Protein-glutamine gamma-glutamyltransferase K

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Q9JLF6 (TGM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 93. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein-glutamine gamma-glutamyltransferase K
EC=2.3.2.13

Alternative name(s):
Epidermal TGase
Transglutaminase K
Short name=TG(K)
Short name=TGK
Short name=TGase K
Transglutaminase-1
Short name=TGase-1

Gene names

Name:

Tgm1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	815 AA.
Sequence status	Complete.
Protein existence	Evidence 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
Sequence similarities	Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
Biological process	Keratinization
Cellular component	Membrane
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	keratinization Inferred from electronic annotation. Source: UniProtKB-KW organ morphogenesis Inferred from mutant phenotype Ref.1. Source: MGI peptide cross-linking Inferred from electronic annotation. Source: InterPro protein metabolic process Traceable author statement Ref.1. Source: MGI
Cellular_component	cell-cell adherens junction Inferred from direct assay Ref.1. Source: MGI intrinsic to membrane Inferred from electronic annotation. Source: Compara
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein-glutamine gamma-glutamyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 815

815

Protein-glutamine gamma-glutamyltransferase K

PRO_0000213702

Sites

Active site

376

By similarity

Active site

435

By similarity

Active site

458

By similarity

Metal binding

498

Calcium By similarity

Metal binding

500

Calcium By similarity

Metal binding

547

Calcium By similarity

Metal binding

552

Calcium By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine Ref.3

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine Ref.3

Modified residue

Phosphoserine Ref.3 Ref.4

Experimental info

Sequence conflict

E → V in AAF35986. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9JLF6 [UniParc].

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

FASTA

815

89,826

        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' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
IPI	IPI00331573.
RefSeq	NP_001155186.1. NM_001161714.1. NP_001155187.1. NM_001161715.1. NP_064368.3. NM_019984.3.
UniGene	Mm.41964.
3D structure databases
ProteinModelPortal	Q9JLF6.
SMR	Q9JLF6. Positions 85-786.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4137626.
PTM databases
PhosphoSite	Q9JLF6.
Proteomic databases
PaxDb	Q9JLF6.
PRIDE	Q9JLF6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000002389; ENSMUSP00000002389; ENSMUSG00000022218. ENSMUST00000168729; ENSMUSP00000128090; ENSMUSG00000022218. ENSMUST00000178034; ENSMUSP00000137642; ENSMUSG00000022218.
GeneID	21816.
KEGG	mmu:21816.
UCSC	uc007uag.2. mouse.
Organism-specific databases
CTD	7051.
MGI	MGI:98730. Tgm1.
Phylogenomic databases
eggNOG	NOG80379.
GeneTree	ENSGT00690000101887.
HOGENOM	HOG000231695.
HOVERGEN	HBG004342.
InParanoid	Q9JLF6.
KO	K05619.
OrthoDB	EOG4VX24R.
Gene expression databases
Bgee	Q9JLF6.
CleanEx	MM_TGM1.
Genevestigator	Q9JLF6.
GermOnline	ENSMUSG00000022218. Mus musculus.
Family and domain databases
Gene3D	2.60.40.10. 3 hits. 3.90.260.10. 1 hit.
InterPro	IPR023608. 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]
PANTHER	PTHR11590. PTHR11590. 1 hit.
Pfam	PF00927. Transglut_C. 2 hits. PF01841. Transglut_core. 1 hit. PF00868. Transglut_N. 1 hit. [Graphical view]
PIRSF	PIRSF000459. TGM_EBP42. 1 hit.
SMART	SM00460. TGc. 1 hit. [Graphical view]
SUPFAM	SSF81296. Ig_E-set. 1 hit. SSF49309. Transglut_C. 2 hits.
PROSITE	PS00547. TRANSGLUTAMINASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	301220.
SOURCE	Search...

Entry information

Entry name

TGM1_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents