1. Gene
    Locus 

2. Homology and Evolution
    Paralogs  Orthologs  Distant Homologs  Homologous Domains 

3. Protein
     Protein internal composition    Primary structure and isoforms   Domains and motifs    Post-translational modifications   Secondary structure  Tertiary structure 

4. Gene expression
     Promoter    Gene expression data   Transcript variants  

5. Function
     Possible transcription factors    Interactions  

6. Clinical significance

7. References

8. Further reading

SOGA2 has two human paralogs, SOGA1 and SOGA3.^[3][4]

In humans, the gene coding sequence is 151,349 base pairs long, with an mRNA of 6092 base pairs, and a protein sequence of 1586 amino acids. The SOGA2 gene is conserved in gorilla, baboon, galago, rat, mouse, cat, and more. There is distant conservation seen in organisms such as zebra finches and anoles.^[5]

SOGA2 is ubiquitously expressed in humans, with especially high expression in brain (especially the cerebellum and hippocampus), colon, pituitary gland, small intestine, spinal cord, testis and fetal brain.^[6]

Gene

Locus

The SOGA2 gene is located from 8717369 - 8832775 on the short arm of chromosome 18 (18p11.22).^[7]

Homology and Evolution

Paralogs

There are two main paralogs to SOGA2: human protein SOGA1 and human protein SOGA3.^[5] SOGA1 has been shown to be involved in suppression of glucose by autophagy.^[8] The rate at which orthologs diverge from SOGA2 human(measured by % identity) places the approximate duplication event of SOGA1 from SOGA2 at ~254.1 MYA and the duplication event of SOGA3 from SOGA2 ~329.1 MYA.

Orthologs

Many orthologs have been identified in Eukaryotes.^[5]

Distant Homologs

Homologous Domains

SOGA2 is conserved farthest back in its N-terminal region, where it contains its three domains of unknown function.^[9]

Protein

Protein internal composition

SOGA2 is rich in glycine (ratio r of SOGA2 composition to average human protein is 1.723), glutamate (r = 1.647), and arganine

(r = 1.357). It also has a lower than usual composition of tyrosine (r = 0.3406), isoleucine (r = 0.4430),

Primary structure and isoforms

Domains and motifs

Post-translational modifications

SOGA2 is expected to undergo a number of post-translational modifications. Modifications of human SOGA2 that are shared by orthologs include:

• Sumoylation at amino acids 87, 152, 235, 392, and 1379.^[14]
• Sulfination at tyrosines 14 and 1249.^[15]
• Phosphorylation at a number of sites, highlighted in the following graphic:

Secondary structure

The consensus of the prediction software PELE,^[17] GOR4,^[18] and SOSUICoil is that the secondary structure of SOGA2 is dominated by alpha helices with interspersed regions of random coil. GOR4 indicated that SOGA2 is dominated by alpha-helices; it predicted a mere 5.61% of

residues in an extended strand (parallel or antiparallel Beta-sheet) conformation, as opposed to

47.79% alpha helix and 46.6% random coils.

Tertiary structure

SOGA2 shares sequence features in its highly conserved N-terminal region. This homology allows prediction of its tertiary structure on the basis of homology to published 3d structures via Phyre2^[20] and NCBI structure.^[21]

Gene expression

Promoter

The promoter for human SOGA2 is below.

Gene expression data

The EST profile shows that, in humans, SOGA2 is highly expressed in many sites throughout the body, including bone, brain, ear, eye, and many others.^[22] There are a large number of transcripts in liver cancer samples. Human microarray data show that SOGA2 is moderately expressed, with especially high expression in brain (especially the cerebellum and hippocampus), colon, pituitary gland, small intestine, spinal cord, testis and fetal brain.^[6] Brain-tissue-specific microarray data show that SOGA2 has high expression throughout the posterior lobe of the cerebellar hemispheres and posterial lobe of the vermis in the mouse brain. There is low expression in most other areas of the brain.^[23]

Transcript variants

In humans, the SOGA2 gene produces 17 different transcripts, 8 of which form a protein product (one undergoes nonsense mediated decay). The main transcript in humans is transcript ID ENST00000359865, or SOGA2-001.^[24]

Function

Possible transcription factors

Possible transcription factors for human SOGA2 include:^[25]

• Modulator recognition factor 2
• cAMP-responsive element binding protein 1
• alternative splicing variant of FOXP1
• MDS1/EVI1-like gene 1
• Ikaros 2, possible regulator of lymphocyte differentiation

Interactions

Protein complex co-immunoprecipitation (Co-IP) experiments revealed interacting proteins such as cell death regulators, ATP-binding cassette (ABC) transporters and protein kinase A binding proteins.^[26]

The 540 interacting proteins include ABCF1, ACTB, ACTL6A, BCLAF1, BCLAF1, CHEK1, and MAGEE2.^[26]

K-nearest neighbor analysis by wolf pSort indicates that in humans, SOGA2 is focused mainly in the nucleus, cytoplasm, and the cytonuclear

space. There is a small chance that it is localizes to the golgi.^[27]

A number of protein interactants were also identified via the STRING database, including MARK2, MARK4, and PPP2R2B.

Clinical significance

SOGA2 has no currently known disease associations or mutations.

References

Further reading

• {{cite journal | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |name-list-format=vanc| author2=Feingold EA | author3=Grouse LH | display-authors=3 | last4=Derge | first4=JG | last5=Klausner | first5=RD | last6=Collins | first6=FS | last7=Wagner | first7=L | last8=Shenmen | first8=CM | last9=Schuler | first9=GD }}
• {{cite journal | author=Brajenovic M |title=Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network |journal=J. Biol. Chem. |volume=279 |issue= 13 |pages= 12804–11 |year= 2004 |pmid= 14676191 |doi= 10.1074/jbc.M312171200 |name-list-format=vanc| author2=Joberty G | author3=Küster B | display-authors=3 | last4=Bouwmeester | first4=T | last5=Drewes | first5=G }}
• {{cite journal | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |name-list-format=vanc| author2=Suzuki Y | author3=Nishikawa T | display-authors=3 | last4=Otsuki | first4=Tetsuji | last5=Sugiyama | first5=Tomoyasu | last6=Irie | first6=Ryotaro | last7=Wakamatsu | first7=Ai | last8=Hayashi | first8=Koji | last9=Sato | first9=Hiroyuki }}
• {{cite journal | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |name-list-format=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }}
• {{cite journal | author=Nusbaum C |title=DNA sequence and analysis of human chromosome 18 |journal=Nature |volume=437 |issue= 7058 |pages= 551–5 |year= 2005 |pmid= 16177791 |doi= 10.1038/nature03983 |name-list-format=vanc| author2=Zody MC | author3=Borowsky ML | display-authors=3 | last4=Kamal | first4=Michael | last5=Kodira | first5=Chinnappa D. | last6=Taylor | first6=Todd D. | last7=Whittaker | first7=Charles A. | last8=Chang | first8=Jean L. | last9=Cuomo | first9=Christina A. }}
• {{cite journal | author=Nousiainen M |title=Phosphoproteome analysis of the human mitotic spindle |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=103 |issue= 14 |pages= 5391–6 |year= 2006 |pmid= 16565220 |doi= 10.1073/pnas.0507066103 | pmc=1459365 |name-list-format=vanc| author2=Silljé HH | author3=Sauer G | display-authors=3 | last4=Nigg | first4=EA | last5=Körner | first5=R }}
• {{cite journal | author=Beausoleil SA |title=A probability-based approach for high-throughput protein phosphorylation analysis and site localization |journal=Nat. Biotechnol. |volume=24 |issue= 10 |pages= 1285–92 |year= 2006 |pmid= 16964243 |doi= 10.1038/nbt1240 |name-list-format=vanc| author2=Villén J | author3=Gerber SA | display-authors=3 | last4=Rush | first4=John | last5=Gygi | first5=Steven P }}
• {{cite journal | author=Olsen JV |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026 |name-list-format=vanc| author2=Blagoev B | author3=Gnad F | display-authors=3 | last4=Macek | first4=Boris | last5=Kumar | first5=Chanchal | last6=Mortensen | first6=Peter | last7=Mann | first7=Matthias }}

• Canonesses Regular of St. Victor
• Canon F1
• Canon FARE
• Canon FD 135mm f/3.5 S.C. (I)
• Canon FL
• Canon FL 300mm lens
• Canon Frome
• Canon Frome Court
• Canon G
• Canon G16
• Canon G1X
• Canon G1 X
• Canon G 1X
• Canon G1 X 2
• Canon G1 X II
• Canon G1 X Mark 2
• Canon G1 X Mark II
• Canon G1 X Mk 2
• Canon G1 X Mk. 2
• Canon G1 X Mk. II
• Canon G1 X Mk II
• Canon G3 X
• Canon G3X
• Canon G 3X
• Canon G7 X