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P22735 (TGM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length817 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.

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, congenital, autosomal recessive 1 (ARCI1) [MIM:242300]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. 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. Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

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 processKeratinization
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Ichthyosis
   LigandCalcium
Metal-binding
   Molecular functionAcyltransferase
Transferase
   PTMLipoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell 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: Ensembl

peptide cross-linking

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell-cell adherens junction

Inferred from electronic annotation. Source: Ensembl

cornified envelope

Traceable author statement PubMed 8824274. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

intrinsic component of membrane

Inferred from direct assay PubMed 8824274. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 10066784PubMed 10510474PubMed 7592852PubMed 9722562. Source: UniProtKB

protein-glutamine gamma-glutamyltransferase activity

Inferred from direct assay PubMed 7961731. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 817817Protein-glutamine gamma-glutamyltransferase K
PRO_0000213701

Regions

Region1 – 100100Membrane anchorage region

Sites

Active site3771 By similarity
Active site4361 By similarity
Active site4591 By similarity
Metal binding4991Calcium By similarity
Metal binding5011Calcium By similarity
Metal binding5481Calcium By similarity
Metal binding5531Calcium By similarity

Amino acid modifications

Modified residue241Phosphoserine Ref.14
Modified residue821Phosphoserine Ref.14
Modified residue851Phosphoserine Ref.14
Modified residue921Phosphoserine Ref.14
Modified residue951Phosphoserine By similarity

Natural variations

Natural variant421S → Y in ARCI1; skin phenotype consistent with lamellar ichthyosis. Ref.9 Ref.17
Corresponds to variant rs41295338 [ dbSNP | Ensembl ].
VAR_015220
Natural variant531C → S in ARCI1.
VAR_058638
Natural variant941G → D in ARCI1.
Corresponds to variant rs121918729 [ dbSNP | Ensembl ].
VAR_058639
Natural variant1021D → V in ARCI1; skin phenotype consistent with lamellar ichthyosis. Ref.21
VAR_020918
Natural variant1261R → C in ARCI1.
VAR_058640
Natural variant1261R → H in ARCI1.
VAR_058641
Natural variant1321D → N.
Corresponds to variant rs2229462 [ dbSNP | Ensembl ].
VAR_029268
Natural variant1341Y → C in ARCI1.
VAR_058642
Natural variant1421R → C in ARCI1.
VAR_058643
Natural variant1421R → H in ARCI1; skin phenotype consistent with lamellar ichthyosis. Ref.18 Ref.19
VAR_007476
Natural variant1421R → P in ARCI1.
VAR_058644
Natural variant1431R → C in ARCI1. Ref.19
VAR_007477
Natural variant1431R → H in ARCI1; skin phenotype consistent with lamellar ichthyosis. Ref.18
VAR_007478
Natural variant1441G → E in ARCI1.
VAR_058645
Natural variant1441G → R in ARCI1.
VAR_058646
Natural variant1601S → C in ARCI1.
VAR_058647
Natural variant2051L → Q in ARCI1.
VAR_058648
Natural variant2091V → F in ARCI1.
VAR_058649
Natural variant2181G → S in ARCI1; skin phenotype consistent with lamellar ichthyosis. Ref.19
VAR_007479
Natural variant2251R → H in ARCI1.
VAR_058650
Natural variant2251R → P in ARCI1.
VAR_058651
Natural variant2431I → S in ARCI1.
VAR_058652
Natural variant2491P → L in ARCI1.
VAR_058653
Natural variant2641R → Q in ARCI1.
VAR_058654
Natural variant2641R → W in ARCI1.
VAR_058655
Natural variant2721S → P in ARCI1.
VAR_058656
Natural variant2761Y → N in ARCI1.
VAR_058657
Natural variant2781G → R in ARCI1.
VAR_058658
Natural variant2851E → K in ARCI1.
VAR_058659
Natural variant2861R → Q in ARCI1.
VAR_058660
Natural variant2891N → T in ARCI1; skin phenotype consistent with lamellar ichthyosis. Ref.21
VAR_020919
Natural variant2931F → V in ARCI1.
VAR_058661
Natural variant3041I → F in ARCI1.
VAR_058662
Natural variant3071R → G in ARCI1. Ref.22
Corresponds to variant rs121918731 [ dbSNP | Ensembl ].
VAR_058663
Natural variant3071R → W in ARCI1; skin phenotype consistent with lamellar ichthyosis. Ref.21
VAR_020920
Natural variant3151R → C in ARCI1.
VAR_058664
Natural variant3151R → H in ARCI1.
VAR_058665
Natural variant3151R → L in ARCI1.
VAR_058666
Natural variant3231R → Q in ARCI1; skin phenotype consistent with lamellar ichthyosis. Ref.17
VAR_015221
Natural variant3231R → W in ARCI1.
VAR_058667
Natural variant3301N → H in ARCI1.
VAR_058668
Natural variant3311S → P in ARCI1.
VAR_058669
Natural variant3421W → R in ARCI1.
VAR_058670
Natural variant3581S → R in ARCI1.
VAR_058671
Natural variant3591V → M in ARCI1.
VAR_058672
Natural variant3651Y → D in ARCI1.
VAR_058673
Natural variant3661L → P in ARCI1.
VAR_058674
Natural variant3721V → I. Ref.9
Corresponds to variant rs41293794 [ dbSNP | Ensembl ].
VAR_055374
Natural variant3791V → L in ARCI1. Ref.19
VAR_007480
Natural variant3821G → R in ARCI1.
VAR_058675
Natural variant3831V → M in ARCI1.
VAR_058676
Natural variant3891R → H in ARCI1; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma. Ref.20
VAR_015222
Natural variant3891R → P in ARCI1.
VAR_058677
Natural variant3921G → D in ARCI1.
VAR_058678
Natural variant3961R → H in ARCI1.
VAR_058679
Natural variant3961R → L in ARCI1; skin phenotype consistent with non-bullous congenital ichthyosiform erythroderma. Ref.19
Corresponds to variant rs121918721 [ dbSNP | Ensembl ].
VAR_007481
Natural variant3961R → S in ARCI1.
VAR_058680
Natural variant4011F → V in ARCI1.
VAR_058681
Natural variant4301D → V in ARCI1.
VAR_058682
Natural variant4731G → S in ARCI1.
VAR_058683
Natural variant4901D → G in ARCI1.
VAR_058684
Natural variant5181V → M. Ref.9
Corresponds to variant rs35312232 [ dbSNP | Ensembl ].
VAR_052550
Natural variant5201E → G in ARCI1.
Corresponds to variant rs142404759 [ dbSNP | Ensembl ].
VAR_058685
Natural variant5441Y → C in ARCI1.
VAR_058686
Natural variant6071R → C. Ref.9
Corresponds to variant rs2229464 [ dbSNP | Ensembl ].
VAR_052551
Natural variant6871R → C in ARCI1.
VAR_058687
Natural variant6871R → H in ARCI1.
VAR_058688
Natural variant7551S → L. Ref.9
Corresponds to variant rs35926651 [ dbSNP | Ensembl ].
VAR_052552
Natural variant7641R → C in ARCI1.
VAR_058689
Natural variant8021D → V. Ref.9
Corresponds to variant rs2228337 [ dbSNP | Ensembl ].
VAR_024660

Experimental info

Sequence conflict119 – 1202Missing in M86360. Ref.5
Sequence conflict3011C → A in AAA61156. Ref.4
Sequence conflict5081Q → H in M86360. Ref.5
Sequence conflict5511D → E in M86360. Ref.5
Sequence conflict5541R → A in AAA61166. Ref.3
Sequence conflict6691V → I in AAA61166. Ref.3

Secondary structure

................... 817
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22735 [UniParc].

Last modified January 4, 2005. Version 4.
Checksum: 4732F28234F5D5F1

FASTA81789,787
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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 ARCI1 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 ARCI1 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 ARCI1 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 ARCI1 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 ARCI1 VAL-102; THR-289 AND TRP-307.
[22]"Genotypic and clinical spectrum of self-improving collodion ichthyosis: ALOX12B, ALOXE3, and TGM1 mutations in Scandinavian patients."
Vahlquist A., Bygum A., Gaanemo A., Virtanen M., Hellstroem-Pigg M., Strauss G., Brandrup F., Fischer J.
J. Invest. Dermatol. 130:438-443(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARCI1 GLY-307.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55183 mRNA. Translation: AAA59474.1.
D90287 mRNA. Translation: BAA14329.1.
M62925 mRNA. Translation: AAA61166.1. Frameshift.
M83230 expand/collapse EMBL AC list , 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.
CCDSCCDS9622.1.
PIRTGHUM1. A43401.
RefSeqNP_000350.1. NM_000359.2.
UniGeneHs.508950.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XZZX-ray2.30A693-787[»]
ProteinModelPortalP22735.
SMRP22735. Positions 110-787.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112909. 4 interactions.
IntActP22735. 5 interactions.
STRING9606.ENSP00000206765.

Chemistry

BindingDBP22735.
ChEMBLCHEMBL2810.
DrugBankDB00130. L-Glutamine.

PTM databases

PhosphoSiteP22735.

Polymorphism databases

DMDM57015359.

Proteomic databases

MaxQBP22735.
PaxDbP22735.
PeptideAtlasP22735.
PRIDEP22735.

Protocols and materials databases

DNASU7051.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000206765; ENSP00000206765; ENSG00000092295.
GeneID7051.
KEGGhsa:7051.
UCSCuc001wod.3. human.

Organism-specific databases

CTD7051.
GeneCardsGC14M024718.
GeneReviewsTGM1.
HGNCHGNC:11777. TGM1.
HPACAB015159.
HPA040171.
MIM190195. gene.
242300. phenotype.
neXtProtNX_P22735.
Orphanet281127. Acral self-healing collodion baby.
100976. Bathing suit ichthyosis.
79394. Congenital non-bullous ichthyosiform erythroderma.
313. Lamellar ichthyosis.
281122. Self-healing collodion baby.
PharmGKBPA36490.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80379.
HOGENOMHOG000231695.
HOVERGENHBG004342.
InParanoidP22735.
KOK05619.
OMAGRWGGNP.
OrthoDBEOG7WT40M.
PhylomeDBP22735.
TreeFamTF324278.

Gene expression databases

ArrayExpressP22735.
BgeeP22735.
CleanExHS_TGM1.
GenevestigatorP22735.

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

GeneWikiKeratinocyte_transglutaminase.
GenomeRNAi7051.
NextBio27569.
PROP22735.
SOURCESearch...

Entry information

Entry nameTGM1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 155 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM