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Protein

CCR4-NOT transcription complex subunit 7

Gene

CNOT7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT8. Catalytic 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. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression. Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti-proliferative activity.4 Publications

Catalytic activityi

Exonucleolytic cleavage of poly(A) to 5'-AMP.3 Publications

Cofactori

Mn2+1 Publication, Mg2+1 Publication, Co2+1 PublicationNote: Binds 2 divalent metal cations per subunit with RNAase activity being higher in presence of Mn2+ than of Mg2+ or Co2+.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Divalent metal cation 1; catalyticCurated
Metal bindingi40 – 401Divalent metal cation 2; catalyticCurated
Metal bindingi42 – 421Divalent metal cation 2; catalyticCurated
Metal bindingi161 – 1611Divalent metal cation 1; catalyticCurated
Metal bindingi230 – 2301Divalent metal cation 2; catalyticCurated
Metal bindingi278 – 2781Divalent metal cation 1; catalyticCurated

GO - Molecular functioni

  • 3'-5'-exoribonuclease activity Source: UniProtKB
  • exoribonuclease activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • poly(A)-specific ribonuclease activity Source: UniProtKB
  • RNA binding Source: UniProtKB-KW
  • signal transducer activity Source: ProtInc
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc

GO - Biological processi

  • carbohydrate metabolic process Source: ProtInc
  • cytoplasmic mRNA processing body assembly Source: Ensembl
  • deadenylation-dependent decapping of nuclear-transcribed mRNA Source: Ensembl
  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  • exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: UniProtKB
  • gene silencing by miRNA Source: UniProtKB
  • gene silencing by RNA Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of gene expression Source: BHF-UCL
  • nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of mRNA catabolic process Source: BHF-UCL
  • positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
  • positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • signal transduction Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease, Repressor

Keywords - Biological processi

RNA-mediated gene silencing, Transcription, Transcription regulation, Translation regulation

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-429947. Deadenylation of mRNA.
R-HSA-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.

Names & Taxonomyi

Protein namesi
Recommended name:
CCR4-NOT transcription complex subunit 7 (EC:3.1.13.4)
Alternative name(s):
BTG1-binding factor 1
CCR4-associated factor 1
Short name:
CAF-1
Caf1a
Gene namesi
Name:CNOT7
Synonyms:CAF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:14101. CNOT7.

Subcellular locationi

GO - Cellular componenti

  • CCR4-NOT complex Source: UniProtKB
  • cytoplasmic mRNA processing body Source: UniProtKB
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401D → N: Abolishes RNA deadenylase activity. 1 Publication
Mutagenesisi42 – 421E → Q: Abolishes RNA deadenylase activity. 1 Publication
Mutagenesisi138 – 1381E → K: Abolishes interaction with CNOT1; when associated with Y-142 and K-149. 1 Publication
Mutagenesisi141 – 1411M → R: Abolishes interaction with CNOT1. 1 Publication
Mutagenesisi142 – 1421T → Y: Abolishes interaction with CNOT1; when associated with K-138 and K-149. 1 Publication
Mutagenesisi149 – 1491E → K: Abolishes interaction with CNOT1; when associated with K-138 and Y-142. 1 Publication
Mutagenesisi161 – 1611D → N: Abolishes RNA deadenylase activity. 1 Publication
Mutagenesisi203 – 2031K → A: Abolishes interaction with TOB1.
Mutagenesisi225 – 2251H → A: Abolishes RNA deadenylase activity. 1 Publication
Mutagenesisi230 – 2301D → N: Abolishes RNA deadenylase activity. 1 Publication

Organism-specific databases

PharmGKBiPA26678.

Polymorphism and mutation databases

BioMutaiCNOT7.
DMDMi41713629.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285CCR4-NOT transcription complex subunit 7PRO_0000212844Add
BLAST

Proteomic databases

EPDiQ9UIV1.
MaxQBiQ9UIV1.
PaxDbiQ9UIV1.
PeptideAtlasiQ9UIV1.
PRIDEiQ9UIV1.

