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A5YKK6

- CNOT1_HUMAN

UniProt

A5YKK6 - CNOT1_HUMAN

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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

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

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
Complete GO annotation...

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

BgeeiA5YKK6.
ExpressionAtlasiA5YKK6. baseline and differential.
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. 34 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 – 8323Combined sources
Turni838 – 8403Combined sources
Helixi841 – 85616Combined sources
Helixi866 – 87712Combined sources
Helixi882 – 89716Combined sources
Helixi899 – 9046Combined sources
Helixi907 – 92216Combined sources
Helixi929 – 94214Combined sources
Helixi949 – 96113Combined sources
Helixi962 – 9676Combined sources
Helixi969 – 9768Combined sources
Helixi981 – 9833Combined sources
Helixi986 – 99611Combined sources
Helixi1076 – 10827Combined sources
Helixi1093 – 110412Combined sources
Turni1108 – 11103Combined sources
Helixi1111 – 112111Combined sources
Helixi1124 – 11263Combined sources
Helixi1127 – 113711Combined sources
Turni1138 – 11414Combined sources
Helixi1143 – 11453Combined sources
Helixi1146 – 115611Combined sources
Helixi1159 – 117719Combined sources
Helixi1186 – 120217Combined sources
Helixi1204 – 12063Combined sources
Turni1212 – 12143Combined sources
Helixi1217 – 122711Combined sources
Helixi1229 – 124315Combined sources
Helixi1244 – 12485Combined sources
Turni1250 – 12523Combined sources
Helixi1257 – 127115Combined sources
Helixi1277 – 128913Combined sources
Helixi1294 – 12963Combined sources
Helixi1302 – 13043Combined sources
Helixi1306 – 13105Combined sources
Helixi1359 – 13613Combined sources
Helixi1367 – 13693Combined sources
Helixi1371 – 13733Combined sources
Helixi1381 – 13855Combined sources
Helixi1387 – 13926Combined sources
Helixi1393 – 142735Combined sources
Turni1428 – 14303Combined sources
Helixi1434 – 147643Combined sources
Helixi1482 – 152241Combined sources
Helixi1524 – 153512Combined sources
Helixi1543 – 155210Combined sources
Helixi1555 – 15573Combined sources
Beta strandi1561 – 15633Combined sources
Helixi1566 – 15694Combined sources
Helixi1570 – 15778Combined sources
Helixi1848 – 186518Combined sources
Helixi1870 – 188516Combined sources
Beta strandi1888 – 18914Combined sources
Helixi1892 – 191524Combined sources
Helixi1926 – 194823Combined sources
Beta strandi1950 – 19545Combined sources
Helixi1957 – 198125Combined sources
Helixi1982 – 19843Combined sources
Helixi1988 – 200013Combined sources
Helixi2006 – 20094Combined sources
Helixi2012 – 202514Combined sources
Turni2028 – 20303Combined sources
Helixi2032 – 20343Combined sources
Helixi2035 – 20428Combined sources
Helixi2045 – 20528Combined sources
Helixi2056 – 20583Combined sources
Helixi2061 – 208020Combined sources
Helixi2086 – 210520Combined sources
Helixi2107 – 21126Combined sources
Helixi2114 – 21207Combined sources
Helixi2126 – 21338Combined sources
Beta strandi2145 – 21473Combined sources
Helixi2152 – 21543Combined sources
Helixi2157 – 21593Combined sources
Helixi2168 – 21714Combined sources
Helixi2174 – 218613Combined sources
Helixi2191 – 220010Combined sources
Beta strandi2205 – 22073Combined sources
Beta strandi2208 – 22103Combined sources
Helixi2212 – 223221Combined sources
Turni2239 – 22413Combined sources
Beta strandi2242 – 22454Combined sources
Helixi2246 – 225712Combined sources
Helixi2260 – 227112Combined sources
Beta strandi2276 – 22783Combined sources
Helixi2279 – 229315Combined sources
Beta strandi2296 – 22983Combined sources
Helixi2299 – 231214Combined sources
Beta strandi2313 – 23164Combined sources
Helixi2320 – 233112Combined sources
Helixi2337 – 23393Combined sources
Turni2342 – 23443Combined sources
Helixi2348 – 236013Combined sources

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, 1069-1310, 1352-1588, 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.
GeneTreeiENSGT00390000014869.
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

        10         20         30         40         50
MNLDSLSLAL SQISYLVDNL TKKNYRASQQ EIQHIVNRHG PEADRHLLRC
60 70 80 90 100
LFSHVDFSGD GKSSGKDFHQ TQFLIQECAL LITKPNFIST LSYAIDNPLH
110 120 130 140 150
YQKSLKPAPH LFAQLSKVLK LSKVQEVIFG LALLNSSSSD LRGFAAQFIK
160 170 180 190 200
QKLPDLLRSY IDADVSGNQE GGFQDIAIEV LHLLLSHLLF GQKGAFGVGQ
210 220 230 240 250
EQIDAFLKTL RRDFPQERCP VVLAPLLYPE KRDILMDRIL PDSGGVAKTM
260 270 280 290 300
MESSLADFMQ EVGYGFCASI EECRNIIVQF GVREVTAAQV ARVLGMMART
310 320 330 340 350
HSGLTDGIPL QSISAPGSGI WSDGKDKSDG AQAHTWNVEV LIDVLKELNP
360 370 380 390 400
SLNFKEVTYE LDHPGFQIRD SKGLHNVVYG IQRGLGMEVF PVDLIYRPWK
410 420 430 440 450
HAEGQLSFIQ HSLINPEIFC FADYPCHTVA TDILKAPPED DNREIATWKS
460 470 480 490 500
LDLIESLLRL AEVGQYEQVK QLFSFPIKHC PDMLVLALLQ INTSWHTLRH
510 520 530 540 550
ELISTLMPIF LGNHPNSAII LHYAWHGQGQ SPSIRQLIMH AMAEWYMRGE
560 570 580 590 600
QYDQAKLSRI LDVAQDLKAL SMLLNGTPFA FVIDLAALAS RREYLKLDKW
610 620 630 640 650
LTDKIREHGE PFIQACMTFL KRRCPSILGG LAPEKDQPKS AQLPPETLAT
660 670 680 690 700
MLACLQACAG SVSQELSETI LTMVANCSNV MNKARQPPPG VMPKGRPPSA
710 720 730 740 750
SSLDAISPVQ IDPLAGMTSL SIGGSAAPHT QSMQGFPPNL GSAFSTPQSP
760 770 780 790 800
AKAFPPLSTP NQTTAFSGIG GLSSQLPVGG LGTGSLTGIG TGALGLPAVN
810 820 830 840 850
NDPFVQRKLG TSGLNQPTFQ QSKMKPSDLS QVWPEANQHF SKEIDDEANS
860 870 880 890 900
YFQRIYNHPP HPTMSVDEVL EMLQRFKDST IKREREVFNC MLRNLFEEYR
910 920 930 940 950
FFPQYPDKEL HITACLFGGI IEKGLVTYMA LGLALRYVLE ALRKPFGSKM
960 970 980 990 1000
YYFGIAALDR FKNRLKDYPQ YCQHLASISH FMQFPHHLQE YIEYGQQSRD
1010 1020 1030 1040 1050
PPVKMQGSIT TPGSIALAQA QAQAQVPAKA PLAGQVSTMV TTSTTTTVAK
1060 1070 1080 1090 1100
TVTVTRPTGV SFKKDVPPSI NTTNIDTLLV ATDQTERIVE PPENIQEKIA
1110 1120 1130 1140 1150
FIFNNLSQSN MTQKVEELKE TVKEEFMPWV SQYLVMKRVS IEPNFHSLYS
1160 1170 1180 1190 1200
NFLDTLKNPE FNKMVLNETY RNIKVLLTSD KAAANFSDRS LLKNLGHWLG
1210 1220 1230 1240 1250
MITLAKNKPI LHTDLDVKSL LLEAYVKGQQ ELLYVVPFVA KVLESSIRSV
1260 1270 1280 1290 1300
VFRPPNPWTM AIMNVLAELH QEHDLKLNLK FEIEVLCKNL ALDINELKPG
1310 1320 1330 1340 1350
NLLKDKDRLK NLDEQLSAPK KDVKQPEELP PITTTTTSTT PATNTTCTAT
1360 1370 1380 1390 1400
VPPQPQYSYH DINVYSLAGL APHITLNPTI PLFQAHPQLK QCVRQAIERA
1410 1420 1430 1440 1450
VQELVHPVVD RSIKIAMTTC EQIVRKDFAL DSEESRMRIA AHHMMRNLTA
1460 1470 1480 1490 1500
GMAMITCREP LLMSISTNLK NSFASALRTA SPQQREMMDQ AAAQLAQDNC
1510 1520 1530 1540 1550
ELACCFIQKT AVEKAGPEMD KRLATEFELR KHARQEGRRY CDPVVLTYQA
1560 1570 1580 1590 1600
ERMPEQIRLK VGGVDPKQLA VYEEFARNVP GFLPTNDLSQ PTGFLAQPMK
1610 1620 1630 1640 1650
QAWATDDVAQ IYDKCITELE QHLHAIPPTL AMNPQAQALR SLLEVVVLSR
1660 1670 1680 1690 1700
NSRDAIAALG LLQKAVEGLL DATSGADADL LLRYRECHLL VLKALQDGRA
1710 1720 1730 1740 1750
YGSPWCNKQI TRCLIECRDE YKYNVEAVEL LIRNHLVNMQ QYDLHLAQSM
1760 1770 1780 1790 1800
ENGLNYMAVA FAMQLVKILL VDERSVAHVT EADLFHTIET LMRINAHSRG
1810 1820 1830 1840 1850
NAPEGLPQLM EVVRSNYEAM IDRAHGGPNF MMHSGISQAS EYDDPPGLRE
1860 1870 1880 1890 1900
KAEYLLREWV NLYHSAAAGR DSTKAFSAFV GQMHQQGILK TDDLITRFFR
1910 1920 1930 1940 1950
LCTEMCVEIS YRAQAEQQHN PAANPTMIRA KCYHNLDAFV RLIALLVKHS
1960 1970 1980 1990 2000
GEATNTVTKI NLLNKVLGIV VGVLLQDHDV RQSEFQQLPY HRIFIMLLLE
2010 2020 2030 2040 2050
LNAPEHVLET INFQTLTAFC NTFHILRPTK APGFVYAWLE LISHRIFIAR
2060 2070 2080 2090 2100
MLAHTPQQKG WPMYAQLLID LFKYLAPFLR NVELTKPMQI LYKGTLRVLL
2110 2120 2130 2140 2150
VLLHDFPEFL CDYHYGFCDV IPPNCIQLRN LILSAFPRNM RLPDPFTPNL
2160 2170 2180 2190 2200
KVDMLSEINI APRILTNFTG VMPPQFKKDL DSYLKTRSPV TFLSDLRSNL
2210 2220 2230 2240 2250
QVSNEPGNRY NLQLINALVL YVGTQAIAHI HNKGSTPSMS TITHSAHMDI
2260 2270 2280 2290 2300
FQNLAVDLDT EGRYLFLNAI ANQLRYPNSH THYFSCTMLY LFAEANTEAI
2310 2320 2330 2340 2350
QEQITRVLLE RLIVNRPHPW GLLITFIELI KNPAFKFWNH EFVHCAPEIE
2360 2370
KLFQSVAQCC MGQKQAQQVM EGTGAS
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, 1069-1310, 1352-1588, 1842-2353.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116660. 34 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.
GeneTreei ENSGT00390000014869.
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

Bgeei A5YKK6.
ExpressionAtlasi A5YKK6. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 76 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

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