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UniProtKB/Swiss-Prot entry Q08188


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TGM3_HUMAN
Primary accession number Q08188
Secondary accession numbers A8K5N6 O95933 Q32ML9 Q32MM0
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on March 18, 2008 (Sequence version 3)
Annotations were last modified on    September 23, 2008 (Entry version 86)
Name and origin of the protein
Protein name Protein-glutamine gamma-glutamyltransferase E [Precursor]
Synonyms TGase E
TGE
TG(E)
EC 2.3.2.13
Transglutaminase-3
Contains Protein-glutamine gamma-glutamyltransferase E 50 kDa non-catalytic chain
Protein-glutamine gamma-glutamyltransferase E 27 kDa catalytic chain
Gene name
Name: TGM3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-562.
TISSUE=Foreskin;
PubMed=8099584 [NCBI, ExPASy, EBI, Israel, Japan]
Kim I.-G., Gorman J.J., Park S.-C., Chung S.-I., Steinert P.M.;
"The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse.";
J. Biol. Chem. 268:12682-12690(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS-SNPs program for genomic applications;
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS THR-13 AND GLY-654.
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-13 AND GLY-654.
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-13 AND 670-684, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=Osteosarcoma;
Bienvenut W.V., Bensaad K., Vousden K.H.;
Submitted (FEB-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L10386; AAA61155.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK290324; BAF83013.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291351; BAF84040.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
EF102483; ABK41960.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031678; CAB37633.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471133; EAX10601.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC109075; AAI09076.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC109076; AAI09077.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A45991; A45991.
RefSeq NP_003236.3; -.
UniGene Hs.2022
3D structure databases
PDB
1L9M; X-ray; 2.10 A; A/B=2-693.[ExPASy / RCSB / EBI]
1L9N; X-ray; 2.10 A; A/B=2-693.[ExPASy / RCSB / EBI]
1NUD; X-ray; 2.70 A; A/B=2-693.[ExPASy / RCSB / EBI]
1NUF; X-ray; 2.70 A; A=2-693.[ExPASy / RCSB / EBI]
1NUG; X-ray; 2.40 A; A/B=2-693.[ExPASy / RCSB / EBI]
1RLE; X-ray; 2.10 A; A/B=2-693.[ExPASy / RCSB / EBI]
1SGX; X-ray; 2.00 A; A/B=2-693.[ExPASy / RCSB / EBI]
1VJJ; X-ray; 1.90 A; A/B=2-693.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1L9M; -.
1L9N; -.
1NUD; -.
1NUF; -.
1NUG; -.
1RLE; -.
1SGX; -.
1VJJ; -.
ModBase Q08188.
Organism-specific databases
H-InvDB HIX0040608; -.
HGNC HGNC:11779; TGM3.
GenAtlas TGM3.
HPA HPA004728; -.
MIM 600238; gene. [NCBI / EBI]
PharmGKB PA36492; -.
GeneCards Q08188.
Gene expression databases
ArrayExpress Q08188; -.
CleanEx HS_TGM3; -.
GermOnline ENSG00000125780; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0031234; Cellular component: extrinsic to internal side of plasma membrane (inferred from direct assay from UniProtKB).
GO:0005509; Molecular function: calcium ion binding (inferred from direct assay from UniProtKB).
GO:0019003; Molecular function: GDP binding (inferred from direct assay from UniProtKB).
GO:0005525; Molecular function: GTP binding (inferred from direct assay from UniProtKB).
GO:0003924; Molecular function: GTPase activity (inferred from direct assay from UniProtKB).
GO:0000287; Molecular function: magnesium ion binding (inferred from direct assay from UniProtKB).
GO:0003810; Molecular function: protein-glutamine gamma-glutamyltransferase activity (inferred from direct assay from UniProtKB).
GO:0043163; Biological process: cell envelope organization (inferred from direct assay from UniProtKB).
GO:0031069; Biological process: hair follicle morphogenesis (traceable author statement from UniProtKB).
GO:0030216; Biological process: keratinocyte differentiation (inferred from expression pattern from UniProtKB).
GO:0018149; Biological process: peptide cross-linking (inferred from direct assay from UniProtKB).
GO:0051262; Biological process: protein tetramerization (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR013783; Ig-like_fold.
IPR008958; Transglutaminase_C.
IPR013808; Transglutaminase_CS.
IPR001102; Transglutaminase_N.
IPR002931; Trnsglumase_like.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.10; Ig-like_fold; 3.
Pfam PF00927; Transglut_C; 2.
PF01841; Transglut_core; 1.
PF00868; Transglut_N; 1.
Pfam graphical view of domain structure.
SMART SM00460; TGc; 1.
SMART graphical view of domain structure.
PROSITE PS00547; TRANSGLUTAMINASES; 1.
BLOCKS Q08188.
Proteomic databases
PeptideAtlas Q08188; -.
Genome annotation databases
Ensembl ENSG00000125780; Homo sapiens. [Contig view]
GeneID 7053; -.
Phylogenomic databases
HOGENOM Q08188; -.
HOVERGEN Q08188; -.
Other
DrugBank DB00130; L-Glutamine.
LinkHub Q08188; -.
SOURCE TGM3; Homo sapiens.
ProtoNet Q08188.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Acyltransferase; Calcium; Direct protein sequencing; Keratinization; Metal-binding; Polymorphism; Transferase; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   470  469     Protein-glutamine gamma-glutamyltransferase E 50 kDa non-catalytic chain. PRO_0000033652
CHAIN   471   693  223     Protein-glutamine gamma-glutamyltransferase E 27 kDa catalytic chain. PRO_0000033653
ACT_SITE   273   273        By similarity. 
ACT_SITE   331   331        By similarity. 
ACT_SITE   354   354        By similarity. 
METAL   394   394        Calcium (By similarity). 
METAL   396   396        Calcium (By similarity). 
METAL   444   444        Calcium (By similarity). 
METAL   449   449        Calcium (By similarity). 
MOD_RES   2     2        N-acetylalanine. 
VARIANT   13    13  1     K -> T (in dbSNP:rs214803 [NCBI]). VAR_040067 [3D]
VARIANT   163   163  1     I -> L (in dbSNP:rs6048066 [NCBI]). VAR_040068 [3D]
VARIANT   249   249  1     S -> N (in dbSNP:rs214814 [NCBI]). VAR_040069 [3D]
VARIANT   562   562  1     K -> R (in dbSNP:rs1042617 [NCBI]). VAR_040070 [3D]
VARIANT   654   654  1     R -> G (in dbSNP:rs214830 [NCBI]). VAR_040071 [3D]
CONFLICT   58    59        VS -> DT (in Ref. 1; AAA61155). 
CONFLICT   251   251        N -> G (in Ref. 1; AAA61155). 
CONFLICT   324   324        S -> G (in Ref. 2; BAF84040). 
CONFLICT   346   346        S -> P (in Ref. 1; AAA61155). 
CONFLICT   674   674        D -> G (in Ref. 2; BAF84040). 
STRAND   6    10  5      
HELIX   13    19  7      
STRAND   31    33  3      
STRAND   38    46  9      
STRAND   53    59  7      
STRAND   61    63  3      
TURN   66    69  4      
STRAND   70    79  10      
STRAND   82    92  11      
STRAND   95   101  7      
STRAND   109   119  11      
STRAND   122   134  13      
HELIX   149   155  7      
STRAND   160   167  8      
STRAND   170   177  8      
HELIX   185   193  9      
HELIX   197   201  5      
HELIX   203   208  6      
HELIX   209   211  3      
HELIX   213   223  11      
TURN   227   229  3      
STRAND   231   235  5      
HELIX   247   249  3      
HELIX   253   262  10      
STRAND   268   271  4      
HELIX   273   287  15      
STRAND   291   300  10      
STRAND   305   313  9      
TURN   322   325  4      
STRAND   326   337  12      
TURN   341   343  3      
STRAND   349   353  5      
HELIX   372   377  6      
TURN   383   385  3      
HELIX   386   394  9      
STRAND   396   403  8      
TURN   404   407  4      
STRAND   408   426  19      
STRAND   433   435  3      
HELIX   437   440  4      
HELIX   447   460  14      
STRAND   482   489  8      
STRAND   499   507  9      
STRAND   509   511  3      
STRAND   513   524  12      
STRAND   530   543  14      
STRAND   548   555  8      
HELIX   557   560  4      
TURN   561   563  3      
STRAND   569   577  9      
STRAND   584   591  8      
STRAND   597   603  7      
STRAND   611   618  8      
STRAND   621   623  3      
STRAND   627   633  7      
TURN   635   637  3      
STRAND   642   646  5      
STRAND   654   661  8      
STRAND   667   677  11      
STRAND   680   692  13      
Sequence information
Length: 693 AA [This is the length of the unprocessed precursor] Molecular weight: 76758 Da [This is the MW of the unprocessed precursor] CRC64: