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UniProtKB/Swiss-Prot entry P21980


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

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Entry information
Entry name TGM2_HUMAN
Primary accession number P21980
Secondary accession numbers Q16436 Q9BTN7 Q9UH35
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on January 23, 2002 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 105)
Name and origin of the protein
Protein name Protein-glutamine gamma-glutamyltransferase 2
Synonyms EC 2.3.2.13
Tissue transglutaminase
TGase C
TGC
TG(C)
Transglutaminase-2
TGase-H
Gene name
Name: TGM2
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] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Endothelial cell;
PubMed=1670766 [NCBI, ExPASy, EBI, Israel, Japan]
Gentile V., Saydak M., Chiocca E.A., Akande O., Birckbichler P.J., Lee K.N., Stein J.P., Davies P.J.A.;
"Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases.";
J. Biol. Chem. 266:478-483(1991).
[2]
NUCLEOTIDE SEQUENCE (ISOFORM 2).
PubMed=1358880 [NCBI, ExPASy, EBI, Israel, Japan]
Fraij B.M., Birckbichler P.J., Patterson M.K. Jr., Lee K.N., Gonzales R.A.;
"A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue.";
J. Biol. Chem. 267:22616-22623(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
DOI=10.1016/0167-4781(95)00219-7; PubMed=8611626 [NCBI, ExPASy, EBI, Israel, Japan]
Fraij B.M., Gonzales R.A.;
"A third human tissue transglutaminase homologue as a result of alternative gene transcripts.";
Biochim. Biophys. Acta 1306:63-74(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 MRNA] (ISOFORM 2).
TISSUE=Kidney;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-369, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-219 AND TYR-369, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[9]
VARIANT [LARGE SCALE ANALYSIS] VAL-660.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
[10]
VARIANTS EARLY-ONSET DIABETES TYPE 2 ARG-330 AND ASN-331.
DOI=10.1002/humu.9511; PubMed=17939176 [NCBI, ExPASy, EBI, Israel, Japan]
Porzio O., Massa O., Cunsolo V., Colombo C., Malaponti M., Bertuzzi F., Hansen T., Johansen A., Pedersen O., Meschi F., Terrinoni A., Melino G., Federici M., Decarlo N., Menicagli M., Campani D., Marchetti P., Ferdaoussi M., Froguel P., Federici G., Vaxillaire M., Barbetti F.;
"Missense mutations in the TGM2 gene encoding transglutaminase 2 are found in patients with early-onset type 2 diabetes.";
Hum. Mutat. 28:1150-1150(2007).
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
M55153; AAA63261.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M98478; AAA36739.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S81734; AAB36379.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031651; CAB66115.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003551; AAH03551.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39045; A39045.
A44302; A44302.
S68092; S68092.
RefSeq NP_004604.2; -.
NP_945189.1; -.
UniGene Hs.517033
3D structure databases
PDB
1FAU; Model; -; A=1-687.[ExPASy / RCSB / EBI]
1KV3; X-ray; 2.80 A; A/B/C/D/E/F=1-687.[ExPASy / RCSB / EBI]
2Q3Z; X-ray; 2.00 A; A=1-687.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FAU; -.
1KV3; -.
2Q3Z; -.
ModBase P21980.
Protein-protein interaction databases
IntAct P21980; -.
PTM databases
PhosphoSite P21980; -.
Organism-specific databases
H-InvDB HIX0015800; -.
HGNC HGNC:11778; TGM2.
GenAtlas TGM2.
HPA CAB002598; -.
MIM 190196; gene. [NCBI / EBI]
PharmGKB PA36491; -.
GeneCards P21980.
Gene expression databases
ArrayExpress P21980; -.
CleanEx HS_TGM2; -.
GermOnline ENSG00000198959; Homo sapiens.
Ontologies
GO
GO:0008415; Molecular function: acyltransferase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0003810; Molecular function: protein-glutamine gamma-glutamyltransferase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0018149; Biological process: peptide cross-linking (inferred from electronic annotation from InterPro).
GO:0045785; Biological process: positive regulation of cell adhesion (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR008957; Fibronectin_typ-III-like_fold.
IPR013783; Ig-like_fold.
IPR008958; Transglutaminase_C.
IPR013808; Transglutaminase_CS.
IPR001102; Transglutaminase_N.
IPR002931; Trnsglumase_like.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.30; FN_III-like; 1.
G3DSA:2.60.40.10; Ig-like_fold; 1.
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.