PTM databases

iPTMnetiQ9UIV1.
PhosphoSiteiQ9UIV1.

Expressioni

Gene expression databases

BgeeiENSG00000198791.
CleanExiHS_CNOT7.
ExpressionAtlasiQ9UIV1. baseline and differential.
GenevisibleiQ9UIV1. HS.

Organism-specific databases

HPAiHPA069543.

Interactioni

Subunit structurei

Component of the CCR4-NOT complex; distinct complexes seem to exist that differ in the participation of probably mutually exclusive catalytic subunits; the complex contains two deadenylase subunits, CNOT6 or CNOT6L, and CNOT7 or CNOT8. In the complex, interacts directly with CNOT1. Interacts with AGO2, TOB1, BTG1, BTG2 and NANOS2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGO2Q9UKV82EBI-2105113,EBI-528269
BTG1P623244EBI-2105113,EBI-742279
BTG2P785435EBI-2105113,EBI-1047576
CNOT1A5YKK67EBI-2105113,EBI-1222758
CNOT6Q9ULM62EBI-2105113,EBI-2104530
TOB1P506166EBI-2105113,EBI-723281
TOB2Q141063EBI-2105113,EBI-2562000
Zfp36P228933EBI-2105113,EBI-647803From a different organism.

Protein-protein interaction databases

BioGridi118938. 51 interactions.
DIPiDIP-41902N.
IntActiQ9UIV1. 29 interactions.
MINTiMINT-155676.
STRINGi9606.ENSP00000355279.

Structurei

Secondary structure

1
285
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 154Combined sources
Helixi17 – 193Combined sources
Helixi20 – 3314Combined sources
Beta strandi36 – 427Combined sources
Helixi57 – 6913Combined sources
Beta strandi76 – 827Combined sources
Beta strandi94 – 996Combined sources
Turni103 – 1053Combined sources
Helixi110 – 11910Combined sources
Helixi123 – 1297Combined sources
Helixi133 – 1419Combined sources
Turni142 – 1443Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi152 – 1576Combined sources
Helixi159 – 17012Combined sources
Helixi178 – 18811Combined sources
Beta strandi192 – 1943Combined sources
Helixi195 – 1984Combined sources
Helixi199 – 2013Combined sources
Helixi209 – 2168Combined sources
Helixi227 – 24418Combined sources
Helixi252 – 2554Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D5RX-ray2.50A11-262[»]
4GMJX-ray2.70B/D/F1-285[»]
ProteinModelPortaliQ9UIV1.
SMRiQ9UIV1. Positions 11-262.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UIV1.

Family & Domainsi

Sequence similaritiesi

Belongs to the CAF1 family.Curated

Phylogenomic databases

eggNOGiKOG0304. Eukaryota.
COG5228. LUCA.
GeneTreeiENSGT00390000000080.
HOGENOMiHOG000173077.
HOVERGENiHBG051044.
InParanoidiQ9UIV1.
KOiK12581.
OMAiGIRDVWG.
OrthoDBiEOG091G0M48.
PhylomeDBiQ9UIV1.
TreeFamiTF314185.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR006941. RNase_CAF1.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF04857. CAF1. 2 hits.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UIV1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPAATVDHSQ RICEVWACNL DEEMKKIRQV IRKYNYVAMD TEFPGVVARP
60 70 80 90 100
IGEFRSNADY QYQLLRCNVD LLKIIQLGLT FMNEQGEYPP GTSTWQFNFK
110 120 130 140 150
FNLTEDMYAQ DSIELLTTSG IQFKKHEEEG IETQYFAELL MTSGVVLCEG
160 170 180 190 200
VKWLSFHSGY DFGYLIKILT NSNLPEEELD FFEILRLFFP VIYDVKYLMK
210 220 230 240 250
SCKNLKGGLQ EVAEQLELER IGPQHQAGSD SLLTGMAFFK MREMFFEDHI
260 270 280
DDAKYCGHLY GLGSGSSYVQ NGTGNAYEEE ANKQS
Length:285
Mass (Da):32,745
Last modified:February 2, 2004 - v3
Checksum:i2AF23ED27E06EFDB
GO
Isoform 2 (identifier: Q9UIV1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     244-285: MFFEDHIDDAKYCGHLYGLGSGSSYVQNGTGNAYEEEANKQS → V

