P21980 (TGM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	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.
Sequence similarities	Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic cell clearance Inferred from direct assay PubMed 19628791. Source: UniProtKB blood vessel remodeling Inferred from electronic annotation. Source: Compara branching involved in salivary gland morphogenesis Inferred from electronic annotation. Source: Compara elevation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Inferred from electronic annotation. Source: Compara induction of apoptosis Inferred from electronic annotation. Source: Compara isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from electronic annotation. Source: Compara positive regulation of cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of inflammatory response Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from electronic annotation. Source: Compara salivary gland cavitation Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	GTP binding Inferred from electronic annotation. Source: Compara metal 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	4	EBI-727668,EBI-1373806
COL18A1	P39060	2	EBI-727668,EBI-2566375
RELA	Q04206	3	EBI-727668,EBI-73886
VHL	P40337	10	EBI-727668,EBI-301246

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.10

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.10

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. Ref.6
Corresponds to variant rs41274720 [ dbSNP | Ensembl ].

VAR_052553

Natural variant

214

1

R → H. Ref.6
Corresponds to variant rs45530133 [ dbSNP | Ensembl ].

VAR_055357

Natural variant

324

1

Q → R. Ref.6
Corresponds to variant rs45567334 [ dbSNP | Ensembl ].

VAR_055358

Natural variant

330

1

M → R in patients with early-onset diabetes type 2; pathological significance unknown. Ref.14

VAR_037998

Natural variant

331

1

I → N in patients with early-onset diabetes type 2; pathological significance unknown. Ref.14

VAR_037999

Natural variant

436

1

R → W. Ref.6
Corresponds to variant rs45629036 [ dbSNP | Ensembl ].

VAR_055359

Natural variant

536

1

P → S. Ref.6
Corresponds to variant rs45556333 [ dbSNP | Ensembl ].

VAR_052554

Natural variant

660

1

G → V in a colorectal cancer sample; somatic mutation. Ref.13

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

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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

Beta strand

306 – 309

4

Helix

311 – 317

7

Beta strand

332 – 342

11

Beta strand

347 – 350

4

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

412 – 414

3

Beta strand

419 – 429

11

Beta strand

433 – 438

6

Helix

440 – 443

4

Beta strand

447 – 449

3

Helix

450 – 460

11

Turn

468 – 471

4

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 [UniParc]. 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) [UniParc]. 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] [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. , 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. , 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. , 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, 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]	"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).
[13]	"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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-660.
[14]	"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] [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.

IPI

IPI00218251.
IPI00218252.
IPI00294578.

PIR

A39045.
A44302.
S68092.

RefSeq

NP_004604.2. NM_004613.2.
NP_945189.1. NM_198951.1.

UniGene

Hs.517033.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3LY6	X-ray	3.14	A/B/C	1-687	[»]
3S3J	X-ray	2.25	A	2-687	[»]
3S3P	X-ray	2.50	A	2-687	[»]
3S3S	X-ray	2.30	A	2-687	[»]

ProteinModelPortal

P21980.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33557N.

IntAct

P21980. 32 interactions.

MINT

MINT-88880.

STRING

9606.ENSP00000355330.

PTM databases

PhosphoSite

P21980.

Polymorphism databases

DMDM

20141877.

Proteomic databases

PaxDb

P21980.

PeptideAtlas

P21980.

PRIDE

P21980.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361475; ENSP00000355330; ENSG00000198959.

GeneID

7052.

KEGG

hsa:7052.

UCSC

uc002xhr.3. human.
uc002xht.3. human.
uc002xhu.3. human.

Organism-specific databases

CTD

7052.

GeneCards

GC20M036756.

HGNC

HGNC:11778. TGM2.

HPA

CAB002598.
HPA021019.
HPA029518.

MIM

190196. gene.

neXtProt

NX_P21980.

PharmGKB

PA36491.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG80379.

HOGENOM

HOG000231695.

HOVERGEN

HBG004342.

InParanoid

P21980.

KO

K05625.

OMA

ANGRDHH.

OrthoDB

EOG4HMJ8W.

PhylomeDB

P21980.

Enzyme and pathway databases

Pathway_Interaction_DB

txa2pathway. Thromboxane A2 receptor signaling.

Gene expression databases

ArrayExpress

P21980.

Bgee

P21980.

CleanEx

HS_TGM2.

Genevestigator

P21980.

GermOnline

ENSG00000198959. 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

P21980.

ChEMBL

CHEMBL2730.

ChiTaRS

TGM2. human.

DrugBank

DB00130. L-Glutamine.

EvolutionaryTrace

P21980.

GenomeRNAi

7052.

NextBio

27573.

PMAP-CutDB

P21980.

SOURCE

Search...

Entry information

Entry name

TGM2_HUMAN

Accession

Primary (citable) accession number: P21980
Secondary accession number(s): E1P5V9 , Q16436, Q6B838, Q9BTN7, Q9UH35

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2002
Last modified:	May 1, 2013
This is version 151 of the entry and version 2 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.