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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{Infobox_gene}}
{{GNF_Protein_box
'''Protein-glutamine gamma-glutamyltransferase E''' is an [[enzyme]] that in humans is encoded by the ''TGM3'' [[gene]].<ref name="pmid7851911">{{cite journal | vauthors = Wang M, Kim IG, Steinert PM, McBride OW | title = Assignment of the human transglutaminase 2 (TGM2) and transglutaminase 3 (TGM3) genes to chromosome 20q11.2 | journal = Genomics | volume = 23 | issue = 3 | pages = 721–2 |date=Mar 1995 | pmid = 7851911 | pmc =  | doi = 10.1006/geno.1994.1571 }}</ref><ref name="pmid9452468">{{cite journal | vauthors = Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF | title = Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes. Detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers | journal = J Biol Chem | volume = 273 | issue = 6 | pages = 3452–60 |date=Mar 1998 | pmid = 9452468 | pmc =  | doi =10.1074/jbc.273.6.3452 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TGM3 transglutaminase 3 (E polypeptide, protein-glutamine-gamma-glutamyltransferase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7053| accessdate = }}</ref>
| image = PBB_Protein_TGM3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1l9m.
| PDB = {{PDB2|1l9m}}, {{PDB2|1l9n}}, {{PDB2|1nud}}, {{PDB2|1nuf}}, {{PDB2|1nug}}, {{PDB2|1rle}}, {{PDB2|1sgx}}, {{PDB2|1vjj}}
| Name = Transglutaminase 3 (E polypeptide, protein-glutamine-gamma-glutamyltransferase)
| HGNCid = 11779
| Symbol = TGM3
| AltSymbols =; MGC126249; MGC126250; TGE
| OMIM = 600238
| ECnumber =
| Homologene = 20690
| MGIid = 98732
  | GeneAtlas_image1 = PBB_GE_TGM3_206004_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003810 |text = protein-glutamine gamma-glutamyltransferase activity}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016746 |text = transferase activity, transferring acyl groups}} {{GNF_GO|id=GO:0019003 |text = GDP binding}}
| Component = {{GNF_GO|id=GO:0001533 |text = cornified envelope}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0031234 |text = extrinsic to internal side of plasma membrane}}
| Process = {{GNF_GO|id=GO:0018149 |text = peptide cross-linking}} {{GNF_GO|id=GO:0030216 |text = keratinocyte differentiation}} {{GNF_GO|id=GO:0031069 |text = hair follicle morphogenesis}} {{GNF_GO|id=GO:0031424 |text = keratinization}} {{GNF_GO|id=GO:0035315 |text = hair cell differentiation}} {{GNF_GO|id=GO:0043163 |text = cell envelope organization and biogenesis}} {{GNF_GO|id=GO:0043588 |text = skin development}} {{GNF_GO|id=GO:0051262 |text = protein tetramerization}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7053
    | Hs_Ensembl = ENSG00000125780
    | Hs_RefseqProtein = NP_003236
    | Hs_RefseqmRNA = NM_003245
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 2224647
    | Hs_GenLoc_end = 2269724
    | Hs_Uniprot = Q08188
    | Mm_EntrezGene = 21818
    | Mm_Ensembl = ENSMUSG00000027401
    | Mm_RefseqmRNA = NM_009374
    | Mm_RefseqProtein = NP_033400
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 129703790
    | Mm_GenLoc_end = 129740002
    | Mm_Uniprot = Q08189
  }}
}}
'''Transglutaminase 3 (E polypeptide, protein-glutamine-gamma-glutamyltransferase)''', also known as '''TGM3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TGM3 transglutaminase 3 (E polypeptide, protein-glutamine-gamma-glutamyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7053| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =
| summary_text = Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene consists of two polypeptide chains activated from a single precursor protein by proteolysis. The encoded protein is involved the later stages of cell envelope formation in the epidermis and hair follicle.<ref name="entrez">{{cite web | title = Entrez Gene: TGM3 transglutaminase 3 (E polypeptide, protein-glutamine-gamma-glutamyltransferase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7053| accessdate = }}</ref>
| summary_text = Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene consists of two polypeptide chains activated from a single precursor protein by proteolysis. The encoded protein is involved the later stages of cell envelope formation in the epidermis and hair follicle.<ref name="entrez" />
}}
}}
==See also==
* Proximal promoter


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| citations =
*{{cite journal  | author=Ahvazi B, Boeshans KM, Rastinejad F |title=The emerging structural understanding of transglutaminase 3. |journal=J. Struct. Biol. |volume=147 |issue= 2 |pages= 200-7 |year= 2005 |pmid= 15193648 |doi= 10.1016/j.jsb.2004.03.009 }}
* {{cite journal  | vauthors=Ahvazi B, Boeshans KM, Rastinejad F |title=The emerging structural understanding of transglutaminase 3 |journal=J. Struct. Biol. |volume=147 |issue= 2 |pages= 200–7 |year= 2005 |pmid= 15193648 |doi= 10.1016/j.jsb.2004.03.009 }}
*{{cite journal  | author=Rice RH, Green H |title=Relation of protein synthesis and transglutaminase activity to formation of the cross-linked envelope during terminal differentiation of the cultured human epidermal keratinocyte. |journal=J. Cell Biol. |volume=76 |issue= 3 |pages= 705-11 |year= 1978 |pmid= 24643 |doi=  }}
* {{cite journal  | vauthors=Rice RH, Green H |title=Relation of protein synthesis and transglutaminase activity to formation of the cross-linked envelope during terminal differentiation of the cultured human epidermal keratinocyte |journal=J. Cell Biol. |volume=76 |issue= 3 |pages= 705–11 |year= 1978 |pmid= 24643 |doi=10.1083/jcb.76.3.705  | pmc=2110014 }}
*{{cite journal  | author=Steck TL |title=Cross-linking the major proteins of the isolated erythrocyte membrane. |journal=J. Mol. Biol. |volume=66 |issue= 2 |pages= 295-305 |year= 1972 |pmid= 5038456 |doi= }}
* {{cite journal  | author=Steck TL |title=Cross-linking the major proteins of the isolated erythrocyte membrane |journal=J. Mol. Biol. |volume=66 |issue= 2 |pages= 295–305 |year= 1972 |pmid= 5038456 |doi=10.1016/0022-2836(72)90481-0  }}
*{{cite journal | author=Mariniello L, Esposito C, Di Pierro P, ''et al.'' |title=Human-immunodeficiency-virus transmembrane glycoprotein gp41 is an amino acceptor and donor substrate for transglutaminase in vitro. |journal=Eur. J. Biochem. |volume=215 |issue= 1 |pages= 99-104 |year= 1993 |pmid= 7688299 |doi= }}
* {{cite journal   |vauthors=Mariniello L, Esposito C, Di Pierro P, etal |title=Human-immunodeficiency-virus transmembrane glycoprotein gp41 is an amino acceptor and donor substrate for transglutaminase in vitro |journal=Eur. J. Biochem. |volume=215 |issue= 1 |pages= 99–104 |year= 1993 |pmid= 7688299 |doi=10.1111/j.1432-1033.1993.tb18011.x  }}
*{{cite journal | author=Wang M, Kim IG, Steinert PM, McBride OW |title=Assignment of the human transglutaminase 2 (TGM2) and transglutaminase 3 (TGM3) genes to chromosome 20q11.2. |journal=Genomics |volume=23 |issue= 3 |pages= 721-2 |year= 1995 |pmid= 7851911 |doi= 10.1006/geno.1994.1571 }}
* {{cite journal   |vauthors=Amendola A, Lombardi G, Oliverio S, etal |title=HIV-1 gp120-dependent induction of apoptosis in antigen-specific human T cell clones is characterized by 'tissue' transglutaminase expression and prevented by cyclosporin A |journal=FEBS Lett. |volume=339 |issue= 3 |pages= 258–64 |year= 1994 |pmid= 7906657 |doi=10.1016/0014-5793(94)80427-3  }}
*{{cite journal | author=Amendola A, Lombardi G, Oliverio S, ''et al.'' |title=HIV-1 gp120-dependent induction of apoptosis in antigen-specific human T cell clones is characterized by 'tissue' transglutaminase expression and prevented by cyclosporin A. |journal=FEBS Lett. |volume=339 |issue= 3 |pages= 258-64 |year= 1994 |pmid= 7906657 |doi=  }}
* {{cite journal   |vauthors=Kim IG, Lee SC, Lee JH, etal |title=Structure and organization of the human transglutaminase 3 gene: evolutionary relationship to the transglutaminase family |journal=J. Invest. Dermatol. |volume=103 |issue= 2 |pages= 137–42 |year= 1994 |pmid= 7913719 |doi=10.1111/1523-1747.ep12392470 }}
*{{cite journal | author=Kim IG, Lee SC, Lee JH, ''et al.'' |title=Structure and organization of the human transglutaminase 3 gene: evolutionary relationship to the transglutaminase family. |journal=J. Invest. Dermatol. |volume=103 |issue= 2 |pages= 137-42 |year= 1994 |pmid= 7913719 |doi=  }}