Note: No experimental confirmation available.
Show »
Length:244
Mass (Da):28,228
Checksum:i1ECD7111D60414F2
GO

Sequence cautioni

The sequence AAF01500 differs from that shown. Reason: Frameshift at position 4. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 52AT → EL in AAP97145 (PubMed:14702039).Curated
Sequence conflicti241 – 2411M → V in BAG51197 (PubMed:16421571).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei244 – 28542MFFED…ANKQS → V in isoform 2. 1 PublicationVSP_045497Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L46722 mRNA. Translation: AAF01500.1. Frameshift.
AF086915 mRNA. Translation: AAP97145.1.
AK021808 mRNA. Translation: BAG51053.1.
AK023466 mRNA. Translation: BAG51197.1.
AC091050 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63820.1.
CH471080 Genomic DNA. Translation: EAW63821.1.
CH471080 Genomic DNA. Translation: EAW63822.1.
CH471080 Genomic DNA. Translation: EAW63823.1.
BC060852 mRNA. Translation: AAH60852.1.
BC070187 mRNA. Translation: AAH70187.1.
CCDSiCCDS55202.1. [Q9UIV1-2]
CCDS6000.2. [Q9UIV1-1]
RefSeqiNP_001309016.1. NM_001322087.1. [Q9UIV1-2]
NP_001309017.1. NM_001322088.1. [Q9UIV1-2]
NP_001309018.1. NM_001322089.1. [Q9UIV1-2]
NP_001309019.1. NM_001322090.1. [Q9UIV1-1]
NP_001309020.1. NM_001322091.1. [Q9UIV1-1]
NP_001309021.1. NM_001322092.1. [Q9UIV1-1]
NP_001309022.1. NM_001322093.1.
NP_001309023.1. NM_001322094.1.
NP_001309024.1. NM_001322095.1.
NP_001309025.1. NM_001322096.1.
NP_001309026.1. NM_001322097.1.
NP_001309027.1. NM_001322098.1.
NP_001309028.1. NM_001322099.1.
NP_001309029.1. NM_001322100.1.
NP_037486.2. NM_013354.6. [Q9UIV1-1]
NP_473367.2. NM_054026.3. [Q9UIV1-2]
XP_005273538.1. XM_005273481.2. [Q9UIV1-1]
UniGeneiHs.587465.
Hs.645009.
Hs.729775.

