HIST1H3C

HIST1H3C
Estruturas disponíveis
PDB	Pesquisa Human UniProt: PDBe RCSB
Lista de códigos id do PDB
	3WKJ, 3B95, 2C1J, 3AYW, 3WA9, 3U4S, 5AVB, 2CV5, 5AV5, 3U31, 2UXN, 3AZK, 2C1N, 5C11, 3QO2, 3X1V, 5C13, 4A0J, 4U68, 5AV8, 4LLB, 3U5O, 1O9S, 4FT2, 4HON, 3W99, 3ZVY, 4Z0R, 5AVC, 1CT6, 1Q3L, 3O37, 3W97, 3SOW, 3KMT, 4YM6, 4A7J, 3UEE, 2KWK, 4F4U, 3UEF, 3UIG, 4BD3, 3AZL, 4QBR, 4F56, 3AFA, 4LKA, 5CPK, 5FFV, 3V43, 5CH1, 3U5P, 3AZI, 3U5N, 3AZH, 3UIK, 4QBQ, 1U35, 4UY4, 2OT7, 5AV9, 2B2W, 3U3D, 3AZF, 3W98, 4I51, 4X3K, 4FWF, 2B2T, 2B2V, 4A0N, 2KWJ, 3WAA, 3QJ6, 5DAH, 3AZG, 3AZE, 3X1T, 3RIY, 2L75, 3A1B, 2VPG, 4QBS, 3O35, 5CPJ, 3ZG6, 4YM5, 3AZJ, 2RI7, 3AZN, 3AVR, 5CPI, 2LBM, 3W96, 3O34, 2M0O, 4L7X, 5CH2, 5AV6, 3AZM, 4UP0, 3X1S, 2OX0, 3UII, 3SOU, 4N4H, 4TN7, 1CS9, 3X1U, 4LXL, 2B2U, 2OQ6, 3RIG, 5C3I, 4YHP, 5B24, 5D6Y, 4YHZ, 4Z2M, 5HJD, 5HJC, 5HJB, 5B2I, 5HYN, 5FB0, 5FB1, 5IQL, 5B2J, 5JIN
Identificadores
Nomes alternativos	HIST1H3C
IDs externos	OMIM: 602812 HomoloGene: 134495 GeneCards: HIST1H3C
Ontologia genética
Função molecular	• DNA binding; • GO:0031493 histone binding; • GO:0001948, GO:0016582 ligação a proteínas plasmáticas; • protein heterodimerization activity; • cadherin binding; • nucleosomal DNA binding;
Componente celular	• membrane; • cariolinfa; • cromossoma; • extracellular region; • nuclear chromosome; • Exossoma; • nucleossoma; • núcleo celular; • GO:0009327 complexo macromolecular;
Processo biológico	• telomere organization; • epigenetic maintenance of chromatin in transcription-competent conformation; • protein heterotetramerization; • coagulação sanguínea; • GO:0034723 DNA replication-dependent chromatin assembly; • rDNA heterochromatin assembly; • negative regulation of gene expression, epigenetic; • GO:0031497, GO:0006336, GO:0034724, GO:0001301, GO:0007580, GO:0034652, GO:0010847 chromatin organization; • GO:1905616 regulation of gene silencing by miRNA; • nucleosome assembly; • interleukin-7-mediated signaling pathway; • regulation of megakaryocyte differentiation; • regulation of hematopoietic stem cell differentiation;
	Sources:Amigo / QuickGO
Ortólogos
	8352
	n/a
	ENSG00000278272
	n/a
	P68431
	n/a
	NM_003531
	n/a
	NP_066298; NP_003520; NP_003525; NP_003527
	n/a
	Wikidata
Ver/Editar Humano

Histone H3.1 é uma proteína que em humanos é codificada pelo gene HIST1H3C.^[2]^[3]^[4]^[5]

As histonas são proteínas nucleares básicas que são responsáveis pela estrutura dos nucleossomos da fibra cromossômica nos eucariotos. Duas moléculas de cada uma das quatro histonas do núcleo (H2A, H2B, H3 e H4) formam um octâmero, em torno do qual aproximadamente 146 pb de DNA é envolvido em unidades repetidas, chamadas nucleossomos. A histona ligante, H1, interage com o DNA ligante entre nucleossomos e funciona na compactação da cromatina em estruturas de ordem superior. Esse gene é sem intron e codifica um membro da família histona H3. Os transcritos desse gene não possuem caudas de poliA, contendo um elemento de terminação palindrômico. Esse gene é encontrado no grande agrupamento de genes de histonas no cromossomo 6.^[5]

