TGM3

Protein-coding gene in the species Homo sapiens
TGM3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1L9M, 1L9N, 1NUD, 1NUF, 1NUG

Identifiers
AliasesTGM3, TGE, transglutaminase 3, UHS2
External IDsOMIM: 600238; MGI: 98732; HomoloGene: 20690; GeneCards: TGM3; OMA:TGM3 - orthologs
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for TGM3
Genomic location for TGM3
Band20p13Start2,296,001 bp[1]
End2,341,079 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for TGM3
Genomic location for TGM3
Band2|2 F1Start129,854,269 bp[2]
End129,892,319 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • skin of leg

  • skin of abdomen

  • right uterine tube

  • tonsil

  • minor salivary glands

  • vagina

  • ectocervix

  • gallbladder

  • blood

  • granulocyte
Top expressed in
  • esophagus

  • left colon

  • lip

  • superior surface of tongue

  • granulocyte

  • hair follicle

  • skin of back

  • skin of abdomen

  • trachea

  • pretectal area
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • metal ion binding
  • calcium ion binding
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • acyltransferase activity
Cellular component
  • extrinsic component of cytoplasmic side of plasma membrane
  • extracellular exosome
  • cytoplasm
Biological process
  • keratinization
  • protein tetramerization
  • hair follicle morphogenesis
  • cell envelope organization
  • peptide cross-linking
  • keratinocyte differentiation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7053

21818

Ensembl

ENSG00000125780

ENSMUSG00000027401

UniProt

Q08188

Q08189

RefSeq (mRNA)

NM_003245

NM_009374

RefSeq (protein)

NP_003236

NP_033400

Location (UCSC)Chr 20: 2.3 – 2.34 MbChr 2: 129.85 – 129.89 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein-glutamine gamma-glutamyltransferase E is an enzyme that in humans is encoded by the TGM3 gene.[5][6][7]

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.[7]

See also

  • Proximal promoter

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000125780 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027401 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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.
  7. ^ a b "Entrez Gene: TGM3 transglutaminase 3 (E polypeptide, protein-glutamine-gamma-glutamyltransferase)".

Further reading

  • Ahvazi B, Boeshans KM, Rastinejad F (2005). "The emerging structural understanding of transglutaminase 3". J. Struct. Biol. 147 (2): 200–7. doi:10.1016/j.jsb.2004.03.009. PMID 15193648.
  • Rice RH, Green H (1978). "Relation of protein synthesis and transglutaminase activity to formation of the cross-linked envelope during terminal differentiation of the cultured human epidermal keratinocyte". J. Cell Biol. 76 (3): 705–11. doi:10.1083/jcb.76.3.705. PMC 2110014. PMID 24643.
  • Steck TL (1972). "Cross-linking the major proteins of the isolated erythrocyte membrane". J. Mol. Biol. 66 (2): 295–305. doi:10.1016/0022-2836(72)90481-0. PMID 5038456.
  • Mariniello L, Esposito C, Di Pierro P, et al. (1993). "Human-immunodeficiency-virus transmembrane glycoprotein gp41 is an amino acceptor and donor substrate for transglutaminase in vitro". Eur. J. Biochem. 215 (1): 99–104. doi:10.1111/j.1432-1033.1993.tb18011.x. PMID 7688299.
  • Amendola A, Lombardi G, Oliverio S, et al. (1994). "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". FEBS Lett. 339 (3): 258–64. doi:10.1016/0014-5793(94)80427-3. PMID 7906657. S2CID 39872629.
  • Kim IG, Lee SC, Lee JH, et al. (1994). "Structure and organization of the human transglutaminase 3 gene: evolutionary relationship to the transglutaminase family". J. Invest. Dermatol. 103 (2): 137–42. doi:10.1111/1523-1747.ep12392470. PMID 7913719.
  • Kim IG, Gorman JJ, Park SC, et al. (1993). "The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse". J. Biol. Chem. 268 (17): 12682–90. doi:10.1016/S0021-9258(18)31442-X. PMID 8099584.
  • Lee JH, Jang SI, Yang JM, et al. (1996). "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". J. Biol. Chem. 271 (8): 4561–8. doi:10.1074/jbc.271.8.4561. PMID 8626812.
  • Hillier LD, Lennon G, Becker M, et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags". Genome Res. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.
  • Kim SY, Grant P, Lee JH, et al. (1999). "Differential expression of multiple transglutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer's disease". J. Biol. Chem. 274 (43): 30715–21. doi:10.1074/jbc.274.43.30715. PMID 10521460.
  • Méhul B, Bernard D, Simonetti L, et al. (2000). "Identification and cloning of a new calmodulin-like protein from human epidermis". J. Biol. Chem. 275 (17): 12841–7. doi:10.1074/jbc.275.17.12841. PMID 10777582.
  • Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.
  • Sárdy M, Kárpáti S, Merkl B, et al. (2002). "Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis". J. Exp. Med. 195 (6): 747–57. doi:10.1084/jem.20011299. PMC 2193738. PMID 11901200.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Ahvazi B, Boeshans KM, Idler W, et al. (2003). "Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme". J. Biol. Chem. 278 (26): 23834–41. doi:10.1074/jbc.M301162200. PMID 12679341.
  • Hitomi K, Presland RB, Nakayama T, et al. (2004). "Analysis of epidermal-type transglutaminase (transglutaminase 3) in human stratified epithelia and cultured keratinocytes using monoclonal antibodies". J. Dermatol. Sci. 32 (2): 95–103. doi:10.1016/S0923-1811(03)00091-4. PMID 12850301.
  • Gonzalez HE, Gujrati M, Frederick M, et al. (2003). "Identification of 9 genes differentially expressed in head and neck squamous cell carcinoma". Arch. Otolaryngol. Head Neck Surg. 129 (7): 754–9. doi:10.1001/archotol.129.7.754. PMID 12874078.
  • v
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  • 1l9m: Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation
    1l9m: Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation
  • 1l9n: Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation
    1l9n: Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation
  • 1nud: Role of Calcium Ions in the Activation and Activity of the Transglutaminase 3 Enzyme (3 calciums, active form)
    1nud: Role of Calcium Ions in the Activation and Activity of the Transglutaminase 3 Enzyme (3 calciums, active form)
  • 1nuf: Role of Calcium Ions in the Activation and Activity of the Transglutaminase 3 Enzyme
    1nuf: Role of Calcium Ions in the Activation and Activity of the Transglutaminase 3 Enzyme
  • 1nug: Role of Calcium Ions in the Activation and Activity of the Transglutaminase 3 Enzyme (2 calciums, 1 Mg, inactive form)
    1nug: Role of Calcium Ions in the Activation and Activity of the Transglutaminase 3 Enzyme (2 calciums, 1 Mg, inactive form)
  • 1rle: Structural Basis for the Coordinated Regulation of Transglutaminase 3 by Guanine Nucleotides and Calcium/Magnesium
    1rle: Structural Basis for the Coordinated Regulation of Transglutaminase 3 by Guanine Nucleotides and Calcium/Magnesium
  • 1sgx: Crystal Structure of Transglutaminase 3 in Complex with Bound GMP: Structural Basis for Alteration in Nucleotide Specificity
    1sgx: Crystal Structure of Transglutaminase 3 in Complex with Bound GMP: Structural Basis for Alteration in Nucleotide Specificity
  • 1vjj: Structural Basis for the Coordinated Regulation of Transglutaminase 3 by Guanine Nucleotides and Calcium/Magnesium
    1vjj: Structural Basis for the Coordinated Regulation of Transglutaminase 3 by Guanine Nucleotides and Calcium/Magnesium
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