CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019545
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase SMG1 
Protein Synonyms/Alias
 SMG-1; hSMG-1; 61E3.4; Lambda/iota protein kinase C-interacting protein; Lambda-interacting protein 
Gene Name
 SMG1 
Gene Synonyms/Alias
 ATX; KIAA0421; LIP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
173LATVKQLKEFIQQPEacetylation[1]
529KLFIPSSKLLFLRYHubiquitination[2, 3]
598EIKHEAFKNHVFNVDubiquitination[2]
819RIRQAFGKLLKSIPLubiquitination[3]
879GNSHRTGKDNWLERLubiquitination[3]
1169SLNGESRKTVLSKPTubiquitination[3]
1232KADFNYIKSLSSFESubiquitination[4]
1287PDPRELQKSIEVQLLubiquitination[3]
1411NQLLEKIKEQTVPIRubiquitination[3]
1468DLVQHFKKLSTQGQVubiquitination[3]
1544KEISGQLKQVYRAQHubiquitination[4]
1632WAYRWGRKVVDNASQubiquitination[3]
1650VRLLPREKSEVQNLLubiquitination[3]
1798RLLRLLVKHAGELRQubiquitination[3]
1989QQLEDEVKRVQNNNTubiquitination[4]
2256PSELYYSKIGPALKTubiquitination[3]
2370KSLRVPEKVPFRMTQubiquitination[3]
2471SSRVAEIKVNWFKNRubiquitination[3]
2729IRQVERLKQEAVTVPubiquitination[3]
3030LKRLQTIKEFFRLCGubiquitination[3]
3065PVQIVNVKTLFRNSCubiquitination[4]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [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] 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]
 [4] 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
 Serine/threonine protein kinase involved in both mRNA surveillance and genotoxic stress response pathways. Recognizes the substrate consensus sequence [ST]-Q. Plays a central role in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating UPF1/RENT1. Recruited by release factors to stalled ribosomes together with SMG8 and SMG9 (forming the SMG1C protein kinase complex), and UPF1 to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD. Also acts as a genotoxic stress-activated protein kinase that displays some functional overlap with ATM. Can phosphorylate p53/TP53 and is required for optimal p53/TP53 activation after cellular exposure to genotoxic stress. Its depletion leads to spontaneous DNA damage and increased sensitivity to ionizing radiation (IR). May activate PRKCI but not PRKCZ. 
Sequence Annotation
 DOMAIN 1131 1866 FAT.
 REPEAT 1817 1852 HEAT.
 DOMAIN 2150 2478 PI3K/PI4K.
 DOMAIN 3629 3661 FATC.
 REGION 1 1977 Interaction with SMG8 and SMG9.
 MOD_RES 173 173 N6-acetyllysine.
 MOD_RES 3550 3550 Phosphothreonine.
 MOD_RES 3556 3556 Phosphoserine.
 MOD_RES 3570 3570 Phosphoserine.
 MOD_RES 3573 3573 Phosphothreonine.
 MOD_RES 3577 3577 Phosphothreonine (By similarity).  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; DNA damage; DNA repair; Kinase; Manganese; Metal-binding; Nonsense-mediated mRNA decay; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3661 AA 
Protein Sequence
MSRRAPGSRL SSGGGGGGTK YPRSWNDWQP RTDSASADPD NLKYSSSRDR GGSSSYGLQP 60
SNSAVVSRQR HDDTRVHADI QNDEKGGYSV NGGSGENTYG RKSLGQELRV NNVTSPEFTS 120
VQHGSRALAT KDMRKSQERS MSYSDESRLS NLLRRITRED DRDRRLATVK QLKEFIQQPE 180
NKLVLVKQLD NILAAVHDVL NESSKLLQEL RQEGACCLGL LCASLSYEAE KIFKWIFSKF 240
SSSAKDEVKL LYLCATYKAL ETVGEKKAFS SVMQLVMTSL QSILENVDTP ELLCKCVKCI 300
LLVARCYPHI FSTNFRDTVD ILVGWHIDHT QKPSLTQQVS GWLQSLEPFW VADLAFSTTL 360
LGQFLEDMEA YAEDLSHVAS GESVDEDVPP PSVSLPKLAA LLRVFSTVVR SIGERFSPIR 420
GPPITEAYVT DVLYRVMRCV TAANQVFFSE AVLTAANECV GVLLGSLDPS MTIHCDMVIT 480
YGLDQLENCQ TCGTDYIISV LNLLTLIVEQ INTKLPSSFV EKLFIPSSKL LFLRYHKEKE 540
VVAVAHAVYQ AVLSLKNIPV LETAYKLILG EMTCALNNLL HSLQLPEACS EIKHEAFKNH 600
VFNVDNAKFV VIFDLSALTT IGNAKNSLIG MWALSPTVFA LLSKNLMIVH SDLAVHFPAI 660
QYAVLYTLYS HCTRHDHFIS SSLSSSSPSL FDGAVISTVT TATKKHFSII LNLLGILLKK 720
DNLNQDTRKL LMTWALEAAV LMKKSETYAP LFSLPSFHKF CKGLLANTLV EDVNICLQAC 780
SSLHALSSSL PDDLLQRCVD VCRVQLVHSG TRIRQAFGKL LKSIPLDVVL SNNNHTEIQE 840
ISLALRSHMS KAPSNTFHPQ DFSDVISFIL YGNSHRTGKD NWLERLFYSC QRLDKRDQST 900
IPRNLLKTDA VLWQWAIWEA AQFTVLSKLR TPLGRAQDTF QTIEGIIRSL AAHTLNPDQD 960
VSQWTTADND EGHGNNQLRL VLLLQYLENL EKLMYNAYEG CANALTSPPK VIRTFFYTNR 1020
QTCQDWLTRI RLSIMRVGLL AGQPAVTVRH GFDLLTEMKT TSLSQGNELE VTIMMVVEAL 1080
CELHCPEAIQ GIAVWSSSIV GKNLLWINSV AQQAEGRFEK ASVEYQEHLC AMTGVDCCIS 1140
SFDKSVLTLA NAGRNSASPK HSLNGESRKT VLSKPTDSSP EVINYLGNKA CECYISIADW 1200
AAVQEWQNAI HDLKKSTSST SLNLKADFNY IKSLSSFESG KFVECTEQLE LLPGENINLL 1260
AGGSKEKIDM KKLLPNMLSP DPRELQKSIE VQLLRSSVCL ATALNPIEQD QKWQSITENV 1320
VKYLKQTSRI AIGPLRLSTL TVSQSLPVLS TLQLYCSSAL ENTVSNRLST EDCLIPLFSE 1380
ALRSCKQHDV RPWMQALRYT MYQNQLLEKI KEQTVPIRSH LMELGLTAAK FARKRGNVSL 1440
ATRLLAQCSE VQLGKTTTAQ DLVQHFKKLS TQGQVDEKWG PELDIEKTKL LYTAGQSTHA 1500
MEMLSSCAIS FCKSVKAEYA VAKSILTLAK WIQAEWKEIS GQLKQVYRAQ HQQNFTGLST 1560
LSKNILTLIE LPSVNTMEEE YPRIESESTV HIGVGEPDFI LGQLYHLSSV QAPEVAKSWA 1620
ALASWAYRWG RKVVDNASQG EGVRLLPREK SEVQNLLPDT ITEEEKERIY GILGQAVCRP 1680
AGIQDEDITL QITESEDNEE DDMVDVIWRQ LISSCPWLSE LDESATEGVI KVWRKVVDRI 1740
FSLYKLSCSA YFTFLKLNAG QIPLDEDDPR LHLSHRVEQS TDDMIVMATL RLLRLLVKHA 1800
GELRQYLEHG LETTPTAPWR GIIPQLFSRL NHPEVYVRQS ICNLLCRVAQ DSPHLILYPA 1860
IVGTISLSSE SQASGNKFST AIPTLLGNIQ GEELLVSECE GGSPPASQDS NKDEPKSGLN 1920
EDQAMMQDCY SKIVDKLSSA NPTMVLQVQM LVAELRRVTV LWDELWLGVL LQQHMYVLRR 1980
IQQLEDEVKR VQNNNTLRKE EKIAIMREKH TALMKPIVFA LEHVRSITAA PAETPHEKWF 2040
QDNYGDAIEN ALEKLKTPLN PAKPGSSWIP FKEIMLSLQQ RAQKRASYIL RLEEISPWLA 2100
