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Reviewed, UniProtKB/Swiss-Prot Q08188 (TGM3_HUMAN)

Last modified January 19, 2010. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein-glutamine gamma-glutamyltransferase E
      Short name=TGase E
      Short name=TGE
      Short name=TG(E)
    EC=2.3.2.13
Alternative name(s):
    Transglutaminase-3
Cleaved into the following 2 chains:
    1- Recommended name:
            Protein-glutamine gamma-glutamyltransferase E 50 kDa non-catalytic chain
    2- Recommended name:
            Protein-glutamine gamma-glutamyltransferase E 27 kDa catalytic chain
Gene names
Name: TGM3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length693 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. It is responsible for the later stages of cell envelope formation in the epidermis and the hair follicle.

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

This enzyme consists of two polypeptide chains, which are synthesized as a precursor form of a single polypeptide.

Post-translational modification

Activated by proteolytic processing.

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 470469Protein-glutamine gamma-glutamyltransferase E 50 kDa non-catalytic chain
PRO_0000033652
Chain471 – 693223Protein-glutamine gamma-glutamyltransferase E 27 kDa catalytic chain
PRO_0000033653

Sites

Active site2731 By similarity
Active site3311 By similarity
Active site3541 By similarity
Metal binding3941Calcium By similarity
Metal binding3961Calcium By similarity
Metal binding4441Calcium By similarity
Metal binding4491Calcium By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue1111Phosphotyrosine Ref.9
Modified residue1121Phosphothreonine Ref.9

Natural variations

Natural variant131T → K: dbSNP rs214803. Ref.7 Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
VAR_040067
Natural variant1631I → L: dbSNP rs6048066. Ref.3
VAR_040068
Natural variant2491S → N: dbSNP rs214814. Ref.3
VAR_040069
Natural variant5621K → R: dbSNP rs1042617. Ref.1
VAR_040070
Natural variant6541G → R: dbSNP rs214830. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
VAR_040071
Natural variant6871L → M: dbSNP rs45581032. Ref.3
VAR_055360

Experimental info

Sequence conflict58 – 592VS → DT in AAA61155. Ref.1
Sequence conflict2511N → G in AAA61155. Ref.1
Sequence conflict3241S → G in BAF84040. Ref.2
Sequence conflict3461S → P in AAA61155. Ref.1
Sequence conflict6741D → G in BAF84040. Ref.2

Secondary structure

.................................................................................................................. 693
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08188-1 [UniParc].

Last modified September 1, 2009. Version 4.
Checksum: EAFAC0C9A8AA5FD6

FASTA69376,632
        10         20         30         40         50         60 
MAALGVQSIN WQTAFNRQAH HTDKFSSQEL ILRRGQNFQV LMIMNKGLGS NERLEFIVST 

        70         80         90        100        110        120 
GPYPSESAMT KAVFPLSNGS SGGWSAVLQA SNGNTLTISI SSPASAPIGR YTMALQIFSQ 

       130        140        150        160        170        180 
GGISSVKLGT FILLFNPWLN VDSVFMGNHA EREEYVQEDA GIIFVGSTNR IGMIGWNFGQ 

       190        200        210        220        230        240 
FEEDILSICL SILDRSLNFR RDAATDVASR NDPKYVGRVL SAMINSNDDN GVLAGNWSGT 

       250        260        270        280        290        300 
YTGGRDPRSW NGSVEILKNW KKSGFSPVRY GQCWVFAGTL NTALRSLGIP SRVITNFNSA 

       310        320        330        340        350        360 
HDTDRNLSVD VYYDPMGNPL DKGSDSVWNF HVWNEGWFVR SDLGPSYGGW QVLDATPQER 

       370        380        390        400        410        420 
SQGVFQCGPA SVIGVREGDV QLNFDMPFIF AEVNADRITW LYDNTTGKQW KNSVNSHTIG 

       430        440        450        460        470        480 
RYISTKAVGS NARMDVTDKY KYPEGSDQER QVFQKALGKL KPNTPFAATS SMGLETEEQE 

       490        500        510        520        530        540 
PSIIGKLKVA GMLAVGKEVN LVLLLKNLSR DTKTVTVNMT AWTIIYNGTL VHEVWKDSAT 

       550        560        570        580        590        600 
MSLDPEEEAE HPIKISYAQY EKYLKSDNMI RITAVCKVPD ESEVVVERDI ILDNPTLTLE 

       610        620        630        640        650        660 
VLNEARVRKP VNVQMLFSNP LDEPVRDCVL MVEGSGLLLG NLKIDVPTLG PKEGSRVRFD 

       670        680        690 
ILPSRSGTKQ LLADFSCNKF PAIKAMLSID VAE 

« Hide

References

« Hide 'large scale' references
[1]"The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse."
Kim I.-G., Gorman J.J., Park S.-C., Chung S.-I., Steinert P.M.
J. Biol. Chem. 268:12682-12690(1993) [PubMed: 8099584] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LYS-13; ARG-562 AND ARG-654.
Tissue: Foreskin.
[2]"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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LYS-13 AND ARG-654.
Tissue: Tongue.
[3]NIEHS SNPs program
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-13; LEU-163; ASN-249; ARG-654 AND MET-687.
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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], VARIANTS LYS-13 AND ARG-654.
[6]"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], VARIANTS LYS-13 AND ARG-654.
[7]Bienvenut W.V., Bensaad K., Vousden K.H.
Submitted (FEB-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13 AND 670-684, VARIANT LYS-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
Tissue: Osteosarcoma.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-111 AND THR-112, MASS SPECTROMETRY.
Tissue: T-cell.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10386 mRNA. Translation: AAA61155.1.
AK290324 mRNA. Translation: BAF83013.1.
AK291351 mRNA. Translation: BAF84040.1.
AK315236 mRNA. Translation: BAG37663.1.
EF102483 Genomic DNA. Translation: ABK41960.1.
AL031678 Genomic DNA. Translation: CAB37633.1.
CH471133 Genomic DNA. Translation: EAX10601.1.
BC109075 mRNA. Translation: AAI09076.1.
BC109076 mRNA. Translation: AAI09077.1.
IPIIPI00300376.
PIRA45991.
RefSeqNP_003236.3.
UniGeneHs.2022

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L9MX-ray2.10A/B2-693[»]
1L9NX-ray2.10A/B2-693[»]
1NUDX-ray2.70A/B2-693[»]
1NUFX-ray2.70A2-693[»]
1NUGX-ray2.40A/B2-693[»]
1RLEX-ray2.10A/B2-693[»]
1SGXX-ray2.00A/B2-693[»]
1VJJX-ray1.90A/B2-693[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ08188. 2 interactions.
STRINGQ08188.

Proteomic databases

PeptideAtlasQ08188.
PRIDEQ08188.

Genome annotation databases

EnsemblENST00000381458; ENSP00000370867; ENSG00000125780; Homo sapiens. [Genome view]
GeneID7053.
KEGGhsa:7053.

Organism-specific databases

CTD7053.
GeneCardsGC20P002224.
H-InvDBHIX0040608.
HGNCHGNC:11779. TGM3.
HPAHPA004728.
MIM600238. gene.
PharmGKBPA36492.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18302.
HOGENOMHBG444754.
HOVERGENQ08188.
InParanoidQ08188.
OMAFSNPLDE.
OrthoDBEOG9B017K.

Enzyme and pathway databases

BRENDA2.3.2.13. 247.

Gene expression databases

ArrayExpressQ08188.
BgeeQ08188.
CleanExHS_TGM3.
GenevestigatorQ08188.
GermOnlineENSG00000125780. Homo sapiens.

Family and domain databases

InterProIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 3 hits.
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

DrugBankDB00130. L-Glutamine.
SOURCESearch...

Entry information

Entry nameTGM3_HUMAN
AccessionPrimary (citable) accession number: Q08188
Secondary accession number(s): A8K5N6 expand/collapse secondary AC list , B2RCR6, O95933, Q32ML9, Q32MM0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 1, 2009
Last modified: January 19, 2010
This is version 104 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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