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C7orf25 protein UPF1015 is a protein encoded on chromosome 7, in open reading frame 25 (C7orf25) and are located at domain of unknown function 1308. C7orf25 is located at the minus strand and encodes 12 proteins, one of them being UPF1015. This protein is believed to be active in the proteosome pathway. C7orf25 protein UPF1015 is not a transmembrane protein and has no signal peptide. UPF1015 has two isoforms, Q9BPX7-1 and Q9BPX7-2. Both consists of two exons that are both highly conserved among vertebrates.
Background Information
edit| Gene Size | Protein Size | # of exons | Promoter Sequence | Signal Peptide | Molecular Weight | Chromosome position | Protein Isoelectric point |
|---|---|---|---|---|---|---|---|
| 1844 bp | 421 aa | 2 | 600bp | No | 46.5 kdal [1] | 7p14 | 5.98 [1] |
Gene Neighborhood
editC7orf25 is an open reading frame that encodes 12 proteins. Most of these are of unknown function. One of these proteins is UPF1015 and another is PSMA2 which is also functional in the proteosome pathway.Cite error: The <ref> tag has too many names (see the help page). Other genes located near C7orf25 protein UPF1015 are TCP1P1, HECW1, MIR3943 and MRPL32.
Predicted mRNA features
editPromoter
editThe promoter for the C7orf25 protein UPF1015 gene spans 600 base pairs from 42,951,804 to 42,952,404 with a predicted transcriptional start site that encodes a sequence of 1844 base pairs. The sequence spans from 42,908,726 to 42,912,090.[2] The promoter region and beginning of the C7orf25 gene (20,008,263 to 20,009,250) is not conserved past primates. This region was used to determine transcription factor interactions.
Transcription factors
Some of the main transcription factors that bind to the promoter are listed below.[3]
| Reference | Detailed Family Information | Start (amino acid) | End (amino acid) | Strand |
|---|---|---|---|---|
| XCPE | Activator-, mediator- and TBP-dependent core promoter element for RNA polymerase II transcription from TATA-less promoters | 360 | 370 | - |
| MIZ1 | Myc-interacting Zn finger protein 1 | 120 | 130 | - |
| PLAG | Pleomorphic adenoma gene | 160 | 182 | - |
| FKHD | Fork head domain factors | 35 | 51 | + |
| E2FF | E2F-myc activator/cell cycle regulator | 357 | 373 | - |
| MZF1 | Myeloid zinc finger 1 factors | 497 | 507 | + |
| HAND | Twist subfamily of class B bHLH transcription factors | 335 | 355 | - |
| RU49 | Zinc finger transcription factor RU49, zinc finger proliferation 1 - Zipro1 | 651 | 657 | - |
| NFKB | Nuclear factor kappa B/c-rel | 219 | 233 | - |
| E2FF | E2F-myc activator/cell cycle regulator | 492 | 508 | + |
| SP1F | GC-Box factors SP1/GC | 490 | 506 | + |
| IKRS | Ikaros zinc finger family | 64 | 76 | + |
| STAT | Signal transducer and activator of transcription | 409 | 427 | - |
| RBP2 | Retinoblastoma-binding proteins with demethylase activity | 538 | 546 | - |
| YY1F | Activator/repressor binding to transcription initiation site | 553 | 575 | - |
| SP1F | GC-Box factors SP1/GC | 359 | 375 | - |
| HEAT | Heat shock factors | 240 | 264 | - |
| BPTF | Bromodomain and PHD domain transcription factors | 423 | 433 | + |
| ZF35 | Zinc finger protein ZNF35 | 309 | 321 | + |
| ETSF | Human and murine ETS1 factors | 235 | 255 | + |
Function and expression
editC7orf25 protein UPF1015 is believed to be active in ATP dependent protein breakdown in the proteosome pathway. It is expressed ubiquitously in humans.[4]
Homology
editUPF0415 protein C7orf25 has one paralog which is FLJ18411.[5] UPF0415 is also highly conserved in vertebrates. The following table shows a small selection of orthologs found using BLAST[6] and BLAT [7] and their identity to C7orf25 protein UPF1015.
| Genus and species | Accession number | Similarity (aa) |
|---|---|---|
| Homo sapiens | NM_001099858 | - |
| Bos taurus (Cow) | NM_001076140.1 | 95% |
| Falco cherrug (Falcon) | XM_005446213.1 | 78% |
| Xenopus laevis (Frog) | XM_005014944.1 | 73% |
Predicted Protein Features
editPost Translational Modifications
editUPF0415 protein C7orf25 is not a transmembrane protein as it has no transmembrane domains. UPF0415 protein C7orf25 has multiple phosphorylation. These sites are believed to be responsible in protein activation.[8]
Multiple stem loops have been identified in both 3` and 5`UTR and these are believed to be functional in gene transcription.[9]
Interactions
editOther proteins that are known to interact with UPF0415 protein C7orf25 are FRA10AC1, FLJ23825 and TUBB (tubulin, beta class I) and only TUBB is associated with proteosome activity.
Conceptual presentation
editAll post transnational modifications, genetic or proteomic factors that are relevant for UPF0415 protein C7orf25 transcription and regulation, mentioned above, are annotated in the conceptual translation.
C7orf25
editC7orf25 encodes 12 different transcripts. Two of these transcripts are (PSMA2 and UPF0415). No specific phenotypes or polymorphisms are yet to be related to mutations in C7orf25. This suggests that this reading frame is important for survival in vertebrates. The picture bellow shows all predicted transcripts encoded in C7orf25.[10]
References
edit- ^ a b "Biology workbench". Cite error: The named reference "Biology workbench, USCI" was defined multiple times with different content (see the help page).
- ^ "El Durado (Genomatix)".
- ^ "Genomatrix_tool_Eldorado".
- ^ "Factors determining peripheral vein tolerance to amino acid infusions". Archives of surgery volume=114: 897–900. 1979. PMID 111645.
{{cite journal}}: Missing pipe in:|journal=(help) - ^ = "FLJ18411".
{{cite web}}: Check|url=value (help) - ^ "NCBI_BLAST".
- ^ "UCSC_BLAT".
- ^ "Technical University of Denmark".
- ^ "Softberry".
- ^ AceView "AceView".
{{cite web}}: Check|url=value (help)
Further reading
edit- A directed protein interaction network for investigating intracellular signal transduction. Vinayagam A, Stelzl U, Foulle R, Plassmann S, Zenkner M, Timm J, Assmus HE, Andrade-Navarro MA, Wanker EE. Sci Signal. 2011 Sep 6;4(189):rs8. doi: 10.1126/scisignal.2001699. PMID 21900206 [PubMed - indexed for MEDLINE]
- A human protein-protein interaction network: a resource for annotating the proteome. Stelzl U1, 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.