词条 | C14orf80 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
释义 |
Uncharacterized protein C14orf80 is a protein which in humans is encoded by the chromosome 14 open reading frame 80, C14orf80, gene. GeneLocationC14orf80 is located on chromosome 14 (14q32.33) starting at 105,489,855bp and ending at 105,499,248bp. C14orf80 is 9,393 base pairs long and contains 11 exons that can be alternatively spliced to form different mRNA variants.[1] VariantsTranscription of C14orf80 can produce 19 mRNA splice variants. Only six of these nineteen variants are predicted to not encode for a protein.[2] Of the mRNA variants that have been found experimentally, the longest is 1,719 base pairs and produces a protein with 426 amino acids.[3]ExpressionC14orf80 has been determined to be expressed in 77 types of tissues and 100 developmental stages.[4] It has also been determined to have a higher level of expression in a few cases of pancreatic and prostate cancer cells compared to normal tissue.[5] HomologyParalogsThere are no paralogs of C14orf80.[6] OrthologsUsing the BLAST program from NCBI, the orthologs of C14orf80 were found to range from primates to invertebrates. Below is a table that contains a variety of these orthologs.[7]
Evolution rateWhen compared to the slow-evolving cytochrome C gene and the fast-evolving fibrinogen gene, gene C14orf80 is also fast-evolving.[7] ProteinGeneral propertiesUncharacterized protein C14orf80 is 426 amino acids long with a molecular weight of 47 kDa.[8] Its isoelectric point is 8.9.[9] CompositionSecondary structureUncharacterized protein C14orf80 is predicted to be entirely composed of alpha helices.[10] Using the program SOUSI-signal, it was predicted that uncharacterized protein C14orf80 does not contain a signal peptide and is a soluble protein.[11] FunctionDomainsUncharacterized protein C14orf80 has two functional domains. The first domain is the domain of unknown function 4509 and the second is the domain of unknown function 4510. As their naming states the functions of these domains are still unknown.[6] DUF4509 is located at amino acid 45 to amino acid 228. In this domain of unknown function there is a conserved WLL sequence motif.[12] DUF4510 is located at amino acid 263 to amino acid 425. In this domain of unknown function there are two conserved sequence motifs: LEA and WMD.[13] Post-translational modificationUncharacterized protein C14orf80 is predicted to have glycation and phosphorylation sites for post-translational modification. Of these sites three are for glycation, eight are for serine phosphorylation and one site is for threonine phosphorylation.[14][15] Subcellular locationUncharacterized protein C14orf80 is not predicted to be a transmembrane protein. It is mainly localized to the golgi apparatus but has been found in the nucleus and cytoplasm also.[16] InteractionsCurrently, there are 21 proteins that are predicted to interact with uncharacterized protein C14orf80. These 21 proteins were found using the databases Mentha,[17] BioGRID,[18] STRING,[19] GeneCards[20] and IntAct.[21] Below is a table of a variety of these 21 proteins.
Clinical significanceUncharacterized protein C14orf80 has been associated with tumors in the breast, CNS, endometrium, large intestine, lung, skin, and stomach.[29] References1. ^ 2. ^http://www.ensembl.org/Homo_sapiens/Transcript/Summary?db=vega;g=OTTHUMG00000170426;r=14:105491268-105499209;t=OTTHUMT00000074613 3. ^https://www.ncbi.nlm.nih.gov/nuccore/NM_001134875.1 4. ^http://bgee.unil.ch/bgee/bgee?page=gene&action=summary&gene_id=ENSG00000185347 5. ^https://www.ncbi.nlm.nih.gov/geoprofiles 6. ^1 https://www.genecards.org/cgi-bin/carddisp.pl?gene=C14orf80 7. ^1 {{cite journal | last1 = Altschul | first1 = S.F. | last2 = Gish | first2 = W. | last3 = Miller | first3 = W. | last4 = Myers | first4 = E.W. | last5 = Lipman | first5 = D.J. | year = 1990 | title = Basic local alignment search tool | url = | journal = J. Mol. Biol. | volume = 215 | issue = 3| pages = 403–410 | doi=10.1006/jmbi.1990.9999}} 8. ^{{cite journal | last1 = Subramaniam | first1 = S | year = 1998 | title = The Biology Workbench--a seamless database and analysis environment for the biologist | url = | journal = Proteins | volume = 32 | issue = 1| pages = 1–2 | doi=10.1002/(sici)1097-0134(19980701)32:1<1::aid-prot1>3.0.co;2-q | pmid=9672036}} 9. ^{{cite journal | last1 = Bjellqvist | first1 = B. | last2 = Basse | first2 = B. | last3 = Olsen | first3 = E. | last4 = Celis | first4 = J.E. | year = 1994 | title = Reference points for comparisons of two-dimensional maps of proteins from