CRYGS: Difference between revisions

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(This gene was incorrectly identified as encoding for a beta-crystallin S protein, when it actually encodes for a gamma-crystallin S protein.)
 
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{{Infobox_gene}}
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'''Gamma-crystallin S''' is a [[protein]] that in humans is encoded by the ''CRYGS'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CRYGS crystallin, gamma S| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1427| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_CRYGS_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a7h.
| PDB = {{PDB2|1a7h}}, {{PDB2|1ha4}}
| Name = Crystallin, gamma S
| HGNCid = 2417
| Symbol = CRYGS
| AltSymbols =; CRYG8
| OMIM = 123730
| ECnumber = 
| Homologene = 40695
| MGIid = 1298216
| GeneAtlas_image1 = PBB_GE_CRYGS_gnf1h01270_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005212 |text = structural constituent of eye lens}}
| Component =
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1427
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_060011
    | Hs_RefseqmRNA = NM_017541
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 12970
    | Mm_Ensembl = ENSMUSG00000033501
    | Mm_RefseqmRNA = NM_009967
    | Mm_RefseqProtein = NP_034097
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 22720538
    | Mm_GenLoc_end = 22726740
    | Mm_Uniprot = Q3UPY3
  }}
}}
'''Crystallin, gamma S''', also known as '''CRYGS''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CRYGS crystallin, gamma S| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1427| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. This gene encodes a protein initially considered to be a beta-crystallin but the encoded protein is monomeric and has greater sequence similarity to other gamma-crystallins. This gene encodes the most significant gamma-crystallin in adult eye lens tissue. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.<ref name="entrez">{{cite web | title = Entrez Gene: CRYGS crystallin, gamma S| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1427| accessdate = }}</ref>
| summary_text = [[Crystallins]] are separated into two classes: taxon-specific, or [[enzyme]], and ubiquitous. The latter class constitutes the major [[Protein|proteins]] of vertebrate eye lens and maintains the transparency and [[refractive index]] of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins.  
 
Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting [[peptide]], and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. This gene encodes a protein initially considered to be a beta-crystallin but the encoded protein is [[monomeric]] and has greater sequence similarity to other gamma-crystallins. This gene encodes the most significant gamma-crystallin in adult eye lens tissue.  
 
Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in [[cataract]] formation.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|CRYGS}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Graw J |title=The crystallins: genes, proteins and diseases. |journal=Biol. Chem. |volume=378 |issue= 11 |pages= 1331-48 |year= 1998 |pmid= 9426193 |doi=  }}
*{{cite journal  | author=Graw J |title=The crystallins: genes, proteins and diseases |journal=Biol. Chem. |volume=378 |issue= 11 |pages= 1331–48 |year= 1998 |pmid= 9426193 |doi=  10.1515/bchm.1997.378.11.1299}}
*{{cite journal  | author=Slingsby C, Clout NJ |title=Structure of the crystallins. |journal=Eye (London, England) |volume=13 ( Pt 3b) |issue=  |pages= 395-402 |year= 2000 |pmid= 10627816 |doi=  }}
*{{cite journal  | vauthors=Slingsby C, Clout NJ |title=Structure of the crystallins |journal=Eye (London, England) |volume=13 ( Pt 3b) |issue=  |pages= 395–402 |year= 2000 |pmid= 10627816 |doi=  10.1038/eye.1999.113}}
*{{cite journal  | author=Zarina S, Abbasi A, Zaidi ZH |title=Primary structure of beta s-crystallin from human lens. |journal=Biochem. J. |volume=287 ( Pt 2) |issue=  |pages= 375-81 |year= 1992 |pmid= 1445197 |doi=  }}
*{{cite journal  | vauthors=Zarina S, Abbasi A, Zaidi ZH |title=Primary structure of beta s-crystallin from human lens |journal=Biochem. J. |volume=287 |issue=  Pt 2|pages= 375–81 |year= 1992 |pmid= 1445197 |doi= 10.1042/bj2870375| pmc=1133175 }}
*{{cite journal  | author=Brakenhoff RH, Aarts HJ, Reek FH, ''et al.'' |title=Human gamma-crystallin genes. A gene family on its way to extinction. |journal=J. Mol. Biol. |volume=216 |issue= 3 |pages= 519-32 |year= 1991 |pmid= 2258929 |doi= }}
*{{cite journal  | author=Brakenhoff RH |title=Human gamma-crystallin genes. A gene family on its way to extinction |journal=J. Mol. Biol. |volume=216 |issue= 3 |pages= 519–32 |year= 1991 |pmid= 2258929 |doi=10.1016/0022-2836(90)90380-5 |name-list-format=vanc| author2=Aarts HJ  | author3=Reek FH  | display-authors=3  | last4=Lubsen  | first4=NH  | last5=Schoenmakers  | first5=JG }}
*{{cite journal | author=Meakin SO, Du RP, Tsui LC, Breitman ML |title=Gamma-crystallins of the human eye lens: expression analysis of five members of the gene family. |journal=Mol. Cell. Biol. |volume=7 |issue= 8 |pages= 2671-9 |year= 1987 |pmid= 3670288 |doi=  }}
*{{cite journal  | vauthors=Meakin SO, Du RP, Tsui LC, Breitman ML |title=Gamma-crystallins of the human eye lens: expression analysis of five members of the gene family |journal=Mol. Cell. Biol. |volume=7 |issue= 8 |pages= 2671–9 |year= 1987 |pmid= 3670288 |doi= | pmc=367883 }}
*{{cite journal  | author=Smith JB, Yang Z, Lin P, ''et al.'' |title=The complete sequence of human lens gamma s-crystallin. |journal=Biochem. J. |volume=307 ( Pt 2) |issue= |pages= 407-10 |year= 1995 |pmid= 7733876 |doi=  }}
*{{cite journal  | author=Smith JB |title=The complete sequence of human lens gamma s-crystallin |journal=Biochem. J. |volume=307 |issue= Pt 2|pages= 407–10 |year= 1995 |pmid= 7733876 |doi=  10.1042/bj3070407| pmc=1136663 |name-list-format=vanc| author2=Yang Z | author3=Lin P  | display-authors=3  | last4=Zaidi  | first4=Z  | last5=Abbasi  | first5=A  | last6=Russell  | first6=P }}
*{{cite journal  | author=Zarina S, Slingsby C, Jaenicke R, ''et al.'' |title=Three-dimensional model and quaternary structure of the human eye lens protein gamma S-crystallin based on beta- and gamma-crystallin X-ray coordinates and ultracentrifugation. |journal=Protein Sci. |volume=3 |issue= 10 |pages= 1840-6 |year= 1995 |pmid= 7849599 |doi=  }}
*{{cite journal  | author=Zarina S |title=Three-dimensional model and quaternary structure of the human eye lens protein gamma S-crystallin based on beta- and gamma-crystallin X-ray coordinates and ultracentrifugation |journal=Protein Sci. |volume=3 |issue= 10 |pages= 1840–6 |year= 1995 |pmid= 7849599 |doi=10.1002/pro.5560031023 | pmc=2142617 |name-list-format=vanc| author2=Slingsby C  | author3=Jaenicke R  | display-authors=3  | last4=Srinivasan  | first4=N. | last5=Slingsby  | first5=C.  | last6=Jaenicke  | first6=R.  }}
*{{cite journal | author=Lampi KJ, Ma Z, Shih M, ''et al.'' |title=Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2268-75 |year= 1997 |pmid= 8999933 |doi=  }}
*{{cite journal  | author=Lampi KJ |title=Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2268–75 |year= 1997 |pmid= 8999933 |doi=10.1074/jbc.272.4.2268  |name-list-format=vanc| author2=Ma Z  | author3=Shih M  | display-authors=3  | last4=Shearer | first4=TR  | last5=Smith | first5=JB  | last6=Smith  | first6=DL  | last7=David  | first7=LL }}
*{{cite journal  | author=Wistow G, Sardarian L, Gan W, Wyatt MK |title=The human gene for gammaS-crystallin: alternative transcripts and expressed sequences from the first intron. |journal=Mol. Vis. |volume=6 |issue= |pages= 79-84 |year= 2000 |pmid= 10837510 |doi=  }}
*{{cite journal  | vauthors=Wistow G, Sardarian L, Gan W, Wyatt MK |title=The human gene for gammaS-crystallin: alternative transcripts and expressed sequences from the first intron |journal=Mol. Vis. |volume=6 |issue= |pages= 79–84 |year= 2000 |pmid= 10837510 |doi=  }}
*{{cite journal | author=Purkiss AG, Bateman OA, Goodfellow JM, ''et al.'' |title=The X-ray crystal structure of human gamma S-crystallin C-terminal domain. |journal=J. Biol. Chem. |volume=277 |issue= 6 |pages= 4199-205 |year= 2002 |pmid= 11706012 |doi= 10.1074/jbc.M110083200 }}
*{{cite journal  | author=Purkiss AG |title=The X-ray crystal structure of human gamma S-crystallin C-terminal domain |journal=J. Biol. Chem. |volume=277 |issue= 6 |pages= 4199–205 |year= 2002 |pmid= 11706012 |doi= 10.1074/jbc.M110083200 |name-list-format=vanc| author2=Bateman OA  | author3=Goodfellow JM  | display-authors=3  | last4=Lubsen  | first4=NH  | last5=Slingsby  | first5=C }}
*{{cite journal | author=MacCoss MJ, McDonald WH, Saraf A, ''et al.'' |title=Shotgun identification of protein modifications from protein complexes and lens tissue. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 12 |pages= 7900-5 |year= 2002 |pmid= 12060738 |doi= 10.1073/pnas.122231399 }}
*{{cite journal  | author=MacCoss MJ |title=Shotgun identification of protein modifications from protein complexes and lens tissue |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 12 |pages= 7900–5 |year= 2002 |pmid= 12060738 |doi= 10.1073/pnas.122231399 | pmc=122992  |name-list-format=vanc| author2=McDonald WH  | author3=Saraf A  | display-authors=3  | last4=Sadygov  | first4=R  | last5=Clark  | first5=JM  | last6=Tasto  | first6=JJ  | last7=Gould | first7=KL  | last8=Wolters  | first8=D  | last9=Washburn  | first9=M }}
*{{cite journal | author=Lapko VN, Purkiss AG, Smith DL, Smith JB |title=Deamidation in human gamma S-crystallin from cataractous lenses is influenced by surface exposure. |journal=Biochemistry |volume=41 |issue= 27 |pages= 8638-48 |year= 2002 |pmid= 12093281 |doi=  }}
*{{cite journal | vauthors=Lapko VN, Purkiss AG, Smith DL, Smith JB |title=Deamidation in human gamma S-crystallin from cataractous lenses is influenced by surface exposure |journal=Biochemistry |volume=41 |issue= 27 |pages= 8638–48 |year= 2002 |pmid= 12093281 |doi=10.1021/bi015924t  }}
*{{cite journal  | author=Lapko VN, Smith DL, Smith JB |title=S-methylated cysteines in human lens gamma S-crystallins. |journal=Biochemistry |volume=41 |issue= 50 |pages= 14645-51 |year= 2003 |pmid= 12475213 |doi=  }}
*{{cite journal  | vauthors=Lapko VN, Smith DL, Smith JB |title=S-methylated cysteines in human lens gamma S-crystallins |journal=Biochemistry |volume=41 |issue= 50 |pages= 14645–51 |year= 2003 |pmid= 12475213 |doi=10.1021/bi0267700  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{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=Annunziata O, Ogun O, Benedek GB |title=Observation of liquid-liquid phase separation for eye lens gammaS-crystallin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 3 |pages= 970-4 |year= 2003 |pmid= 12529503 |doi= 10.1073/pnas.242746499 }}
*{{cite journal  | vauthors=Annunziata O, Ogun O, Benedek GB |title=Observation of liquid–liquid phase separation for eye lens γS-crystallin |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 3 |pages= 970–4 |year= 2003 |pmid= 12529503 |doi= 10.1073/pnas.242746499  | pmc=298710 }}
*{{cite journal  | author=Craghill J, Cronshaw AD, Harding JJ |title=The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens. |journal=Biochem. J. |volume=379 |issue= Pt 3 |pages= 595-600 |year= 2004 |pmid= 14763903 |doi= 10.1042/BJ20031367 }}
*{{cite journal  | vauthors=Craghill J, Cronshaw AD, Harding JJ |title=The identification of a reaction site of glutathione mixed-disulphide formation on gammaS-crystallin in human lens |journal=Biochem. J. |volume=379 |issue= Pt 3 |pages= 595–600 |year= 2004 |pmid= 14763903 |doi= 10.1042/BJ20031367  | pmc=1224128 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 }}
*{{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=Sun H, Ma Z, Li Y, ''et al.'' |title=Gamma-S crystallin gene (CRYGS) mutation causes dominant progressive cortical cataract in humans. |journal=J. Med. Genet. |volume=42 |issue= 9 |pages= 706-10 |year= 2006 |pmid= 16141006 |doi= 10.1136/jmg.2004.028274 }}
*{{cite journal  | author=Sun H |title=Gamma-S crystallin gene (CRYGS) mutation causes dominant progressive cortical cataract in humans |journal=J. Med. Genet. |volume=42 |issue= 9 |pages= 706–10 |year= 2006 |pmid= 16141006 |doi= 10.1136/jmg.2004.028274 | pmc=1736139  |name-list-format=vanc| author2=Ma Z  | author3=Li Y  | display-authors=3  | last4=Liu  | first4=B  | last5=Li  | first5=Z  | last6=Ding  | first6=X  | last7=Gao  | first7=Y  | last8=Ma  | first8=W  | last9=Tang  | first9=X }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=1427}}
{{Eye proteins}}
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Latest revision as of 19:44, 31 July 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

n/a

RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Gamma-crystallin S is a protein that in humans is encoded by the CRYGS gene.[1]

Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins.

Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. This gene encodes a protein initially considered to be a beta-crystallin but the encoded protein is monomeric and has greater sequence similarity to other gamma-crystallins. This gene encodes the most significant gamma-crystallin in adult eye lens tissue.

Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: CRYGS crystallin, gamma S".

External links

Further reading



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