Referências

↑ «Human PubMed Reference:»
↑ Kardalinou E, Eick S, Albig W, Doenecke D (dezembro de 1993). «Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones». Journal of Cellular Biochemistry. 52 (4): 375–83. PMID 8227173. doi:10.1002/jcb.240520402
↑ Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D (abril de 1997). «Human histone gene organization: nonregular arrangement within a large cluster». Genomics. 40 (2): 314–22. PMID 9119399. doi:10.1006/geno.1996.4592
↑ Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (outubro de 2002). «The human and mouse replication-dependent histone genes». Genomics. 80 (5): 487–98. PMID 12408966. doi:10.1016/S0888-7543(02)96850-3
↑ ^a ^b «Entrez Gene: HIST1H3C histone cluster 1, H3c»

Leitura adicional editar

Albig W, Doenecke D (1998). «The human histone gene cluster at the D6S105 locus.». Human Genetics. 101 (3): 284–94. PMID 9439656. doi:10.1007/s004390050630
El Kharroubi A, Piras G, Zensen R, Martin MA (1998). «Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter.». Molecular and Cellular Biology. 18 (5): 2535–44. PMC 110633 . PMID 9566873. doi:10.1128/mcb.18.5.2535
Munakata T, Adachi N, Yokoyama N, et al. (2000). «A human homologue of yeast anti-silencing factor has histone chaperone activity.». Genes to Cells. 5 (3): 221–33. PMID 10759893. doi:10.1046/j.1365-2443.2000.00319.x
Hsu JY, Sun ZW, Li X, et al. (2000). «Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes.». Cell. 102 (3): 279–91. PMID 10975519. doi:10.1016/S0092-8674(00)00034-9
Deng L, de la Fuente C, Fu P, et al. (2001). «Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones.». Virology. 277 (2): 278–95. PMID 11080476. doi:10.1006/viro.2000.0593
Lachner M, O'Carroll D, Rea S, et al. (2001). «Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.». Nature. 410 (6824): 116–20. PMID 11242053. doi:10.1038/35065132
Deng L, Wang D, de la Fuente C, et al. (2001). «Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA.». Virology. 289 (2): 312–26. PMID 11689053. doi:10.1006/viro.2001.1129
Yang L, Xia L, Wu DY, et al. (2002). «Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor.». Oncogene. 21 (1): 148–52. PMID 11791185. doi:10.1038/sj.onc.1204998
Nielsen PR, Nietlispach D, Mott HR, et al. (2002). «Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9.». Nature. 416 (6876): 103–7. PMID 11882902. doi:10.1038/nature722
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). «Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.». Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899
Umehara T, Horikoshi M (2003). «Transcription initiation factor IID-interactive histone chaperone CIA-II implicated in mammalian spermatogenesis.». Journal of Biological Chemistry. 278 (37): 35660–7. PMID 12842904. doi:10.1074/jbc.M303549200
Lusic M, Marcello A, Cereseto A, Giacca M (2004). «Regulation of HIV-1 gene expression by histone acetylation and factor recruitment at the LTR promoter.». The EMBO Journal. 22 (24): 6550–61. PMC 291826 . PMID 14657027. doi:10.1093/emboj/cdg631
Black BE, Foltz DR, Chakravarthy S, et al. (2004). «Structural determinants for generating centromeric chromatin.». Nature. 430 (6999): 578–82. PMID 15282608. doi:10.1038/nature02766

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[1] «Human PubMed Reference:»

[pmid8227173-2] Kardalinou E, Eick S, Albig W, Doenecke D (dezembro de 1993). «Association of a human H1 histone gene with an H2A pseudogene and genes encoding H2B.1 and H3.1 histones». Journal of Cellular Biochemistry. 52 (4): 375–83. PMID 8227173. doi:10.1002/jcb.240520402

[pmid9119399-3] Albig W, Kioschis P, Poustka A, Meergans K, Doenecke D (abril de 1997). «Human histone gene organization: nonregular arrangement within a large cluster». Genomics. 40 (2): 314–22. PMID 9119399. doi:10.1006/geno.1996.4592

[pmid12408966-4] Marzluff WF, Gongidi P, Woods KR, Jin J, Maltais LJ (outubro de 2002). «The human and mouse replication-dependent histone genes». Genomics. 80 (5): 487–98. PMID 12408966. doi:10.1016/S0888-7543(02)96850-3

[entrez-5] «Entrez Gene: HIST1H3C histone cluster 1, H3c»

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[4]

[5]

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