* {{cite journal   |vauthors=Kim IG, Gorman JJ, Park SC, etal |title=The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse |journal=J. Biol. Chem. |volume=268 |issue= 17 |pages= 12682–90 |year= 1993 |pmid= 8099584 |doi=  }}
*{{cite journal | author=Kim IG, Gorman JJ, Park SC, ''et al.'' |title=The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse. |journal=J. Biol. Chem. |volume=268 |issue= 17 |pages= 12682-90 |year= 1993 |pmid= 8099584 |doi=  }}
* {{cite journal   |vauthors=Lee JH, Jang SI, Yang JM, etal |title=The proximal promoter of the human transglutaminase 3 gene. Stratified squamous epithelial-specific expression in cultured cells is mediated by binding of Sp1 and ets transcription factors to a proximal promoter element |journal=J. Biol. Chem. |volume=271 |issue= 8 |pages= 4561–8 |year= 1996 |pmid= 8626812 |doi=  10.1074/jbc.271.8.4561}}
*{{cite journal | author=Lee JH, Jang SI, Yang JM, ''et al.'' |title=The proximal promoter of the human transglutaminase 3 gene. Stratified squamous epithelial-specific expression in cultured cells is mediated by binding of Sp1 and ets transcription factors to a proximal promoter element. |journal=J. Biol. Chem. |volume=271 |issue= 8 |pages= 4561-8 |year= 1996 |pmid= 8626812 |doi= }}
* {{cite journal   |vauthors=Hillier LD, Lennon G, Becker M, etal |title=Generation and analysis of 280,000 human expressed sequence tags |journal=Genome Res. |volume=6 |issue= 9 |pages= 807–28 |year= 1997 |pmid= 8889549 |doi=10.1101/gr.6.9.807  }}
*{{cite journal | author=Hillier LD, Lennon G, Becker M, ''et al.'' |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807-28 |year= 1997 |pmid= 8889549 |doi=  }}
* {{cite journal   |vauthors=Kim SY, Grant P, Lee JH, etal |title=Differential expression of multiple transglutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer's disease |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30715–21 |year= 1999 |pmid= 10521460 |doi=10.1074/jbc.274.43.30715 }}
*{{cite journal | author=Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF |title=Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes. Detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3452-60 |year= 1998 |pmid= 9452468 |doi= }}
* {{cite journal   |vauthors=Méhul B, Bernard D, Simonetti L, etal |title=Identification and cloning of a new calmodulin-like protein from human epidermis |journal=J. Biol. Chem. |volume=275 |issue= 17 |pages= 12841–7 |year= 2000 |pmid= 10777582 |doi=10.1074/jbc.275.17.12841  }}
*{{cite journal | author=Kim SY, Grant P, Lee JH, ''et al.'' |title=Differential expression of multiple transglutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer's disease. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30715-21 |year= 1999 |pmid= 10521460 |doi= }}
* {{cite journal   |vauthors=Deloukas P, Matthews LH, Ashurst J, etal |title=The DNA sequence and comparative analysis of human chromosome 20 |journal=Nature |volume=414 |issue= 6866 |pages= 865–71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Méhul B, Bernard D, Simonetti L, ''et al.'' |title=Identification and cloning of a new calmodulin-like protein from human epidermis. |journal=J. Biol. Chem. |volume=275 |issue= 17 |pages= 12841-7 |year= 2000 |pmid= 10777582 |doi= }}
* {{cite journal   |vauthors=Sárdy M, Kárpáti S, Merkl B, etal |title=Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis |journal=J. Exp. Med. |volume=195 |issue= 6 |pages= 747–57 |year= 2002 |pmid= 11901200 |doi=10.1084/jem.20011299  | pmc=2193738  }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
* {{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 }}
*{{cite journal | author=Sárdy M, Kárpáti S, Merkl B, ''et al.'' |title=Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis. |journal=J. Exp. Med. |volume=195 |issue= 6 |pages= 747-57 |year= 2002 |pmid= 11901200 |doi= }}
* {{cite journal   |vauthors=Ahvazi B, Boeshans KM, Idler W, etal |title=Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 23834–41 |year= 2003 |pmid= 12679341 |doi= 10.1074/jbc.M301162200 }}
*{{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   |vauthors=Hitomi K, Presland RB, Nakayama T, etal |title=Analysis of epidermal-type transglutaminase (transglutaminase 3) in human stratified epithelia and cultured keratinocytes using monoclonal antibodies |journal=J. Dermatol. Sci. |volume=32 |issue= 2 |pages= 95–103 |year= 2004 |pmid= 12850301 |doi=10.1016/S0923-1811(03)00091-4 }}
*{{cite journal  | author=Ahvazi B, Boeshans KM, Idler W, ''et al.'' |title=Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme. |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 23834-41 |year= 2003 |pmid= 12679341 |doi= 10.1074/jbc.M301162200 }}
* {{cite journal   |vauthors=Gonzalez HE, Gujrati M, Frederick M, etal |title=Identification of 9 genes differentially expressed in head and neck squamous cell carcinoma |journal=Arch. Otolaryngol. Head Neck Surg. |volume=129 |issue= 7 |pages= 754–9 |year= 2003 |pmid= 12874078 |doi= 10.1001/archotol.129.7.754 }}
*{{cite journal  | author=Hitomi K, Presland RB, Nakayama T, ''et al.'' |title=Analysis of epidermal-type transglutaminase (transglutaminase 3) in human stratified epithelia and cultured keratinocytes using monoclonal antibodies. |journal=J. Dermatol. Sci. |volume=32 |issue= 2 |pages= 95-103 |year= 2004 |pmid= 12850301 |doi= }}
* {{cite journal   |vauthors=Ahvazi B, Boeshans KM, Idler W, etal |title=Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium |journal=J. Biol. Chem. |volume=279 |issue= 8 |pages= 7180–92 |year= 2004 |pmid= 14645372 |doi= 10.1074/jbc.M312310200 }}
*{{cite journal | author=Gonzalez HE, Gujrati M, Frederick M, ''et al.'' |title=Identification of 9 genes differentially expressed in head and neck squamous cell carcinoma. |journal=Arch. Otolaryngol. Head Neck Surg. |volume=129 |issue= 7 |pages= 754-9 |year= 2003 |pmid= 12874078 |doi= 10.1001/archotol.129.7.754 }}
*{{cite journal | author=Ahvazi B, Boeshans KM, Idler W, ''et al.'' |title=Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium. |journal=J. Biol. Chem. |volume=279 |issue= 8 |pages= 7180-92 |year= 2004 |pmid= 14645372 |doi= 10.1074/jbc.M312310200 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=7053}}
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Latest revision as of 11:49, 15 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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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

Protein-glutamine gamma-glutamyltransferase E is an enzyme that in humans is encoded by the TGM3 gene.[1][2][3]

Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene consists of two polypeptide chains activated from a single precursor protein by proteolysis. The encoded protein is involved the later stages of cell envelope formation in the epidermis and hair follicle.[3]

See also

  • Proximal promoter

References

  1. ↑ Wang M, Kim IG, Steinert PM, McBride OW (Mar 1995). "Assignment of the human transglutaminase 2 (TGM2) and transglutaminase 3 (TGM3) genes to chromosome 20q11.2". Genomics. 23 (3): 721–2. doi:10.1006/geno.1994.1571. PMID 7851911.
  2. ↑ Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF (Mar 1998). "Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes. Detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers". J Biol Chem. 273 (6): 3452–60. doi:10.1074/jbc.273.6.3452. PMID 9452468.
  3. ↑ 3.0 3.1 "Entrez Gene: TGM3 transglutaminase 3 (E polypeptide, protein-glutamine-gamma-glutamyltransferase)".

Further reading



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