P22735 (TGM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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
Synonyms:	KTG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	817 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.
Catalytic activity	Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.
Cofactor	Binds 1 calcium ion per subunit.
Subcellular location	Membrane; Lipid-anchor.
Post-translational modification	The membrane anchorage region possesses a cluster of five cysteines within which fatty acid(s) may become thioester-linked. It is subject to phorbol ester-stimulated phosphorylation and is hypersensitive to proteolysis, which releases the enzyme in a soluble form.
Involvement in disease	Ichthyosis, lamellar, 1 (LI1) [MIM:242300]: A non-bullous ichthyosis, a skin disorder characterized by abnormal cornification of the epidermis. It is one of the most severe forms of ichthyoses apparent at birth and persisting throughout life. LI patients are born encased in a tight, shiny, translucent covering called collodion membrane. Over the first weeks of life, the collodion membrane is gradually replaced by generalized large, dark brown, plate-like scales with minimal to no erythroderma. Tautness of facial skin commonly results in ectropion, eclabium and scarring alopecia of the scalp. Common complications are severe heat intolerance and recurrent ear infections. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.18 Ref.19 Ref.21 Erythroderma, ichthyosiform, congenital non-bullous (NCIE) [MIM:242100]: A non-bullous ichthyosis, a skin disorder characterized by abnormal cornification of the epidermis. Most affected individuals are born with a tight, shiny, translucent covering called collodion membrane. The collodion membrane subsequently evolves into generalized scaling and intense redness of the skin. Clinical features are milder than in lamellar ichthyoses and demonstrate a greater variability in the intensity of erythema, size and type of scales. In contrast to lamellar ichthyoses, scales are usually white, fine and powdery, and palms and soles are severely affected. Patients suffer from palmoplantar keratoderma, often with painful fissures, digital contractures, and loss of pulp volume. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ichthyosis, congenital, autosomal recessive, TGM1-related (ARCI-TGM1) [MIM:242300]: A disorder of keratinization with abnormal differentiation and desquamation of the epidermis resulting in two major clinical entities. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the transglutaminase superfamily. Transglutaminase family.
Sequence caution	The sequence AAA61166.1 differs from that shown. Reason: Frameshift at position 16. The sequence M86360 differs from that shown. Reason: Frameshift at positions 16, 421 and 651.

Ontologies

Keywords
Biological process	Keratinization
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Ichthyosis
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Lipoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell envelope organization Traceable author statement PubMed 14645372. Source: UniProtKB cellular protein modification process Non-traceable author statement Ref.1. Source: UniProtKB keratinization Inferred from electronic annotation. Source: UniProtKB-KW keratinocyte differentiation Inferred from direct assay PubMed 8824274. Source: UniProtKB organ morphogenesis Inferred from electronic annotation. Source: Compara peptide cross-linking Inferred from electronic annotation. Source: InterPro
Cellular_component	cell-cell adherens junction Inferred from electronic annotation. Source: Compara cornified envelope Traceable author statement PubMed 8824274. Source: UniProtKB intrinsic to membrane Inferred from direct assay PubMed 8824274. Source: UniProtKB
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein-glutamine gamma-glutamyltransferase activity Inferred from direct assay PubMed 7961731. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 817

817

Protein-glutamine gamma-glutamyltransferase K

PRO_0000213701

Regions

Region

1 – 100

100

Membrane anchorage region

Sites

Active site

377

1

By similarity

Active site

436

1

By similarity

Active site

459

1

By similarity

Metal binding

499

1

Calcium By similarity

Metal binding

501

1

Calcium By similarity

Metal binding

548

1

Calcium By similarity

Metal binding

553

1

Calcium By similarity

Amino acid modifications

Modified residue

24

1

Phosphoserine Ref.14

Modified residue

68

1

Phosphoserine By similarity

Modified residue

82

1

Phosphoserine Ref.14

Modified residue

85

1

Phosphoserine Ref.14

Modified residue

92

1

Phosphoserine Ref.14

Modified residue

95

1

Phosphoserine By similarity

Natural variations

Natural variant

42

1

S → Y in LI1. Ref.9 Ref.17
Corresponds to variant rs41295338 [ dbSNP | Ensembl ].

VAR_015220

Natural variant

53

1

C → S in ARCI-TGM1.

