(2019) Pre-eklampsian vakavuus riippuu tästä EGLN1-geenistä sikäli, että se voi mutatoitua.
(2018) EGLN1-geenin puute ko-operoi BRAF:in kanssa melanomageneesissä. (B-Raf https://en.wikipedia.org/wiki/BRAF_(gene). Luomen muuttuessa melanomaksi PHD2 proteiinin määrä on alentunut ja PHD2- geeni alassäätynyt taudin pahemmassa kulussa.
(2018) EGLN1 assosioituu ihmisen adaptaatiokykyyn vuoristom alempaan happipitoisuuteen ja altistukseen fysiologiselle alentuneelle happipitoisuudelle ja happiosapaineeseelle ( hypobaariselle hypoxialle)
(2017) Ferroptoosia estää EGL1/c-Myc- indusoima kromatiinin moduloijan LSH, lymfoidispesifisen helikaasin. LSH pystyy estämään ferroptoosin lipidiaineenvaihdunnan geeniexpressiota säätelmällä. (Deubikitinaasi, joka puolestaan stabiloi LSH:n on UCHL3)
EGLN1/c-Myc Induced Lymphoid-Specific Helicase Inhibits Ferroptosis
through Lipid Metabolic Gene Expression Changes.
(2001) Semenza: HIF and 3 PHD HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the
nucleus
(2001) EGL geeniperheen luonnehdinta.(2000) SM-20 geenihomologi (C1orf12) luonnehdittu.
(1996) SM-20 on 40 kD kokoinen proteiini, jonka geeni-ilmenemä on rajoittunut arterian sisäpinnalle sileässä lihaksessa (Smooth Muscle).
Tässä
ZMYND6 (1q42.2)
https://www.ncbi.nlm.nih.gov/gene/54583
- Official Symbol
- EGLN1provided by HGNC
- Official Full Name
- egl-9 family hypoxia inducible factor 1provided by HGNC
- Also known as
- HPH2; PHD2; SM20; ECYT3; HALAH; HPH-2; HIFPH2; ZMYND6; C1orf12; HIF-PH2
- Summary
- The protein encoded by this gene catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. HIF is a transcriptional complex that plays a central role in mammalian oxygen homeostasis. This protein functions as a cellular oxygen sensor, and under normal oxygen concentration, modification by prolyl hydroxylation is a key regulatory event that targets HIF subunits for proteasomal destruction via the von Hippel-Lindau ubiquitylation complex. Mutations in this gene are associated with erythrocytosis familial type 3 (ECYT3). [provided by RefSeq, Nov 2009]
- Expression
- Ubiquitous expression in kidney (RPKM 11.5), brain (RPKM 11.3) and 25 other tissues See more
- Preferred Names
- egl nine homolog 1
- Names
- HIF-prolyl hydroxylase 2
- egl nine-like protein 1
- hypoxia-inducible factor prolyl hydroxylase 2
- prolyl hydroxylase domain-containing protein 2
- zinc finger MYND domain-containing protein 6
- smart00702
Location:220 → 391 - P4Hc; Prolyl 4-hydroxylase alpha subunit homologues
- pfam01753
Location:21 → 58 - zf-MYND;
(otan koko peptiditekstin)
egl nine homolog 1 [Homo sapiens]
NCBI Reference Sequence: NP_071334.1
LOCUS NP_071334 426 aa linear PRI 03-SEP-2019 DEFINITION egl nine homolog 1 [Homo sapiens]. ACCESSION NP_071334 VERSION NP_071334.1 DBSOURCE REFSEQ: accession NM_022051.2 KEYWORDS RefSeq; RefSeq Select. 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 426) AUTHORS Kumar K S P, Arcot M, Munisamaiah M and Balakrishna S. TITLE Novel association of SNP rs479200 in EGLN1 gene with predisposition to preeclampsia JOURNAL Gene 705, 1-4 (2019) PUBMED 31009679 REMARK GeneRIF: Results show that SNP rs479200 in EGLN1 gene is associated with the predisposition to preeclampsia and this association is modified by the severity. REFERENCE 2 (residues 1 to 426) AUTHORS Liu S, Zhang G, Guo J, Chen X, Lei J, Ze K, Dong L, Dai X, Gao Y, Song D, Ecker BL, Yang R, Feltcher C, Peng K, Feng C, Chen H, Lee RX, Kerestes H, Niu J, Kumar S, Xu W, Zhang J, Wei Z, Martin JS, Liu X, Mills G, Lu Y, Guo W, Sun L, Zhang L, Weeraratna A, Herlyn M, Wei W, Lee FS and Xu X. TITLE Loss of Phd2 cooperates with BRAF(V600E) to drive melanomagenesis JOURNAL Nat Commun 9 (1), 5426 (2018) PUBMED 30575721 REMARK GeneRIF: During the transition of nevi to melanoma, the expression of PHD2 protein is significantly decreased, and lower expression of PHD2 in melanoma is associated with worse clinical outcome. Knockdown of PHD2 leads to elevated Akt phosphorylation in melanocytes. Erratum:[Nat Commun. 2019 Mar 11;10(1):1211. PMID: 30858377] Publication Status: Online-Only REFERENCE 3 (residues 1 to 426) AUTHORS Abboud MI, Chowdhury R, Leung IKH, Lippl K, Loenarz C, Claridge TDW and Schofield CJ. TITLE Studies on the Substrate Selectivity of the Hypoxia-Inducible Factor Prolyl Hydroxylase 2 Catalytic Domain JOURNAL Chembiochem 19 (21), 2262-2267 (2018) PUBMED 30144273 REMARK GeneRIF: The overall results indicate how the Hypoxia-Inducible Factor Prolyl Hydroxylase 2 Catalytic Domain achieves selectivity for HIFalpha oxygen-dependent degradation domains. REFERENCE 4 (residues 1 to 426) AUTHORS Yasukochi Y, Nishimura T, Motoi M and Watanuki S. TITLE Association of EGLN1 genetic polymorphisms with SpO2 responses to acute hypobaric hypoxia in a Japanese cohort JOURNAL J Physiol Anthropol 37 (1), 9 (2018) PUBMED 29625625 REMARK GeneRIF: Studied the association between SNPs around the EGLN1 genomic region, possibly involved in high-altitude adaptation, and physiological changes to hypobaric hypoxia exposure in a cohort of Japanese lowlanders. Publication Status: Online-Only REFERENCE 5 (residues 1 to 426) AUTHORS Jiang Y, Mao C, Yang R, Yan B, Shi Y, Liu X, Lai W, Liu Y, Wang X, Xiao D, Zhou H, Cheng Y, Yu F, Cao Y, Liu S, Yan Q and Tao Y. TITLE EGLN1/c-Myc Induced Lymphoid-Specific Helicase Inhibits Ferroptosis through Lipid Metabolic Gene Expression Changes JOURNAL Theranostics 7 (13), 3293-3305 (2017) PUBMED 28900510 REMARK GeneRIF: This study elucidates the molecular basis of the c-Myc/EGLN1-mediated induction of LSH expression that inhibits ferroptosis Publication Status: Online-Only REFERENCE 6 (residues 1 to 426) AUTHORS Semenza GL.(NOBEL 2019!) TITLE HIF-1, O(2), and the 3 PHDs: how animal cells signal hypoxia to the nucleus JOURNAL Cell 107 (1), 1-3 (2001) PUBMED 11595178 REMARK Review article REFERENCE 7 (residues 1 to 426) AUTHORS Taylor MS. TITLE Characterization and comparative analysis of the EGLN gene family JOURNAL Gene 275 (1), 125-132 (2001) PUBMED 11574160 REFERENCE 8 (residues 1 to 426) AUTHORS Dupuy D, Aubert I, Duperat VG, Petit J, Taine L, Stef M, Bloch B and Arveiler B. TITLE Mapping, characterization, and expression analysis of the SM-20 human homologue, c1orf12, and identification of a novel related gene, SCAND2 JOURNAL Genomics 69 (3), 348-354 (2000) PUBMED 11056053 REFERENCE 9 (residues 1 to 426) AUTHORS Dominguez O, Ashhab Y, Sabater L, Belloso E, Caro P and Pujol-Borrell R. TITLE Cloning of ARE-containing genes by AU-motif-directed display JOURNAL Genomics 54 (2), 278-286 (1998) PUBMED 9828130 REFERENCE 10 (residues 1 to 426) AUTHORS Wax SD, Tsao L, Lieb ME, Fallon JT and Taubman MB. TITLE SM-20 is a novel 40-kd protein whose expression in the arterial wall is restricted to smooth muscle JOURNAL Lab. Invest. 