تناسین-آر

تناسین-آر (انگلیسی: Tenascin-R‎) نام پروتئینی است که در انسان توسط ژن «TNR» کُد می‌شود.[4][5][6]

TNR
معین‌کننده‌ها
نام‌های دیگر	TNR, TN-R, tenascin R
شناسه‌های بیرونی	OMIM: 601995 MGI: 99516 HomoloGene: 124416 GeneCards: TNR
Gene location (Mouse) Chr. Chromosome 1 (mouse)[1] Band 1|1 H1 Start 159,523,769 bp[1] End 159,931,729 bp[1]
الگوی گسترش RNA More reference expression data
هستی‌شناسی ژن عملکرد ملکولی • GO:0001948 پیوند پروتئینی ترکیبات سلولی • extracellular region • cell surface • لیپید رفت • perineuronal net • collagen-containing extracellular matrix • GO:0005578 بافت‌مانه برون‌یاخته‌ای • Schaffer collateral - CA1 synapse • glutamatergic synapse فرایند زیستی • negative regulation of neuron projection development • positive regulation of synaptic transmission, glutamatergic • extracellular matrix organization • axon guidance • synapse organization • positive regulation of transmission of nerve impulse • neuron cell-cell adhesion • negative regulation of cell-cell adhesion • telencephalon cell migration • negative regulation of axon extension • locomotory exploration behavior • long-term synaptic potentiation • neuromuscular process controlling balance • regulation of neurogenesis • negative regulation of axon extension involved in regeneration • negative regulation of synaptic transmission • modulation of chemical synaptic transmission • associative learning • cell adhesion Sources:آمیگو / کوئیک‌گو
هم‌ساخت‌شناسی
گونه‌ها	انسان	موش
Entrez	7143	21960
آنسامبل	ENSG00000116147	ENSMUSG00000015829
یونی‌پروت	Q92752	Q8BYI9
RefSeq (mRNA)	NM_003285، NM_001328635، XM_017002218، XM_017002219 XM_011509949، NM_003285، NM_001328635، XM_017002218، XM_017002219	XM_006496742، XM_006496743، XM_006496744، XM_006496745، XM_006496746، XM_030252973، XM_030252974، XM_030252975، XM_030252976، XM_030252977 NM_022312، XM_006496742، XM_006496743، XM_006496744، XM_006496745، XM_006496746، XM_030252973، XM_030252974، XM_030252975، XM_030252976، XM_030252977
RefSeq (پروتئین)	NP_003276، XP_011508251، XP_016857707، XP_016857708 NP_001315564، NP_003276، XP_011508251، XP_016857707، XP_016857708 NP_003276.3	XP_006496805، XP_006496806، XP_006496807، XP_006496808، XP_006496809، XP_030108834، XP_030108835، XP_030108837، XP_036019452، XP_036019453، XP_036019454، XP_036019456 NP_071707، XP_006496805، XP_006496806، XP_006496807، XP_006496808، XP_006496809، XP_030108834، XP_030108835، XP_030108837، XP_036019452، XP_036019453، XP_036019454، XP_036019456
موقعیت (UCSC)	n/a	Chr : 159.52 – 159.93 Mb
جستجوی PubMed	[2]	[3]
ویکی‌داده
مشاهده/ویرایش Human View/Edit Mouse

تناسین-آر یک پروتئین ماتریکس برون‌یاخته‌ای است که دستگاه عصبی مرکزی دیده می‌شود و عضوی از خانوادهٔ تناسین‌هاست که در پستانداران، دست‌کم ۳ ژن دارد.

منابع

1. GRCm38: Ensembl release 89: ENSMUSG00000015829 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Carnemolla B, Leprini A, Borsi L, Querzé G, Urbini S, Zardi L (April 1996). "Human tenascin-R. Complete primary structure, pre-mRNA alternative splicing and gene localization on chromosome 1q23-q24". The Journal of Biological Chemistry. 271 (14): 8157–60. doi:10.1074/jbc.271.14.8157. PMID 8626505.
5. Leprini A, Gherzi R, Siri A, Querzé G, Viti F, Zardi L (December 1996). "The human tenascin-R gene". The Journal of Biological Chemistry. 271 (49): 31251–4. doi:10.1074/jbc.271.49.31251. PMID 8940128.
6. "Entrez Gene: TNR tenascin R (restrictin, janusin)".

• مشارکت‌کنندگان ویکی‌پدیا. «Tenascin-R». در دانشنامهٔ ویکی‌پدیای انگلیسی، بازبینی‌شده در ۲۴ دسامبر ۲۰۱۷.

بیشتر بخوانید

• Erickson HP (October 1993). "Tenascin-C, tenascin-R and tenascin-X: a family of talented proteins in search of functions". Current Opinion in Cell Biology. 5 (5): 869–76. doi:10.1016/0955-0674(93)90037-Q. PMID 7694605.
• Xiao ZC, Taylor J, Montag D, Rougon G, Schachner M (April 1996). "Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11". The European Journal of Neuroscience. 8 (4): 766–82. doi:10.1111/j.1460-9568.1996.tb01262.x. PMID 9081628.
• Aspberg A, Miura R, Bourdoulous S, Shimonaka M, Heinegârd D, Schachner M, Ruoslahti E, Yamaguchi Y (September 1997). "The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety". Proceedings of the National Academy of Sciences of the United States of America. 94 (19): 10116–21. doi:10.1073/pnas.94.19.10116. PMC 23322. PMID 9294172.
• Xiao ZC, Hillenbrand R, Schachner M, Thermes S, Rougon G, Gomez S (September 1997). "Signaling events following the interaction of the neuronal adhesion molecule F3 with the N-terminal domain of tenascin-R". Journal of Neuroscience Research. 49 (6): 698–709. doi:10.1002/(SICI)1097-4547(19970915)49:6<698::AID-JNR4>3.0.CO;2-2. PMID 9335257.
• Arrigo G, Gherzi R, Bonaglia MC, Leprini A, Zuffardi O, Zardi L (1997). "Assignment of the tenascin-R gene (Tnr) to mouse chromosome 4 band E2 by fluorescence in situ hybridization; refinement of the human TNR location to chromosome 1q24". Cytogenetics and Cell Genetics. 78 (2): 145–6. doi:10.1159/000134650. PMID 9371410.
• Volkmer H, Zacharias U, Nörenberg U, Rathjen FG (August 1998). "Dissection of complex molecular interactions of neurofascin with axonin-1, F11, and tenascin-R, which promote attachment and neurite formation of tectal cells". The Journal of Cell Biology. 142 (4): 1083–93. doi:10.1083/jcb.142.4.1083. PMC 2132869. PMID 9722619.
• Zamze S, Harvey DJ, Pesheva P, Mattu TS, Schachner M, Dwek RA, Wing DR (August 1999). "Glycosylation of a CNS-specific extracellular matrix glycoprotein, tenascin-R, is dominated by O-linked sialylated glycans and "brain-type" neutral N-glycans". Glycobiology. 9 (8): 823–31. doi:10.1093/glycob/9.8.823. PMID 10406848.
• Olin AI, Mörgelin M, Sasaki T, Timpl R, Heinegård D, Aspberg A (January 2001). "The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding". The Journal of Biological Chemistry. 276 (2): 1253–61. doi:10.1074/jbc.M006783200. PMID 11038354.
• Xu XR, Huang J, Xu ZG, Qian BZ, Zhu ZD, Yan Q, Cai T, Zhang X, Xiao HS, Qu J, Liu F, Huang QH, Cheng ZH, Li NG, Du JJ, Hu W, Shen KT, Lu G, Fu G, Zhong M, Xu SH, Gu WY, Huang W, Zhao XT, Hu GX, Gu JR, Chen Z, Han ZG (December 2001). "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver". Proceedings of the National Academy of Sciences of the United States of America. 98 (26): 15089–94. doi:10.1073/pnas.241522398. PMC 64988. PMID 11752456.
• Woodworth A, Pesheva P, Fiete D, Baenziger JU (March 2004). "Neuronal-specific synthesis and glycosylation of tenascin-R". The Journal of Biological Chemistry. 279 (11): 10413–21. doi:10.1074/jbc.M312466200. PMID 14681222.
• Bukalo O, Schachner M, Dityatev A (May 2007). "Hippocampal metaplasticity induced by deficiency in the extracellular matrix glycoprotein tenascin-R". The Journal of Neuroscience. 27 (22): 6019–28. doi:10.1523/JNEUROSCI.1022-07.2007. PMID 17537973.