CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001677
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase LATS1 
Protein Synonyms/Alias
 Large tumor suppressor homolog 1; WARTS protein kinase; h-warts 
Gene Name
 LATS1 
Gene Synonyms/Alias
 WARTS 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
688MRKMLCQKESNYIRLubiquitination[1]
860FRWTHDSKYYQSGDHubiquitination[2]
1005KNGADEIKAHPFFKTubiquitination[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] 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] 
Functional Description
 Negative regulator of YAP1 in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. Acts as a tumor suppressor which plays a critical role in maintenance of ploidy through its actions in both mitotic progression and the G1 tetraploidy checkpoint. Negatively regulates G2/M transition by down-regulating CDK1 kinase activity. Involved in the control of p53 expression. Affects cytokinesis by regulating actin polymerization through negative modulation of LIMK1. May also play a role in endocrine function. 
Sequence Annotation
 DOMAIN 100 141 UBA.
 DOMAIN 705 1010 Protein kinase.
 DOMAIN 1011 1090 AGC-kinase C-terminal.
 NP_BIND 711 719 ATP (By similarity).
 REGION 526 655 Interaction with YAP1.
 MOTIF 373 376 PPxY motif 1.
 MOTIF 556 559 PPxY motif 2.
 ACT_SITE 828 828 Proton acceptor (By similarity).
 BINDING 734 734 ATP.
 MOD_RES 246 246 Phosphothreonine.
 MOD_RES 278 278 Phosphoserine.
 MOD_RES 464 464 Phosphoserine; by NUAK1 and NUAK2.
 MOD_RES 674 674 Phosphoserine.
 MOD_RES 909 909 Phosphoserine; by STK3/MST2.
 MOD_RES 1079 1079 Phosphothreonine; by STK3/MST2.  
Keyword
 Alternative splicing; ATP-binding; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1130 AA 
Protein Sequence
MKRSEKPEGY RQMRPKTFPA SNYTVSSRQM LQEIRESLRN LSKPSDAAKA EHNMSKMSTE 60
DPRQVRNPPK FGTHHKALQE IRNSLLPFAN ETNSSRSTSE VNPQMLQDLQ AAGFDEDMVI 120
QALQKTNNRS IEAAIEFISK MSYQDPRREQ MAAAAARPIN ASMKPGNVQQ SVNRKQSWKG 180
SKESLVPQRH GPPLGESVAY HSESPNSQTD VGRPLSGSGI SAFVQAHPSN GQRVNPPPPP 240
QVRSVTPPPP PRGQTPPPRG TTPPPPSWEP NSQTKRYSGN MEYVISRISP VPPGAWQEGY 300
PPPPLNTSPM NPPNQGQRGI SSVPVGRQPI IMQSSSKFNF PSGRPGMQNG TGQTDFMIHQ 360
NVVPAGTVNR QPPPPYPLTA ANGQSPSALQ TGGSAAPSSY TNGSIPQSMM VPNRNSHNME 420
LYNISVPGLQ TNWPQSSSAP AQSSPSSGHE IPTWQPNIPV RSNSFNNPLG NRASHSANSQ 480
PSATTVTAIT PAPIQQPVKS MRVLKPELQT ALAPTHPSWI PQPIQTVQPS PFPEGTASNV 540
TVMPPVAEAP NYQGPPPPYP KHLLHQNPSV PPYESISKPS KEDQPSLPKE DESEKSYENV 600
DSGDKEKKQI TTSPITVRKN KKDEERRESR IQSYSPQAFK FFMEQHVENV LKSHQQRLHR 660
KKQLENEMMR VGLSQDAQDQ MRKMLCQKES NYIRLKRAKM DKSMFVKIKT LGIGAFGEVC 720
LARKVDTKAL YATKTLRKKD VLLRNQVAHV KAERDILAEA DNEWVVRLYY SFQDKDNLYF 780
VMDYIPGGDM MSLLIRMGIF PESLARFYIA ELTCAVESVH KMGFIHRDIK PDNILIDRDG 840
HIKLTDFGLC TGFRWTHDSK YYQSGDHPRQ DSMDFSNEWG DPSSCRCGDR LKPLERRAAR 900
QHQRCLAHSL VGTPNYIAPE VLLRTGYTQL CDWWSVGVIL FEMLVGQPPF LAQTPLETQM 960
KVINWQTSLH IPPQAKLSPE ASDLIIKLCR GPEDRLGKNG ADEIKAHPFF KTIDFSSDLR 1020
QQSASYIPKI THPTDTSNFD PVDPDKLWSD DNEEENVNDT LNGWYKNGKH PEHAFYEFTF 1080
RRFFDDNGYP YNYPKPIEYE YINSQGSEQQ SDEDDQNTGS EIKNRDLVYV 1130 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
 GO:0000922; C:spindle pole; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0051220; P:cytoplasmic sequestering of protein; IMP:BHF-UCL.
 GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
 GO:0035329; P:hippo signaling cascade; IDA:BHF-UCL.
 GO:0009755; P:hormone-mediated signaling pathway; ISS:UniProtKB.
 GO:0030216; P:keratinocyte differentiation; IEA:Compara.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IMP:BHF-UCL.
 GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
 GO:0030833; P:regulation of actin filament polymerization; IDA:UniProtKB.
 GO:0000819; P:sister chromatid segregation; IDA:UniProtKB. 
Interpro
 IPR000961; AGC-kinase_C.
 IPR011009; Kinase-like_dom.
 IPR017892; Pkinase_C.
 IPR000719; Prot_kinase_cat_dom.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS.
 IPR009060; UBA-like.
 IPR000449; UBA/transl_elong_EF1B_N.
 IPR015940; UBA/transl_elong_EF1B_N_euk. 
Pfam
 PF00069; Pkinase
 PF00433; Pkinase_C
 PF00627; UBA 
SMART
 SM00133; S_TK_X
 SM00220; S_TKc 
PROSITE
 PS51285; AGC_KINASE_CTER
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST
 PS50030; UBA 
PRINTS