ProtoNet P21980.
Proteomic databases
PeptideAtlas P21980; -.
Genome annotation databases
Ensembl ENSG00000198959; Homo sapiens. [Contig view]
GeneID 7052; -.
KEGG hsa:7052; -.
Phylogenomic databases
HOGENOM P21980; -.
HOVERGEN P21980; -.
Other
DrugBank DB00130; L-Glutamine.
NextBio 27573; -.
SOURCE TGM2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Acyltransferase; Alternative splicing; Calcium; Diabetes mellitus; Direct protein sequencing; Disease mutation; Metal-binding; Phosphoprotein; Polymorphism; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   687  686     Protein-glutamine gamma-glutamyltransferase 2. PRO_0000213707
ACT_SITE   277   277        By similarity. 
ACT_SITE   335   335        By similarity. 
ACT_SITE   358   358        By similarity. 
METAL   398   398        Calcium (By similarity). 
METAL   400   400        Calcium (By similarity). 
METAL   447   447        Calcium (By similarity). 
METAL   452   452        Calcium (By similarity). 
MOD_RES   2     2        N-acetylalanine (By similarity). 
MOD_RES   219   219        Phosphotyrosine. 
MOD_RES   369   369        Phosphotyrosine. 
MOD_RES   427   427        Phosphoserine. 
VAR_SEQ   287   349        VLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEFGEIQGD KSEMIWNFHCWVESWMTRPDLQP -> GELHAGMWVMSPGRGHEEHWSRNQDIPALVLPPATNTLNA LCGLEPVTTLSGPLSNSHPSSGC (in isoform 3). VSP_006413
VAR_SEQ   350   687        Missing (in isoform 3). VSP_006414
VAR_SEQ   539   548        EKSVPLCILY -> GKALCSWSIC (in isoform 2). VSP_006411
VAR_SEQ   549   687        Missing (in isoform 2). VSP_006412
VARIANT   330   330  1     M -> R (in early-onset diabetes type 2). VAR_037998 [3D]
VARIANT   331   331  1     I -> N (in early-onset diabetes type 2). VAR_037999 [3D]
VARIANT   660   660  1     G -> V (in a colorectal cancer sample; somatic mutation). VAR_036554 [3D]
CONFLICT   51    51        E -> Q (in Ref. 1; AAA63261). 
CONFLICT   186   186        E -> Q (in Ref. 1; AAA63261). 
CONFLICT   224   224        V -> G (in Ref. 1; AAA63261). 
CONFLICT   533   533        N -> T (in Ref. 1; AAA63261). 
CONFLICT   655   655        L -> V (in Ref. 1; AAA63261). 
STRAND   7    11  5      
HELIX   14    20  7      
HELIX   24    26  3      
STRAND   28    30  3      
STRAND   32    34  3      
STRAND   39    48  10      
TURN   52    54  3      
STRAND   55    66  12      
TURN   69    72  4      
STRAND   73    79  7      
STRAND   89    95  7      
STRAND   97   105  9      
STRAND   113   123  11      
STRAND   126   138  13      
HELIX   153   159  7      
STRAND   164   170  7      
STRAND   172   181  10      
HELIX   189   198  10      
HELIX   201   205  5      
HELIX   207   213  7      
HELIX   217   226  10      
TURN   227   229  3      
TURN   231   234  4      
STRAND   235   239  5      
TURN   251   253  3      
HELIX   258   266  9      
TURN   267   269  3      
STRAND   272   275  4      
HELIX   277   291  15      
STRAND   295   304  10      
HELIX   311   317  7      
STRAND   332   342  11      
STRAND   353   357  5      
STRAND   365   369  5      
HELIX   376   380  5      
TURN   387   389  3      
HELIX   390   397  8      
STRAND   400   404  5      
STRAND   419   429  11      
STRAND   433   438  6      
HELIX   440   443  4      
HELIX   450   460  11      
STRAND   473   478  6      
STRAND   489   497  9      
STRAND   499   501  3      
STRAND   503   514  12      
STRAND   520   534  15      
STRAND   538   546  9      
HELIX   548   551  4      
TURN   552   554  3      
STRAND   560   569  10      
TURN   570   573  4      
STRAND   574   583  10      
STRAND   590   595  6      
STRAND   598   601  4      
STRAND   603   610  8      
STRAND   613   615  3      
STRAND   619   625  7      
TURN   627   629  3      
STRAND   634   638  5      
STRAND   647   654  8      
STRAND   658   660  3