CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023296
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Endoribonuclease Dicer 
Protein Synonyms/Alias
 Helicase with RNase motif; Helicase MOI 
Gene Name
 DICER1 
Gene Synonyms/Alias
 DICER; HERNA; KIAA0928 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
652PFTHLAPKCRTRELPubiquitination[1, 2]
1350LSYMRSKKVSNCNLYubiquitination[1]
1465MGSGAFVKKISLSPFubiquitination[3, 4]
1466GSGAFVKKISLSPFSubiquitination[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] 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]
 [3] 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]
 [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] 
Functional Description
 Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. Also cleaves double-stranded RNA to produce short interfering RNAs (siRNAs) which target the selective destruction of complementary RNAs. 
Sequence Annotation
 DOMAIN 51 227 Helicase ATP-binding.
 DOMAIN 433 602 Helicase C-terminal.
 DOMAIN 630 722 Dicer dsRNA-binding fold.
 DOMAIN 891 1042 PAZ.
 DOMAIN 1276 1403 RNase III 1.
 DOMAIN 1666 1824 RNase III 2.
 DOMAIN 1849 1914 DRBM.
 NP_BIND 64 71 ATP (By similarity).
 REGION 256 595 Required for interaction with PRKRA and
 MOTIF 175 178 DECH box.
 METAL 1316 1316 Magnesium or manganese 1 (By similarity).
 METAL 1395 1395 Magnesium or manganese 1 (By similarity).
 METAL 1398 1398 Magnesium or manganese 1 (By similarity).
 METAL 1705 1705 Magnesium or manganese 2.
 METAL 1810 1810 Magnesium or manganese 2.
 METAL 1813 1813 Magnesium or manganese 2.
 MOD_RES 413 413 Phosphoserine.
 MOD_RES 415 415 Phosphoserine.
 MOD_RES 1016 1016 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Disease mutation; Endonuclease; Helicase; Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1922 AA 
Protein Sequence
MKSPALQPLS MAGLQLMTPA SSPMGPFFGL PWQQEAIHDN IYTPRKYQVE LLEAALDHNT 60
IVCLNTGSGK TFIAVLLTKE LSYQIRGDFS RNGKRTVFLV NSANQVAQQV SAVRTHSDLK 120
VGEYSNLEVN ASWTKERWNQ EFTKHQVLIM TCYVALNVLK NGYLSLSDIN LLVFDECHLA 180
ILDHPYREIM KLCENCPSCP RILGLTASIL NGKCDPEELE EKIQKLEKIL KSNAETATDL 240
VVLDRYTSQP CEIVVDCGPF TDRSGLYERL LMELEEALNF INDCNISVHS KERDSTLISK 300
QILSDCRAVL VVLGPWCADK VAGMMVRELQ KYIKHEQEEL HRKFLLFTDT FLRKIHALCE 360
EHFSPASLDL KFVTPKVIKL LEILRKYKPY ERQQFESVEW YNNRNQDNYV SWSDSEDDDE 420
DEEIEEKEKP ETNFPSPFTN ILCGIIFVER RYTAVVLNRL IKEAGKQDPE LAYISSNFIT 480
GHGIGKNQPR NKQMEAEFRK QEEVLRKFRA HETNLLIATS IVEEGVDIPK CNLVVRFDLP 540
TEYRSYVQSK GRARAPISNY IMLADTDKIK SFEEDLKTYK AIEKILRNKC SKSVDTGETD 600
IDPVMDDDDV FPPYVLRPDD GGPRVTINTA IGHINRYCAR LPSDPFTHLA PKCRTRELPD 660
GTFYSTLYLP INSPLRASIV GPPMSCVRLA ERVVALICCE KLHKIGELDD HLMPVGKETV 720
KYEEELDLHD EEETSVPGRP GSTKRRQCYP KAIPECLRDS YPRPDQPCYL YVIGMVLTTP 780
LPDELNFRRR KLYPPEDTTR CFGILTAKPI PQIPHFPVYT RSGEVTISIE LKKSGFMLSL 840
QMLELITRLH QYIFSHILRL EKPALEFKPT DADSAYCVLP LNVVNDSSTL DIDFKFMEDI 900
EKSEARIGIP STKYTKETPF VFKLEDYQDA VIIPRYRNFD QPHRFYVADV YTDLTPLSKF 960
PSPEYETFAE YYKTKYNLDL TNLNQPLLDV DHTSSRLNLL TPRHLNQKGK ALPLSSAEKR 1020
KAKWESLQNK QILVPELCAI HPIPASLWRK AVCLPSILYR LHCLLTAEEL RAQTASDAGV 1080
GVRSLPADFR YPNLDFGWKK SIDSKSFISI SNSSSAENDN YCKHSTIVPE NAAHQGANRT 1140
SSLENHDQMS VNCRTLLSES PGKLHVEVSA DLTAINGLSY NQNLANGSYD LANRDFCQGN 1200
QLNYYKQEIP VQPTTSYSIQ NLYSYENQPQ PSDECTLLSN KYLDGNANKS TSDGSPVMAV 1260
MPGTTDTIQV LKGRMDSEQS PSIGYSSRTL GPNPGLILQA LTLSNASDGF NLERLEMLGD 1320
SFLKHAITTY LFCTYPDAHE GRLSYMRSKK VSNCNLYRLG KKKGLPSRMV VSIFDPPVNW 1380
LPPGYVVNQD KSNTDKWEKD EMTKDCMLAN GKLDEDYEEE DEEEESLMWR APKEEADYED 1440
DFLEYDQEHI RFIDNMLMGS GAFVKKISLS PFSTTDSAYE WKMPKKSSLG SMPFSSDFED 1500
FDYSSWDAMC YLDPSKAVEE DDFVVGFWNP SEENCGVDTG KQSISYDLHT EQCIADKSIA 1560
DCVEALLGCY LTSCGERAAQ LFLCSLGLKV LPVIKRTDRE KALCPTRENF NSQQKNLSVS 1620
CAAASVASSR SSVLKDSEYG CLKIPPRCMF DHPDADKTLN HLISGFENFE KKINYRFKNK 1680
AYLLQAFTHA SYHYNTITDC YQRLEFLGDA ILDYLITKHL YEDPRQHSPG VLTDLRSALV 1740
NNTIFASLAV KYDYHKYFKA VSPELFHVID DFVQFQLEKN EMQGMDSELR RSEEDEEKEE 1800
DIEVPKAMGD IFESLAGAIY MDSGMSLETV WQVYYPMMRP LIEKFSANVP RSPVRELLEM 1860
EPETAKFSPA ERTYDGKVRV TVEVVGKGKF KGVGRSYRIA KSAAARRALR SLKANQPQVP 1920
NS 1922 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016442; C:RNA-induced silencing complex; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
 GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0035198; F:miRNA binding; IEA:Compara.
 GO:0004525; F:ribonuclease III activity; IDA:UniProtKB.
 GO:0001525; P:angiogenesis; IEA:Compara.
 GO:0006915; P:apoptotic process; IEA:Compara.
 GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Compara.
 GO:0055013; P:cardiac muscle cell development; IEA:Compara.
 GO:0021987; P:cerebral cortex development; IEA:Compara.
 GO:0051607; P:defense response to virus; IEA:Compara.
 GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Compara.
 GO:0071335; P:hair follicle cell proliferation; IEA:Compara.
 GO:0031069; P:hair follicle morphogenesis; IEA:Compara.
 GO:0060119; P:inner ear receptor cell development; IEA:Compara.
 GO:0060576; P:intestinal epithelial cell development; IEA:Compara.
 GO:0030324; P:lung development; IEA:Compara.
 GO:0035264; P:multicellular organism growth; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0010626; P:negative regulation of Schwann cell proliferation; ISS:BHF-UCL.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
 GO:0021675; P:nerve development; ISS:BHF-UCL.
 GO:0048812; P:neuron projection morphogenesis; ISS:BHF-UCL.
 GO:0021889; P:olfactory bulb interneuron differentiation; IEA:Compara.
 GO:0032290; P:peripheral nervous system myelin formation; ISS:BHF-UCL.
 GO:2000630; P:positive regulation of miRNA metabolic process; IEA:Compara.
 GO:0031643; P:positive regulation of myelination; ISS:BHF-UCL.
 GO:0014040; P:positive regulation of Schwann cell differentiation; ISS:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0009791; P:post-embryonic development; IEA:Compara.
 GO:0031054; P:pre-miRNA processing; IDA:UniProtKB.
 GO:0030422; P:production of siRNA involved in RNA interference; IDA:UniProtKB.
 GO:0051726; P:regulation of cell cycle; IEA:Compara.
 GO:0070173; P:regulation of enamel mineralization; IEA:Compara.
 GO:0045664; P:regulation of neuron differentiation; IEA:Compara.
 GO:0048713; P:regulation of oligodendrocyte differentiation; IEA:Compara.
 GO:0045069; P:regulation of viral genome replication; IEA:Compara.
 GO:0021522; P:spinal cord motor neuron differentiation; IEA:Compara.
 GO:0051225; P:spindle assembly; IEA:Compara.
 GO:0048536; P:spleen development; IEA:Compara.
 GO:0019827; P:stem cell maintenance; IEA:Compara.
 GO:0030423; P:targeting of mRNA for destruction involved in RNA interference; IMP:UniProtKB.
 GO:0010070; P:zygote asymmetric cell division; IEA:Compara. 
Interpro
 IPR005034; Dicer_dsRNA_binding_fold.
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR001159; Ds-RNA-bd.
 IPR014720; dsRNA-bd-like_dom.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR003100; PAZ.
 IPR000999; RNase_III_dom. 
Pfam
 PF00270; DEAD
 PF03368; dsRNA_bind
 PF00271; Helicase_C
 PF02170; PAZ
 PF00636; Ribonuclease_3 
SMART
 SM00487; DEXDc
 SM00358; DSRM
 SM00490; HELICc
 SM00949; PAZ
 SM00535; RIBOc 
PROSITE
 PS51327; DICER_DSRBF
 PS50137; DS_RBD
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS50821; PAZ
 PS00517; RNASE_3_1
 PS50142; RNASE_3_2 
PRINTS