VAR_058638

Natural variant

94

1

G → D in ARCI-TGM1.

VAR_058639

Natural variant

102

1

D → V in LI1. Ref.21

VAR_020918

Natural variant

126

1

R → C in ARCI-TGM1.

VAR_058640

Natural variant

126

1

R → H in ARCI-TGM1.

VAR_058641

Natural variant

132

1

D → N.
Corresponds to variant rs2229462 [ dbSNP | Ensembl ].

VAR_029268

Natural variant

134

1

Y → C in ARCI-TGM1.

VAR_058642

Natural variant

142

1

R → C in ARCI-TGM1.

VAR_058643

Natural variant

142

1

R → H in LI1. Ref.18 Ref.19

VAR_007476

Natural variant

142

1

R → P in ARCI-TGM1.

VAR_058644

Natural variant

143

1

R → C in LI1 and NCIE. Ref.19

VAR_007477

Natural variant

143

1

R → H in LI1. Ref.18

VAR_007478

Natural variant

144

1

G → E in ARCI-TGM1.

VAR_058645

Natural variant

144

1

G → R in ARCI-TGM1.

VAR_058646

Natural variant

160

1

S → C in ARCI-TGM1.

VAR_058647

Natural variant

205

1

L → Q in ARCI-TGM1.

VAR_058648

Natural variant

209

1

V → F in ARCI-TGM1.

VAR_058649

Natural variant

218

1

G → S in LI1. Ref.19

VAR_007479

Natural variant

225

1

R → H in ARCI-TGM1.

VAR_058650

Natural variant

225

1

R → P in ARCI-TGM1.

VAR_058651

Natural variant

243

1

I → S in ARCI-TGM1.

VAR_058652

Natural variant

249

1

P → L in ARCI-TGM1.

VAR_058653

Natural variant

264

1

R → Q in ARCI-TGM1.

VAR_058654

Natural variant

264

1

R → W in ARCI-TGM1.

VAR_058655

Natural variant

272

1

S → P in ARCI-TGM1.

VAR_058656

Natural variant

276

1

Y → N in ARCI-TGM1.

VAR_058657

Natural variant

278

1

G → R in ARCI-TGM1.

VAR_058658

Natural variant

285

1

E → K in ARCI-TGM1.

VAR_058659

Natural variant

286

1

R → Q in ARCI-TGM1.

VAR_058660

Natural variant

289

1

N → T in LI1. Ref.21

VAR_020919

Natural variant

293

1

F → V in ARCI-TGM1.

VAR_058661

Natural variant

304

1

I → F in ARCI-TGM1.

VAR_058662

Natural variant

307

1

R → G in ARCI-TGM1.

VAR_058663

Natural variant

307

1

R → W in LI1. Ref.21

VAR_020920

Natural variant

315

1

R → C in ARCI-TGM1.

VAR_058664

Natural variant

315

1

R → H in ARCI-TGM1.

VAR_058665

Natural variant

315

1

R → L in ARCI-TGM1.

VAR_058666

Natural variant

323

1

R → Q in LI1. Ref.17

VAR_015221

Natural variant

323

1

R → W in ARCI-TGM1.

VAR_058667

Natural variant

330

1

N → H in ARCI-TGM1.

VAR_058668

Natural variant

331

1

S → P in ARCI-TGM1.

VAR_058669

Natural variant

342

1

W → R in ARCI-TGM1.

VAR_058670

Natural variant

358

1

S → R in ARCI-TGM1.

VAR_058671

Natural variant

359

1

V → M in ARCI-TGM1.

VAR_058672

Natural variant

365

1

Y → D in ARCI-TGM1.

VAR_058673

Natural variant

366

1

L → P in ARCI-TGM1.

VAR_058674

Natural variant

372

1

V → I. Ref.9
Corresponds to variant rs41293794 [ dbSNP | Ensembl ].

VAR_055374

Natural variant

379

1

V → L in LI1 and NCIE. Ref.19

VAR_007480

Natural variant

382

1

G → R in ARCI-TGM1.

VAR_058675

Natural variant

383

1

V → M in ARCI-TGM1.

VAR_058676

Natural variant

389

1

R → H in NCIE. Ref.20

VAR_015222

Natural variant

389

1

R → P in ARCI-TGM1.

VAR_058677

Natural variant

392

1

G → D in ARCI-TGM1.

VAR_058678

Natural variant

396

1

R → H in ARCI-TGM1.

VAR_058679

Natural variant

396

1

R → L in NCIE. Ref.19

VAR_007481

Natural variant

396

1

R → S in ARCI-TGM1.

VAR_058680

Natural variant

401

1

F → V in ARCI-TGM1.

VAR_058681

Natural variant

430

1

D → V in ARCI-TGM1.

VAR_058682

Natural variant

473

1

G → S in ARCI-TGM1.

VAR_058683

Natural variant

490

1

D → G in ARCI-TGM1.

VAR_058684

Natural variant

518

1

V → M. Ref.9
Corresponds to variant rs35312232 [ dbSNP | Ensembl ].

VAR_052550

Natural variant

520

1

E → G in ARCI-TGM1.

VAR_058685

Natural variant

544

1

Y → C in ARCI-TGM1.

VAR_058686

Natural variant

607

1

R → C. Ref.9
Corresponds to variant rs2229464 [ dbSNP | Ensembl ].

VAR_052551

Natural variant

687

1

R → C in ARCI-TGM1.

VAR_058687

Natural variant

687

1

R → H in ARCI-TGM1.

VAR_058688

Natural variant

755

1

S → L. Ref.9
Corresponds to variant rs35926651 [ dbSNP | Ensembl ].

VAR_052552

Natural variant

764

1

R → C in ARCI-TGM1.

VAR_058689

Natural variant

802

1

D → V. Ref.9
Corresponds to variant rs2228337 [ dbSNP | Ensembl ].

VAR_024660

Experimental info

Sequence conflict

119 – 120

2

Missing in M86360. Ref.5

Sequence conflict

301

1

C → A in AAA61156. Ref.4

Sequence conflict

508

1

Q → H in M86360. Ref.5

Sequence conflict

551

1

D → E in M86360. Ref.5

Sequence conflict

554

1

R → A in AAA61166. Ref.3

Sequence conflict

669

1

V → I in AAA61166. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

817

Helix Strand Turn

Details...