different human cell types defined in a pH scale where isoelectric points correlate with polypeptide compositions | url = | journal = Electrophoresis | volume = 15 | issue = | pages = 529–539 | doi=10.1002/elps.1150150171}} 10. ^{{cite journal | last1 = Brendel | first1 = V. | last2 = Bucher | first2 = P. | last3 = Nourbakhsh | first3 = I.R. | last4 = Blaisdell | first4 = B.E. | last5 = Karlin | first5 = S. | year = 1992 | title = Methods and algorithms for statistical analysis of protein sequences | pmc = 48584 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 89 | issue = | pages = 2002–2006 | pmid=1549558 | doi=10.1073/pnas.89.6.2002 }} 11. ^{{cite journal | last1 = Gomi | first1 = M. | last2 = Sonoyama | first2 = M. | last3 = Mitaku | first3 = S. | year = 2004 | title = High performance system for signal peptide prediction: SOSUIsignal | url = | journal = Chem-Bio Info. J. | volume = 4 | issue = 4| pages = 142–147 | doi=10.1273/cbij.4.142}} 12. ^http://pfam.xfam.org/family/PF14970#tabview=tab0 13. ^http://pfam.xfam.org/family/PF14971 14. ^http://www.cbs.dtu.dk/services/NetGlycate/ 15. ^http://www.cbs.dtu.dk/services/NetPhos/ 16. ^http://www.proteinatlas.org/ENSG00000185347-C14orf80/subcellular 17. ^{{cite journal | last1 = Calderone | first1 = Alberto | last2 = Castagnoli | first2 = Luisa | last3 = Cesareni | first3 = Gianni | year = 2013 | title = mentha: a resource for browsing integrated protein-interaction networks | url = | journal = Nature Methods | volume = 10 | issue = 8| pages = 690–691 | doi = 10.1038/nmeth.2561 | pmid=23900247}} 18. ^{{cite journal | last1 = Stark | first1 = C | last2 = Breitkreutz | first2 = BJ | last3 = Reguly | first3 = T | last4 = Boucher | first4 = L | last5 = Breitkreutz | first5 = A | last6 = Tyers | first6 = M | year = 2006| title = Biogrid: A General Repository for Interaction Datasets | url = | journal = Nucleic Acids Res. | volume = 34 | issue = Database issue| pages = D535–9 | doi=10.1093/nar/gkj109 | pmid=16381927 | pmc=1347471}} 19. ^Szklarczyk D., Franceschini A., Wyder S., Forslund K., Heller D., Huerta-Cepas J., et al. . (2015). STRING v10: protein–protein interaction networks, integrated over the tree of life. Nuc. Acids Res. 43, D447–D452. 10.1093/nar/gku1003 20. ^Safran M, Dalah I, Alexander J, Rosen N, Iny Stein T, Shmoish M, Nativ N, Bahir I, Doniger T, Krug H, Sirota-Madi A, Olender T, Golan Y, Stelzer G, Harel A and Lancet D. GeneCards Version 3: the human gene integrator 21. ^{{cite journal | last1 = Orchard | first1 = S. | display-authors = etal | year = 2014 | title = The MIntAct project—IntAct as a common curation platform for 11 molecular interaction databases | journal = Nucleic Acids Res | volume = 42 | issue = Database issue| pages = D358–D363 | doi=10.1093/nar/gkt1115 | pmid=24234451 | pmc=3965093}} 22. ^1 Network organization of the human autophagy system. (Behrends C1, Sowa ME, Gygi SP, Harper JW.) 23. ^Methods for Quantification of in vivo Changes in Protein Ubiquitination following Proteasome and Deubiquitinase Inhibition (ND Udenshi et el) 24. ^A Quantitative Chaperone Interaction Network Reveals the Architecture of Cellular Protein Homeostasis Pathways (Mikko Taipale, George Tucker, Jian Peng, Irina Krykbaeva, Zhen-Yuan Lin, Brett Larsen, Hyungwon Choi, Bonnie Berger, Anne-Claude Gingras, Susan Lindquist) 25. ^High-resolution comparative genomic hybridization of inflammatory breast cancer and identification of candidate genes. (Bekhouche I1, Finetti P, Adelaïde J, Ferrari A, Tarpin C, Charafe-Jauffret E, Charpin C, Houvenaeghel G, Jacquemier J, Bidaut G, Birnbaum D, Viens P, Chaffanet M, Bertucci F.) 26. ^Construction and characterization of a normalized yeast two-hybrid library derived from a human protein-coding clone collection. (DeGrado-Warren J1, Dufford M, Chen J, Bartel PL, Shattuck D, Frech GC.) 27. ^High-Throughput Proteomic Mapping of Human Interaction Networks via Affinity-Purification Mass Spectrometry (Huttlin EL, Ting L, Bruckner RJ, Paulo JA, Gygi MP, Rad R, Kolippakkam D, Szpyt J, Zarraga G, Tam S, Gebreab F, Colby G, Pontano-Vaites L, Obar RA, Guarani-Pereira V, Harris T, Artavanis-Tsakonas S, Sowa ME, Harper JW, Gygi SP) 28. ^Pathway Analysis of ChIP-Seq-Based NRF1 Target Genes Suggests a Logical Hypothesis of their Involvement in the Pathogenesis of Neurodegenerative Diseases (Jun-ichi Satoh, Natsuki Kawana and Yoji Yamamoto) 29. ^http://www.ensembl.org/Homo_sapiens/Gene/Phenotype?db=vega;g=OTTHUMG00000170426;r=14:105491268-105499209;t=OTTHUMT00000074610 1 : Human proteins |
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