AMTNTEIALP GEVSARDTVT IHSVGGTITI LPTKTKPKKL LFLGSDGKSY PYLFKGLEDL 2160
HLDERIMQFL SIVNTMFATI NRQETPRFHA RHYSVTPLGT RSGLIQWVDG ATPLFGLYKR 2220
WQQREAALQA QKAQDSYQTP QNPGIVPRPS ELYYSKIGPA LKTVGLSLDV SRRDWPLHVM 2280
KAVLEELMEA TPPNLLAKEL WSSCTTPDEW WRVTQSYARS TAVMSMVGYI IGLGDRHLDN 2340
VLIDMTTGEV VHIDYNVCFE KGKSLRVPEK VPFRMTQNIE TALGVTGVEG VFRLSCEQVL 2400
HIMRRGRETL LTLLEAFVYD PLVDWTAGGE AGFAGAVYGG GGQQAESKQS KREMEREITR 2460
SLFSSRVAEI KVNWFKNRDE MLVVLPKLDG SLDEYLSLQE QLTDVEKLQG KLLEEIEFLE 2520
GAEGVDHPSH TLQHRYSEHT QLQTQQRAVQ EAIQVKLNEF EQWITHYQAA FNNLEATQLA 2580
SLLQEISTQM DLGPPSYVPA TAFLQNAGQA HLISQCEQLE GEVGALLQQR RSVLRGCLEQ 2640
LHHYATVALQ YPKAIFQKHR IEQWKTWMEE LICNTTVERC QELYRKYEMQ YAPQPPPTVC 2700
QFITATEMTL QRYAADINSR LIRQVERLKQ EAVTVPVCED QLKEIERCIK VFLHENGEEG 2760
SLSLASVIIS ALCTLTRRNL MMEGAASSAG EQLVDLTSRD GAWFLEELCS MSGNVTCLVQ 2820
LLKQCHLVPQ DLDIPNPMEA SETVHLANGV YTSLQELNSN FRQIIFPEAL RCLMKGEYTL 2880
ESMLHELDGL IEQTTDGVPL QTLVESLQAY LRNAAMGLEE ETHAHYIDVA RLLHAQYGEL 2940
IQPRNGSVDE TPKMSAGQML LVAFDGMFAQ VETAFSLLVE KLNKMEIPIA WRKIDIIREA 3000
RSTQVNFFDD DNHRQVLEEI FFLKRLQTIK EFFRLCGTFS KTLSGSSSLE DQNTVNGPVQ 3060
IVNVKTLFRN SCFSEDQMAK PIKAFTADFV RQLLIGLPNQ ALGLTLCSFI SALGVDIIAQ 3120
VEAKDFGAES KVSVDDLCKK AVEHNIQIGK FSQLVMNRAT VLASSYDTAW KKHDLVRRLE 3180
TSISSCKTSL QRVQLHIAMF QWQHEDLLIN RPQAMSVTPP PRSAILTSMK KKLHTLSQIE 3240
TSIATVQEKL AALESSIEQR LKWAGGANPA LAPVLQDFEA TIAERRNLVL KESQRASQVT 3300
FLCSNIIHFE SLRTRTAEAL NLDAALFELI KRCQQMCSFA SQFNSSVSEL ELRLLQRVDT 3360
GLEHPIGSSE WLLSAHKQLT QDMSTQRAIQ TEKEQQIETV CETIQNLVDN IKTVLTGHNR 3420
QLGDVKHLLK AMAKDEEAAL ADGEDVPYEN SVRQFLGEYK SWQDNIQTVL FTLVQAMGQV 3480
RSQEHVEMLQ EITPTLKELK TQSQSIYNNL VSFASPLVTD ATNECSSPTS SATYQPSFAA 3540
AVRSNTGQKT QPDVMSQNAR KLIQKNLATS ADTPPSTVPG TGKSVACSPK KAVRDPKTGK 3600
AVQERNSYAV SVWKRVKAKL EGRDVDPNRR MSVAEQVDYV IKEATNLDNL AQLYEGWTAW 3660
V 3661 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0010467; P:gene expression; TAS:Reactome.
 GO:0006406; P:mRNA export from nucleus; TAS:UniProtKB.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB.
 GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
 GO:0046854; P:phosphatidylinositol phosphorylation; IDA:UniProtKB.
 GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
 GO:0006950; P:response to stress; IDA:UniProtKB. 
Interpro
 IPR016024; ARM-type_fold.
 IPR003152; FATC.
 IPR011009; Kinase-like_dom.
 IPR000403; PI3/4_kinase_cat_dom.
 IPR018936; PI3/4_kinase_CS.
 IPR014009; PIK_FAT. 
Pfam
 PF02260; FATC
 PF00454; PI3_PI4_kinase 
SMART
 SM00146; PI3Kc 
PROSITE
 PS51189; FAT
 PS51190; FATC
 PS50077; HEAT_REPEAT
 PS00915; PI3_4_KINASE_1
 PS00916; PI3_4_KINASE_2
 PS50290; PI3_4_KINASE_3 
PRINTS