CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024447
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CCR4-NOT transcription complex subunit 1 
Protein Synonyms/Alias
 CCR4-associated factor 1; Negative regulator of transcription subunit 1 homolog; NOT1H; hNOT1 
Gene Name
 CNOT1 
Gene Synonyms/Alias
 CDC39; KIAA1007; NOT1; AD-005 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
231APLLYPEKRDILMDRubiquitination[1]
355LNPSLNFKEVTYELDubiquitination[1]
372GFQIRDSKGLHNVVYubiquitination[1]
556GEQYDQAKLSRILDVubiquitination[1, 2, 3]
808NDPFVQRKLGTSGLNubiquitination[1, 2, 4]
1163LKNPEFNKMVLNETYubiquitination[5, 6]
1426TCEQIVRKDFALDSEubiquitination[1, 2]
1514IQKTAVEKAGPEMDKacetylation[4]
1514IQKTAVEKAGPEMDKubiquitination[1]
1560MPEQIRLKVGGVDPKubiquitination[1]
1567KVGGVDPKQLAVYEEubiquitination[1, 2, 4]
1600GFLAQPMKQAWATDDubiquitination[2]
1708YGSPWCNKQITRCLIubiquitination[1, 4, 7]
1851DPPGLREKAEYLLREubiquitination[1]
1959EATNTVTKINLLNKVubiquitination[2]
2086LRNVELTKPMQILYKubiquitination[5, 6]
2151DPFTPNLKVDMLSEIubiquitination[2, 3, 8]
2178VMPPQFKKDLDSYLKubiquitination[1]
2185KDLDSYLKTRSPVTFubiquitination[1, 2, 3, 4]
2364AQCCMGQKQAQQVMEubiquitination[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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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] 
Functional Description
 Scaffolding component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA- mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Its scaffolding function implies its interaction with the catalytic complex module and diverse RNA-binding proteins mediating the complex recruitment to selected mRNA 3'UTRs. Involved in degradation of AU-rich element (ARE)-containing mRNAs probably via association with ZFP36. Mediates the recruitment of the CCR4-NOT complex to miRNA targets and to the RISC complex via association with TNRC6A, TNRC6B or TNRC6C. Acts as a transcriptional repressor. Represses the ligand-dependent transcriptional activation by nuclear receptors. Involved in the maintenance of emryonic stem (ES) cell identity. 
Sequence Annotation
 REGION 1090 1605 Interaction with CNOT6, CNOT6L, CNOT7 and
 MOTIF 153 157 LXXLL.
 MOTIF 181 185 LXXLL.
 MOTIF 223 227 LXXLL.
 MOTIF 570 574 LXXLL.
 MOTIF 1639 1643 LXXLL.
 MOTIF 1942 1946 LXXLL.
 MOTIF 2096 2100 LXXLL.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Developmental protein; Nucleus; Polymorphism; Reference proteome; Repressor; RNA-mediated gene silencing; Transcription; Transcription regulation; Translation regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2376 AA 
Protein Sequence
MNLDSLSLAL SQISYLVDNL TKKNYRASQQ EIQHIVNRHG PEADRHLLRC LFSHVDFSGD 60
GKSSGKDFHQ TQFLIQECAL LITKPNFIST LSYAIDNPLH YQKSLKPAPH LFAQLSKVLK 120
LSKVQEVIFG LALLNSSSSD LRGFAAQFIK QKLPDLLRSY IDADVSGNQE GGFQDIAIEV 180
LHLLLSHLLF GQKGAFGVGQ EQIDAFLKTL RRDFPQERCP VVLAPLLYPE KRDILMDRIL 240
PDSGGVAKTM MESSLADFMQ EVGYGFCASI EECRNIIVQF GVREVTAAQV ARVLGMMART 300
HSGLTDGIPL QSISAPGSGI WSDGKDKSDG AQAHTWNVEV LIDVLKELNP SLNFKEVTYE 360
LDHPGFQIRD SKGLHNVVYG IQRGLGMEVF PVDLIYRPWK HAEGQLSFIQ HSLINPEIFC 420
FADYPCHTVA TDILKAPPED DNREIATWKS LDLIESLLRL AEVGQYEQVK QLFSFPIKHC 480
PDMLVLALLQ INTSWHTLRH ELISTLMPIF LGNHPNSAII LHYAWHGQGQ SPSIRQLIMH 540
AMAEWYMRGE QYDQAKLSRI LDVAQDLKAL SMLLNGTPFA FVIDLAALAS RREYLKLDKW 600
LTDKIREHGE PFIQACMTFL KRRCPSILGG LAPEKDQPKS AQLPPETLAT MLACLQACAG 660
SVSQELSETI LTMVANCSNV MNKARQPPPG VMPKGRPPSA SSLDAISPVQ IDPLAGMTSL 720
SIGGSAAPHT QSMQGFPPNL GSAFSTPQSP AKAFPPLSTP NQTTAFSGIG GLSSQLPVGG 780
LGTGSLTGIG TGALGLPAVN NDPFVQRKLG TSGLNQPTFQ QSKMKPSDLS QVWPEANQHF 840
SKEIDDEANS YFQRIYNHPP HPTMSVDEVL EMLQRFKDST IKREREVFNC MLRNLFEEYR 900
FFPQYPDKEL HITACLFGGI IEKGLVTYMA LGLALRYVLE ALRKPFGSKM YYFGIAALDR 960
FKNRLKDYPQ YCQHLASISH FMQFPHHLQE YIEYGQQSRD PPVKMQGSIT TPGSIALAQA 1020
QAQAQVPAKA PLAGQVSTMV TTSTTTTVAK TVTVTRPTGV SFKKDVPPSI NTTNIDTLLV 1080
ATDQTERIVE PPENIQEKIA FIFNNLSQSN MTQKVEELKE TVKEEFMPWV SQYLVMKRVS 1140
IEPNFHSLYS NFLDTLKNPE FNKMVLNETY RNIKVLLTSD KAAANFSDRS LLKNLGHWLG 1200
MITLAKNKPI LHTDLDVKSL LLEAYVKGQQ ELLYVVPFVA KVLESSIRSV VFRPPNPWTM 1260
AIMNVLAELH QEHDLKLNLK FEIEVLCKNL ALDINELKPG NLLKDKDRLK NLDEQLSAPK 1320
KDVKQPEELP PITTTTTSTT PATNTTCTAT VPPQPQYSYH DINVYSLAGL APHITLNPTI 1380
PLFQAHPQLK QCVRQAIERA VQELVHPVVD RSIKIAMTTC EQIVRKDFAL DSEESRMRIA 1440
AHHMMRNLTA GMAMITCREP LLMSISTNLK NSFASALRTA SPQQREMMDQ AAAQLAQDNC 1500
ELACCFIQKT AVEKAGPEMD KRLATEFELR KHARQEGRRY CDPVVLTYQA ERMPEQIRLK 1560
VGGVDPKQLA VYEEFARNVP GFLPTNDLSQ PTGFLAQPMK QAWATDDVAQ IYDKCITELE 1620
QHLHAIPPTL AMNPQAQALR SLLEVVVLSR NSRDAIAALG LLQKAVEGLL DATSGADADL 1680
LLRYRECHLL VLKALQDGRA YGSPWCNKQI TRCLIECRDE YKYNVEAVEL LIRNHLVNMQ 1740
QYDLHLAQSM ENGLNYMAVA FAMQLVKILL VDERSVAHVT EADLFHTIET LMRINAHSRG 1800
NAPEGLPQLM EVVRSNYEAM IDRAHGGPNF MMHSGISQAS EYDDPPGLRE KAEYLLREWV 1860
NLYHSAAAGR DSTKAFSAFV GQMHQQGILK TDDLITRFFR LCTEMCVEIS YRAQAEQQHN 1920
PAANPTMIRA KCYHNLDAFV RLIALLVKHS GEATNTVTKI NLLNKVLGIV VGVLLQDHDV 1980
RQSEFQQLPY HRIFIMLLLE LNAPEHVLET INFQTLTAFC NTFHILRPTK APGFVYAWLE 2040
LISHRIFIAR MLAHTPQQKG WPMYAQLLID LFKYLAPFLR NVELTKPMQI LYKGTLRVLL 2100
VLLHDFPEFL CDYHYGFCDV IPPNCIQLRN LILSAFPRNM RLPDPFTPNL KVDMLSEINI 2160
APRILTNFTG VMPPQFKKDL DSYLKTRSPV TFLSDLRSNL QVSNEPGNRY NLQLINALVL 2220
YVGTQAIAHI HNKGSTPSMS TITHSAHMDI FQNLAVDLDT EGRYLFLNAI ANQLRYPNSH 2280
THYFSCTMLY LFAEANTEAI QEQITRVLLE RLIVNRPHPW GLLITFIELI KNPAFKFWNH 2340
EFVHCAPEIE KLFQSVAQCC MGQKQAQQVM EGTGAS 2376 
Gene Ontology
 GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB.
 GO:0000932; C:cytoplasmic mRNA processing body; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
 GO:0030331; F:estrogen receptor binding; IDA:UniProtKB.
 GO:0042974; F:retinoic acid receptor binding; IDA:UniProtKB.
 GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
 GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
 GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
 GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
 GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IDA:UniProtKB.
 GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IMP:UniProtKB.
 GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; IMP:UniProtKB.
 GO:2000036; P:regulation of stem cell maintenance; IMP:UniProtKB.
 GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR007196; CCR4-Not_Not1_C.
 IPR024557; CCR4-Not_Not1su_DUF3819. 
Pfam
 PF12842; DUF3819
 PF04054; Not1 
SMART
  
PROSITE
  
PRINTS