ATF3

ATF3
Identifikatori
Aliasi	ATF3
Vanjski ID-jevi	OMIM: 603148 MGI: 109384 HomoloGene: 1265 GeneCards: ATF3
Lokacija gena (čovjek)
Hrom.	Hromosom 1 (čovjek)
Kraj	212,620,777 bp
Lokacija gena (miš)
Hrom.	Hromosom 1 (miš)
Kraj	190,950,236 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• GO:0000975 transcription cis-regulatory region binding; • protein homodimerization activity; • GO:0001948, GO:0016582 vezivanje za proteine; • RNA polymerase II transcription regulatory region sequence-specific DNA binding; • GO:0001078, GO:0001214, GO:0001206 DNA-binding transcription repressor activity, RNA polymerase II-specific; • protein heterodimerization activity; • vezivanje identičnih proteina; • GO:0001077, GO:0001212, GO:0001213, GO:0001211, GO:0001205 DNA-binding transcription activator activity, RNA polymerase II-specific; • vezivanje sa DNK; • GO:0001106 transcription corepressor activity; • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity; • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding; • GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific;
Ćelijska komponenta	• Jedarce; • nukleoplazma; • CHOP-ATF3 complex; • jedro;
Biološki proces	• GO:0044324, GO:0003256, GO:1901213, GO:0046019, GO:0046020, GO:1900094, GO:0061216, GO:0060994, GO:1902064, GO:0003258, GO:0072212 regulation of transcription by RNA polymerase II; • positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; • positive regulation of cell population proliferation; • skeletal muscle cell differentiation; • regulation of transcription from RNA polymerase II promoter in response to arsenic-containing substance; • Glukoneogeneza; • cellular response to amino acid starvation; • GO:0045996 negative regulation of transcription, DNA-templated; • GO:0009373 regulation of transcription, DNA-templated; • positive regulation of TRAIL-activated apoptotic signaling pathway; • transcription, DNA-templated; • GO:1901313 positive regulation of gene expression; • PERK-mediated unfolded protein response; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • negative regulation of ERK1 and ERK2 cascade; • GO:1901227 negative regulation of transcription by RNA polymerase II; • endoplasmic reticulum unfolded protein response; • transcription by RNA polymerase II; • positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway;
	Izvori:Amigo / QuickGO
Ortolozi
	467
	11910
	ENSG00000162772
	ENSMUSG00000026628
	P18847
	Q60765
NM_001030287; NM_001040619; NM_001206484; NM_001206485; NM_001206486;
	NM_001206488; NM_001674; NM_004024
	NM_007498
NP_001025458; NP_001035709; NP_001193413; NP_001193415; NP_001193417;
	NP_001665
	NP_031524
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

CAMP-ovisni transkripcijski faktor ATF-3 jest protein koji je kod ljudi kodiran genom ATF3 sa hromosoma 1.^[5]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 181 aminokiselina, a molekulska težina 20.576 Da.^[6]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MMLQHPGQVS	ASEVSASAIV	PCLSPPGSLV	FEDFANLTPF	VKEELRFAIQ
NKHLCHRMSS	ALESVTVSDR	PLGVSITKAE	VAPEEDERKK	RRRERNKIAA
AKCRNKKKEK	TECLQKESEK	LESVNAELKA	QIEELKNEKQ	HLIYMLNLHR
PTCIVRAQNG	RTPEDERNLF	IQQIKEGTLQ	S

Funkcija

Aktivirajući transkripcijski faktor 3 je član porodice proteina transkripcijskih faktora aktivacije sisarakog/cAMP koji reaguje na elemente koji vezuju (CREB). Za ovaj gen pronađeno je više varijanti transkripta, koje kodiraju dvije različite izoforme. Duža izoformi potiskuje, a ne aktivira transkripciju sa promotora sa ATF veznim elementima. Kraćoj izoformi (deltaZip2) nedostaje leucinski zatvarač, motiv dimerizacije proteina i ne vezuje se za DNK, a stimulira transkripciju, pretpostavlja se, izdvajanjem inhibitornih kofaktora od promotora. Moguće je da alternativna prerada ATF3 gena može biti fiziološki važna u regulaciji ciljnih gena.^[7]

Klinički značaj

ATF-3 ie induciran fiziološkim stresom u različitim tkivima.^[8] Također je marker regeneracije nakon ozljede ganglijskih neurona dorzalnog korijena, jer ozlijeđeni regenerirajući neuroni aktiviraju ovaj transkripcijski faktor.^[9] Studije funkcionalne validacije pokazale su da ATF3 može promovirati regeneraciju perifernih neurona, ali nije sposoban promovirati regeneraciju neurona centralnog nervnog sistema.^[10]

Interakcije

Pokazalo se da je ATF3 u interakciji sa:

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000162772 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026628 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Chen BP, Liang G, Whelan J, Hai T (juni 1994). "ATF3 and ATF3 delta Zip. Transcriptional repression versus activation by alternatively spliced isoforms". The Journal of Biological Chemistry. 269 (22): 15819–26. doi:10.1016/S0021-9258(17)40754-X. PMID 7515060.
^ "UniProt, P18847" (jezik: en.). Pristupljeno 7. 12. 2021.CS1 održavanje: nepoznati jezik (link)
^ "Entrez Gene: ATF3 activating transcription factor 3".
^ ^a ^b ^c Chen BP, Wolfgang CD, Hai T (mart 1996). "Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10". Molecular and Cellular Biology. 16 (3): 1157–68. doi:10.1128/MCB.16.3.1157. PMC 231098. PMID 8622660.
^ Lindå H, Sköld MK, Ochsmann T (2011). "Activating transcription factor 3, a useful marker for regenerative response after nerve root injury". Frontiers in Neurology. 2: 30. doi:10.3389/fneur.2011.00030. PMC 3099310. PMID 21629765.
^ Mahar M, Cavalli V (juni 2018). "Intrinsic mechanisms of neuronal axon regeneration". Nature Reviews. Neuroscience (jezik: engleski). 19 (6): 323–337. doi:10.1038/s41583-018-0001-8. PMC 5987780. PMID 29666508.
^ Pearson AG, Gray CW, Pearson JF, Greenwood JM, During MJ, Dragunow M (decembar 2003). "ATF3 enhances c-Jun-mediated neurite sprouting". Brain Research. Molecular Brain Research. 120 (1): 38–45. doi:10.1016/j.molbrainres.2003.09.014. PMID 14667575.
^ Hai T, Curran T (maj 1991). "Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity". Proceedings of the National Academy of Sciences of the United States of America. 88 (9): 3720–4. Bibcode:1991PNAS...88.3720H. doi:10.1073/pnas.88.9.3720. PMC 51524. PMID 1827203.
^ Chu HM, Tan Y, Kobierski LA, Balsam LB, Comb MJ (januar 1994). "Activating transcription factor-3 stimulates 3',5'-cyclic adenosine monophosphate-dependent gene expression". Molecular Endocrinology. 8 (1): 59–68. doi:10.1210/mend.8.1.8152431. PMID 8152431.
^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (septembar 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
^ Yan C, Wang H, Boyd DD (mart 2002). "ATF3 represses 72-kDa type IV collagenase (MMP-2) expression by antagonizing p53-dependent trans-activation of the collagenase promoter". The Journal of Biological Chemistry. 277 (13): 10804–12. doi:10.1074/jbc.M112069200. PMID 11792711.
^ Kang Y, Chen CR, Massagué J (april 2003). "A self-enabling TGFbeta response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells". Molecular Cell. 11 (4): 915–26. doi:10.1016/s1097-2765(03)00109-6. PMID 12718878.