Beta strand

693 – 699

7

Beta strand

703 – 705

3

Beta strand

707 – 714

8

Beta strand

717 – 719

3

Beta strand

723 – 730

8

Turn

731 – 733

3

Beta strand

734 – 741

8

Beta strand

749 – 756

8

Beta strand

767 – 771

5

Helix

773 – 776

4

Sequences

	Sequence		Length	Mass (Da)
	P22735 [UniParc]. Last modified January 4, 2005. Version 4. Checksum: 4732F28234F5D5F1	FASTA	817	89,787
	10 20 30 40 50 60 MMDGPRSDVG RWGGNPLQPP TTPSPEPEPE PDGRSRRGGG RSFWARCCGC CSCRNAADDD 70 80 90 100 110 120 WGPEPSDSRG RGSSSGTRRP GSRGSDSRRP VSRGSGVNAA GDGTIREGML VVNGVDLLSS 130 140 150 160 170 180 RSDQNRREHH TDEYEYDELI VRRGQPFHML LLLSRTYESS DRITLELLIG NNPEVGKGTH 190 200 210 220 230 240 VIIPVGKGGS GGWKAQVVKA SGQNLNLRVH TSPNAIIGKF QFTVRTQSDA GEFQLPFDPR 250 260 270 280 290 300 NEIYILFNPW CPEDIVYVDH EDWRQEYVLN ESGRIYYGTE AQIGERTWNY GQFDHGVLDA 310 320 330 340 350 360 CLYILDRRGM PYGGRGDPVN VSRVISAMVN SLDDNGVLIG NWSGDYSRGT NPSAWVGSVE 370 380 390 400 410 420 ILLSYLRTGY SVPYGQCWVF AGVTTTVLRC LGLATRTVTN FNSAHDTDTS LTMDIYFDEN 430 440 450 460 470 480 MKPLEHLNHD SVWNFHVWND CWMKRPDLPS GFDGWQVVDA TPQETSSGIF CCGPCSVESI 490 500 510 520 530 540 KNGLVYMKYD TPFIFAEVNS DKVYWQRQDD GSFKIVYVEE KAIGTLIVTK AISSNMREDI 550 560 570 580 590 600 TYLYKHPEGS DAERKAVETA AAHGSKPNVY ANRGSAEDVA MQVEAQDAVM GQDLMVSVML 610 620 630 640 650 660 INHSSSRRTV KLHLYLSVTF YTGVSGTIFK ETKKEVELAP GASDRVTMPV AYKEYRPHLV 670 680 690 700 710 720 DQGAMLLNVS GHVKESGQVL AKQHTFRLRT PDLSLTLLGA AVVGQECEVQ IVFKNPLPVT 730 740 750 760 770 780 LTNVVFRLEG SGLQRPKILN VGDIGGNETV TLRQSFVPVR PGPRQLIASL DSPQLSQVHG 790 800 810 VIQVDVAPAP GDGGFFSDAG GDSHLGETIP MASRGGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of keratinocyte transglutaminase." Phillips M.A., Stewart B.E., Qin Q., Chakravarty R., Floyd E.E., Jetten A.M., Rice R.H. Proc. Natl. Acad. Sci. U.S.A. 87:9333-9337(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning of human epidermal transglutaminase cDNA from keratinocytes in culture." Yamanishi K., Liew F.M., Konishi K., Yasuno H., Doi H., Hirano J., Fukushima S. Biochem. Biophys. Res. Commun. 175:906-913(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Keratinocyte.
[3]	"The complete amino acid sequence of the human transglutaminase K enzyme deduced from the nucleic acid sequences of cDNA clones." Kim H.C., Idler W.W., Kim I.-G., Han J.H., Chung S.-I., Steinert P.M. J. Biol. Chem. 266:536-539(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Genomic structure of keratinocyte transglutaminase. Recruitment of new exon for modified function." Phillips M.A., Stewart B.E., Rice R.H. J. Biol. Chem. 267:2282-2286(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[5]	"Structure and organization of the human transglutaminase 1 gene." Kim I.-G., McBride O.W., Wang M., Kim S.-Y., Idler W.W., Steinert P.M. J. Biol. Chem. 267:7710-7717(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Structure of the gene for human transglutaminase 1." Yamanishi K., Inazawa J., Liew F., Nonomura K., Ariyama T., Yasuno H., Abe T., Doi H., Hirano J., Fukushima S. J. Biol. Chem. 267:17858-17863(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[7]	"Organization and evolution of the human epidermal keratinocyte transglutaminase I gene." Polakowska R.R., Eickbush T., Falciano V., Razvi F., Goldsmith L.A. Proc. Natl. Acad. Sci. U.S.A. 89:4476-4480(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[8]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Esophagus.
[9]	NIEHS SNPs program Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TYR-42; ILE-372; MET-518; CYS-607; LEU-755 AND VAL-802.
[10]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	"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]. Tissue: Skin.
[12]	"Isolation of cDNA for human epidermal type I transglutaminase." Polakowska R., Herting E., Goldsmith L.A. J. Invest. Dermatol. 96:285-288(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-551.
[13]	"Type I keratinocyte transglutaminase: expression in human skin and psoriasis." Schroeder W., Thacher S., Stewart-Galetka S., Annarella M., Chema D., Sicliano M., Davies P., Tang H.Y., Sowa B., Duvic M. J. Invest. Dermatol. 99:27-34(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 375-817. Tissue: Skin.
[14]	"Identification of phosphorylation sites in keratinocyte transglutaminase." Rice R.H., Mehrpouyan M., Quin Q., Phillips M.A., Lee Y.M. Biochem. J. 320:547-550(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-24; SER-82; SER-85 AND SER-92.
[15]	"Transglutaminase-1 gene mutations in autosomal recessive congenital ichthyosis: summary of mutations (including 23 novel) and modeling of TGase-1." Herman M.L., Farasat S., Steinbach P.J., Wei M.H., Toure O., Fleckman P., Blake P., Bale S.J., Toro J.R. Hum. Mutat. 30:537-547(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[16]	"Crystal structure of the human transglutaminase 1 beta-barrel domain." Structural genomics consortium (SGC) Submitted (JAN-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 693-787.
[17]	"Mutations of keratinocyte transglutaminase in lamellar ichthyosis." Huber M., Rettler I., Bernasconi K., Frenk E., Lavrijsen S.P.M., Ponec M., Bon A., Lautenschlager S., Schorderet D.F., Hohl D. Science 267:525-528(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LI1 TYR-42 AND GLN-323.
[18]	"Mutations in the gene for transglutaminase 1 in autosomal recessive lamellar ichthyosis." Russell L.J., Digiovanna J.J., Rogers G.R., Steinert P.M., Hashem N., Compton J.G., Bale S.J. Nat. Genet. 9:279-283(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LI1 HIS-142 AND HIS-143.
[19]	"Transglutaminase 1 mutations in autosomal recessive congenital ichthyosis: private and recurrent mutations in an isolated population." Laiho E., Ignatius J., Mikkola H., Yee V.C., Teller D.C., Niemi K.-M., Saarialho-Kere U., Kere J., Palotie A. Am. J. Hum. Genet. 61:529-538(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LI1/NCIE HIS-142; CYS-143; SER-218; LEU-379 AND LEU-396.
[20]	"Novel mutations of TGM1 in a child with congenital ichthyosiform erythroderma." Akiyama M., Takizawa Y., Kokaji T., Shimizu H. Br. J. Dermatol. 144:401-407(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT NCIE HIS-389.
[21]	"Novel mutations of the transglutaminase 1 gene in lamellar ichthyosis." Yang J.M., Ahn K.S., Cho M.O., Yoneda K., Lee C.H., Lee J.H., Lee E.S., Candi E., Melino G., Ahvazi B., Steinert P.M. J. Invest. Dermatol. 117:214-218(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS LI1 VAL-102; THR-289 AND TRP-307.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M55183 mRNA. Translation: AAA59474.1.
D90287 mRNA. Translation: BAA14329.1.
M62925 mRNA. Translation: AAA61166.1. Frameshift.
M83230 , M83227, M83228, M83229 Genomic DNA. Translation: AAA61156.1.
M86360 Genomic DNA. No translation available.
D10353 Genomic DNA. Translation: BAA34203.1.
M98447 Genomic DNA. Translation: AAA96667.1.
AK315843 mRNA. Translation: BAF98734.1.
DQ640500 Genomic DNA. Translation: ABF70204.1.
CH471078 Genomic DNA. Translation: EAW66047.1.
BC034699 mRNA. Translation: AAH34699.1.
X57974 mRNA. Translation: CAA41040.1.

