ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P21981


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TGM2_MOUSE
Primary accession number P21981
Secondary accession numbers O88901 Q3TLV2 Q8C217 Q91VG9 Q9R1F7
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on March 18, 2008 (Sequence version 4)
Annotations were last modified on    September 2, 2008 (Entry version 86)
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
Gene name
Name: Tgm2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Macrophage;
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 [MRNA].
STRAIN=129/SvJ;
DOI=10.1006/abbi.1999.1189; PubMed=10334875 [NCBI, ExPASy, EBI, Israel, Japan]
Nanda N., Iismaa S.E., Copeland N.G., Gilbert D.J., Jenkins N., Graham R.M., Sutrave P.;
"Organization and chromosomal mapping of mouse Gh/tissue transglutaminase gene (Tgm2).";
Arch. Biochem. Biophys. 366:151-156(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/sj.cdd.4400494; PubMed=10200571 [NCBI, ExPASy, EBI, Israel, Japan]
D'Amato M., Iannicola C., Monteriu G., Piacentini M.;
"Mapping and sequencing of the murine 'tissue' transglutaminase (Tgm2) gene: absence of mutations in MRLlpr/lpr mice.";
Cell Death Differ. 6:216-217(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Brain cortex, Dendritic cell, Embryonic heart, Heart, Macrophage, Mammary gland, and Spleen;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI;
TISSUE=Mammary tumor;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
STRAIN=Swiss;
DOI=10.1074/jbc.271.8.4355; PubMed=8626785 [NCBI, ExPASy, EBI, Israel, Japan]
Nagy L., Saydak M., Shipley N., Lu S., Basilion J.P., Yan Z.H., Syka P., Chandraratna R.A.S., Stein J.P., Heyman R.A., Davies P.J.A.;
"Identification and characterization of a versatile retinoid response element (retinoic acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter.";
J. Biol. Chem. 271:4355-4365(1996).
[8]
PROTEIN SEQUENCE OF 2-19; 41-74; 158-173; 215-222; 290-327; 550-561; 564-589; 601-609; 634-648 AND 651-671, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=Embryonic fibroblast;
Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.;
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
M55154; AAA40420.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF114266; AAD37501.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF076928; AAC62014.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK052912; BAC35200.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK080224; BAC37852.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK080593; BAC37952.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK089481; BAC40899.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK143712; BAE25511.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK151776; BAE30682.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK152152; BAE30987.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK152627; BAE31370.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK159255; BAE34936.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK166302; BAE38690.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK168990; BAE40790.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK169356; BAE41105.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL669824; CAM23188.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016492; AAH16492.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U24148; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
PIR B39045; B39045.
RefSeq NP_033399.1; -.
UniGene Mm.330731
3D structure databases
HSSP P21980; 1KV3. [HSSP ENTRY / PDB]
SMR P21981; 15-686.
ModBase P21981.
PTM databases
PhosphoSite P21981; -.
Organism-specific databases
MGI MGI:98731; Tgm2.
Gene expression databases
ArrayExpress P21981; -.
CleanEx MM_TGM2; -.
GermOnline ENSMUSG00000037820; Mus musculus.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from UniProtKB).
GO:0016020; Cellular component: membrane (traceable author statement from UniProtKB).
GO:0005578; Cellular component: proteinaceous extracellular matrix (traceable author statement from UniProtKB).
GO:0005509; Molecular function: calcium ion binding (non-traceable author statement from UniProtKB).
GO:0005525; Molecular function: GTP binding (non-traceable author statement from UniProtKB).
GO:0003810; Molecular function: protein-glutamine gamma-glutamyltransferase activity (inferred from mutant phenotype from UniProtKB).
GO:0007186; Biological process: G-protein coupled receptor protein signaling pathway (traceable author statement from UniProtKB).
GO:0018149; Biological process: peptide cross-linking (traceable author statement from UniProtKB).
GO:0045785; Biological process: positive regulation of cell adhesion (inferred from mutant phenotype 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.
BLOCKS P21981.
Genome annotation databases
Ensembl ENSMUSG00000037820; Mus musculus. [Contig view]
GeneID 21817; -.
KEGG mmu:21817; -.
Phylogenomic databases
HOGENOM P21981; -.
HOVERGEN P21981; -.
Other
SOURCE Tgm2; Mus musculus.
ProtoNet P21981.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Acyltransferase; Calcium; Direct protein sequencing; Metal-binding; Phosphoprotein; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   686  685     Protein-glutamine gamma-glutamyltransferase 2. PRO_0000213708
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. 
MOD_RES   219   219        Phosphotyrosine (By similarity). 
MOD_RES   369   369        Phosphotyrosine (By similarity). 
MOD_RES   427   427        Phosphoserine (By similarity). 
CONFLICT   32    33        VL -> LV (in Ref. 1; AAA40420). 
CONFLICT   51    51        E -> Q (in Ref. 1; AAA40420 and 2; AAD37501). 
CONFLICT   186   186        E -> Q (in Ref. 1; AAA40420). 
CONFLICT   226   226        A -> D (in Ref. 1; AAA40420). 
CONFLICT   325   325        S -> T (in Ref. 1; AAA40420). 
CONFLICT   357   357        I -> L (in Ref. 1; AAA40420 and 2; AAD37501). 
CONFLICT   396   396        E -> K (in Ref. 4; BAC40899). 
CONFLICT   408   409        ED -> DE (in Ref. 1; AAA40420). 
CONFLICT   415   416        SI -> WM (in Ref. 1; AAA40420). 
CONFLICT   421   421        V -> I (in Ref. 1; AAA40420). 
CONFLICT   481   485        DSMSM -> QYEH (in Ref. 1; AAA40420). 
CONFLICT   539   539        N -> K (in Ref. 4; BAE38690). 
CONFLICT   552   552        G -> D (in Ref. 1; AAA40420). 
CONFLICT   583   583        L -> V (in Ref. 1; AAA40420 and 2; AAD37501). 
CONFLICT   654   654        F -> S (in Ref. 1; AAA40420). 
Sequence information
Length: 686 AA [This is the length of the unprocessed precursor] Molecular weight: 77061 Da [This is the MW of the unprocessed precursor] CRC64: 9B64B074D3F837DE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAEELLLERC DLEIQANGRD HHTADLCQEK LVLRRGQRFR LTLYFEGRGY EASVDSLTFG 

        70         80         90        100        110        120 
AVTGPDPSEE AGTKARFSLS DNVEEGSWSA SVLDQQDNVL SLQLCTPANA PIGLYRLSLE 

       130        140        150        160        170        180 
ASTGYQGSSF VLGHFILLYN AWCPADDVYL DSEEERREYV LTQQGFIYQG SVKFIKSVPW 

       190        200        210        220        230        240 
NFGQFEDGIL DTCLMLLDMN PKFLKNRSRD CSRRSSPIYV GRVVSAMVNC NDDQGVLLGR 

       250        260        270        280        290        300 
WDNNYGDGIS PMAWIGSVDI LRRWKEHGCQ QVKYGQCWVF AAVACTVLRC LGIPTRVVTN 

       310        320        330        340        350        360 
YNSAHDQNSN LLIEYFRNEF GELESNKSEM IWNFHCWVES WMTRPDLQPG YEGWQAIDPT 

       370        380        390        400        410        420 
PQEKSEGTYC CGPVSVRAIK EGDLSTKYDA PFVFAEVNAD VVDWIRQEDG SVLKSINRSL 

       430        440        450        460        470        480 
VVGQKISTKS VGRDDREDIT HTYKYPEGSP EEREVFTKAN HLNKLAEKEE TGVAMRIRVG 

       490        500        510        520        530        540 
DSMSMGNDFD VFAHIGNDTS ETRECRLLLC ARTVSYNGVL GPECGTEDIN LTLDPYSENS 

       550        560        570        580        590        600 
IPLRILYEKY SGCLTESNLI KVRGLLIEPA ANSYLLAERD LYLENPEIKI RVLGEPKQNR 

       610        620        630        640        650        660 
KLVAEVSLKN PLSDPLYDCI FTVEGAGLTK EQKSVEVSDP VPAGDLVKAR VDLFPTDIGL 

       670        680 
HKLVVNFQCD KLKSVKGYRN VIIGPA 

P21981 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!