Dopunska literatura

Hai TW, Liu F, Coukos WJ, Green MR (decembar 1989). "Transcription factor ATF cDNA clones: an extensive family of leucine zipper proteins able to selectively form DNA-binding heterodimers". Genes & Development. 3 (12B): 2083–90. doi:10.1101/gad.3.12b.2083. PMID 2516827.
Kaszubska W, Hooft van Huijsduijnen R, Ghersa P, DeRaemy-Schenk AM, Chen BP, Hai T, DeLamarter JF, Whelan J (novembar 1993). "Cyclic AMP-independent ATF family members interact with NF-kappa B and function in the activation of the E-selectin promoter in response to cytokines". Molecular and Cellular Biology. 13 (11): 7180–90. doi:10.1128/MCB.13.11.7180. PMC 364779. PMID 7692236.
Chu HM, Tan Y, Kobierski LA, Balsam LB, Comb MJ (januar 1994). "Activating transcription factor-3 stimulates 3',5'-cyclic adenosine monophosphate-dependent gene expression". Molecular Endocrinology. 8 (1): 59–68. doi:10.1210/mend.8.1.8152431. PMID 8152431.
Liang G, Wolfgang CD, Chen BP, Chen TH, Hai T (januar 1996). "ATF3 gene. Genomic organization, promoter, and regulation". The Journal of Biological Chemistry. 271 (3): 1695–701. doi:10.1074/jbc.271.3.1695. PMID 8576171.
Chen BP, Wolfgang CD, Hai T (mart 1996). "Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10". Molecular and Cellular Biology. 16 (3): 1157–68. doi:10.1128/MCB.16.3.1157. PMC 231098. PMID 8622660.
Hagmeyer BM, Duyndam MC, Angel P, de Groot RP, Verlaan M, Elfferich P, van der Eb A, Zantema A (mart 1996). "Altered AP-1/ATF complexes in adenovirus-E1-transformed cells due to EIA-dependent induction of ATF3". Oncogene. 12 (5): 1025–32. PMID 8649793.
Allan AL, Albanese C, Pestell RG, LaMarre J (juli 2001). "Activating transcription factor 3 induces DNA synthesis and expression of cyclin D1 in hepatocytes". The Journal of Biological Chemistry. 276 (29): 27272–80. doi:10.1074/jbc.M103196200. PMID 11375399.
Zhang C, Kawauchi J, Adachi MT, Hashimoto Y, Oshiro S, Aso T, Kitajima S (decembar 2001). "Activation of JNK and transcriptional repressor ATF3/LRF1 through the IRE1/TRAF2 pathway is implicated in human vascular endothelial cell death by homocysteine". Biochemical and Biophysical Research Communications. 289 (3): 718–24. doi:10.1006/bbrc.2001.6044. PMID 11726207.
Yan C, Wang H, Boyd DD (mart 2002). "ATF3 represses 72-kDa type IV collagenase (MMP-2) expression by antagonizing p53-dependent trans-activation of the collagenase promoter". The Journal of Biological Chemistry. 277 (13): 10804–12. doi:10.1074/jbc.M112069200. PMID 11792711.
Shaheduzzaman S, Krishnan V, Petrovic A, Bittner M, Meltzer P, Trent J, Venkatesan S, Zeichner S (2002). "Effects of HIV-1 Nef on cellular gene expression profiles". Journal of Biomedical Science. 9 (1): 82–96. doi:10.1007/BF02256581. PMID 11810028.
Hashimoto Y, Zhang C, Kawauchi J, Imoto I, Adachi MT, Inazawa J, Amagasa T, Hai T, Kitajima S (juni 2002). "An alternatively spliced isoform of transcriptional repressor ATF3 and its induction by stress stimuli". Nucleic Acids Research. 30 (11): 2398–406. doi:10.1093/nar/30.11.2398. PMC 117192. PMID 12034827.
Kawauchi J, Zhang C, Nobori K, Hashimoto Y, Adachi MT, Noda A, Sunamori M, Kitajima S (oktobar 2002). "Transcriptional repressor activating transcription factor 3 protects human umbilical vein endothelial cells from tumor necrosis factor-alpha-induced apoptosis through down-regulation of p53 transcription". The Journal of Biological Chemistry. 277 (41): 39025–34. doi:10.1074/jbc.M202974200. PMID 12161427.
Zhang C, Gao C, Kawauchi J, Hashimoto Y, Tsuchida N, Kitajima S (oktobar 2002). "Transcriptional activation of the human stress-inducible transcriptional repressor ATF3 gene promoter by p53". Biochemical and Biophysical Research Communications. 297 (5): 1302–10. doi:10.1016/S0006-291X(02)02382-3. PMID 12372430.
Fan F, Jin S, Amundson SA, Tong T, Fan W, Zhao H, Zhu X, Mazzacurati L, Li X, Petrik KL, Fornace AJ, Rajasekaran B, Zhan Q (oktobar 2002). "ATF3 induction following DNA damage is regulated by distinct signaling pathways and over-expression of ATF3 protein suppresses cells growth". Oncogene. 21 (49): 7488–96. doi:10.1038/sj.onc.1205896. PMID 12386811.
Nobori K, Ito H, Tamamori-Adachi M, Adachi S, Ono Y, Kawauchi J, Kitajima S, Marumo F, Isobe M (oktobar 2002). "ATF3 inhibits doxorubicin-induced apoptosis in cardiac myocytes: a novel cardioprotective role of ATF3". Journal of Molecular and Cellular Cardiology. 34 (10): 1387–97. doi:10.1006/jmcc.2002.2091. PMID 12392999.
Kang Y, Chen CR, Massagué J (april 2003). "A self-enabling TGFbeta response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells". Molecular Cell. 11 (4): 915–26. doi:10.1016/S1097-2765(03)00109-6. PMID 12718878.
Newman JR, Keating AE (juni 2003). "Comprehensive identification of human bZIP interactions with coiled-coil arrays". Science. 300 (5628): 2097–101. Bibcode:2003Sci...300.2097N. doi:10.1126/science.1084648. PMID 12805554. S2CID 36715183.
Kool J, Hamdi M, Cornelissen-Steijger P, van der Eb AJ, Terleth C, van Dam H (juli 2003). "Induction of ATF3 by ionizing radiation is mediated via a signaling pathway that includes ATM, Nibrin1, stress-induced MAPkinases and ATF-2". Oncogene. 22 (27): 4235–42. doi:10.1038/sj.onc.1206611. PMID 12833146.

Vanjski linkovi

Lokacija ljudskog genoma ATF3 i stranica sa detaljima o genu ATF3 u UCSC Genome Browseru.
ATF3 protein, human na US National Library of Medicine Medical Subject Headings (MeSH)

Ovaj članak uključuje tekst iz Nacionalne medicinske biblioteke Sjedinjenih Država, koji je u javnom vlasništvu.

MMP2, adiponektin^[1]

^ Koh EH, Park JY, Park HS, Jeon MJ, Ryu JW, Kim M, Kim SY, Kim MS, Kim SW, Park IS, Youn JH, Lee KU (decembar 2007). "Essential role of mitochondrial function in adiponectin synthesis in adipocytes". Diabetes. 56 (12): 2973–81. doi:10.2337/db07-0510. PMID 17827403.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000162772 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000026628 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7515060-5] Chen BP, Liang G, Whelan J, Hai T (juni 1994). "ATF3 and ATF3 delta Zip. Transcriptional repression versus activation by alternatively spliced isoforms". The Journal of Biological Chemistry. 269 (22): 15819–26. doi:10.1016/S0021-9258(17)40754-X. PMID 7515060.

[UniProt-6] "UniProt, P18847" (jezik: en.). Pristupljeno 7. 12. 2021.CS1 održavanje: nepoznati jezik (link)

[entrez-7] "Entrez Gene: ATF3 activating transcription factor 3".

[pmid8622660-8] Chen BP, Wolfgang CD, Hai T (mart 1996). "Analysis of ATF3, a transcription factor induced by physiological stresses and modulated by gadd153/Chop10". Molecular and Cellular Biology. 16 (3): 1157–68. doi:10.1128/MCB.16.3.1157. PMC 231098. PMID 8622660.

[pmid21629765-9] Lindå H, Sköld MK, Ochsmann T (2011). "Activating transcription factor 3, a useful marker for regenerative response after nerve root injury". Frontiers in Neurology. 2: 30. doi:10.3389/fneur.2011.00030. PMC 3099310. PMID 21629765.

[10] Mahar M, Cavalli V (juni 2018). "Intrinsic mechanisms of neuronal axon regeneration". Nature Reviews. Neuroscience (jezik: engleski). 19 (6): 323–337. doi:10.1038/s41583-018-0001-8. PMC 5987780. PMID 29666508.

[pmid14667575-11] Pearson AG, Gray CW, Pearson JF, Greenwood JM, During MJ, Dragunow M (decembar 2003). "ATF3 enhances c-Jun-mediated neurite sprouting". Brain Research. Molecular Brain Research. 120 (1): 38–45. doi:10.1016/j.molbrainres.2003.09.014. PMID 14667575.

[pmid1827203-12] Hai T, Curran T (maj 1991). "Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity". Proceedings of the National Academy of Sciences of the United States of America. 88 (9): 3720–4. Bibcode:1991PNAS...88.3720H. doi:10.1073/pnas.88.9.3720. PMC 51524. PMID 1827203.

[pmid8152431-13] Chu HM, Tan Y, Kobierski LA, Balsam LB, Comb MJ (januar 1994). "Activating transcription factor-3 stimulates 3',5'-cyclic adenosine monophosphate-dependent gene expression". Molecular Endocrinology. 8 (1): 59–68. doi:10.1210/mend.8.1.8152431. PMID 8152431.

[pmid16169070-14] Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (septembar 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.

[pmid11792711-15] Yan C, Wang H, Boyd DD (mart 2002). "ATF3 represses 72-kDa type IV collagenase (MMP-2) expression by antagonizing p53-dependent trans-activation of the collagenase promoter". The Journal of Biological Chemistry. 277 (13): 10804–12. doi:10.1074/jbc.M112069200. PMID 11792711.

[pmid12718878-16] Kang Y, Chen CR, Massagué J (april 2003). "A self-enabling TGFbeta response coupled to stress signaling: Smad engages stress response factor ATF3 for Id1 repression in epithelial cells". Molecular Cell. 11 (4): 915–26. doi:10.1016/s1097-2765(03)00109-6. PMID 12718878.

[pmid17827403_group_=_note-17] Koh EH, Park JY, Park HS, Jeon MJ, Ryu JW, Kim M, Kim SY, Kim MS, Kim SW, Park IS, Youn JH, Lee KU (decembar 2007). "Essential role of mitochondrial function in adiponectin synthesis in adipocytes". Diabetes. 56 (12): 2973–81. doi:10.2337/db07-0510. PMID 17827403.

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