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Protein

CCR4-NOT transcription complex subunit 4

Gene

CNOT4

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

Functioni

Has E3 ubiquitin ligase activity. Involved in activation of the JAK/STAT pathway.2 Publications

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri14 – 5744RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri190 – 21728C3H1-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • ubiquitin-protein transferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_20514. Deadenylation of mRNA.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
CCR4-NOT transcription complex subunit 4 (EC:6.3.2.-)
Alternative name(s):
CCR4-associated factor 4
E3 ubiquitin-protein ligase CNOT4
Potential transcriptional repressor NOT4Hp
Gene namesi
Name:CNOT4
Synonyms:NOT4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:7880. CNOT4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi16 – 161L → A or E: Abolishes interaction with E2 ubiquitin ligases. 1 Publication
Mutagenesisi17 – 171C → A: Abolishes interaction with E2 ubiquitin ligases. 1 Publication
Mutagenesisi18 – 181M → A: Strongly reduces interaction with E2 ubiquitin ligases. 1 Publication
Mutagenesisi33 – 331C → R: Abolishes interaction with E2 ubiquitin ligases. 1 Publication
Mutagenesisi42 – 421W → A: Strongly reduces interaction with E2 ubiquitin ligases. 1 Publication
Mutagenesisi44 – 441R → A or E: Strongly reduces interaction with E2 ubiquitin ligases. 1 Publication
Mutagenesisi45 – 451I → A or W: Strongly reduces interaction with E2 ubiquitin ligases. 1 Publication
Mutagenesisi49 – 491E → A: Strongly reduces interaction with E2 ubiquitin ligases. 2 Publications
Mutagenesisi49 – 491E → K: Strongly reduced interaction with UBE2D2. 2 Publications
Mutagenesisi54 – 541P → A: Strongly reduces interaction with E2 ubiquitin ligases. 1 Publication
Mutagenesisi57 – 571R → A or E: Strongly reduces interaction with E2 ubiquitin ligases. 1 Publication

Organism-specific databases

PharmGKBiPA26675.

Polymorphism and mutation databases

BioMutaiCNOT4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575CCR4-NOT transcription complex subunit 4PRO_0000081679Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711Phosphoserine1 Publication
Modified residuei324 – 3241Phosphoserine3 Publications
Modified residuei432 – 4321Phosphoserine1 Publication
Modified residuei490 – 4901Phosphoserine1 Publication

Post-translational modificationi

Autoubiquitinated.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO95628.
PaxDbiO95628.
PRIDEiO95628.

PTM databases

PhosphoSiteiO95628.

Expressioni

Gene expression databases

BgeeiO95628.
CleanExiHS_CNOT4.
ExpressionAtlasiO95628. baseline and differential.
GenevisibleiO95628. HS.

Organism-specific databases

HPAiHPA005737.

Interactioni

Subunit structurei

Interacts with CNOT1 via its C-terminus but does not stably associate with the CCR4-NOT complex. Binds E2 ubiquitin ligases via its RING domain. Interacts (via RING domain) with UBE2D2.3 Publications

Protein-protein interaction databases

BioGridi110912. 16 interactions.
IntActiO95628. 9 interactions.
STRINGi9606.ENSP00000445508.

