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Reviewed, UniProtKB/Swiss-Prot Q9JLF6 (TGM1_MOUSE)

Last modified January 19, 2010. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein-glutamine gamma-glutamyltransferase K
    EC=2.3.2.13
Alternative name(s):
    Transglutaminase K
      Short name=TGase K
      Short name=TGK
      Short name=TG(K)
    Transglutaminase-1
    Epidermal TGase
Gene names
Name: Tgm1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length815 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross-linking epidermal proteins during formation of the stratum corneum By similarity.

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Membrane; Peripheral membrane protein By similarity.

Tissue specificity

Expressed in large amounts in epithelial tissues (lung, liver and kidney). Ref.1

Post-translational modification

Tyrosine-phosphorylated. Ref.1 Ref.3 Ref.4

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 815815Protein-glutamine gamma-glutamyltransferase K
PRO_0000213702

Sites

Active site3761 By similarity
Active site4351 By similarity
Active site4581 By similarity
Metal binding4981Calcium By similarity
Metal binding5001Calcium By similarity
Metal binding5471Calcium By similarity
Metal binding5521Calcium By similarity

Amino acid modifications

Modified residue711Phosphoserine Ref.3
Modified residue911Phosphoserine Ref.3
Modified residue941Phosphoserine Ref.3 Ref.4

Experimental info

Sequence conflict291E → V in AAF35986. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9JLF6-1 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 326DD4E512AEA23E

FASTA81589,826
        10         20         30         40         50         60 
MEGPRSDVGR WGRSPWQPPT TPSPEPEPEP EPDRRSRSRR GGGRSFWARC CGCCSCGNRG 

        70         80         90        100        110        120 
DDDWGPEPSG SRSRGTSSRG RDSRGGRRPE SRGSGVNAAG DGTIREGMLV VTGVDLLCSR 

       130        140        150        160        170        180 
SDQNRREHHT DEFEYDELIV RRGQPFHMIL FLNREYESSD RIALELLIGS NPEVGKGTHV 

       190        200        210        220        230        240 
IIPVGKGGSG GWKAQVTKNN GHNLNLRVHT SPNAIIGKFQ FTVRTRSEAG EFQLPFDPRN 

       250        260        270        280        290        300 
EIYILFNPWC PEDIVYVDHE DWRQEYVLNE SGRIYYGTEA QIGERTWNYG QFDHGVLDAC 

       310        320        330        340        350        360 
LYILDRRGMP YGGRGDPVSV SRVVSAMVNS LDDNGVLIGN WTGDYSRGTN PSAWVGSVEI 

       370        380        390        400        410        420 
LLSYLRTGYS VPYGQCWVFA GVTTTVLRCL GFATRTVTNF NSAHDTDTSL TMDIYFDENM 

       430        440        450        460        470        480 
KPLEHLNHDS VWNFHVWNDC WMKRPDLPSG FDGWQVVDAT PQETSSGIFC CGPCSVESVK 

       490        500        510        520        530        540 
NGLVYMKYDT PFIFAEVNSD KVYWQRQDDG SFKIVYVEEK AIGTLIVTKA IHSNNREDIT 

       550        560        570        580        590        600 
HIYKHPEGSE AERRAVEKAA AHGSKPNVYA TRDSAEDVAM QVEAQDAVMG QDLAVSVVLT 

       610        620        630        640        650        660 
NRGSSRRTVK LHLYLCVTYY TGVSGPTFKE AKKEVTLAPG ASDSVTMPVA YKEYKPHLVD 

       670        680        690        700        710        720 
QGAMLLNVSG HVKESGQVLA KQHTFRLRTP DLSLTLLGAA VVGQECGVQI VFKNPLPVTL 

       730        740        750        760        770        780 
TNVVFRLEGS GLQRPKVLNV GDIGGNETVT LRQTFVPVRP GPRQLIASLD SPQLSQVHGV 

       790        800        810 
IQVDVAPASG GSGFSDAGGD SRSGENIPMA YRGGA 

« Hide

References

« Hide 'large scale' references
[1]"Transglutaminase type 1 and its cross-linking activity are concentrated at adherens junctions in simple epithelial cells."
Hiiragi T., Sasaki H., Nagafuchi A., Sabe H., Shen S.C., Matsuki M., Yamanishi K., Tsukita S.
J. Biol. Chem. 274:34148-34154(1999) [PubMed: 10567386] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, TISSUE SPECIFICITY.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-91 AND SER-94, MASS SPECTROMETRY.
Tissue: Liver.
[4]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed: 18630941] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF186373 mRNA. Translation: AAF35986.1.
BC026422 mRNA. Translation: AAH26422.1.
IPIIPI00331573.
RefSeqNP_001155186.1.
NP_001155187.1.
NP_064368.3.
UniGeneMm.41964

3D structure databases

SMRQ9JLF6. Positions 105-786.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JLF6.

PTM databases

PhosphoSiteQ9JLF6.

Proteomic databases

PRIDEQ9JLF6.

Genome annotation databases

EnsemblENSMUST00000002389; ENSMUSP00000002389; ENSMUSG00000022218; Mus musculus. [Genome view]
GeneID21816.
KEGGmmu:21816.
UCSCuc007uag.1. mouse.

Organism-specific databases

CTD21816.
MGIMGI:98730. Tgm1.

Phylogenomic databases

eggNOGroNOG07181.
HOGENOMHBG444754.
HOVERGENQ9JLF6.
InParanoidQ9JLF6.
OrthoDBEOG9B017K.

Enzyme and pathway databases

BRENDA2.3.2.13. 244.

Gene expression databases

ArrayExpressQ9JLF6.
BgeeQ9JLF6.
CleanExMM_TGM1.
GenevestigatorQ9JLF6.
GermOnlineENSMUSG00000022218. Mus musculus.

Family and domain databases

InterProIPR008957. Fibronectin_typ-III-like_fold.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PfamPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
SMARTSM00460. TGc. 1 hit.
[Graphical view]
PROSITEPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio301220.
SOURCESearch...

Entry information

Entry nameTGM1_MOUSE
AccessionPrimary (citable) accession number: Q9JLF6
Secondary accession number(s): Q8R0T9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: January 19, 2010
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents