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The function of C22orf25 is not currently known.  It is characterized by the NRDE superfamily domain (DUF883), which is strictly known for the conserved [[amino acid]] sequence of (N)-[[Asparagine]] (R)-[[Arginine]] (D)-[[Aspartic Acid]] (E)-[[Glutamic Acid]].  This domain is found among distantly related [[species]] from the six kingdoms:<ref>{{cite web|title=BLAST (NCBI)|url=http://blast.ncbi.nlm.nih.gov/Blast.cgi}}</ref> [[Eubacteria]], [[Archaebacteria]], [[Protista]], [[Fungi]], [[Plantae]], and [[Animalia]] and is known to be involved in [[Golgi apparatus|Golgi]] organization and protein secretion.<ref>{{cite web|title=Conserved Domains (NCBI)|url=https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=120558}}</ref>  It is likely that it localizes in the [[cytoplasm]] but is anchored in the [[cell membrane]] by the second amino acid.<ref name=autogenerated2>{{cite web|title=CSS-Palm|url=http://csspalm.biocuckoo.org/}}</ref><ref>{{cite web|title=PSORTII|url=http://www.psort.org/}}</ref>    C22orf25 is also [[xenolog]]ous to T10 like proteins in the [[Fowlpox|Fowlpox Virus]] and [[Canarypox|Canarypox Virus]].  The gene coding for C22orf25 is located on [[chromosome 22]] and the location q11.21, so it is often associated with [[22q11.2 deletion syndrome]].<ref name=autogenerated1>{{cite web|title=Gene (NCBI)|url=https://www.ncbi.nlm.nih.gov/gene/128989}}</ref>
The function of C22orf25 is not currently known.  It is characterized by the NRDE superfamily domain (DUF883), which is strictly known for the conserved [[amino acid]] sequence of (N)-[[Asparagine]] (R)-[[Arginine]] (D)-[[Aspartic Acid]] (E)-[[Glutamic Acid]].  This domain is found among distantly related [[species]] from the six kingdoms:<ref>{{cite web|title=BLAST (NCBI)|url=http://blast.ncbi.nlm.nih.gov/Blast.cgi}}</ref> [[Eubacteria]], [[Archaebacteria]], [[Protista]], [[Fungi]], [[Plantae]], and [[Animalia]] and is known to be involved in [[Golgi apparatus|Golgi]] organization and protein secretion.<ref>{{cite web|title=Conserved Domains (NCBI)|url=https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=120558}}</ref>  It is likely that it localizes in the [[cytoplasm]] but is anchored in the [[cell membrane]] by the second amino acid.<ref name=autogenerated2>{{cite web|title=CSS-Palm|url=http://csspalm.biocuckoo.org/}}</ref><ref>{{cite web|title=PSORTII|url=http://www.psort.org/}}</ref>    C22orf25 is also [[xenolog]]ous to T10 like proteins in the [[Fowlpox|Fowlpox Virus]] and [[Canarypox|Canarypox Virus]].  The gene coding for C22orf25 is located on [[chromosome 22]] and the location q11.21, so it is often associated with [[22q11.2 deletion syndrome]].<ref name=autogenerated1>{{cite web|title=Gene (NCBI)|url=https://www.ncbi.nlm.nih.gov/gene/128989}}</ref>


== Protein ==
== Protein ==
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! Gene Size !! Protein Size !! # of exons !! Promoter Sequence !! Signal Peptide !! Molecular Weight !! Domain Length
! Gene Size !! Protein Size !! # of exons !! Promoter Sequence !! Signal Peptide !! Molecular Weight !! Domain Length
|-
|-
| 2271 bp || 276 aa || 9<ref>{{cite web|title=ElDorado (Genomatix)|url=http://www.genomatix.de/}}</ref>  || 687 bp || No<ref>{{cite web|title=SignalP (ExPASy)|url=http://expasy.org/tools}}</ref>  || 30.9 kDa<ref>{{cite web|title=Statistical Analysis of Protein Sequence (Biology Workbench)|url=http://seqtool.sdsc.edu/CGI/BW.cgi#!}}</ref>  || 270 aa
| 2271 bp || 276 aa || 9<ref>{{cite web|title=ElDorado (Genomatix)|url=http://www.genomatix.de/}}</ref>  || 687 bp || No<ref>{{cite web|title=SignalP (ExPASy)|url=http://expasy.org/tools}}</ref>  || 30.9 kDa<ref>{{cite web|title=Statistical Analysis of Protein Sequence (Biology Workbench)|url=http://seqtool.sdsc.edu/CGI/BW.cgi#!}}{{Dead link|date=June 2018 |bot=InternetArchiveBot |fix-attempted=no }}</ref>  || 270 aa
|-
|-
|}
|}
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== Expression analysis ==
== Expression analysis ==


Expression data from [[Expressed Sequence Tag]] mapping, [[microarray]] and [[in situ hybridization|''in situ'' hybridization]] show high expression for ''Homo sapiens'' in the [[blood]], [[bone marrow]] and [[nerves]].<ref>{{cite web|title=Unigene NCBI|url=http://www.ncbi.nim.nih.gov/}}</ref><ref>{{cite web|title=GEO Profiles NCBI|url=https://www.ncbi.nlm.nih.gov/}}</ref><ref>{{cite web|title=Bio GPS|url=http://biogps.org/#goto=genereport&id=128989}}</ref>  Expression is not restricted to these areas and low expression is seen elsewhere in the body. In ''[[Caenorhabditis elegans]]'', the snt-1 gene (C22orf25 homologue) was expressed in the nerve ring, ventral and dorsal cord processes, sites of neuromuscular junctions, and in neurons.<ref>{{cite web|title=WormBase|url=http://www.wormbase.org/}}</ref>
Expression data from [[Expressed Sequence Tag]] mapping, [[microarray]] and [[in situ hybridization|''in situ'' hybridization]] show high expression for ''Homo sapiens'' in the [[blood]], [[bone marrow]] and [[nerves]].<ref>{{cite web|title=Unigene NCBI|url=http://www.ncbi.nim.nih.gov/|access-date=2012-04-26|archive-url=https://web.archive.org/web/20130712201927/http://ncbi.nim.nih.gov/#|archive-date=2013-07-12|dead-url=yes|df=}}</ref><ref>{{cite web|title=GEO Profiles NCBI|url=https://www.ncbi.nlm.nih.gov/}}</ref><ref>{{cite web|title=Bio GPS|url=http://biogps.org/#goto=genereport&id=128989}}</ref>  Expression is not restricted to these areas and low expression is seen elsewhere in the body. In ''[[Caenorhabditis elegans]]'', the snt-1 gene (C22orf25 homologue) was expressed in the nerve ring, ventral and dorsal cord processes, sites of neuromuscular junctions, and in neurons.<ref>{{cite web|title=WormBase|url=http://www.wormbase.org/}}</ref>


== Evolutionary history ==
== Evolutionary history ==
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=== Predicted topology ===
=== Predicted topology ===