Structurei

Secondary structure

1
575
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni15 – 173Combined sources
Turni23 – 275Combined sources
Helixi39 – 457Combined sources
Turni54 – 563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E4UNMR-A1-78[»]
1UR6NMR-B12-63[»]
ProteinModelPortaliO95628.
SMRiO95628. Positions 1-78, 103-198.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95628.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 18981RRMPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili68 – 10437Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 C3H1-type zinc finger.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri14 – 5744RING-type; degeneratePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri190 – 21728C3H1-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiCOG5175.
GeneTreeiENSGT00390000000068.
HOGENOMiHOG000065696.
HOVERGENiHBG051043.
InParanoidiO95628.
KOiK10643.
OMAiASWNPYS.
OrthoDBiEOG790G0K.
PhylomeDBiO95628.
TreeFamiTF106134.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR000571. Znf_CCCH.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95628-1) [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
MSRSPDAKED PVECPLCMEP LEIDDINFFP CTCGYQICRF CWHRIRTDEN
60 70 80 90 100
GLCPACRKPY PEDPAVYKPL SQEELQRIKN EKKQKQNERK QKISENRKHL
110 120 130 140 150
ASVRVVQKNL VFVVGLSQRL ADPEVLKRPE YFGKFGKIHK VVINNSTSYA
160 170 180 190 200
GSQGPSASAY VTYIRSEDAL RAIQCVNNVV VDGRTLKASL GTTKYCSYFL
210 220 230 240 250
KNMQCPKPDC MYLHELGDEA ASFTKEEMQA GKHQEYEQKL LQELYKLNPN
260 270 280 290 300
FLQLSTGSVD KNKNKVTPLQ RYDTPIDKPS DSLSIGNGDN SQQISNSDTP
310 320 330 340 350
SPPPGLSKSN PVIPISSSNH SARSPFEGAV TESQSLFSDN FRHPNPIPSG
360 370 380 390 400
LPPFPSSPQT SSDWPTAPEP QSLFTSETIP VSSSTDWQAA FGFGSSKQPE
410 420 430 440 450
DDLGFDPFDV TRKALADLIE KELSVQDQPS LSPTSLQNSS SHTTTAKGPG
460 470 480 490 500
SGFLHPAAAT NANSLNSTFS VLPQRFPQFQ QHRAVYNSFS FPGQAARYPW
510 520 530 540 550
MAFPRNSIMH LNHTANPTSN SNFLDLNLPP QHNTGLGGIP VAGEEEVKVS
560 570
TMPLSTSSHS LQQGQQPTSL HTTVA
Length:575
Mass (Da):63,510
Last modified:October 3, 2006 - v3
Checksum:iC41762D4EC4222BC
GO
Isoform 2 (identifier: O95628-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     271-274: RYDT → S

Show »
Length:572
Mass (Da):63,062
Checksum:i717835C74D66B540
GO
Isoform 3 (identifier: O95628-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.

Note: No experimental confirmation available.
Show »
Length:558
Mass (Da):61,651
Checksum:iDAE0356900B05FE4
GO
Isoform 4 (identifier: O95628-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     544-575: EEEVKVSTMPLSTSSHSLQQGQQPTSLHTTVA → IPASSGNSLD...LLQSSTLDRH

Note: No experimental confirmation available.
Show »
Length:642
Mass (Da):70,787
Checksum:i3D432CA88242C77E
GO
Isoform 5 (identifier: O95628-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     419-433: IEKELSVQDQPSLSP → TEPIERKRLAVLKRR
     434-575: Missing.

Show »
Length:433
Mass (Da):48,485
Checksum:i8B120FF952B46883
GO
Isoform 6 (identifier: O95628-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     543-575: GEEEVKVSTMPLSTSSHSLQQGQQPTSLHTTVA → DNSSSIESLN...HLFINCKNFC

Note: No experimental confirmation available.
Show »
Length:767
Mass (Da):84,747
Checksum:i43A198C595008B1C
GO
Isoform 7 (identifier: O95628-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     544-575: EEEVKVSTMPLSTSSHSLQQGQQPTSLHTTVA → IPASSGNSLD...PTAPFSSLMF

Note: No experimental confirmation available.
Show »
Length:675
Mass (Da):74,524
Checksum:iFA54396714B4A41B
GO
Isoform 8 (identifier: O95628-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     271-274: RYDT → S
     544-575: EEEVKVSTMPLSTSSHSLQQGQQPTSLHTTVA → IPASSGNSLD...LLQSSTLDRH

Note: No experimental confirmation available.
Show »
Length:639
Mass (Da):70,339
Checksum:iC22E9F609FFFF456
GO
Isoform 9 (identifier: O95628-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     271-274: RYDT → S
     543-575: GEEEVKVSTMPLSTSSHSLQQGQQPTSLHTTVA → DNSSSVESLN...LLQSSTLDRH

Note: No experimental confirmation available.Curated
Show »
Length:710
Mass (Da):77,809
Checksum:i118DE9B8D4B7AD79
GO
Isoform 10 (identifier: O95628-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     543-575: GEEEVKVSTMPLSTSSHSLQQGQQPTSLHTTVA → DNSSSVESLN...LLQSSTLDRH

Note: No experimental confirmation available.
Show »
Length:713
Mass (Da):78,257
Checksum:iA66182988D096173
GO

Sequence cautioni

The sequence AAC72963.1 differs from that shown.Sequencing errors.Curated
The sequence AAC72963.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AAD00180.1 differs from that shown. Reason: Frameshift at positions 358 and 400. Curated
The sequence BAC11125.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781N → D in BAH13270 (PubMed:14702039).Curated
Sequence conflicti201 – 2011K → R in BAH13270 (PubMed:14702039).Curated
Sequence conflicti340 – 3401N → I in AAH35590 (PubMed:15489334).Curated
Sequence conflicti570 – 5701L → F in AAD00179 (Ref. 1) Curated
Sequence conflicti570 – 5701L → F in AAD00180 (Ref. 1) Curated
Isoform 9 (identifier: O95628-9)
Sequence conflicti545 – 5451V → I in BAH13270 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71A → G.1 Publication
Corresponds to variant rs17480616 [ dbSNP | Ensembl ].
VAR_027833

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1717Missing in isoform 3. 1 PublicationVSP_009923Add
BLAST
Alternative sequencei271 – 2744RYDT → S in isoform 2, isoform 8 and isoform 9. 3 PublicationsVSP_009924
Alternative sequencei419 – 43315IEKEL…PSLSP → TEPIERKRLAVLKRR in isoform 5. 1 PublicationVSP_009925Add
BLAST
Alternative sequencei434 – 575142Missing in isoform 5. 1 PublicationVSP_009926Add
BLAST
Alternative sequencei543 – 57533GEEEV…HTTVA → DNSSSIESLNMKEWQDGLRA LLPNININFGGLPNSSSPSN ANHSAPTSNTATTDSLSWDS PGSWTDPAIITGIPASSGNS LDSLQDDNPPHWLKSLQALT EMDGPSAAPSQTHHSAPFST QIPLHRASWNPYPPPSNPSS FHSPPPQIYYRVQHWTAIRQ RGATIRKCRICPTLFSPSQP TTHSSLLISYVLKNPVPDQF FFSLTPDAMRSQGHYHLFIN CKNFC in isoform 6. 1 PublicationVSP_009927Add
BLAST
Alternative sequencei543 – 57533GEEEV…HTTVA → DNSSSVESLNMKEWQDGLRA LLPNININFGGLPNSSSPSN ANHSAPTSNTATTDSLSWDS PGSWTDPAIITGIPASSGNS LDSLQDDNPPHWLKSLQALT EMDGPSAAPSQTHHSAPFST QIPLHRASWNPYPPPSNPSS FHSPPPGFQTAFRPPSKTPT DLLQSSTLDRH in isoform 9 and isoform 10. 1 PublicationVSP_045469Add
BLAST
Alternative sequencei544 – 57532EEEVK…HTTVA → IPASSGNSLDSLQDDNPPHW LKSLQALTEMDGPSAAPSQT HHSAPFSTQIPLHRASWNPY PPPSNPSSFHSPPPGFQTAF RPPSKTPTDLLQSSTLDRH in isoform 4 and isoform 8. 1 PublicationVSP_009928Add
BLAST
Alternative sequencei544 – 57532EEEVK…HTTVA → IPASSGNSLDSLQDDNPPHW LKSLQALTEMDGQRCSITDP PQRPLQHTDPAAQSQLESLP SSFKPFQLPLPTPRLSDGLQ TPQQNPHRFTTEFNTGPPLG KEEQPLENAGFVPLCFLPLS PPPTAPFSSLMF in isoform 7. 1 PublicationVSP_009929Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U71267 mRNA. Translation: AAD00179.1. Frameshift.
U71268 mRNA. Translation: AAD00180.1. Frameshift.
AF180475 mRNA. Translation: AAF29829.1.
AL389980 mRNA. Translation: CAB97536.1.
AK074671 mRNA. Translation: BAC11125.1. Different initiation.
AK300365 mRNA. Translation: BAH13270.1.
AC083871 Genomic DNA. No translation available.
AC074002 Genomic DNA. No translation available.
BC035590 mRNA. Translation: AAH35590.1.
AF091094 mRNA. Translation: AAC72963.1. Sequence problems.
CCDSiCCDS43650.1. [O95628-8]
CCDS47719.1. [O95628-2]
CCDS55164.1. [O95628-4]
CCDS55165.1. [O95628-10]
CCDS55166.1. [O95628-1]
CCDS55167.1. [O95628-9]
RefSeqiNP_001008226.1. NM_001008225.2. [O95628-2]
NP_001177776.1. NM_001190847.1. [O95628-4]
NP_001177777.1. NM_001190848.1. [O95628-1]
NP_001177778.1. NM_001190849.1. [O95628-9]
NP_001177779.1. NM_001190850.1. [O95628-10]
NP_037448.2. NM_013316.3. [O95628-8]
UniGeneiHs.490224.

Genome annotation databases

EnsembliENST00000315544; ENSP00000326731; ENSG00000080802. [O95628-1]
ENST00000361528; ENSP00000354673; ENSG00000080802. [O95628-8]
ENST00000414802; ENSP00000416532; ENSG00000080802. [O95628-5]
ENST00000423368; ENSP00000406777; ENSG00000080802. [O95628-4]
ENST00000428680; ENSP00000399108; ENSG00000080802. [O95628-2]
ENST00000451834; ENSP00000388491; ENSG00000080802. [O95628-9]
ENST00000541284; ENSP00000445508; ENSG00000080802. [O95628-10]
GeneIDi4850.
KEGGihsa:4850.
UCSCiuc003vss.3. human. [O95628-8]
uc003vst.3. human. [O95628-4]
uc003vsu.2. human. [O95628-2]
uc003vsv.2. human. [O95628-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U71267 mRNA. Translation: AAD00179.1. Frameshift.
U71268 mRNA. Translation: AAD00180.1. Frameshift.
AF180475 mRNA. Translation: AAF29829.1.
AL389980 mRNA. Translation: CAB97536.1.
AK074671 mRNA. Translation: BAC11125.1. Different initiation.
AK300365 mRNA. Translation: BAH13270.1.
AC083871 Genomic DNA. No translation available.
AC074002 Genomic DNA. No translation available.
BC035590 mRNA. Translation: AAH35590.1.
AF091094 mRNA. Translation: AAC72963.1. Sequence problems.
CCDSiCCDS43650.1. [O95628-8]
CCDS47719.1. [O95628-2]
CCDS55164.1. [O95628-4]
CCDS55165.1. [O95628-10]
CCDS55166.1. [O95628-1]
CCDS55167.1. [O95628-9]
RefSeqiNP_001008226.1. NM_001008225.2. [O95628-2]
NP_001177776.1. NM_001190847.1. [O95628-4]
NP_001177777.1. NM_001190848.1. [O95628-1]
NP_001177778.1. NM_001190849.1. [O95628-9]
NP_001177779.1. NM_001190850.1. [O95628-10]
NP_037448.2. NM_013316.3. [O95628-8]
UniGeneiHs.490224.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E4UNMR-A1-78[»]
1UR6NMR-B12-63[»]
ProteinModelPortaliO95628.
SMRiO95628. Positions 1-78, 103-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110912. 16 interactions.
IntActiO95628. 9 interactions.
STRINGi9606.ENSP00000445508.

PTM databases

PhosphoSiteiO95628.

Polymorphism and mutation databases

BioMutaiCNOT4.

