ZZ_tyyppiset
sinkkisormiproteiinit (ZZZ)
Näitä ryhmiä on
listattuna eräässä artikkelissa kolmekymmentä, kuten juuri mainitsin ja ne ovat
luokiteltuna sinkkisormen rakenteen mukaan. kahdentenatoista ryhmänä
mainitaan ryhmä ZZZ eli "ZZ_ tyyppiset ZNF proteiinit".
Sinkkisormirakenne on C-x-C-x-C-x-C ja siitä annetaan netissä enemmänkin selvitystä.
Tässä ZZZ- ryhmässä
kerrotaan olevan 18 jäsentä ja niistä kolme on
transkriptiotekijää.(Kirjoitin ryhmät edelliseen tekstiin juuri näkyville tänään netistä)
ZZZ ryhmä:
Tärkeimpinä tai
tutkituimpina mainitaan:HERC2, NBR1 ja CREBBP.
Nyt Duodecim, joka on vastikään tullut, kertoo
eräästä proteiinista , joka kuuluu aggresomia muodostaviin ja sen nimi on CPEB. Kun tarkistan sen ryhmän, se näyttää
kuuluvaan erään artikkelin mukaan ZZ_ tyyppisiin ZNF- proteiineihin, joten se on "ZZZ"
nimistä ryhmää, vaikka juuri sen nimisenä en sitä löydä
näistä aiemmin mainituista 18sta.
Ensinnä lisätieto PubMed hakulaitteella tästä geenistä englanniksi. Suomalaisen selityksen saa Duodecimista ja otan siitäkin myöhemmin sitaattia muistiin.
GEENI ”CPEB” : Cytoplasmic polyadenylation element-binding protein 1 (15q25.2)
- Also known as CPEB; CPEB-1; h-CPEB; CPE-BP1; hCPEB-1
- Summary. This gene encodes a member of the cytoplasmic polyadenylation element binding protein family. This highly conserved protein binds to a specific RNA sequence, called the cytoplasmic polyadenylation element, found in the 3' untranslated region of some mRNAs. The encoded protein functions in both the cytoplasm and the nucleus. It is involved in the regulation of mRNA translation, as well as processing of the 3' untranslated region, and may play a role in cell proliferation and tumorigenesis. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014] Expression. Biased expression in testis (RPKM 19.2), brain (RPKM 6.3) and 8 other tissues See more Orthologs mouse all
- Preferred Names
- cytoplasmic polyadenylation element-binding protein 1
- Names
- CPE-binding protein 1"
(Peptidisekvenssistä ja historiasta. Isoformi 2)
(Konservoidut domeenit)
- Konserved Domains (4) summary
-
cd12723
Location:234 → 341 - RRM1_CPEB1; RNA recognition motif 1 in cytoplasmic polyadenylation element-binding protein 1 (CPEB-1) and similar proteins
-
cd12725
Location:352 → 437 - RRM2_CPEB1; RNA recognition motif 2 in cytoplasmic polyadenylation element-binding protein 1 (CPEB-1) and similar proteins
-
pfam16366
Location:429 → 484 - CEBP_ZZ; Cytoplasmic polyadenylation element-binding protein ZZ domain
-
pfam16368
Location:1 → 232 - CEBP1_N; Cytoplasmic polyadenylation element-binding protein 1 N-terminus
(Suom) CPEB-proteiinin C-terminaalinen alue on ZZ-_domeeni, jolla on kyky tehdä proteiini-proteiini-interaktioita.
- J Mol Biol. 2013 Jun 12;425(11):2015-2026. doi: 10.1016/j.jmb.2013.03.009. Epub 2013 Mar 13.
- The C-terminal region of cytoplasmic polyadenylation element binding protein is a ZZ domain with potential for protein-protein interactions. Merkel DJ1, Wells SB1, Hilburn BC1, Elazzouzi F1, Pérez-Alvarado GC1, Lee BM2
- Cytoplasmic polyadenylation element binding protein (CPEB) provides temporal and spatial control of protein synthesis required for early development and neuronal synaptic plasticity. CPEB regulates protein expression by inhibiting polyadenylation of selected mRNA transcripts, which prevents binding of the ribosome for protein synthesis.
- Two RNA recognition motif domains and a C-terminal binuclear zinc-binding domain are required for mRNA binding, but the zinc-binding domain is not required for sequence-specific recognition of the targeted mRNA transcript.
- The structure and function of the zinc-binding domain of CPEB are unknown (2013).
- The C-terminal region of CPEB may participate in assembly of the ribonucleoprotein complex that includes the scaffold protein, Symplekin, and the cleavage and polyadenylation specificity factor. Sumoylation of Symplekin is required for polyadenylation, and both cleavage and polyadenylation specificity factor and poly(A) polymerase are sumoylated.
- The foreshortened poly(A) tail is maintained by poly(A) ribonuclease, which associates with CPEB.
- While zinc-binding domains are renowned for nucleic acid recognition, binuclear zinc-binding structural motifs, such as LIM (Lin-11, Isl-1, Mec-3), RING (really interesting new gene), PHD (plant homeodomain) and ZZ (ZZ-type zinc finger) domains, participate in protein-protein interactions.
- Here, we report the solution structure of the C-terminal zinc-binding domain of CPEB1 (CPEB1-ZZ), which has a cross-braced zinc binding topology.
- The structural similarity to other ZZ domains suggests that the CPEB1-ZZ domain recruits sumoylated proteins during assembly of the ribonucleoprotein complex prior to mRNA export from the nucleus.
PMID:
23500490
DOI:
(RAKENNE, HISTORIAPubMed Geenilähteestä Tämä on isoformi2 ja siinä on aminohappoja 491)
LOCUS NP_001073001 491 aa linear PRI 03-JUN-2018 DEFINITION cytoplasmic polyadenylation element-binding protein 1 isoform 2 [Homo sapiens]. ACCESSION NP_001073001 VERSION NP_001073001.1 DBSOURCE REFSEQ: accession NM_001079533.1 KEYWORDS RefSeq. SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 491) AUTHORS Shin J, Paek KY, Ivshina M, Stackpole EE and Richter JD. TITLE Essential role for non-canonical poly(A) polymerase GLD4 in cytoplasmic polyadenylation and carbohydrate metabolism JOURNAL Nucleic Acids Res. 45 (11), 6793-6804 (2017) PUBMED 28383716 REFERENCE 2 (residues 1 to 491) AUTHORS Batra R, Stark TJ, Clark E, Belzile JP, Wheeler EC, Yee BA, Huang H, Gelboin-Burkhart C, Huelga SC, Aigner S, Roberts BT, Bos TJ, Sathe S, Donohue JP, Rigo F, Ares M Jr, Spector DH and Yeo GW. TITLE RNA-binding protein CPEB1 remodels host and viral RNA landscapes JOURNAL Nat. Struct. Mol. Biol. 23 (12), 1101-1110 (2016) PUBMED 27775709 REMARK GeneRIF: The host RNA-binding protein CPEB1 was highly induced after cytomegalovirus infection and ectopic expression of CPEB1 in non-infected cells recapitulated infection-related post-transcriptional changes. CPEB1 was also required for poly(A)-tail lengthening of viral RNAs important for productive infection. REFERENCE 3 (residues 1 to 491) AUTHORS Galardi S, Petretich M, Pinna G, D'Amico S, Loreni F, Michienzi A, Groisman I and Ciafre SA. TITLE CPEB1 restrains proliferation of Glioblastoma cells through the regulation of p27(Kip1) mRNA translation JOURNAL Sci Rep 6, 25219 (2016) PUBMED 27142352 REMARK GeneRIF: Upon binding to p27(Kip1) 3'UTR, CPEB1 promotes elongation of poly-A tail and the subsequent translation of p27(Kip1) mRNA. This leads to higher levels of p27(Kip1) in the cell, in turn significantly inhibiting cell proliferation, and confers to CPEB1 a potential value as a tumor suppressor in Glioblastoma. Publication Status: Online-Only REFERENCE 4 (residues 1 to 491) AUTHORS Chen M, Zheng W and Wolynes PG. TITLE Energy landscapes of a mechanical prion and their implications for the molecular mechanism of long-term memory JOURNAL Proc. Natl. Acad. Sci. U.S.A. 113 (18), 5006-5011 (2016) PUBMED 27091989 REMARK GeneRIF: This mechanical catalysis makes possible a positive feedback loop that would help localize the formation of CPEB fibers to active synapse areas and mark those synapses for forming a long-term memory after the prion form is established. The functional role of the CPEB helical oligomers in this mechanism carries with it implications for targeting such species in neurodegenerative diseases. REFERENCE 5 (residues 1 to 491) AUTHORS Kratassiouk G, Pritchard LL, Cuvellier S, Vislovukh A, Meng Q, Groisman R, Degerny C, Deforzh E, Harel-Bellan A and Groisman I. TITLE The WEE1 regulators CPEB1 and miR-15b switch from inhibitor to activators at G2/M JOURNAL Cell Cycle 15 (5), 667-677 (2016) PUBMED 27027998 REMARK GeneRIF: WEE1 is regulated at the translational level by CPEB1 and miR-15b in a coordinated and cell-cycle-dependent manner. REFERENCE 6 (residues 1 to 491) AUTHORS Hagele S, Kuhn U, Boning M and Katschinski DM. TITLE Cytoplasmic polyadenylation-element-binding protein (CPEB)1 and 2 bind to the HIF-1alpha mRNA 3'-UTR and modulate HIF-1alpha protein expression JOURNAL Biochem. J. 417 (1), 235-246 (2009) PUBMED 18752464 REFERENCE 7 (residues 1 to 491) AUTHORS Sasayama T, Marumoto T, Kunitoku N, Zhang D, Tamaki N, Kohmura E, Saya H and Hirota T. TITLE Over-expression of Aurora-A targets cytoplasmic polyadenylation element binding protein and promotes mRNA polyadenylation of Cdk1 and cyclin B1 JOURNAL Genes Cells 10 (7), 627-638 (2005) PUBMED 15966895 REFERENCE 8 (residues 1 to 491) AUTHORS Wilczynska A, Aigueperse C, Kress M, Dautry F and Weil D. TITLE The translational regulator CPEB1 provides a link between dcp1 bodies and stress granules JOURNAL J. Cell. Sci. 118 (Pt 5), 981-992 (2005) PUBMED 15731006 REMARK GeneRIF: CPEB1 has a role in compartmentalization of mRNA metabolism in the cytoplasm, between dcp1 bodies and stress granules REFERENCE 9 (residues 1 to 491) AUTHORS Mendez R and Richter JD. TITLE Translational control by CPEB: a means to the end JOURNAL Nat. Rev. Mol. Cell Biol. 2 (7), 521-529 (2001) PUBMED 11433366 REMARK Review article REFERENCE 10 (residues 1 to 491) AUTHORS Welk JF, Charlesworth A, Smith GD and MacNicol AM. TITLE Identification and characterization of the gene encoding human cytoplasmic polyadenylation element binding protein JOURNAL Gene 263 (1-2), 113-120 (2001) PUBMED 11223249 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from DA705313.1, AF329403.1, AC010724.6 and AL832156.1. Summary: This gene encodes a member of the cytoplasmic polyadenylation element binding protein family. This highly conserved protein binds to a specific RNA sequence, called the cytoplasmic polyadenylation element, found in the 3' untranslated region of some mRNAs. The encoded protein functions in both the cytoplasm and the nucleus. It is involved in the regulation of mRNA translation, as well as processing of the 3' untranslated region, and may play a role in cell proliferation and tumorigenesis. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]. Transcript Variant: This variant (2), also known as short, contains a distinct 5' UTR, lacks an in-frame portion of the 5' coding region, and uses an alternate in-frame splice site in the central coding region, compared to variant 1. The resulting isoform (2) has a shorter N-terminus and lacks a central 5 aa segment, compared to isoform 1. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AF329403.1, SRR1660807.143381.1 [ECO:0000332] RNAseq introns :: mixed/partial sample support SAMEA1965299, SAMEA1966682 [ECO:0000350] ##Evidence-Data-END## FEATURES Location/Qualifiers source 1..491 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="15" /map="15q25.2" Protein 1..491 /product="cytoplasmic polyadenylation element-binding protein 1 isoform 2" /note="CPE-binding protein 1" /calculated_mol_wt=54032 Region <1 ..232="" cdd="" cddsrv.cgi="" db_xref="CDD:<a href=" https:="" note="Cytoplasmic polyadenylation element-binding protein 1 N-terminus; pfam16368" region_name="CEBP1_N" tructure="" uid="292978" www.ncbi.nlm.nih.gov="">2929781>" Region 234..341 /region_name="RRM1_CPEB1" /note="RNA recognition motif 1 in cytoplasmic polyadenylation element-binding protein 1 (CPEB-1) and similar proteins; cd12723" /db_xref="CDD:241167"
Region 352..437 /region_name="RRM2_CPEB1" /note="RNA recognition motif 2 in cytoplasmic polyadenylation element-binding protein 1 (CPEB-1) and similar proteins; cd12725" /db_xref="CDD:241169"
Region 429..484 /region_name="CEBP_ZZ" /note="Cytoplasmic polyadenylation element-binding protein ZZ domain; pfam16366" /db_xref="CDD:292976" CDS 1..491 /gene="CPEB1" /gene_synonym="CPE-BP1; CPEB; CPEB-1; h-CPEB; hCPEB-1" /coded_by="NM_001079533.1:226..1701" /note="isoform 2 is encoded by transcript variant 2" /db_xref="CCDS:CCDS42072.2" /db_xref="GeneID:64506" /db_xref="HGNC:HGNC:21744" /db_xref="MIM:607342"
ORIGIN 1 mlfptsaqes srglpdandl clglqslslt gwdrpwstqd sdssaqssth svlsmlhnpl 61 gnvlgkppls flpldplgsd lvdkfpapsv rgsrldtrpi ldsrssspsd sdtsgfssgs 121 dhlsdlissl rispplpfls lsgggprdpl kmgvgsrmdq eqaalaavtp sptsaskrwp 181 gasvwpswdl leapkdpfsi erearlhrqa aavneatctw sgqlpprnyk npiysckvfl 241 ggvpwditea glvntfrvfg slsvewpgkd gkhprcppkg nmpkgyvylv feleksvrsl 301 lqacshdpls pdglseyyfk mssrrmrcke vqvipwvlad snfvrspsqr ldpsrtvfvg 361 alhgmlnaea laailndlfg gvvyagidtd khkypigsgr vtfnnqrsyl kavsaafvei 421 kttkftkkvq idpyledslc hicssqpgpf fcrdqvcfky fcrscwhwrh smeglrhhsp 481 lmrnqknrds s //
(Kliinisempää tekstiä löytää PubMed artikkeleista. Merkel et al. kirjoittamaan koetan asettaa suomennosta , koska se kuvaa ZZZ ryhmään kuuluvan proteiinin rakennetta).
Related articles in PubMed ( About CPEB1)
-
RNA-binding protein CPEB1 remodels host and viral RNA landscapes. Batra R, et al. Nat Struct Mol Biol, 2016 Dec. PMID 27775709, Free PMC Article
-
Energy landscapes of a mechanical prion and their implications for the molecular mechanism of long-term memory. Chen M, et al. Proc Natl Acad Sci U S A, 2016 May 3. PMID 27091989, Free PMC Article
-
Specificity factors in cytoplasmic polyadenylation. Charlesworth A, et al. Wiley Interdiscip Rev RNA, 2013 Jul-Aug. PMID 23776146, Free PMC Article
-
The C-terminal region of cytoplasmic polyadenylation element binding protein is a ZZ domain with potential for protein-protein interactions. Merkel DJ, et al. J Mol Biol, 2013 Jun 12. PMID 23500490
-
Translational
control of cell growth and malignancy by the CPEBs. D'Ambrogio
A, et al. Nat Rev Cancer, 2013 Apr. PMID 23446545
GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?
(Onkohan CPEB 2,3,4
myös ZZZ? Onkohan nämä neuronivälittäjäaineita? Otan vain linkit esiin tähän musitakin.
About CPEB2
CPBE2 näyttää toimivan CPEB1:n
vahvistajana.
About CPEB3
CPEB3
Funktionaalinen prioni, josta on hyötyä.
Abstract
The mouse cytoplasmic polyadenylation element-binding protein 3
(CPEB3) is a translational regulator implicated in long-term memory
maintenance. Invertebrate orthologs of CPEB3 in Aplysia and
Drosophila are functional prions that are physiologically active in
the aggregated state. To determine if this principle applies to the
mammalian CPEB3, we expressed it in yeast and found that it forms
heritable aggregates that are the hallmark of known prions. In
addition, we confirm in the mouse the importance of CPEB3's prion
formation for CPEB3 function. Interestingly, deletion analysis of the
CPEB3 prion domain uncovered a tripartite organization: two
aggregation-promoting domains surround a regulatory module that
affects interaction with the actin cytoskeleton. In all, our data
provide direct evidence that CPEB3 is a functional prion in the
mammalian brain and underline the potential importance of an
actin/CPEB3 feedback loop for the synaptic plasticity underlying the
persistence of long-term memory.PMID:26074072
- DOI:10.1016/j.celrep.2015.04.060
- [Indexed for MEDLINE] Free full text
About CPEB4
(CPEB4:n circadinen ja UPR kontrolli välittää translationaalista vastetta, joka vastavaikuttaa maksan rasvoittumiseen ER-stressin aikana, kun on suuri vaatimus ER-proteiinien laskostamisest). .
Alla oleva linkki käsittää tekstiä CPB4.stä
ticle
|
Published:
Circadian- and UPR-dependent control of CPEB4 mediates a translational response to counteract hepatic steatosis under ER stress
The cytoplasmic polyadenylation element-binding (CPEB) proteins
regulate pre-mRNA processing and translation of CPE-containing
mRNAs in early embryonic development and synaptic activity.
However, specific functions in adult organisms are poorly
understood. Here we show that CPEB4 is required for adaptation
to high-fat-diet- and ageing-induced endoplasmic reticulum (ER)
stress, and subsequent hepatosteatosis. Stress-activated liver
CPEB4 expression is dual-mode regulated. First, Cpeb4 mRNA
transcription is controlled by the circadian clock, and then its
translation is regulated by the unfolded protein response (UPR)
through upstream open reading frames within the 5′UTR. Thus, the
CPEB4 protein is synthesized only following ER stress but the
induction amplitude is circadian. In turn, CPEB4 activates a second
wave of UPR translation required to maintain ER and mitochondrial
homeostasis. Our results suggest that combined transcriptional and
translational Cpeb4 regulation generates a ‘circadian
mediator’, which coordinates hepatic UPR activity with periods of
high ER-protein-folding demand. Accordingly, CPEB4 deficiency
results in non-alcoholic fatty liver disease.
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