Reviewed, UniProtKB/Swiss-Prot P21980 (TGM2_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein-glutamine gamma-glutamyltransferase 2
    EC=2.3.2.13
Alternative name(s):
    Tissue transglutaminase
    TGase C
      Short name=TGC
      Short name=TG(C)
    Transglutaminase-2
    TGase-H

Gene names

Name:

TGM2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	687 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Involvement in disease	Defects in TGM2 are involved in early-onset diabetes type 2.
Sequence similarities	Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Diabetes mellitus Disease mutation
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	positive regulation of cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein-glutamine gamma-glutamyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AKAP13	Q12802	3	EBI-727668,EBI-1373806
RELA	Q04206	2	EBI-727668,EBI-73886

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 687

686

Protein-glutamine gamma-glutamyltransferase 2

PRO_0000213707

Sites

Active site

277

1

By similarity

Active site

335

1

By similarity

Active site

358

1

By similarity

Metal binding

398

1

Calcium By similarity

Metal binding

400

1

Calcium By similarity

Metal binding

447

1

Calcium By similarity

Metal binding

452

1

Calcium By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

219

1

Phosphotyrosine Ref.12

Modified residue

369

1

Phosphotyrosine Ref.12 Ref.11

Modified residue

427

1

Phosphoserine Ref.13

Natural variations

Alternative sequence

287 – 349

63

VLRCL…PDLQP → GELHAGMWVMSPGRGHEEHW SRNQDIPALVLPPATNTLNA LCGLEPVTTLSGPLSNSHPS SGC in isoform 3.

VSP_006413

Alternative sequence

350 – 687

338

Missing in isoform 3.

VSP_006414

Alternative sequence

539 – 548

10

EKSVPLCILY → GKALCSWSIC in isoform 2.

VSP_006411

Alternative sequence

549 – 687

139

Missing in isoform 2.

VSP_006412

Natural variant

76

1

R → H: dbSNP rs41274720.

VAR_052553

Natural variant

214

1

R → H: dbSNP rs45530133.

VAR_055357

Natural variant

324

1

Q → R: dbSNP rs45567334.

VAR_055358

Natural variant

330

1

M → R in early-onset diabetes type 2. Ref.17

VAR_037998

Natural variant

331

1

I → N in early-onset diabetes type 2. Ref.17

VAR_037999

Natural variant

436

1

R → W: dbSNP rs45629036.

VAR_055359

Natural variant

536

1

P → S: dbSNP rs45556333.

VAR_052554

Natural variant

660

1

G → V in a colorectal cancer sample; somatic mutation. Ref.16

VAR_036554

Experimental info

Sequence conflict

51

1

E → Q in AAA63261. Ref.1

Sequence conflict

186

1

E → Q in AAA63261. Ref.1

Sequence conflict

224

1

V → G in AAA63261. Ref.1

Sequence conflict

533

1

N → T in AAA63261. Ref.1

Sequence conflict

655

1

L → V in AAA63261. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

687

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Helix

14 – 20

7

Helix

24 – 26

3

Beta strand

28 – 30

3

Beta strand

32 – 34

3

Beta strand

39 – 48

10

Turn

52 – 54

3

Beta strand

55 – 66

12

Turn

69 – 72

4

Beta strand

73 – 79

7

Beta strand

89 – 95

7

Beta strand

97 – 105

9

Beta strand

113 – 123

11

Beta strand

126 – 138

13

Helix

153 – 159

7

Beta strand

164 – 170

7

Beta strand

172 – 181

10

Helix

189 – 198

10

Helix

201 – 205

5

Helix

207 – 213

7

Helix

217 – 226

10

Turn

227 – 229

3

Turn

231 – 234

4

Beta strand

235 – 239

5

Turn

251 – 253

3

Helix

258 – 266

9

Turn

267 – 269

3

Beta strand

272 – 275

4

Helix

277 – 291

15

Beta strand

295 – 304

10

Helix

311 – 317

7

Beta strand

332 – 342

11

Beta strand

353 – 357

5

Beta strand

365 – 369

5

Helix

376 – 380

5

Turn

387 – 389

3

Helix

390 – 397

8

Beta strand

400 – 404

5

Beta strand

419 – 429

11

Beta strand

433 – 438

6

Helix

440 – 443

4

Helix

450 – 460

11

Beta strand

473 – 478

6

Beta strand

489 – 497

9

Beta strand

499 – 501

3

Beta strand

503 – 514

12

Beta strand

520 – 534

15

Beta strand

538 – 546

9

Helix

548 – 551

4

Turn

552 – 554

3

Beta strand

560 – 569

10

Turn

570 – 573

4

Beta strand

574 – 583

10

Beta strand

590 – 595

6

Beta strand

598 – 601

4

Beta strand

603 – 610

8

Beta strand

613 – 615

3

Beta strand

619 – 625

7

Turn

627 – 629

3

Beta strand

634 – 638

5

Beta strand

647 – 654

8

Beta strand

658 – 660

3

Beta strand

662 – 669

8

Beta strand

671 – 673

3

Beta strand

676 – 682

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2002. Version 2. Checksum: 7DA33FF335DE7B37	FASTA	687	77,329
	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
	Isoform 2. Checksum: 8C2F43A4D1029AC2	FASTA	548	61,678
	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 NLNLEPFSGK ALCSWSIC
	Isoform 3 (TGH2). Checksum: 37E1EE27C243CCC5	FASTA	349	38,671
	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 AAVACTGELH AGMWVMSPGR 310 320 330 340 GHEEHWSRNQ DIPALVLPPA TNTLNALCGL EPVTTLSGPL SNSHPSSGC

References

	« Hide 'large scale' referencesShow '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: 1670766] [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: 1358880] [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: 8611626] [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. , 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] (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. , 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].
[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. , 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: 15489334] [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, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[11]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-369, MASS SPECTROMETRY.
[12]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-219 AND TYR-369, MASS SPECTROMETRY.
[13]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, MASS SPECTROMETRY.
[14]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"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: 18092889] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[16]	"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. , 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: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-660.
[17]	"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. , Froguel P., Federici G., Vaxillaire M., Barbetti F. Hum. Mutat. 28:1150-1150(2007) [PubMed: 17939176] [Abstract] Cited for: VARIANTS EARLY-ONSET DIABETES TYPE 2 ARG-330 AND ASN-331.
+	Additional computationally mapped references.

Web resources

Wikipedia

Tissue transglutaminase entry

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
BC003551 mRNA. Translation: AAH03551.1.

IPI

IPI00218251.
IPI00218252.
IPI00294578.

PIR

A39045.
A44302.
S68092.

RefSeq

NP_004604.2.
NP_945189.1.

UniGene

Hs.517033

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FAU	model	-	A	1-687	[»]
1KV3	X-ray	2.80	A/B/C/D/E/F	1-687	[»]
2Q3Z	X-ray	2.00	A	1-687	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P21980. 4 interactions.

PTM databases

PhosphoSite

P21980.

Proteomic databases

PeptideAtlas

P21980.

PRIDE

P21980.

Genome annotation databases

Ensembl

ENSG00000198959. Homo sapiens. [Contig view]

GeneID

7052.

KEGG

hsa:7052.

Organism-specific databases

GeneCards

GC20M036190.

H-InvDB

HIX0015800.

HGNC

HGNC:11778. TGM2.

HPA

CAB002598.

MIM

190196. gene.

PharmGKB

PA36491.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P21980.

HOVERGEN

P21980.

Enzyme and pathway databases

BRENDA

2.3.2.13. 247.

Pathway_Interaction_DB

txa2pathway. Thromboxane A2 receptor signaling.

Gene expression databases

ArrayExpress

P21980.

Bgee

P21980.

CleanEx

HS_TGM2.

GermOnline

ENSG00000198959. Homo sapiens.

Family and domain databases

InterPro

IPR008957. Fibronectin_typ-III-like_fold.
IPR013783. Ig-like_fold.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]

Gene3D

G3DSA:2.60.40.30. FN_III-like. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

Pfam

PF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]

SMART

SM00460. TGc. 1 hit.
[Graphical view]

PROSITE

PS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00130. L-Glutamine.

NextBio

27573.

PMAP-CutDB

P21980.

SOURCE

Search...

Entry information

Entry name

TGM2_HUMAN

Accession

Primary (citable) accession number: P21980
Secondary accession number(s): Q16436 , Q6B838, Q9BTN7, Q9UH35

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2002
Last modified:	June 16, 2009
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)