Proteomic databases

MaxQBiO95628.
PaxDbiO95628.
PRIDEiO95628.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315544; ENSP00000326731; ENSG00000080802. [O95628-1]
ENST00000361528; ENSP00000354673; ENSG00000080802. [O95628-8]
ENST00000414802; ENSP00000416532; ENSG00000080802. [O95628-5]
ENST00000423368; ENSP00000406777; ENSG00000080802. [O95628-4]
ENST00000428680; ENSP00000399108; ENSG00000080802. [O95628-2]
ENST00000451834; ENSP00000388491; ENSG00000080802. [O95628-9]
ENST00000541284; ENSP00000445508; ENSG00000080802. [O95628-10]
GeneIDi4850.
KEGGihsa:4850.
UCSCiuc003vss.3. human. [O95628-8]
uc003vst.3. human. [O95628-4]
uc003vsu.2. human. [O95628-2]
uc003vsv.2. human. [O95628-1]

Organism-specific databases

CTDi4850.
GeneCardsiGC07M135046.
H-InvDBHIX0007112.
HGNCiHGNC:7880. CNOT4.
HPAiHPA005737.
MIMi604911. gene.
neXtProtiNX_O95628.
PharmGKBiPA26675.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5175.
GeneTreeiENSGT00390000000068.
HOGENOMiHOG000065696.
HOVERGENiHBG051043.
InParanoidiO95628.
KOiK10643.
OMAiASWNPYS.
OrthoDBiEOG790G0K.
PhylomeDBiO95628.
TreeFamiTF106134.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_20514. Deadenylation of mRNA.

Miscellaneous databases

EvolutionaryTraceiO95628.
GenomeRNAii4850.
NextBioi18678.
PROiO95628.
SOURCEiSearch...

Gene expression databases

BgeeiO95628.
CleanExiHS_CNOT4.
ExpressionAtlasiO95628. baseline and differential.
GenevisibleiO95628. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR000571. Znf_CCCH.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
PS50103. ZF_C3H1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of human and murine homologues of yeast NOT4 gene."
    Chiang P.-W.
    Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
  2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  3. The European IMAGE consortium
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT GLY-7.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-575 (ISOFORM 6).
    Tissue: Mammary gland and Placenta.
  5. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 2).
    Tissue: Testis.
  7. "Full-insert sequence of mapped XREF EST."
    Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 294-575 (ISOFORM 7).
  8. "Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex."
    Albert T.K., Hanzawa H., Legtenberg Y.I.A., de Ruwe M.J., van den Heuvel F.A.J., Collart M.A., Boelens R., Timmers H.T.M.
    EMBO J. 21:355-364(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH CNOT1 AND UBIQUITIN E2 LIGASES, MUTAGENESIS OF LEU-16; CYS-17; MET-18; CYS-33; TRP-42; ARG-44; ILE-45; GLU-49; PRO-54 AND ARG-57, STRUCTURE BY NMR OF 1-78.
  9. "An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair."
    Winkler G.S., Albert T.K., Dominguez C., Legtenberg Y.I., Boelens R., Timmers H.T.
    J. Mol. Biol. 337:157-165(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBE2D2, AUTOUBIQUITINATION, MUTAGENESIS OF GLU-49.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-432 AND SER-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Not4 enhances JAK/STAT pathway-dependent gene expression in Drosophila and in human cells."
    Gronholm J., Kaustio M., Myllymaki H., Kallio J., Saarikettu J., Kronhamn J., Valanne S., Silvennoinen O., Ramet M.
    FASEB J. 26:1239-1250(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "The structure of the C4C4 ring finger of human NOT4 reveals features distinct from those of C3HC4 RING fingers."
    Hanzawa H., de Ruwe M.J., Albert T.K., van Der Vliet P.C., Timmers H.T.M., Boelens R.
    J. Biol. Chem. 276:10185-10190(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-78 IN COMPLEX WITH ZINC IONS.

Entry informationi

Entry nameiCNOT4_HUMAN
AccessioniPrimary (citable) accession number: O95628
Secondary accession number(s): B7Z6I4
, E7ET38, F8VQP3, O95339, O95627, Q8IYM7, Q8NCL0, Q9NPQ1, Q9NZN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: October 3, 2006
Last modified: June 24, 2015
This is version 144 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 7
    Human chromosome 7: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.