74 (4), 797-808 (1996) PUBMED 8606489 COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AF229245.1, AL117352.12 and AI017372.1. This sequence is a reference standard in the RefSeqGene project. Summary: The protein encoded by this gene catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. HIF is a transcriptional complex that plays a central role in mammalian oxygen homeostasis. This protein functions as a cellular oxygen sensor, and under normal oxygen concentration, modification by prolyl hydroxylation is a key regulatory event that targets HIF subunits for proteasomal destruction via the von Hippel-Lindau ubiquitylation complex. Mutations in this gene are associated with erythrocytosis familial type 3 (ECYT3). [provided by RefSeq, Nov 2009]. 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 :: AF229245.1, AJ310543.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## RefSeq Select criteria :: based on conservation, expression,
(ZMYND6 - Proteiinin piirteitä): 426 amino acids longest protein
##RefSeq-Attributes-END## FEATURES Location/Qualifiers source 1..426 /organism="Homo sapiens" /db_xref="taxon:9606" /chromosome="1" /map="1q42.2" Protein 1..426 /product="egl nine homolog 1" /EC_number="1.14.11.29" /note="prolyl hydroxylase domain
-containing protein 2; zinc finger MYND domain-containing protein 6; hypoxia-inducible factor prolyl hydroxylase 2; egl nine-like protein 1; HIF-prolyl hydroxylase 2" /calculated_mol_wt=45890 Site 2 /site_type="acetylation" /experiment="experimental evidence, no additional details recorded" /note="N-acetylalanine. {ECO:0000244|PubMed:19413330, ECO:0000244|PubMed:22814378}; propagated from UniProtKB/Swiss-Prot (Q9GZT9.1)" Region 6..20 /region_name="Required for nuclear export" /experiment="experimental evidence, no additional details recorded" /note="propagated from UniProtKB/Swiss-Prot (Q9GZT9.1)" Site 12 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q9GZT9.1)" Region 21..58
ORIGIN 1 celcgkmenl lrCsrCrssf yCCkeHqrqd wkkHklvC /region_name="zf-MYND" /note="MYND finger; pfam01753" /db_xref="CDD:280009" Site 125 /site_type="phosphorylation" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine. {ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163}; propagated from UniProtKB/Swiss-Prot (Q9GZT9.1)" Site 201 /site_type="nitrosylation" /experiment="experimental evidence, no additional details recorded" /note="S-nitrosocysteine. {ECO:0000269|PubMed:21601578}; propagated from UniProtKB/Swiss-Prot (Q9GZT9.1)" Site 208 /site_type="nitrosylation" /experiment="experimental evidence, no additional details recorded" /note="S-nitrosocysteine. {ECO:0000269|PubMed:21601578}; propagated from UniProtKB/Swiss-Prot (Q9GZT9.1)" Region 220..391 /region_name="P4Hc" /note="Prolyl 4-hydroxylase alpha subunit homologues; smart00702" /db_xref="CDD:214780" Region 241..251 /region_name="Beta(2)beta(3) 'finger-like' loop. {ECO:0000269|PubMed:18063574}" /experiment="experimental evidence, no additional details recorded" /note="propagated from UniProtKB/Swiss-Prot (Q9GZT9.1)" Site 302 /site_type="nitrosylation" /experiment="experimental evidence, no additional details recorded" /note="S-nitrosocysteine. {ECO:0000269|PubMed:21601578}; propagated from UniProtKB/Swiss-Prot (Q9GZT9.1)" Site 323 /site_type="nitrosylation" /experiment="experimental evidence, no additional details recorded" /note="S-nitrosocysteine. {ECO:0000269|PubMed:21601578}; propagated from UniProtKB/Swiss-Prot (Q9GZT9.1)" Site 326 /site_type="nitrosylation" /experiment="experimental evidence, no additional details recorded" /note="S-nitrosocysteine. {ECO:0000269|PubMed:21601578}; propagated from UniProtKB/Swiss-Prot (Q9GZT9.1)" CDS 1..426 /gene="EGLN1" /gene_synonym="C1orf12; ECYT3; HALAH; HIF-PH2; HIFPH2; HPH-2; HPH2; PHD2; SM20; ZMYND6" /coded_by="NM_022051.2:3157..4437" /db_xref="CCDS:CCDS1595.1" /db_xref="GeneID:54583" /db_xref="HGNC:HGNC:1232" /db_xref="MIM:606425" ORIGIN 1 mandsggpgg pspserdrqy celcgkmenl lrcsrcrssf ycckehqrqd wkkhklvcqg 61 segalghgvg phqhsgpapp aavpppraga reprkaaarr dnasgdaakg kvkakppadp 121 aaaaspcraa aggqgsavaa eaepgkeepp arsslfqeka nlyppsntpg dalspggglr 181 pngqtkplpa lklaleyivp cmnkhgicvv ddflgketgq qigdevralh dtgkftdgql 241 vsqksdsskd irgdkitwie gkepgcetig llmssmddli rhcngklgsy kingrtkamv 301 acypgngtgy vrhvdnpngd grcvtciyyl nkdwdakvsg gilrifpegk aqfadiepkf 361 drllffwsdr rnphevqpay atryaitvwy fdaderarak vkyltgekgv rvelnkpsds 421 vgkdvf //
mikä on EGLN2 ja EGLN3? Onko niissä sinkkisormea.
Ilmeisesti ei . Dioxygenaasiriippuvuutta ja Ferro- rautatarvetta.
Kuitenkin kaikki kolme EGLN proteiinia toimivat HIF-prolyylihydroxylaaseina . Onko eroja kohde HIF- proteiinissa? ( Pitää hakea vastaus vielä)
EGLN2
https://www.ncbi.nlm.nih.gov/gene/112398
- Preferred Names
- egl nine homolog 2
- Names
- HIF-prolyl hydroxylase 1
- estrogen-induced tag 6
- hypoxia-inducible factor prolyl hydroxylase 1
- prolyl hydroxylase domain-containing protein 1
? Ei ole mainitaa sinkkisormesta. Sen sijaan on fosforylaatiokohta ja jokin beta-beta-sormi. Ilmeisesti ferrorauta kuuluu asiaan . Sen PHD4 domeenialayksiköstä mainitaan
"Prrolyl 4-hydroxylase alpha subunit homologues.
Mammalian
enzymes catalyse hydroxylation of collagen, for example. Prokaryotic
enzymes might catalyse hydroxylation of antibiotic peptides. These are
2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and
dioxygen as cosubstrates and ferrous iron as a cofactor".Entä EGLN3?
https://www.ncbi.nlm.nih.gov/gene/112399
https://www.ncbi.nlm.nih.gov/protein/NP_001295032.1
PUBMED 29339541 REMARK GeneRIF: This study links the oxygen sensor PHD3 to metastasis and drug resistance in cancer, with implications for therapeutic improvement by targeting this system.
- Official Full Name
- egl-9 family hypoxia inducible factor 3provided by HGNC
- Also known as
- PHD3; HIFPH3; HIFP4H3
- Expression
- Broad expression in skin (RPKM 31.3), heart (RPKM 27.7) and 16 other tissues See more
- Orthologs mouse all
- Preferred Names
- egl nine homolog 3
- Names
- HIF-PH3
- HIF-prolyl hydroxylase 3
- HPH-1
- HPH-3
- egl nine-like protein 3 isoform
- hypoxia-inducible factor prolyl hydroxylase 3
- prolyl hydroxylase domain-containing protein 3
-
Prolyl 4-hydroxylase alpha subunit homologues.Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.
- ..
- Voi taas ajatella kysyä toisinkin päin: Jos ZMYND6 , joka on Zf-MYND sinkkisormirakenteinen prolyylihydroksylaasi, onko muut ZMYND- protetiinit prolyylihydroksylaaseja?
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