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A5YKK6

- CNOT1_HUMAN

UniProt

A5YKK6 - CNOT1_HUMAN

Protein

CCR4-NOT transcription complex subunit 1

Gene

CNOT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    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.7 Publications

    GO - Molecular functioni

    1. estrogen receptor binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. retinoic acid receptor binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. gene silencing by RNA Source: UniProtKB-KW
    3. mRNA metabolic process Source: Reactome
    4. multicellular organismal development Source: UniProtKB-KW
    5. negative regulation of intracellular estrogen receptor signaling pathway Source: UniProtKB
    6. negative regulation of retinoic acid receptor signaling pathway Source: UniProtKB
    7. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    8. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    9. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
    10. positive regulation of cytoplasmic mRNA processing body assembly Source: UniProtKB
    11. positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
    12. positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: UniProtKB
    13. regulation of stem cell maintenance Source: UniProtKB
    14. regulation of translation Source: UniProtKB-KW
    15. RNA metabolic process Source: Reactome
    16. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
    17. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Repressor

    Keywords - Biological processi

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

    Enzyme and pathway databases

    ReactomeiREACT_20514. Deadenylation of mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CCR4-NOT transcription complex subunit 1
    Alternative name(s):
    CCR4-associated factor 1
    Negative regulator of transcription subunit 1 homolog
    Short name:
    NOT1H
    Short name:
    hNOT1
    Gene namesi
    Name:CNOT1
    Synonyms:CDC39, KIAA1007, NOT1
    ORF Names:AD-005
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:7877. CNOT1.

    Subcellular locationi

    CytoplasmP-body 1 Publication. Nucleus 1 Publication
    Note: NANOS2 promotes its localization to P-body.By similarity

    GO - Cellular componenti

    1. CCR4-NOT complex Source: UniProtKB
    2. cytoplasmic mRNA processing body Source: UniProtKB
    3. cytosol Source: Reactome
    4. extracellular space Source: UniProt
    5. membrane Source: UniProtKB
    6. nucleus Source: HPA
    7. peroxisomal membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1208 – 12081K → E: Impairs interaction with CNOT7; when associated with Y-1212 and E-1218. 1 Publication
    Mutagenesisi1209 – 12091P → Y: Abolishes interaction with CNOT7; when associated with Y-1257.
    Mutagenesisi1212 – 12121H → Y: Impairs interaction with CNOT7; when associated with E-1208 and E-1218. 1 Publication
    Mutagenesisi1218 – 12181K → E: Impairs interaction with CNOT7; when associated with E-1208 and Y-1212. 1 Publication
    Mutagenesisi1251 – 12511V → R: Abolishes interaction with CNOT7.
    Mutagenesisi1257 – 12571P → Y: Abolishes interaction with CNOT7; when associated with Y-1209.

    Organism-specific databases

    PharmGKBiPA26672.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 23762376CCR4-NOT transcription complex subunit 1PRO_0000315541Add
    BLAST

    Proteomic databases

    MaxQBiA5YKK6.
    PaxDbiA5YKK6.
    PeptideAtlasiA5YKK6.
    PRIDEiA5YKK6.

    PTM databases

    PhosphoSiteiA5YKK6.

    Expressioni

    Tissue specificityi

    Strongly expressed in brain, heart, thymus, spleen, kidney, liver, placenta and lung. Weakly expressed in skeletal muscle and colon.1 Publication

    Developmental stagei

    Expressed in embryonic stem (ES) cells.1 Publication

    Gene expression databases

    ArrayExpressiA5YKK6.
    BgeeiA5YKK6.
    GenevestigatoriA5YKK6.

    Organism-specific databases

    HPAiHPA046577.
    HPA049664.

    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. In the complex, interacts directly with CNOT6, CNOT6L, CNOT7 or CNOT8. Interacts in a ligand-dependent fashion with ESR1 and RXRA. Interacts with NANOS2, TOB1 and ZFP36. Interacts with TNRC6A, TNRC6B or TNRC6C; the interactions are direct.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CNOT11Q9UKZ13EBI-1222758,EBI-2562014
    CNOT2Q9NZN83EBI-1222758,EBI-743033
    CNOT6Q9ULM62EBI-1222758,EBI-2104530
    CNOT6LQ96LI52EBI-1222758,EBI-1046635
    CNOT7Q9UIV16EBI-1222758,EBI-2105113
    CNOT8Q9UFF95EBI-1222758,EBI-742299
    TNRC6AQ8NDV72EBI-1222758,EBI-2269715
    TNRC6BQ9UPQ94EBI-1222758,EBI-947158
    TNRC6CQ9HCJ06EBI-1222758,EBI-6507625
    TOB1P506163EBI-1222758,EBI-723281
    Zfp36P228935EBI-1222758,EBI-647803From a different organism.

    Protein-protein interaction databases

    BioGridi116660. 28 interactions.
    DIPiDIP-44954N.
    IntActiA5YKK6. 38 interactions.
    MINTiMINT-3084598.

    Structurei

    Secondary structure

    1
    2376
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni830 – 8323
    Turni838 – 8403
    Helixi841 – 85616
    Helixi866 – 87712
    Helixi882 – 89716
    Helixi899 – 9046
    Helixi907 – 92216
    Helixi929 – 94214
    Helixi949 – 96113
    Helixi962 – 9676
    Helixi969 – 9768
    Helixi981 – 9833
    Helixi986 – 99611
    Helixi1076 – 10827
    Helixi1093 – 110412
    Turni1108 – 11103
    Helixi1111 – 112111
    Helixi1124 – 11263
    Helixi1127 – 113711
    Turni1138 – 11414
    Helixi1143 – 11453
    Helixi1146 – 115611
    Helixi1159 – 117719
    Helixi1186 – 120217
    Helixi1204 – 12063
    Turni1212 – 12143
    Helixi1217 – 122711
    Helixi1229 – 124315
    Helixi1244 – 12485
    Turni1250 – 12523
    Helixi1257 – 127115
    Helixi1277 – 128913
    Helixi1294 – 12963
    Helixi1302 – 13043
    Helixi1306 – 13105
    Helixi1359 – 13613
    Helixi1367 – 13693
    Helixi1371 – 13733
    Helixi1381 – 13855
    Helixi1387 – 13926
    Helixi1393 – 142735
    Turni1428 – 14303
    Helixi1434 – 147643
    Helixi1482 – 152241
    Helixi1524 – 153512
    Helixi1543 – 155210
    Helixi1555 – 15573
    Beta strandi1561 – 15633
    Helixi1566 – 15694
    Helixi1570 – 15778
    Helixi1848 – 186518
    Helixi1870 – 188516
    Beta strandi1888 – 18914
    Helixi1892 – 191524
    Helixi1926 – 194823
    Beta strandi1950 – 19545
    Helixi1957 – 198125
    Helixi1982 – 19843
    Helixi1988 – 200013
    Helixi2006 – 20094
    Helixi2012 – 202514
    Turni2028 – 20303
    Helixi2032 – 20343
    Helixi2035 – 20428
    Helixi2045 – 20528
    Helixi2056 – 20583
    Helixi2061 – 208020
    Helixi2086 – 210520
    Helixi2107 – 21126
    Helixi2114 – 21207
    Helixi2126 – 21338
    Beta strandi2145 – 21473
    Helixi2152 – 21543
    Helixi2157 – 21593
    Helixi2168 – 21714
    Helixi2174 – 218613
    Helixi2191 – 220010
    Beta strandi2205 – 22073
    Beta strandi2208 – 22103
    Helixi2212 – 223221
    Turni2239 – 22413
    Beta strandi2242 – 22454
    Helixi2246 – 225712
    Helixi2260 – 227112
    Beta strandi2276 – 22783
    Helixi2279 – 229315
    Beta strandi2296 – 22983
    Helixi2299 – 231214
    Beta strandi2313 – 23164
    Helixi2320 – 233112
    Helixi2337 – 23393
    Turni2342 – 23443
    Helixi2348 – 236013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4C0DX-ray3.20A1565-2371[»]
    4CQOX-ray2.80A/C1833-2361[»]
    4CRUX-ray1.65A1356-1607[»]
    4CRVX-ray2.05A1356-1607[»]
    4CRWX-ray1.75A1093-1317[»]
    4CT4X-ray2.30A/C1063-1314[»]
    4CT6X-ray2.10A1352-1594[»]
    4CT7X-ray1.90A1352-1594[»]
    4GMJX-ray2.70A/C/E1093-1317[»]
    4GMLX-ray2.90A/B/C/D/E/F1093-1317[»]
    4J8SX-ray1.55A800-1004[»]
    ProteinModelPortaliA5YKK6.
    SMRiA5YKK6. Positions 827-1004, 1093-1317, 1842-2353.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni800 – 1015216Interaction with ZFP36Add
    BLAST
    Regioni1090 – 1605516Interaction with CNOT6, CNOT6L, CNOT7 and CNOT8Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi153 – 1575LXXLL
    Motifi181 – 1855LXXLL
    Motifi223 – 2275LXXLL
    Motifi570 – 5745LXXLL
    Motifi1639 – 16435LXXLL
    Motifi1942 – 19465LXXLL
    Motifi2096 – 21005LXXLL

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1333 – 135018Thr-richAdd
    BLAST

    Domaini

    Contains Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, a motif known to be important for the association with nuclear receptors.1 Publication

    Sequence similaritiesi

    Belongs to the CNOT1 family.Curated

    Phylogenomic databases

    eggNOGiCOG5103.
    HOVERGENiHBG060834.
    InParanoidiA5YKK6.
    KOiK12604.
    OMAiIAQDNCE.
    OrthoDBiEOG744T85.
    PhylomeDBiA5YKK6.
    TreeFamiTF105630.

    Family and domain databases

    InterProiIPR007196. CCR4-Not_Not1_C.
    IPR024557. CCR4-Not_Not1su_DUF3819.
    [Graphical view]
    PfamiPF12842. DUF3819. 1 hit.
    PF04054. Not1. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: A5YKK6-1) [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

    MNLDSLSLAL SQISYLVDNL TKKNYRASQQ EIQHIVNRHG PEADRHLLRC     50
    LFSHVDFSGD GKSSGKDFHQ TQFLIQECAL LITKPNFIST LSYAIDNPLH 100
    YQKSLKPAPH LFAQLSKVLK LSKVQEVIFG LALLNSSSSD LRGFAAQFIK 150
    QKLPDLLRSY IDADVSGNQE GGFQDIAIEV LHLLLSHLLF GQKGAFGVGQ 200
    EQIDAFLKTL RRDFPQERCP VVLAPLLYPE KRDILMDRIL PDSGGVAKTM 250
    MESSLADFMQ EVGYGFCASI EECRNIIVQF GVREVTAAQV ARVLGMMART 300
    HSGLTDGIPL QSISAPGSGI WSDGKDKSDG AQAHTWNVEV LIDVLKELNP 350
    SLNFKEVTYE LDHPGFQIRD SKGLHNVVYG IQRGLGMEVF PVDLIYRPWK 400
    HAEGQLSFIQ HSLINPEIFC FADYPCHTVA TDILKAPPED DNREIATWKS 450
    LDLIESLLRL AEVGQYEQVK QLFSFPIKHC PDMLVLALLQ INTSWHTLRH 500
    ELISTLMPIF LGNHPNSAII LHYAWHGQGQ SPSIRQLIMH AMAEWYMRGE 550
    QYDQAKLSRI LDVAQDLKAL SMLLNGTPFA FVIDLAALAS RREYLKLDKW 600
    LTDKIREHGE PFIQACMTFL KRRCPSILGG LAPEKDQPKS AQLPPETLAT 650
    MLACLQACAG SVSQELSETI LTMVANCSNV MNKARQPPPG VMPKGRPPSA 700
    SSLDAISPVQ IDPLAGMTSL SIGGSAAPHT QSMQGFPPNL GSAFSTPQSP 750
    AKAFPPLSTP NQTTAFSGIG GLSSQLPVGG LGTGSLTGIG TGALGLPAVN 800
    NDPFVQRKLG TSGLNQPTFQ QSKMKPSDLS QVWPEANQHF SKEIDDEANS 850
    YFQRIYNHPP HPTMSVDEVL EMLQRFKDST IKREREVFNC MLRNLFEEYR 900
    FFPQYPDKEL HITACLFGGI IEKGLVTYMA LGLALRYVLE ALRKPFGSKM 950
    YYFGIAALDR FKNRLKDYPQ YCQHLASISH FMQFPHHLQE YIEYGQQSRD 1000
    PPVKMQGSIT TPGSIALAQA QAQAQVPAKA PLAGQVSTMV TTSTTTTVAK 1050
    TVTVTRPTGV SFKKDVPPSI NTTNIDTLLV ATDQTERIVE PPENIQEKIA 1100
    FIFNNLSQSN MTQKVEELKE TVKEEFMPWV SQYLVMKRVS IEPNFHSLYS 1150
    NFLDTLKNPE FNKMVLNETY RNIKVLLTSD KAAANFSDRS LLKNLGHWLG 1200
    MITLAKNKPI LHTDLDVKSL LLEAYVKGQQ ELLYVVPFVA KVLESSIRSV 1250
    VFRPPNPWTM AIMNVLAELH QEHDLKLNLK FEIEVLCKNL ALDINELKPG 1300
    NLLKDKDRLK NLDEQLSAPK KDVKQPEELP PITTTTTSTT PATNTTCTAT 1350
    VPPQPQYSYH DINVYSLAGL APHITLNPTI PLFQAHPQLK QCVRQAIERA 1400
    VQELVHPVVD RSIKIAMTTC EQIVRKDFAL DSEESRMRIA AHHMMRNLTA 1450
    GMAMITCREP LLMSISTNLK NSFASALRTA SPQQREMMDQ AAAQLAQDNC 1500
    ELACCFIQKT AVEKAGPEMD KRLATEFELR KHARQEGRRY CDPVVLTYQA 1550
    ERMPEQIRLK VGGVDPKQLA VYEEFARNVP GFLPTNDLSQ PTGFLAQPMK 1600
    QAWATDDVAQ IYDKCITELE QHLHAIPPTL AMNPQAQALR SLLEVVVLSR 1650
    NSRDAIAALG LLQKAVEGLL DATSGADADL LLRYRECHLL VLKALQDGRA 1700
    YGSPWCNKQI TRCLIECRDE YKYNVEAVEL LIRNHLVNMQ QYDLHLAQSM 1750
    ENGLNYMAVA FAMQLVKILL VDERSVAHVT EADLFHTIET LMRINAHSRG 1800
    NAPEGLPQLM EVVRSNYEAM IDRAHGGPNF MMHSGISQAS EYDDPPGLRE 1850
    KAEYLLREWV NLYHSAAAGR DSTKAFSAFV GQMHQQGILK TDDLITRFFR 1900
    LCTEMCVEIS YRAQAEQQHN PAANPTMIRA KCYHNLDAFV RLIALLVKHS 1950
    GEATNTVTKI NLLNKVLGIV VGVLLQDHDV RQSEFQQLPY HRIFIMLLLE 2000
    LNAPEHVLET INFQTLTAFC NTFHILRPTK APGFVYAWLE LISHRIFIAR 2050
    MLAHTPQQKG WPMYAQLLID LFKYLAPFLR NVELTKPMQI LYKGTLRVLL 2100
    VLLHDFPEFL CDYHYGFCDV IPPNCIQLRN LILSAFPRNM RLPDPFTPNL 2150
    KVDMLSEINI APRILTNFTG VMPPQFKKDL DSYLKTRSPV TFLSDLRSNL 2200
    QVSNEPGNRY NLQLINALVL YVGTQAIAHI HNKGSTPSMS TITHSAHMDI 2250
    FQNLAVDLDT EGRYLFLNAI ANQLRYPNSH THYFSCTMLY LFAEANTEAI 2300
    QEQITRVLLE RLIVNRPHPW GLLITFIELI KNPAFKFWNH EFVHCAPEIE 2350
    KLFQSVAQCC MGQKQAQQVM EGTGAS 2376
    Length:2,376
    Mass (Da):266,939
    Last modified:January 15, 2008 - v2
    Checksum:i937A0899537BA615
    GO
    Isoform 2 (identifier: A5YKK6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         822-827: SKMKPS → T

    Show »
    Length:2,371
    Mass (Da):266,381
    Checksum:i23D129C7F9CE775B
    GO
    Isoform 3 (identifier: A5YKK6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         822-827: SKMKPS → T
         2152-2155: VDML → SLTL
         2156-2376: Missing.

    Show »
    Length:2,150
    Mass (Da):241,260
    Checksum:iBBB731593591523C
    GO
    Isoform 4 (identifier: A5YKK6-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1479-1551: TASPQQREMM...DPVVLTYQAE → VSWLFPWYRY...FFLLYSQHDV
         1552-2376: Missing.

    Show »
    Length:1,551
    Mass (Da):173,792
    Checksum:i00329322012ABAD2
    GO

    Sequence cautioni

    The sequence AAF14861.1 differs from that shown. Reason: Frameshift at positions 1969 and 2273.
    The sequence CAH18093.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181D → G in CAD97851. (PubMed:17974005)Curated
    Sequence conflicti323 – 3231D → G in CAD97851. (PubMed:17974005)Curated
    Sequence conflicti922 – 9221E → G in ABQ66268. (PubMed:17974005)Curated
    Sequence conflicti1063 – 10631K → R in CAH18093. (PubMed:17974005)Curated
    Sequence conflicti1417 – 14171M → V in CAD97851. (PubMed:17974005)Curated
    Sequence conflicti1799 – 17991R → G in CAD97851. (PubMed:17974005)Curated
    Sequence conflicti1936 – 19361L → P in CAH18093. (PubMed:17974005)Curated
    Sequence conflicti2198 – 22003SNL → RTV in AAF14861. (PubMed:10931946)Curated
    Sequence conflicti2358 – 23581Q → R in ABQ66268. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti603 – 6031D → A.1 Publication
    Corresponds to variant rs17854028 [ dbSNP | Ensembl ].
    VAR_038254

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei822 – 8276SKMKPS → T in isoform 2 and isoform 3. 2 PublicationsVSP_030559
    Alternative sequencei1479 – 155173TASPQ…TYQAE → VSWLFPWYRYKTYYCLSVII FFFVYIWHWALPLILNNHHI CLMSSIILDCNSVRQSIMSV CFFFFLLYSQHDV in isoform 4. 1 PublicationVSP_030560Add
    BLAST
    Alternative sequencei1552 – 2376825Missing in isoform 4. 1 PublicationVSP_030561Add
    BLAST
    Alternative sequencei2152 – 21554VDML → SLTL in isoform 3. 1 PublicationVSP_030562
    Alternative sequencei2156 – 2376221Missing in isoform 3. 1 PublicationVSP_030563Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL117492 mRNA. Translation: CAB55960.1.
    BX537840 mRNA. Translation: CAD97851.1.
    CR749237 mRNA. Translation: CAH18093.1. Different initiation.
    EF553522 mRNA. Translation: ABQ66268.1.
    AC009118 Genomic DNA. No translation available.
    AC010287 Genomic DNA. No translation available.
    BC000779 mRNA. Translation: AAH00779.2.
    BC024317 mRNA. Translation: AAH24317.1.
    BC040523 mRNA. Translation: AAH40523.1.
    AB023224 mRNA. Translation: BAA76851.2.
    AF110778 mRNA. Translation: AAF14861.1. Frameshift.
    CCDSiCCDS10799.1. [A5YKK6-1]
    CCDS45501.1. [A5YKK6-4]
    CCDS58468.1. [A5YKK6-2]
    PIRiT17270.
    RefSeqiNP_001252541.1. NM_001265612.1. [A5YKK6-2]
    NP_057368.3. NM_016284.4. [A5YKK6-1]
    NP_996882.1. NM_206999.2. [A5YKK6-4]
    UniGeneiHs.460923.
    Hs.731691.

    Genome annotation databases

    EnsembliENST00000317147; ENSP00000320949; ENSG00000125107. [A5YKK6-1]
    ENST00000441024; ENSP00000413113; ENSG00000125107. [A5YKK6-4]
    ENST00000567188; ENSP00000456649; ENSG00000125107. [A5YKK6-3]
    ENST00000569240; ENSP00000455635; ENSG00000125107. [A5YKK6-2]
    GeneIDi23019.
    KEGGihsa:23019.
    UCSCiuc002enu.5. human. [A5YKK6-2]
    uc002env.4. human. [A5YKK6-1]
    uc002enx.4. human. [A5YKK6-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL117492 mRNA. Translation: CAB55960.1 .
    BX537840 mRNA. Translation: CAD97851.1 .
    CR749237 mRNA. Translation: CAH18093.1 . Different initiation.
    EF553522 mRNA. Translation: ABQ66268.1 .
    AC009118 Genomic DNA. No translation available.
    AC010287 Genomic DNA. No translation available.
    BC000779 mRNA. Translation: AAH00779.2 .
    BC024317 mRNA. Translation: AAH24317.1 .
    BC040523 mRNA. Translation: AAH40523.1 .
    AB023224 mRNA. Translation: BAA76851.2 .
    AF110778 mRNA. Translation: AAF14861.1 . Frameshift.
    CCDSi CCDS10799.1. [A5YKK6-1 ]
    CCDS45501.1. [A5YKK6-4 ]
    CCDS58468.1. [A5YKK6-2 ]
    PIRi T17270.
    RefSeqi NP_001252541.1. NM_001265612.1. [A5YKK6-2 ]
    NP_057368.3. NM_016284.4. [A5YKK6-1 ]
    NP_996882.1. NM_206999.2. [A5YKK6-4 ]
    UniGenei Hs.460923.
    Hs.731691.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4C0D X-ray 3.20 A 1565-2371 [» ]
    4CQO X-ray 2.80 A/C 1833-2361 [» ]
    4CRU X-ray 1.65 A 1356-1607 [» ]
    4CRV X-ray 2.05 A 1356-1607 [» ]
    4CRW X-ray 1.75 A 1093-1317 [» ]
    4CT4 X-ray 2.30 A/C 1063-1314 [» ]
    4CT6 X-ray 2.10 A 1352-1594 [» ]
    4CT7 X-ray 1.90 A 1352-1594 [» ]
    4GMJ X-ray 2.70 A/C/E 1093-1317 [» ]
    4GML X-ray 2.90 A/B/C/D/E/F 1093-1317 [» ]
    4J8S X-ray 1.55 A 800-1004 [» ]
    ProteinModelPortali A5YKK6.
    SMRi A5YKK6. Positions 827-1004, 1093-1317, 1842-2353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116660. 28 interactions.
    DIPi DIP-44954N.
    IntActi A5YKK6. 38 interactions.
    MINTi MINT-3084598.

    PTM databases

    PhosphoSitei A5YKK6.

    Proteomic databases

    MaxQBi A5YKK6.
    PaxDbi A5YKK6.
    PeptideAtlasi A5YKK6.
    PRIDEi A5YKK6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317147 ; ENSP00000320949 ; ENSG00000125107 . [A5YKK6-1 ]
    ENST00000441024 ; ENSP00000413113 ; ENSG00000125107 . [A5YKK6-4 ]
    ENST00000567188 ; ENSP00000456649 ; ENSG00000125107 . [A5YKK6-3 ]
    ENST00000569240 ; ENSP00000455635 ; ENSG00000125107 . [A5YKK6-2 ]
    GeneIDi 23019.
    KEGGi hsa:23019.
    UCSCi uc002enu.5. human. [A5YKK6-2 ]
    uc002env.4. human. [A5YKK6-1 ]
    uc002enx.4. human. [A5YKK6-4 ]

    Organism-specific databases

    CTDi 23019.
    GeneCardsi GC16M058553.
    H-InvDB HIX0013093.
    HGNCi HGNC:7877. CNOT1.
    HPAi HPA046577.
    HPA049664.
    MIMi 604917. gene.
    neXtProti NX_A5YKK6.
    PharmGKBi PA26672.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5103.
    HOVERGENi HBG060834.
    InParanoidi A5YKK6.
    KOi K12604.
    OMAi IAQDNCE.
    OrthoDBi EOG744T85.
    PhylomeDBi A5YKK6.
    TreeFami TF105630.

    Enzyme and pathway databases

    Reactomei REACT_20514. Deadenylation of mRNA.

    Miscellaneous databases

    ChiTaRSi CNOT1. human.
    GeneWikii CNOT1.
    GenomeRNAii 23019.
    NextBioi 43960.
    PROi A5YKK6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi A5YKK6.
    Bgeei A5YKK6.
    Genevestigatori A5YKK6.

    Family and domain databases

    InterProi IPR007196. CCR4-Not_Not1_C.
    IPR024557. CCR4-Not_Not1su_DUF3819.
    [Graphical view ]
    Pfami PF12842. DUF3819. 1 hit.
    PF04054. Not1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 244-2376 (ISOFORM 1).
      Tissue: Cervix, Fetal kidney and Testis.
    2. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 757-2376 (ISOFORM 1), VARIANT ALA-603.
      Tissue: Choriocarcinoma, Leiomyosarcoma and Testis.
    4. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 537-2376 (ISOFORM 2).
      Tissue: Brain.
    5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1964-2374 (ISOFORM 1).
      Tissue: Adrenal gland.
    7. "Isolation and characterization of human orthologs of yeast CCR4-NOT complex subunits."
      Albert T.K., Lemaire M., van Berkum N.L., Gentz R., Collart M.A., Timmers H.T.M.
      Nucleic Acids Res. 28:809-817(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CNOT2; CNOT4 AND CNOT8, TISSUE SPECIFICITY.
    8. "Human Ccr4-Not complex is a ligand-dependent repressor of nuclear receptor-mediated transcription."
      Winkler G.S., Mulder K.W., Bardwell V.J., Kalkhoven E., Timmers H.T.
      EMBO J. 25:3089-3099(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, INTERACTION WITH CNOT2; CNOT3; CNOT8; ESR1 AND RXRA.
    9. "Interaction of antiproliferative protein Tob with the CCR4-NOT deadenylase complex."
      Miyasaka T., Morita M., Ito K., Suzuki T., Fukuda H., Takeda S., Inoue J., Semba K., Yamamoto T.
      Cancer Sci. 99:755-761(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TOB1.
    10. Cited for: IDENTIFICATION IN THE CCR4-NOT COMPLEX, COMPOSITION OF THE CCR4-NOT COMPLEX.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets."
      Braun J.E., Huntzinger E., Fauser M., Izaurralde E.
      Mol. Cell 44:120-133(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TNRC6A; TNRC6B AND TNRC6C.
    13. "miRNA-mediated deadenylation is orchestrated by GW182 through two conserved motifs that interact with CCR4-NOT."
      Fabian M.R., Cieplak M.K., Frank F., Morita M., Green J., Srikumar T., Nagar B., Yamamoto T., Raught B., Duchaine T.F., Sonenberg N.
      Nat. Struct. Mol. Biol. 18:1211-1217(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TNRC6C.
    14. "Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin."
      Sandler H., Kreth J., Timmers H.T., Stoecklin G.
      Nucleic Acids Res. 39:4373-4386(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZFP36.
    15. "The role of the CNOT1 subunit of the CCR4-NOT complex in mRNA deadenylation and cell viability."
      Ito K., Takahashi A., Morita M., Suzuki T., Yamamoto T.
      Protein Cell 2:755-763(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    16. "Cnot1, Cnot2, and Cnot3 maintain mouse and human ESC identity and inhibit extraembryonic differentiation."
      Zheng X., Dumitru R., Lackford B.L., Freudenberg J.M., Singh A.P., Archer T.K., Jothi R., Hu G.
      Stem Cells 30:910-922(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    17. "The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4-NOT deadenylase complex."
      Petit A.P., Wohlbold L., Bawankar P., Huntzinger E., Schmidt S., Izaurralde E., Weichenrieder O.
      Nucleic Acids Res. 40:11058-11072(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1093-1317 IN COMPLEX WITH CNOT7, INTERACTION WITH CNOT8; CNOT6 AND CNOT6L, MUTAGENESIS OF LYS-1208; HIS-1212 AND LYS-1218.
    18. "Structural basis for the recruitment of the human CCR4-NOT deadenylase complex by tristetraprolin."
      Fabian M.R., Frank F., Rouya C., Siddiqui N., Lai W.S., Karetnikov A., Blackshear P.J., Nagar B., Sonenberg N.
      Nat. Struct. Mol. Biol. 20:735-739(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 800-1004 IN COMPLEX WITH ZFP36, INTERACTION WITH ZFP36, FUNCTION.

    Entry informationi

    Entry nameiCNOT1_HUMAN
    AccessioniPrimary (citable) accession number: A5YKK6
    Secondary accession number(s): Q68DX7
    , Q7Z3K2, Q8IWB8, Q8TB53, Q9BVZ6, Q9UFR8, Q9UI27, Q9Y2L0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 75 of the entry and version 2 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 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3