Genome annotation databases

EnsembliENST00000361272; ENSP00000355279; ENSG00000198791. [Q9UIV1-1]
ENST00000523917; ENSP00000429093; ENSG00000198791. [Q9UIV1-2]
GeneIDi29883.
KEGGihsa:29883.
UCSCiuc003wxg.2. human. [Q9UIV1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L46722 mRNA. Translation: AAF01500.1. Frameshift.
AF086915 mRNA. Translation: AAP97145.1.
AK021808 mRNA. Translation: BAG51053.1.
AK023466 mRNA. Translation: BAG51197.1.
AC091050 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63820.1.
CH471080 Genomic DNA. Translation: EAW63821.1.
CH471080 Genomic DNA. Translation: EAW63822.1.
CH471080 Genomic DNA. Translation: EAW63823.1.
BC060852 mRNA. Translation: AAH60852.1.
BC070187 mRNA. Translation: AAH70187.1.
CCDSiCCDS55202.1. [Q9UIV1-2]
CCDS6000.2. [Q9UIV1-1]
RefSeqiNP_001309016.1. NM_001322087.1. [Q9UIV1-2]
NP_001309017.1. NM_001322088.1. [Q9UIV1-2]
NP_001309018.1. NM_001322089.1. [Q9UIV1-2]
NP_001309019.1. NM_001322090.1. [Q9UIV1-1]
NP_001309020.1. NM_001322091.1. [Q9UIV1-1]
NP_001309021.1. NM_001322092.1. [Q9UIV1-1]
NP_001309022.1. NM_001322093.1.
NP_001309023.1. NM_001322094.1.
NP_001309024.1. NM_001322095.1.
NP_001309025.1. NM_001322096.1.
NP_001309026.1. NM_001322097.1.
NP_001309027.1. NM_001322098.1.
NP_001309028.1. NM_001322099.1.
NP_001309029.1. NM_001322100.1.
NP_037486.2. NM_013354.6. [Q9UIV1-1]
NP_473367.2. NM_054026.3. [Q9UIV1-2]
XP_005273538.1. XM_005273481.2. [Q9UIV1-1]
UniGeneiHs.587465.
Hs.645009.
Hs.729775.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D5RX-ray2.50A11-262[»]
4GMJX-ray2.70B/D/F1-285[»]
ProteinModelPortaliQ9UIV1.
SMRiQ9UIV1. Positions 11-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118938. 51 interactions.
DIPiDIP-41902N.
IntActiQ9UIV1. 29 interactions.
MINTiMINT-155676.
STRINGi9606.ENSP00000355279.

PTM databases

iPTMnetiQ9UIV1.
PhosphoSiteiQ9UIV1.

Polymorphism and mutation databases

BioMutaiCNOT7.
DMDMi41713629.

Proteomic databases

EPDiQ9UIV1.
MaxQBiQ9UIV1.
PaxDbiQ9UIV1.
PeptideAtlasiQ9UIV1.
PRIDEiQ9UIV1.

Protocols and materials databases

DNASUi29883.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361272; ENSP00000355279; ENSG00000198791. [Q9UIV1-1]
ENST00000523917; ENSP00000429093; ENSG00000198791. [Q9UIV1-2]
GeneIDi29883.
KEGGihsa:29883.
UCSCiuc003wxg.2. human. [Q9UIV1-1]

Organism-specific databases

CTDi29883.
GeneCardsiCNOT7.
HGNCiHGNC:14101. CNOT7.
HPAiHPA069543.
MIMi604913. gene.
neXtProtiNX_Q9UIV1.
PharmGKBiPA26678.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0304. Eukaryota.
COG5228. LUCA.
GeneTreeiENSGT00390000000080.
HOGENOMiHOG000173077.
HOVERGENiHBG051044.
InParanoidiQ9UIV1.
KOiK12581.
OMAiGIRDVWG.
OrthoDBiEOG091G0M48.
PhylomeDBiQ9UIV1.
TreeFamiTF314185.

Enzyme and pathway databases

ReactomeiR-HSA-429947. Deadenylation of mRNA.
R-HSA-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.

Miscellaneous databases

ChiTaRSiCNOT7. human.
EvolutionaryTraceiQ9UIV1.
GeneWikiiCNOT7.
GenomeRNAii29883.
PROiQ9UIV1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198791.
CleanExiHS_CNOT7.
ExpressionAtlasiQ9UIV1. baseline and differential.
GenevisibleiQ9UIV1. HS.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR006941. RNase_CAF1.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF04857. CAF1. 2 hits.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCNOT7_HUMAN
AccessioniPrimary (citable) accession number: Q9UIV1
Secondary accession number(s): A8MZM5
, B3KMP1, B3KN35, D3DSP6, G3V108, Q7Z530
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: February 2, 2004
Last modified: September 7, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.