IPI

IPI00305622.

PIR

TGHUM1. A43401.

RefSeq

NP_000350.1. NM_000359.2.

UniGene

Hs.508950.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2XZZ	X-ray	2.30	A	693-787	[»]

ProteinModelPortal

P22735.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22735. 3 interactions.

STRING

9606.ENSP00000206765.

PTM databases

PhosphoSite

P22735.

Polymorphism databases

DMDM

57015359.

Proteomic databases

PaxDb

P22735.

PeptideAtlas

P22735.

PRIDE

P22735.

Protocols and materials databases

DNASU

7051.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000206765; ENSP00000206765; ENSG00000092295.

GeneID

7051.

KEGG

hsa:7051.

UCSC

uc001wod.3. human.

Organism-specific databases

CTD

7051.

GeneCards

GC14M024718.

HGNC

HGNC:11777. TGM1.

HPA

CAB015159.

MIM

190195. gene.
242100. phenotype.
242300. phenotype.

neXtProt

NX_P22735.

Orphanet

281127. Acral self-healing collodion baby.
100976. Bathing suit ichthyosis.
79394. Congenital nonbullous ichthyosiform erythroderma.
313. Lamellar ichthyosis.
281122. Self-healing collodion baby.

PharmGKB

PA36490.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG80379.

HOGENOM

HOG000231695.

HOVERGEN

HBG004342.

InParanoid

P22735.

KO

K05619.

OMA

GRWGGNP.

OrthoDB

EOG4VX24R.

PhylomeDB

P22735.

Gene expression databases

ArrayExpress

P22735.

Bgee

P22735.

CleanEx

HS_TGM1.

Genevestigator

P22735.

GermOnline

ENSG00000092295. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

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

BindingDB

P22735.

ChEMBL

CHEMBL2810.

DrugBank

DB00130. L-Glutamine.

GenomeRNAi

7051.

NextBio

27569.

SOURCE

Search...

Entry information

Entry name

TGM1_HUMAN

Accession

Primary (citable) accession number: P22735
Secondary accession number(s): Q197M4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 4, 2005
Last modified:	May 1, 2013
This is version 143 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.