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P21980 (TGM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-glutamine gamma-glutamyltransferase 2

EC=2.3.2.13
Alternative name(s):
Tissue transglutaminase
Transglutaminase C
Short name=TG(C)
Short name=TGC
Short name=TGase C
Transglutaminase H
Short name=TGase H
Transglutaminase-2
Short name=TGase-2
Gene names
Name:TGM2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length687 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.

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subunit structure

Monomer.

Induction

By retinoic acid.

Sequence similarities

Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandCalcium
Metal-binding
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic cell clearance

Inferred from direct assay PubMed 19628791. Source: UniProtKB

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

branching involved in salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

salivary gland cavitation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 9442029. Source: UniProtKB

protein-glutamine gamma-glutamyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P21980-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P21980-2)

The sequence of this isoform differs from the canonical sequence as follows:
     539-548: EKSVPLCILY → GKALCSWSIC
     549-687: Missing.
Isoform 3 (identifier: P21980-3)

Also known as: TGH2;

The sequence of this isoform differs from the canonical sequence as follows:
     287-349: VLRCLGIPTR...SWMTRPDLQP → GELHAGMWVM...LSNSHPSSGC
     350-687: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 687686Protein-glutamine gamma-glutamyltransferase 2
PRO_0000213707

Sites

Active site2771 By similarity
Active site3351 By similarity
Active site3581 By similarity
Metal binding3981Calcium By similarity
Metal binding4001Calcium By similarity
Metal binding4471Calcium By similarity
Metal binding4521Calcium By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.12
Modified residue4681N6-acetyllysine By similarity

Natural variations

Alternative sequence287 – 34963VLRCL…PDLQP → GELHAGMWVMSPGRGHEEHW SRNQDIPALVLPPATNTLNA LCGLEPVTTLSGPLSNSHPS SGC in isoform 3.
VSP_006413
Alternative sequence350 – 687338Missing in isoform 3.
VSP_006414
Alternative sequence539 – 54810EKSVPLCILY → GKALCSWSIC in isoform 2.
VSP_006411
Alternative sequence549 – 687139Missing in isoform 2.
VSP_006412
Natural variant761R → H. Ref.6
Corresponds to variant rs41274720 [ dbSNP | Ensembl ].
VAR_052553
Natural variant2141R → H. Ref.6
Corresponds to variant rs45530133 [ dbSNP | Ensembl ].
VAR_055357
Natural variant3241Q → R. Ref.6
Corresponds to variant rs45567334 [ dbSNP | Ensembl ].
VAR_055358
Natural variant3301M → R in patients with early-onset diabetes type 2; pathological significance unknown. Ref.15
VAR_037998
Natural variant3311I → N in patients with early-onset diabetes type 2; pathological significance unknown. Ref.15
VAR_037999
Natural variant4361R → W. Ref.6
Corresponds to variant rs45629036 [ dbSNP | Ensembl ].
VAR_055359
Natural variant5361P → S. Ref.6
Corresponds to variant rs45556333 [ dbSNP | Ensembl ].
VAR_052554
Natural variant6601G → V in a colorectal cancer sample; somatic mutation. Ref.14
VAR_036554

Experimental info

Sequence conflict511E → Q in AAA63261. Ref.1
Sequence conflict1861E → Q in AAA63261. Ref.1
Sequence conflict2241V → G in AAA63261. Ref.1
Sequence conflict5331N → T in AAA63261. Ref.1
Sequence conflict6551L → V in AAA63261. Ref.1

Secondary structure

................................................................................................................................... 687
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 7DA33FF335DE7B37

FASTA68777,329
        10         20         30         40         50         60 
MAEELVLERC DLELETNGRD HHTADLCREK LVVRRGQPFW LTLHFEGRNY EASVDSLTFS 

        70         80         90        100        110        120 
VVTGPAPSQE AGTKARFPLR DAVEEGDWTA TVVDQQDCTL SLQLTTPANA PIGLYRLSLE 

       130        140        150        160        170        180 
ASTGYQGSSF VLGHFILLFN AWCPADAVYL DSEEERQEYV LTQQGFIYQG SAKFIKNIPW 

       190        200        210        220        230        240 
NFGQFEDGIL DICLILLDVN PKFLKNAGRD CSRRSSPVYV GRVVSGMVNC NDDQGVLLGR 

       250        260        270        280        290        300 
WDNNYGDGVS PMSWIGSVDI LRRWKNHGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN 

       310        320        330        340        350        360 
YNSAHDQNSN LLIEYFRNEF GEIQGDKSEM IWNFHCWVES WMTRPDLQPG YEGWQALDPT 

       370        380        390        400        410        420 
PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA PFVFAEVNAD VVDWIQQDDG SVHKSINRSL 

       430        440        450        460        470        480 
IVGLKISTKS VGRDEREDIT HTYKYPEGSS EEREAFTRAN HLNKLAEKEE TGMAMRIRVG 

       490        500        510        520        530        540 
QSMNMGSDFD VFAHITNNTA EEYVCRLLLC ARTVSYNGIL GPECGTKYLL NLNLEPFSEK 

       550        560        570        580        590        600 
SVPLCILYEK YRDCLTESNL IKVRALLVEP VINSYLLAER DLYLENPEIK IRILGEPKQK 

       610        620        630        640        650        660 
RKLVAEVSLQ NPLPVALEGC TFTVEGAGLT EEQKTVEIPD PVEAGEEVKV RMDLLPLHMG 

       670        680 
LHKLVVNFES DKLKAVKGFR NVIIGPA 

« Hide

Isoform 2 [UniParc].

Checksum: 8C2F43A4D1029AC2
Show »

FASTA54861,678
Isoform 3 (TGH2) [UniParc].

Checksum: 37E1EE27C243CCC5
Show »

FASTA34938,671

References

« Hide 'large scale' references
[1]"Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases."
Gentile V., Saydak M., Chiocca E.A., Akande O., Birckbichler P.J., Lee K.N., Stein J.P., Davies P.J.A.
J. Biol. Chem. 266:478-483(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
Tissue: Endothelial cell.
[2]"A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue."
Fraij B.M., Birckbichler P.J., Patterson M.K. Jr., Lee K.N., Gonzales R.A.
J. Biol. Chem. 267:22616-22623(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"A third human tissue transglutaminase homologue as a result of alternative gene transcripts."
Fraij B.M., Gonzales R.A.
Biochim. Biophys. Acta 1306:63-74(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]Bayardo M.P., de Urraza P., Chirdo F.G.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon adenocarcinoma.
[5]"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] (ISOFORM 1).
Tissue: Placenta.
[6]NIEHS SNPs program
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-76; HIS-214; ARG-324; TRP-436 AND SER-536.
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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].
[9]"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] (ISOFORM 2).
Tissue: Kidney.
[10]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-9; 365-377; 565-590; 635-649 AND 664-674, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Transglutaminase 2 undergoes a large conformational change upon activation."
Pinkas D.M., Strop P., Brunger A.T., Khosla C.
PLoS Biol. 5:E327-E327(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[14]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-660.
[15]"Missense mutations in the TGM2 gene encoding transglutaminase 2 are found in patients with early-onset type 2 diabetes."
Porzio O., Massa O., Cunsolo V., Colombo C., Malaponti M., Bertuzzi F., Hansen T., Johansen A., Pedersen O., Meschi F., Terrinoni A., Melino G., Federici M., Decarlo N., Menicagli M., Campani D., Marchetti P., Ferdaoussi M. expand/collapse author list , Froguel P., Federici G., Vaxillaire M., Barbetti F.
Hum. Mutat. 28:1150-1150(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-330 AND ASN-331.
+Additional computationally mapped references.

Web resources

Wikipedia

Tissue transglutaminase entry

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55153 mRNA. Translation: AAA63261.1.
M98478 mRNA. Translation: AAA36739.1.
S81734 mRNA. Translation: AAB36379.1.
AY675221 mRNA. Translation: AAT79353.1.
AK291714 mRNA. Translation: BAF84403.1.
AK314618 mRNA. Translation: BAG37184.1.
DQ523828 Genomic DNA. Translation: ABF47109.1.
AL031651 Genomic DNA. Translation: CAB66115.1.
CH471077 Genomic DNA. Translation: EAW76040.1.
CH471077 Genomic DNA. Translation: EAW76042.1.
CH471077 Genomic DNA. Translation: EAW76044.1.
BC003551 mRNA. Translation: AAH03551.1.
CCDSCCDS13302.1. [P21980-1]
PIRA39045.
A44302.
S68092.
RefSeqNP_004604.2. NM_004613.2. [P21980-1]
NP_945189.1. NM_198951.1. [P21980-2]
UniGeneHs.517033.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FAUmodel-A1-687[»]
1KV3X-ray2.80A/B/C/D/E/F1-687[»]
2Q3ZX-ray2.00A1-687[»]
3LY6X-ray3.14A/B/C1-687[»]
3S3JX-ray2.25A2-687[»]
3S3PX-ray2.50A2-687[»]
3S3SX-ray2.30A2-687[»]
ProteinModelPortalP21980.
SMRP21980. Positions 4-687.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112910. 64 interactions.
DIPDIP-33557N.
IntActP21980. 40 interactions.
MINTMINT-88880.
STRING9606.ENSP00000355330.

Chemistry

BindingDBP21980.
ChEMBLCHEMBL2730.
DrugBankDB00130. L-Glutamine.

PTM databases

PhosphoSiteP21980.

Polymorphism databases

DMDM20141877.

Proteomic databases

MaxQBP21980.
PaxDbP21980.
PeptideAtlasP21980.
PRIDEP21980.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361475; ENSP00000355330; ENSG00000198959. [P21980-1]
GeneID7052.
KEGGhsa:7052.
UCSCuc002xhr.3. human. [P21980-1]
uc002xht.3. human. [P21980-2]
uc002xhu.3. human. [P21980-3]

Organism-specific databases

CTD7052.
GeneCardsGC20M036756.
HGNCHGNC:11778. TGM2.
HPACAB002598.
HPA021019.
HPA029518.
MIM190196. gene.
neXtProtNX_P21980.
PharmGKBPA36491.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG80379.
HOGENOMHOG000231695.
HOVERGENHBG004342.
InParanoidP21980.
KOK05625.
OMAANGRDHH.
OrthoDBEOG7WT40M.
PhylomeDBP21980.
TreeFamTF324278.

Enzyme and pathway databases

SignaLinkP21980.

Gene expression databases

ArrayExpressP21980.
BgeeP21980.
CleanExHS_TGM2.
GenevestigatorP21980.

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

ChiTaRSTGM2. human.
EvolutionaryTraceP21980.
GeneWikiTissue_transglutaminase.
GenomeRNAi7052.
NextBio27573.
PMAP-CutDBP21980.
PROP21980.
SOURCESearch...

Entry information

Entry nameTGM2_HUMAN
AccessionPrimary (citable) accession number: P21980
Secondary accession number(s): E1P5V9 expand/collapse secondary AC list , Q16436, Q6B838, Q9BTN7, Q9UH35
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 164 of the entry and version 2 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 20

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