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P21981 (TGM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-glutamine gamma-glutamyltransferase 2

EC=2.3.2.13
Alternative name(s):
Tissue transglutaminase
Transglutaminase C
Short name=TG(C)
Short name=TGC
Short name=TGase C
Transglutaminase-2
Short name=TGase-2
Gene names
Name:Tgm2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length686 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.

Catalytic activity

Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Monomer.

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
   LigandCalcium
Metal-binding
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 11274171. Source: UniProtKB

apoptotic cell clearance

Inferred from electronic annotation. Source: Ensembl

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

branching involved in salivary gland morphogenesis

Inferred from mutant phenotype PubMed 15970210. Source: MGI

isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine

Inferred from electronic annotation. Source: Ensembl

peptide cross-linking

Traceable author statement PubMed 11274171. Source: UniProtKB

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from sequence alignment PubMed 7911253. Source: MGI

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell adhesion

Inferred from mutant phenotype PubMed 11274171. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

salivary gland cavitation

Inferred from mutant phenotype PubMed 15970210. Source: MGI

   Cellular_componentcytoplasm

Inferred from sequence alignment PubMed 7911253. Source: MGI

cytosol

Traceable author statement PubMed 11274171. Source: UniProtKB

membrane

Traceable author statement PubMed 11274171. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

proteinaceous extracellular matrix

Traceable author statement PubMed 11274171. Source: UniProtKB

   Molecular_functionGTP binding

Non-traceable author statement Ref.2. Source: UniProtKB

calcium ion binding

Non-traceable author statement PubMed 11274171. Source: UniProtKB

protein-glutamine gamma-glutamyltransferase activity

Inferred from mutant phenotype PubMed 11274171. Source: UniProtKB

transaminase activity

Inferred from sequence orthology PubMed 11723121. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 686685Protein-glutamine gamma-glutamyltransferase 2
PRO_0000213708

Sites

Active site2771 By similarity
Active site3351 By similarity
Active site3581 By similarity
Metal binding3981Calcium By similarity
Metal binding4001Calcium By similarity
Metal binding4471Calcium By similarity
Metal binding4521Calcium By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue4681N6-acetyllysine Ref.10

Experimental info

Sequence conflict32 – 332VL → LV in AAA40420. Ref.1
Sequence conflict511E → Q in AAA40420. Ref.1
Sequence conflict511E → Q in AAD37501. Ref.2
Sequence conflict1861E → Q in AAA40420. Ref.1
Sequence conflict2261A → D in AAA40420. Ref.1
Sequence conflict3251S → T in AAA40420. Ref.1
Sequence conflict3571I → L in AAA40420. Ref.1
Sequence conflict3571I → L in AAD37501. Ref.2
Sequence conflict3961E → K in BAC40899. Ref.4
Sequence conflict408 – 4092ED → DE in AAA40420. Ref.1
Sequence conflict415 – 4162SI → WM in AAA40420. Ref.1
Sequence conflict4211V → I in AAA40420. Ref.1
Sequence conflict481 – 4855DSMSM → QYEH in AAA40420. Ref.1
Sequence conflict5391N → K in BAE38690. Ref.4
Sequence conflict5521G → D in AAA40420. Ref.1
Sequence conflict5831L → V in AAA40420. Ref.1
Sequence conflict5831L → V in AAD37501. Ref.2
Sequence conflict6541F → S in AAA40420. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P21981 [UniParc].

Last modified March 18, 2008. Version 4.
Checksum: 9B64B074D3F837DE

FASTA68677,061
        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 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases."
Gentile V., Saydak M., Chiocca E.A., Akande O., Birckbichler P.J., Lee K.N., Stein J.P., Davies P.J.A.
J. Biol. Chem. 266:478-483(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Macrophage.
[2]"Organization and chromosomal mapping of mouse Gh/tissue transglutaminase gene (Tgm2)."
Nanda N., Iismaa S.E., Copeland N.G., Gilbert D.J., Jenkins N., Graham R.M., Sutrave P.
Arch. Biochem. Biophys. 366:151-156(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/SvJ.
[3]"Mapping and sequencing of the murine 'tissue' transglutaminase (Tgm2) gene: absence of mutations in MRLlpr/lpr mice."
D'Amato M., Iannicola C., Monteriu G., Piacentini M.
Cell Death Differ. 6:216-217(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Brain cortex, Dendritic cell, Embryonic heart, Heart, Macrophage, Mammary gland and Spleen.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NMRI.
Tissue: Mammary tumor.
[7]"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."
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.
J. Biol. Chem. 271:4355-4365(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
Strain: Swiss.
[8]Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.
Submitted (FEB-2008) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
[9]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 378-387, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[10]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55154 mRNA. Translation: AAA40420.1.
AF114266 mRNA. Translation: AAD37501.1.
AF076928 mRNA. Translation: AAC62014.1.
AK052912 mRNA. Translation: BAC35200.1.
AK080224 mRNA. Translation: BAC37852.1.
AK080593 mRNA. Translation: BAC37952.1.
AK089481 mRNA. Translation: BAC40899.1.
AK143712 mRNA. Translation: BAE25511.1.
AK151776 mRNA. Translation: BAE30682.1.
AK152152 mRNA. Translation: BAE30987.1.
AK152627 mRNA. Translation: BAE31370.1.
AK159255 mRNA. Translation: BAE34936.1.
AK166302 mRNA. Translation: BAE38690.1.
AK168990 mRNA. Translation: BAE40790.1.
AK169356 mRNA. Translation: BAE41105.1.
AL669824 Genomic DNA. Translation: CAM23188.1.
BC016492 mRNA. Translation: AAH16492.1.
U24148 Genomic DNA. No translation available.
PIRB39045.
RefSeqNP_033399.1. NM_009373.3.
UniGeneMm.330731.

3D structure databases

ProteinModelPortalP21981.
SMRP21981. Positions 4-686.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204168. 2 interactions.
IntActP21981. 3 interactions.
MINTMINT-1869474.

Chemistry

ChEMBLCHEMBL2079853.

PTM databases

PhosphoSiteP21981.

Proteomic databases

PaxDbP21981.
PRIDEP21981.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103122; ENSMUSP00000099411; ENSMUSG00000037820.
GeneID21817.
KEGGmmu:21817.
UCSCuc008npr.1. mouse.

Organism-specific databases

CTD7052.
MGIMGI:98731. Tgm2.

Phylogenomic databases

eggNOGNOG80379.
GeneTreeENSGT00740000115156.
HOGENOMHOG000231695.
HOVERGENHBG004342.
InParanoidP21981.
KOK05625.
OMAANGRDHH.
OrthoDBEOG7WT40M.
PhylomeDBP21981.
TreeFamTF324278.

Gene expression databases

ArrayExpressP21981.
BgeeP21981.
CleanExMM_TGM2.
GenevestigatorP21981.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProIPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
PANTHERPTHR11590. PTHR11590. 1 hit.
PfamPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFPIRSF000459. TGM_EBP42. 1 hit.
SMARTSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301224.
PROP21981.
SOURCESearch...

Entry information

Entry nameTGM2_MOUSE
AccessionPrimary (citable) accession number: P21981
Secondary accession number(s): O88901 expand/collapse secondary AC list , Q3TLV2, Q8C217, Q91VG9, Q9R1F7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: March 18, 2008
Last modified: April 16, 2014
This is version 137 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot