEARNTAQ HLTVSGFSL 879 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0032154; C:cleavage furrow; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:UniProtKB.
 GO:0007067; P:mitosis; IMP:UniProtKB.
 GO:0034048; P:negative regulation of protein phosphatase type 2A activity; IMP:UniProtKB.
 GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
 GO:0006974; P:response to DNA damage stimulus; ISS:UniProtKB. 
Interpro
 IPR000961; AGC-kinase_C.
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
 SM00133; S_TK_X 
PROSITE
 PS51285; AGC_KINASE_CTER
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS