HUMAN:TGM1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	TGM1 (synonyms: KTG)
Protein Name(s)	Protein-glutamine gamma-glutamyltransferase K Epidermal TGase Transglutaminase K TG(K) TGK TGase K Transglutaminase-1 TGase-1
External Links
UniProt	P22735
EMBL	M55183 D90287 M62925 M83230 M83227 M83228 M83229 M86360 D10353 M98447 AK301652 AK315843 DQ640500 AL096870 CH471078 BC034699 X57974
CCDS	CCDS9622.1
PIR	A43401
RefSeq	NP_000350.1
UniGene	Hs.508950
PDB	2XZZ
PDBsum	2XZZ
ProteinModelPortal	P22735
SMR	P22735
BioGrid	112909
IntAct	P22735
STRING	9606.ENSP00000206765
BindingDB	P22735
ChEMBL	CHEMBL2810
DrugBank	DB00130
PhosphoSite	P22735
DMDM	57015359
MaxQB	P22735
PaxDb	P22735
PeptideAtlas	P22735
PRIDE	P22735
DNASU	7051
Ensembl	ENST00000206765 ENST00000544573
GeneID	7051
KEGG	hsa:7051
UCSC	uc001wod.3
CTD	7051
GeneCards	GC14M024718
GeneReviews	TGM1
HGNC	HGNC:11777
HPA	CAB015159 HPA040171
MIM	190195 242300
neXtProt	NX_P22735
Orphanet	281127 100976 79394 313 281122
PharmGKB	PA36490
eggNOG	NOG80379
GeneTree	ENSGT00760000119108
HOGENOM	HOG000231695
HOVERGEN	HBG004342
InParanoid	P22735
KO	K05619
OMA	GRWGGNP
OrthoDB	EOG7WT40M
PhylomeDB	P22735
TreeFam	TF324278
GeneWiki	Keratinocyte_transglutaminase
GenomeRNAi	7051
NextBio	27569
PRO	PR:P22735
Proteomes	UP000005640
Bgee	P22735
CleanEx	HS_TGM1
ExpressionAtlas	P22735
Genevestigator	P22735
GO	GO:0005913 GO:0001533 GO:0070062 GO:0031224 GO:0046872 GO:0003810 GO:0043163 GO:0006464 GO:0031424 GO:0030216 GO:0009887 GO:0018149
Gene3D	2.60.40.10 3.90.260.10
InterPro	IPR023608 IPR013783 IPR014756 IPR002931 IPR008958 IPR013808 IPR001102
PANTHER	PTHR11590
Pfam	PF00927 PF01841 PF00868
PIRSF	PIRSF000459
SMART	SM00460
SUPFAM	SSF49309 SSF81296
PROSITE	PS00547

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0003810	protein-glutamine gamma-glutamyltransferase activity	PMID:9722562^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0018149	peptide cross-linking	PMID:9722562^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045787	positive regulation of cell cycle	PMID:26220141^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010838	positive regulation of keratinocyte proliferation	PMID:26220141^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003810	protein-glutamine gamma-glutamyltransferase activity	PMID:21282207^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P07476)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[4]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
part_of	GO:0031224	intrinsic component of membrane	PMID:8824274^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0030216	keratinocyte differentiation	PMID:8824274^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006464	cellular protein modification process	PMID:1979171^[6]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003810	protein-glutamine gamma-glutamyltransferase activity	PMID:7961731^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003810	protein-glutamine gamma-glutamyltransferase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR008958 InterPro:IPR023608 InterPro:IPR036238	F		Seeded From UniProt	complete
involved_in	GO:0018149	peptide cross-linking	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001102 InterPro:IPR008958 InterPro:IPR013808 InterPro:IPR023608 InterPro:IPR036238	P		Seeded From UniProt	complete
enables	GO:0003810	protein-glutamine gamma-glutamyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.3.2.13	F		Seeded From UniProt	complete
involved_in	GO:0043163	cell envelope organization	PMID:14645372^[8]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0001533	cornified envelope	PMID:8824274^[5] Reactome:R-HSA-6814764	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0070268	cornification	Reactome:R-HSA-6809371	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-6810894	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-6814764 Reactome:R-HSA-6814734 Reactome:R-HSA-6814387 Reactome:R-HSA-6814298 Reactome:R-HSA-6811539 Reactome:R-HSA-6810937 Reactome:R-HSA-6810899 Reactome:R-HSA-6810894	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
enables	GO:0016746	transferase activity, transferring acyl groups	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0012	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
involved_in	GO:0031424	keratinization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0417	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472 UniProtKB-SubCell:SL-0162	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Tarcsa, E et al. (1998) Structural and transglutaminase substrate properties of the small proline-rich 2 family of cornified cell envelope proteins. J. Biol. Chem. 273 23297-303 PubMed GONUTS page
↑ ^2.0 ^2.1 Zhang, SQ et al. (2016) Identification and functional characterization of a novel transglutaminase 1 gene mutation associated with autosomal recessive congenital ichthyosis. Int. J. Dermatol. 55 201-7 PubMed GONUTS page
↑ Henry, J et al. (2011) Hornerin is a component of the epidermal cornified cell envelopes. FASEB J. 25 1567-76 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Steinert, PM et al. (1996) The transglutaminase 1 enzyme is variably acylated by myristate and palmitate during differentiation in epidermal keratinocytes. J. Biol. Chem. 271 26242-50 PubMed GONUTS page
↑ Phillips, MA et al. (1990) Primary structure of keratinocyte transglutaminase. Proc. Natl. Acad. Sci. U.S.A. 87 9333-7 PubMed GONUTS page
↑ Kim, SY et al. (1994) The structure of the transglutaminase 1 enzyme. Deletion cloning reveals domains that regulate its specific activity and substrate specificity. J. Biol. Chem. 269 27979-86 PubMed GONUTS page
↑ Ahvazi, B et al. (2004) Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium. J. Biol. Chem. 279 7180-92 PubMed GONUTS page

[PMID:9722562-1] 1.0 ^1.1 Tarcsa, E et al. (1998) Structural and transglutaminase substrate properties of the small proline-rich 2 family of cornified cell envelope proteins. J. Biol. Chem. 273 23297-303 PubMed GONUTS page

[PMID:26220141-2] 2.0 ^2.1 Zhang, SQ et al. (2016) Identification and functional characterization of a novel transglutaminase 1 gene mutation associated with autosomal recessive congenital ichthyosis. Int. J. Dermatol. 55 201-7 PubMed GONUTS page

[PMID:21282207-3] Henry, J et al. (2011) Hornerin is a component of the epidermal cornified cell envelopes. FASEB J. 25 1567-76 PubMed GONUTS page

[PMID:19199708-4] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:8824274-5] 5.0 ^5.1 ^5.2 Steinert, PM et al. (1996) The transglutaminase 1 enzyme is variably acylated by myristate and palmitate during differentiation in epidermal keratinocytes. J. Biol. Chem. 271 26242-50 PubMed GONUTS page

[PMID:1979171-6] Phillips, MA et al. (1990) Primary structure of keratinocyte transglutaminase. Proc. Natl. Acad. Sci. U.S.A. 87 9333-7 PubMed GONUTS page

[PMID:7961731-7] Kim, SY et al. (1994) The structure of the transglutaminase 1 enzyme. Deletion cloning reveals domains that regulate its specific activity and substrate specificity. J. Biol. Chem. 269 27979-86 PubMed GONUTS page

[PMID:14645372-8] Ahvazi, B et al. (2004) Structural basis for the coordinated regulation of transglutaminase 3 by guanine nucleotides and calcium/magnesium. J. Biol. Chem. 279 7180-92 PubMed GONUTS page

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HUMAN:TGM1

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