C22orf25 localizes to the cytoplasm and is anchored to the cell membrane by the second amino acid.  As mentioned previously, the second amino acid is modified by palmitoylation.  Palmitoylation is known to contribute to membrane association<ref>{{cite journal | vauthors = Resh MD | title = Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules | journal = Science STKE | issue = 359 | pages = 14 | year = 2006 | pmid = 17077383 | doi = 10.1126/stke.3592006re14 | volume=2006}}</ref> because it contributes to enhanced hydrophobicity.<ref name=autogenerated2 /> Palmitoylation is known to play a role in the modulation of proteins' trafficking,<ref>{{cite journal | vauthors = Draper JM, Xia Z, Smith CD | title = Cellular palmitoylation and trafficking of lipated peptides | journal = NIH Public Access | volume = 48 | issue = 8 | pages = 1873–1884 | date = Aug 2007 | pmid = 17525474 | doi = 10.1194/jlr.m700179-jlr200 | pmc=2895159}}</ref> stability<ref>{{cite journal | vauthors = Linder ME, Deschenes RJ | title = Palmitoylation: policing protein stability and traffic | journal = Nature Reviews Molecular Cell Biology | volume = 8 | issue = 1 | pages = 74–84 | date = Jan 2007 | pmid = 17183362 | doi = 10.1038/nrm2084 }}</ref> and sorting.<ref>{{cite journal | vauthors = Greaves J, Chamberlain LH | title = Palmitoylation-dependent protein sorting | journal = Cellular Biology | volume = 176 | issue = 3 | pages = 249–254 | date = Jan 2007 | pmid = 17242068 | doi = 10.1083/jcb.200610151 | pmc=2063950}}</ref> Palmitoylation is also involved in cellular signaling<ref name="pmid7716512">{{cite journal | vauthors = Casey PJ | title = Protein lipidation in cell signaling | journal = Science | volume = 268 | issue = 5208 | pages = 221–5 | year = 1995 | pmid = 7716512 | doi = 10.1126/science.7716512 }}</ref> and neuronal transmission.<ref>{{cite journal | vauthors = Roth AF, Wan J, Bailey AO, Sun B, Kuchar JA, Green WN, Phinney BS, Yates JR, Davis NG | title = Global analysis of protein palmitoylation in yeast | journal = Cell | volume = 125 | issue = 5 | pages = 1003–1013 | date = June 2006 | pmid = 16751107 | doi = 10.1016/j.cell.2006.03.042 | pmc=2246083}}</ref>
C22orf25 localizes to the cytoplasm and is anchored to the cell membrane by the second amino acid.  As mentioned previously, the second amino acid is modified by palmitoylation.  Palmitoylation is known to contribute to membrane association<ref>{{cite journal | vauthors = Resh MD | title = Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules | journal = Science's STKE | issue = 359 | pages = 14 | year = 2006 | pmid = 17077383 | doi = 10.1126/stke.3592006re14 | volume=2006}}</ref> because it contributes to enhanced hydrophobicity.<ref name=autogenerated2 /> Palmitoylation is known to play a role in the modulation of proteins' trafficking,<ref>{{cite journal | vauthors = Draper JM, Xia Z, Smith CD | title = Cellular palmitoylation and trafficking of lipated peptides | journal = NIH Public Access | volume = 48 | issue = 8 | pages = 1873–1884 | date = Aug 2007 | pmid = 17525474 | doi = 10.1194/jlr.m700179-jlr200 | pmc=2895159}}</ref> stability<ref>{{cite journal | vauthors = Linder ME, Deschenes RJ | title = Palmitoylation: policing protein stability and traffic | journal = Nature Reviews Molecular Cell Biology | volume = 8 | issue = 1 | pages = 74–84 | date = Jan 2007 | pmid = 17183362 | doi = 10.1038/nrm2084 }}</ref> and sorting.<ref>{{cite journal | vauthors = Greaves J, Chamberlain LH | title = Palmitoylation-dependent protein sorting | journal = Cellular Biology | volume = 176 | issue = 3 | pages = 249–254 | date = Jan 2007 | pmid = 17242068 | doi = 10.1083/jcb.200610151 | pmc=2063950}}</ref> Palmitoylation is also involved in cellular signaling<ref name="pmid7716512">{{cite journal | vauthors = Casey PJ | title = Protein lipidation in cell signaling | journal = Science | volume = 268 | issue = 5208 | pages = 221–5 | year = 1995 | pmid = 7716512 | doi = 10.1126/science.7716512 }}</ref> and neuronal transmission.<ref>{{cite journal | vauthors = Roth AF, Wan J, Bailey AO, Sun B, Kuchar JA, Green WN, Phinney BS, Yates JR, Davis NG | title = Global analysis of protein palmitoylation in yeast | journal = Cell | volume = 125 | issue = 5 | pages = 1003–1013 | date = June 2006 | pmid = 16751107 | doi = 10.1016/j.cell.2006.03.042 | pmc=2246083}}</ref>


=== Protein Interactions ===
=== Protein Interactions ===


C22orf25 has been shown to interact with [[NFKB1]],<ref name=autogenerated3>{{cite web|title=Molecular Interaction Database|url=http://mint.bio.uniroma2.it/mint/Welcome.do}}</ref>  [[RELA]],<ref name=autogenerated3 /> [[RELB]],<ref name=autogenerated3 /> [[BTRC (gene)|BTRC]],<ref name=autogenerated3 /> [[RPS27A]],<ref name=autogenerated3 /> [[BCL3]],<ref>{{cite web|title=Molecular Interaction  Database|url=http://mint.bio.uniroma2.it/mint/Welcome.do}}</ref> [[MAP3K8]],<ref name=autogenerated3 /> [[NFKBIA]],<ref name=autogenerated3 /> [[SIN3A]],<ref name=autogenerated3 /> [[SUMO1]],<ref name=autogenerated3 /> [[Tat (HIV)|Tat]].<ref>{{cite web|title=Viral Molecular Interaction Database|url=http://mint.bio.uniroma2.it/virusmint/Welcome.do}}</ref>
C22orf25 has been shown to interact with [[NFKB1]],<ref name=autogenerated3>{{cite web|title=Molecular Interaction Database|url=http://mint.bio.uniroma2.it/mint/Welcome.do|deadurl=yes|archiveurl=https://web.archive.org/web/20060506110418/http://mint.bio.uniroma2.it/mint/Welcome.do|archivedate=2006-05-06|df=}}</ref>  [[RELA]],<ref name=autogenerated3 /> [[RELB]],<ref name=autogenerated3 /> [[BTRC (gene)|BTRC]],<ref name=autogenerated3 /> [[RPS27A]],<ref name=autogenerated3 /> [[BCL3]],<ref>{{cite web|title=Molecular Interaction  Database|url=http://mint.bio.uniroma2.it/mint/Welcome.do|deadurl=yes|archiveurl=https://web.archive.org/web/20060506110418/http://mint.bio.uniroma2.it/mint/Welcome.do|archivedate=2006-05-06|df=}}</ref> [[MAP3K8]],<ref name=autogenerated3 /> [[NFKBIA]],<ref name=autogenerated3 /> [[SIN3A]],<ref name=autogenerated3 /> [[SUMO1]],<ref name=autogenerated3 /> [[Tat (HIV)|Tat]].<ref>{{cite web|title=Viral Molecular Interaction Database|url=http://mint.bio.uniroma2.it/virusmint/Welcome.do|deadurl=yes|archiveurl=https://web.archive.org/web/20150215025855/http://mint.bio.uniroma2.it/virusmint/Welcome.do|archivedate=2015-02-15|df=}}</ref>


== Clinical significance ==
== Clinical significance ==
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==External links==
==External links==
[https://www.tango2.it] www.tango2.it - Disease website
* [https://www.tango2.it] www.tango2.it - Disease website
* [http://tango2research.org] www.tango2research.org - Research disease website -

Revision as of 07:42, 17 November 2018

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Orthologs
SpeciesHumanMouse
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RefSeq (protein)

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Wikidata
View/Edit Human

Transport and golgi organization 2 homolog (TANGO2) also known as chromosome 22 open reading frame 25 (C22orf25) is a protein that in humans is encoded by the TANGO2 gene.

The function of C22orf25 is not currently known. It is characterized by the NRDE superfamily domain (DUF883), which is strictly known for the conserved amino acid sequence of (N)-Asparagine (R)-Arginine (D)-Aspartic Acid (E)-Glutamic Acid. This domain is found among distantly related species from the six kingdoms:[1] Eubacteria, Archaebacteria, Protista, Fungi, Plantae, and Animalia and is known to be involved in Golgi organization and protein secretion.[2] It is likely that it localizes in the cytoplasm but is anchored in the cell membrane by the second amino acid.[3][4] C22orf25 is also xenologous to T10 like proteins in the Fowlpox Virus and Canarypox Virus. The gene coding for C22orf25 is located on chromosome 22 and the location q11.21, so it is often associated with 22q11.2 deletion syndrome.[5]

Protein

Gene Size Protein Size # of exons Promoter Sequence Signal Peptide Molecular Weight Domain Length
2271 bp 276 aa 9[6] 687 bp No[7] 30.9 kDa[8] 270 aa

Gene neighborhood

The C22orf25 gene is located on the long arm (q) of chromosome 22 in region 1, band 1, and sub-band 2 (22q11.21) starting at 20,008,631 base pairs and ending at 20,053,447 base pairs.[5] There is a 1.5-3.0 Mb deletion containing around 30-40 genes, spanning this region that causes the most survivable genetic deletion disorder known as 22q11.2 deletion syndrome, which is most commonly known as DiGeorge syndrome or Velocaridofacial syndrome.[9][10] 22q11.2 deletion syndrome has a vast array of phenotypes and is not attributed to the loss of a single gene. The vast phenotypes arise from deletions of not only DiGeorge Syndrome Critical Region (DGCR) genes and disease genes but other unidentified genes as well.[11]

C22orf25 is in close proximity to DGCR8 as well as other genes known to play a part in DiGeorge Syndrome such as armadillo repeat gene deleted in Velocardiofacial syndrome (ARVCF), Cathechol-O-methyltransferase (COMT) and T-box 1 (TBX1).[12][13]

Gene Neighborhood of C22orf25
Gene Neighborhood of C22orf25

Predicted mRNA features

Promoter

The promoter for the C22orf25 gene spans 687 base pairs from 20,008,092 to 20,008,878 with a predicted transcriptional start site that is 104 base pairs and spans from 20,008,591 to 20,008,694.[14] The promoter region and beginning of the C22orf25 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.[15]

Reference Detailed Family Information Start (amino acid) End (amino acid) Strand
XBBF X-box binding factors 227 245 -
GCMF Chorion-specific transcription factors (with a GCM DNA binding domain) 151 165 -
YBXF Y-box binding transcription factors 158 170 -
RUSH SWI/SNF related nucleophosphoproteins (with a RING finger binding motif) 222 232 -
NEUR NeuroD, Beta2, HLH domain 214 226 -
PCBE PREB core-binding element 148 162 -
NR2F Nuclear receptor subfamily 2 factors 169 193 -
AP1R MAF and AP1 related factors 201 221 -
ZF02 C2H2 zinc finger transcription factors 2 108 130 -
TALE TALE homeodomain class recognizing TG motifs 216 232 -
WHNF Winged helix transcription factors 271 281 -
FKHD Forkhead domain factors 119 135 +
MYOD Myoblast determining factors 218 234 +
AP1F AP1, activating protein 1 118 130 +
BCL6 POZ domain zinc finger expressed in B cells 190 206 +
CARE Calcium response elements 196 206 +
EVI1 EVI1 nuclear transcription factor 90 106 +
ETSF ETS transcription factor 162 182 +
TEAF TEA/ATTS DNA binding domain factors 176 188 +

Expression analysis

Expression data from Expressed Sequence Tag mapping, microarray and in situ hybridization show high expression for Homo sapiens in the blood, bone marrow and nerves.[16][17][18] Expression is not restricted to these areas and low expression is seen elsewhere in the body. In Caenorhabditis elegans, the snt-1 gene (C22orf25 homologue) was expressed in the nerve ring, ventral and dorsal cord processes, sites of neuromuscular junctions, and in neurons.[19]

Evolutionary history

The NRDE (DUF883) domain, is a domain of unknown function spanning majority of the C22orf25 gene and is found among distantly related species, including viruses.

Genus and Species Common Name Accession Number Seq.
Length		 Seq.
Identity		 Seq.
Similarity		 Kingdom Time of Divergence
Homo sapiens humans NP_690870.3 276aa - - Animalia -
Pan troglodytes common chimpanzee BAK62258.1 276aa 99% 100% Animalia 6.4 mya
Ailuropoda melanoleuca giant panda XP_002920626 276aa 91% 94% Animalia 94.4 mya
Mus musculus house mouse NP_613049.2 276aa 88% 95% Animalia 92.4 mya
Meleagris gallopavo turkey XP_003210928 276aa 74% 88% Animalia 301.7 mya
Gallus gallus Red Junglefowl NP_001007837 276aa 73% 88% Animalia 301.7 mya
Xenopus laevis African clawed frog NP_001083694 275aa 69% 86% Animalia 371.2 mya
Xenopus (Silurana) tropicalis Western clawed frog NP_001004885.1 276aa 68% 85% Animalia 371.2 mya
Salmo salar Atlantic salmon NP_001167100 274aa 66% 79% Animalia 400.1 mya
Danio rerio zebrafish NP_001003781 273aa 64% 78% Animalia 400.1 mya
Canarypox virus NP_955117 275aa 50% 69% - -
Fowlpox virus NP_039033 273aa 44% 63% - -
Cupriavidus proteobacteria YP_002005507.1 275aa 38% 52% Eubacteria 2313.2 mya
Burkholderia proteobacteria YP_004977059 273aa 37% 53% Eubacteria 2313.2 mya
Physcomitrella patens moss XP_001781807 275aa 37% 54% Plantae 1369 mya
Zea mays maize/corn ACG35095 266aa 33% 53% Plantae 1369 mya
Trichophyton rubrum fungus XP_003236126 306aa 32% 47% Fungi 1215.8 mya
Sporisorium reilianum Plant pathogen CBQ69093 321aa 32% 43% Fungi 1215.8 mya
Perkinsus marinus pathogen of oysters XP_002787624 219aa 31% 48% Protista 1381.2 mya
Tetrahymena thermophilia Ciliate protozoa XP_001010229 277aa 26% 44% Protista 1381.2 mya
Natrialba magadii extremophile YP_003481665 300aa 25% 39% Archaebacteria 3556.3 mya
Halopiger xanaduensis halophilic archaeon YP_004597780.1 264aa 24% 39% Archaebacteria 3556.3 mya

Predicted protein features

Post translational modifications

Post translational modifications of the C22orf25 gene that are evolutionarily conserved in the Animalia and Plantae kingdoms as well as the Canarypox Virus include glycosylation (C-mannosylation),[20] glycation,[21] phosphorylation (kinase specific),[22] and palmitoylation.[23]

Predicted topology

C22orf25 localizes to the cytoplasm and is anchored to the cell membrane by the second amino acid. As mentioned previously, the second amino acid is modified by palmitoylation. Palmitoylation is known to contribute to membrane association[24] because it contributes to enhanced hydrophobicity.[3] Palmitoylation is known to play a role in the modulation of proteins' trafficking,[25] stability[26] and sorting.[27] Palmitoylation is also involved in cellular signaling[28] and neuronal transmission.[29]

Protein Interactions

C22orf25 has been shown to interact with NFKB1,[30] RELA,[30] RELB,[30] BTRC,[30] RPS27A,[30] BCL3,[31] MAP3K8,[30] NFKBIA,[30] SIN3A,[30] SUMO1,[30] Tat.[32]

Clinical significance

Mutations in the TANGO2 gene may cause defects in mitochondrial β-oxidation[33] and increased endoplasmic reticulum stress and a reduction in Golgi volume density.[34] These mutations results in early onset hypoglycemia, hyperammonemia, rhabdomyolysis, cardiac arrhythmias, and encephalopathy that later develops into cognitive impairment.[33][34]

References

  1. ↑ "BLAST (NCBI)".
  2. ↑ "Conserved Domains (NCBI)".
  3. ↑ 3.0 3.1 "CSS-Palm".
  4. ↑ "PSORTII".
  5. ↑ 5.0 5.1 "Gene (NCBI)".
  6. ↑ "ElDorado (Genomatix)".
  7. ↑ "SignalP (ExPASy)".
  8. ↑ "Statistical Analysis of Protein Sequence (Biology Workbench)".[permanent dead link]
  9. ↑ Meechan DW, Maynard TM, Tucker ES, LaMantia AS (2011). "Three phases of DiGeorge/22q11 deletion syndrome pathogenesis during brain development: Patterning, proliferation, and mitochondrial functions of 22q11 genes". International Journal of Developmental Neuroscience. 29 (3): 283–294. doi:10.1016/j.ijdevneu.2010.08.005. PMC 3770287. PMID 20833244.
  10. ↑ Kniffin C. "DiGeorge Syndrome; DGS. Retrieved April 2012, from Online Mendelian Inheritance in Man".
  11. ↑ Scambler PJ (2000). "The 22q11 deletion syndromes". Hum. Mol. Genet. 9 (16): 2421–6. doi:10.1093/hmg/9.16.2421. PMID 11005797.
  12. ↑ "22q11.2 Deletion Syndrome".
  13. ↑ "BLAT UCSC Genome Browser".
  14. ↑ "El Durado (Genomatix)".
  15. ↑ "El Durado-Genomatix".
  16. ↑ "Unigene NCBI". Archived from the original on 2013-07-12. Retrieved 2012-04-26.
  17. ↑ "GEO Profiles NCBI".
  18. ↑ "Bio GPS".
  19. ↑ "WormBase".
  20. ↑ "NetCGly (ExPASy)".
  21. ↑ "NetGlycate (ExPASy)".
  22. ↑ "Phos (ExPASy)".
  23. ↑ "CSS Palm (ExPASy)".
  24. ↑ Resh MD (2006). "Palmitoylation of Ligands, Receptors, and Intracellular Signaling Molecules". Science's STKE. 2006 (359): 14. doi:10.1126/stke.3592006re14. PMID 17077383.
  25. ↑ Draper JM, Xia Z, Smith CD (Aug 2007). "Cellular palmitoylation and trafficking of lipated peptides". NIH Public Access. 48 (8): 1873–1884. doi:10.1194/jlr.m700179-jlr200. PMC 2895159. PMID 17525474.
  26. ↑ Linder ME, Deschenes RJ (Jan 2007). "Palmitoylation: policing protein stability and traffic". Nature Reviews Molecular Cell Biology. 8 (1): 74–84. doi:10.1038/nrm2084. PMID 17183362.
  27. ↑ Greaves J, Chamberlain LH (Jan 2007). "Palmitoylation-dependent protein sorting". Cellular Biology. 176 (3): 249–254. doi:10.1083/jcb.200610151. PMC 2063950. PMID 17242068.
  28. ↑ Casey PJ (1995). "Protein lipidation in cell signaling". Science. 268 (5208): 221–5. doi:10.1126/science.7716512. PMID 7716512.
  29. ↑ Roth AF, Wan J, Bailey AO, Sun B, Kuchar JA, Green WN, Phinney BS, Yates JR, Davis NG (June 2006). "Global analysis of protein palmitoylation in yeast". Cell. 125 (5): 1003–1013. doi:10.1016/j.cell.2006.03.042. PMC 2246083. PMID 16751107.
  30. ↑ 30.0 30.1 30.2 30.3 30.4 30.5 30.6 30.7 30.8 "Molecular Interaction Database". Archived from the original on 2006-05-06.
  31. ↑ "Molecular Interaction Database". Archived from the original on 2006-05-06.
  32. ↑ "Viral Molecular Interaction Database". Archived from the original on 2015-02-15.
  33. ↑ 33.0 33.1 Kremer LS, Distelmaier F, Alhaddad B, Hempel M, Iuso A, Küpper C, et al. (2016). "Bi-allelic Truncating Mutations in TANGO2 Cause Infancy-Onset Recurrent Metabolic Crises with Encephalocardiomyopathy". American Journal of Human Genetics. 98 (2): 358–62. doi:10.1016/j.ajhg.2015.12.009. PMC 4746337. PMID 26805782.
  34. ↑ 34.0 34.1 Lalani SR, Liu P, Rosenfeld JA, Watkin LB, Chiang T, Leduc MS, et al. (2016). "Recurrent Muscle Weakness with Rhabdomyolysis, Metabolic Crises, and Cardiac Arrhythmia Due to Bi-allelic TANGO2 Mutations". American Journal of Human Genetics. 98 (2): 347–57. doi:10.1016/j.ajhg.2015.12.008. PMC 4746334. PMID 26805781.

External links

  • [2] www.tango2.it - Disease website
  • [3] www.tango2research.org - Research disease website -
Retrieved from "https://www.wikidoc.org/index.php?title=TANGO2&oldid=1518960"