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9  structures 551  species 0  interactions 834  sequences 46  architectures

Family: Not1 (PF04054)

Summary: CCR4-Not complex component, Not1

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This is the Wikipedia entry entitled "CNOT1". More...

CNOT1 Edit Wikipedia article

CCR4-NOT transcription complex, subunit 1
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols CNOT1 ; AD-005; CDC39; NOT1; NOT1H
External IDs OMIM604917 MGI2442402 HomoloGene9453 GeneCards: CNOT1 Gene
RNA expression pattern
PBB GE CNOT1 200860 s at tn.png
PBB GE CNOT1 200861 at tn.png
More reference expression data
Species Human Mouse
Entrez 23019 234594
Ensembl ENSG00000125107 ENSMUSG00000036550
UniProt A5YKK6 Q6ZQ08
RefSeq (mRNA) NM_001265612 NM_001205226
RefSeq (protein) NP_001252541 NP_001192155
Location (UCSC) Chr 16:
58.52 – 58.63 Mb
Chr 8:
95.72 – 95.81 Mb
PubMed search [1] [2]
CCR4-Not complex component, Not1
Symbol Not1
Pfam PF04054
InterPro IPR007196

CCR4-NOT transcription complex subunit 1 is a protein that in humans is encoded by the CNOT1 gene.[1][2]

It is a part of the Ccr4-Not complex, which deadenylates mRNAs.[3] CNOT1 acts as a scaffold protein, binding other subunits of the complex.[4][5][6]


CNOT1 has been shown to interact with CNOT8.[7][8]


  1. ^ Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, et al. (December 2003). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.  Check date values in: |year= / |date= mismatch (help)
  2. ^ "Entrez Gene: CNOT1 CCR4-NOT transcription complex, subunit 1". 
  3. ^ Garneau NL, Wilusz J, Wilusz CJ (Feb 2007). "The highways and byways of mRNA decay". Nat. Rev. Mol. Cell Biol. 8 (2): 113–26. doi:10.1038/nrm2104. PMID 17245413. 
  4. ^ Sandler H, Kreth J, Timmers HT, Stoecklin G (May 2011). "Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin". Nucleic Acids Res. 39 (10): 4373–86. doi:10.1093/nar/gkr011. PMC 3105394. PMID 21278420. 
  5. ^ Petit AP, Wohlbold L, Bawankar P, Huntzinger E, Schmidt S, Izaurralde E, et al. (Nov 2012). "The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4-NOT deadenylase complex". Nucleic Acids Res. 40 (21): 11058–72. doi:10.1093/nar/gks883. PMC 3510486. PMID 22977175. 
  6. ^ Basquin J, Roudko VV, Rode M, Basquin C, Séraphin B, Conti E (Oct 26, 2012). "Architecture of the nuclease module of the yeast Ccr4-not complex: the Not1-Caf1-Ccr4 interaction". Mol. Cell 48 (2): 207–18. doi:10.1016/j.molcel.2012.08.014. PMID 22959269. 
  7. ^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. 
  8. ^ Albert TK, Lemaire M, van Berkum NL, Gentz R, Collart MA, Timmers HT (February 2000). "Isolation and characterization of human orthologs of yeast CCR4-NOT complex subunits". Nucleic Acids Res. 28 (3): 809–17. doi:10.1093/nar/28.3.809. PMC 102560. PMID 10637334. 

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Further reading

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

CCR4-Not complex component, Not1 Provide feedback

The Ccr4-Not complex is a global regulator of transcription that affects genes positively and negatively and is thought to regulate transcription factor TFIID [1].

Literature references

  1. Maillet L, Collart MA; , J Biol Chem 2002;277:2835-2842.: Interaction between Not1p, a component of the Ccr4-not complex, a global regulator of transcription, and Dhh1p, a putative RNA helicase. PUBMED:11696541 EPMC:11696541

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR007196

The Ccr4-Not complex is a global regulator of gene expression that is conserved from yeast to human. It affects genes positively and negatively and is thought to regulate transcription factor IID function. In Saccharomyces cerevisiae, it exists in two prominent forms and consists of at least nine core subunits: the five Not proteins (Not1p to Not5p), Caf1p, Caf40p, Caf130p and Ccr4p [PUBMED:10637334]. The Ccr4-Not complex regulates many different cellular functions, including RNA degradation and transcription initiation. It may be a regulatory platform that senses nutrient levels and stress [PUBMED:12957374]. Caf1p and Ccr4p, are directly involved in mRNA deadenylation, and Caf1p is associated with Dhh1p, a putative RNA helicase thought to be a component of the decapping complex [PUBMED:11696541]. Pop2, a component of the Ccr4-Not complex, functions as a deadenylase [PUBMED:18430587].

The Ccr4-Not complex is a global regulator of transcription that affects genes positively and negatively and is thought to regulate transcription factor TFIID [PUBMED:11696541].

Domain organisation

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Seed source: Pfam-B_13503 (release 7.3);
Previous IDs: none
Type: Family
Author: Wood V, Finn RD
Number in seed: 114
Number in full: 834
Average length of the domain: 319.90 aa
Average identity of full alignment: 37 %
Average coverage of the sequence by the domain: 17.00 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.7 22.7
Trusted cut-off 25.6 23.6
Noise cut-off 21.7 21.4
Model length: 367
Family (HMM) version: 11
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Species distribution

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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Not1 domain has been found. There are 9 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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