Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P21980

- TGM2_HUMAN

UniProt

P21980 - TGM2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein-glutamine gamma-glutamyltransferase 2

Gene

TGM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.

Catalytic activityi

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

Cofactori

Binds 1 calcium ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei277 – 2771PROSITE-ProRule annotation
Active sitei335 – 3351PROSITE-ProRule annotation
Active sitei358 – 3581PROSITE-ProRule annotation
Metal bindingi398 – 3981CalciumBy similarity
Metal bindingi400 – 4001CalciumBy similarity
Metal bindingi447 – 4471CalciumBy similarity
Metal bindingi452 – 4521CalciumBy similarity

GO - Molecular functioni

  1. GTP binding Source: Ensembl
  2. metal ion binding Source: UniProtKB-KW
  3. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB

GO - Biological processi

  1. apoptotic cell clearance Source: UniProtKB
  2. blood vessel remodeling Source: Ensembl
  3. branching involved in salivary gland morphogenesis Source: Ensembl
  4. isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine Source: Ensembl
  5. negative regulation of endoplasmic reticulum calcium ion concentration Source: UniProt
  6. positive regulation of apoptotic process Source: UniProt
  7. positive regulation of cell adhesion Source: UniProtKB
  8. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: Ensembl
  9. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  10. positive regulation of inflammatory response Source: Ensembl
  11. positive regulation of mitochondrial calcium ion concentration Source: UniProt
  12. positive regulation of smooth muscle cell proliferation Source: Ensembl
  13. protein homooligomerization Source: Ensembl
  14. salivary gland cavitation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

SignaLinkiP21980.

Names & Taxonomyi

Protein namesi
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 namesi
Name:TGM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:11778. TGM2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProt
  2. extracellular vesicular exosome Source: UniProtKB
  3. focal adhesion Source: UniProtKB
  4. mitochondrion Source: UniProt
  5. plasma membrane Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36491.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 687686Protein-glutamine gamma-glutamyltransferase 2PRO_0000213707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei468 – 4681N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP21980.
PaxDbiP21980.
PeptideAtlasiP21980.
PRIDEiP21980.

PTM databases

PhosphoSiteiP21980.

Miscellaneous databases

PMAP-CutDBP21980.

Expressioni

Inductioni

By retinoic acid.

Gene expression databases

BgeeiP21980.
CleanExiHS_TGM2.
ExpressionAtlasiP21980. baseline and differential.
GenevestigatoriP21980.

Organism-specific databases

HPAiCAB002598.
HPA021019.
HPA029518.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
AKAP13Q128024EBI-727668,EBI-1373806
COL18A1P390602EBI-727668,EBI-2566375
FN1P027513EBI-727668,EBI-1220319
RELAQ042063EBI-727668,EBI-73886
VHLP4033710EBI-727668,EBI-301246

Protein-protein interaction databases

BioGridi112910. 65 interactions.
DIPiDIP-33557N.
IntActiP21980. 40 interactions.
MINTiMINT-88880.
STRINGi9606.ENSP00000355330.

Structurei

Secondary structure

1
687
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115
Helixi14 – 207
Helixi24 – 263
Beta strandi28 – 303
Beta strandi32 – 343
Beta strandi39 – 4810
Turni52 – 543
Beta strandi55 – 6612
Turni69 – 724
Beta strandi73 – 797
Beta strandi89 – 957
Beta strandi97 – 1059
Beta strandi113 – 12311
Beta strandi126 – 13813
Helixi153 – 1597
Beta strandi164 – 1707
Beta strandi172 – 18110
Helixi189 – 19810
Helixi201 – 2055
Helixi207 – 2137
Helixi217 – 22610
Turni227 – 2293
Turni231 – 2344
Beta strandi235 – 2395
Turni251 – 2533
Helixi258 – 2669
Turni267 – 2693
Beta strandi272 – 2754
Helixi277 – 29115
Beta strandi295 – 30410
Beta strandi306 – 3094
Helixi311 – 3177
Beta strandi332 – 34211
Beta strandi347 – 3504
Beta strandi353 – 3575
Beta strandi365 – 3695
Helixi376 – 3805
Turni387 – 3893
Helixi390 – 3978
Beta strandi400 – 4045
Beta strandi412 – 4143
Beta strandi419 – 42911
Beta strandi433 – 4386
Helixi440 – 4434
Beta strandi447 – 4493
Helixi450 – 46011
Turni468 – 4714
Beta strandi473 – 4786
Beta strandi489 – 4979
Beta strandi499 – 5013
Beta strandi503 – 51412
Beta strandi520 – 53415
Beta strandi538 – 5469
Helixi548 – 5514
Turni552 – 5543
Beta strandi560 – 56910
Turni570 – 5734
Beta strandi574 – 58310
Beta strandi590 – 5956
Beta strandi598 – 6014
Beta strandi603 – 6108
Beta strandi613 – 6153
Beta strandi619 – 6257
Turni627 – 6293
Beta strandi634 – 6385
Beta strandi647 – 6548
Beta strandi658 – 6603
Beta strandi662 – 6698
Beta strandi671 – 6733
Beta strandi676 – 6827

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP21980.
SMRiP21980. Positions 4-687.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21980.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG80379.
HOGENOMiHOG000231695.
HOVERGENiHBG004342.
InParanoidiP21980.
KOiK05625.
OMAiANGRDHH.
OrthoDBiEOG7WT40M.
PhylomeDBiP21980.
TreeFamiTF324278.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProiIPR023608. 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]
PANTHERiPTHR11590. PTHR11590. 1 hit.
PfamiPF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
SMARTiSM00460. TGc. 1 hit.
[Graphical view]
SUPFAMiSSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P21980) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAEELVLERC DLELETNGRD HHTADLCREK LVVRRGQPFW LTLHFEGRNY
60 70 80 90 100
EASVDSLTFS VVTGPAPSQE AGTKARFPLR DAVEEGDWTA TVVDQQDCTL
110 120 130 140 150
SLQLTTPANA PIGLYRLSLE ASTGYQGSSF VLGHFILLFN AWCPADAVYL
160 170 180 190 200
DSEEERQEYV LTQQGFIYQG SAKFIKNIPW NFGQFEDGIL DICLILLDVN
210 220 230 240 250
PKFLKNAGRD CSRRSSPVYV GRVVSGMVNC NDDQGVLLGR WDNNYGDGVS
260 270 280 290 300
PMSWIGSVDI LRRWKNHGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN
310 320 330 340 350
YNSAHDQNSN LLIEYFRNEF GEIQGDKSEM IWNFHCWVES WMTRPDLQPG
360 370 380 390 400
YEGWQALDPT PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA PFVFAEVNAD
410 420 430 440 450
VVDWIQQDDG SVHKSINRSL IVGLKISTKS VGRDEREDIT HTYKYPEGSS
460 470 480 490 500
EEREAFTRAN HLNKLAEKEE TGMAMRIRVG QSMNMGSDFD VFAHITNNTA
510 520 530 540 550
EEYVCRLLLC ARTVSYNGIL GPECGTKYLL NLNLEPFSEK SVPLCILYEK
560 570 580 590 600
YRDCLTESNL IKVRALLVEP VINSYLLAER DLYLENPEIK IRILGEPKQK
610 620 630 640 650
RKLVAEVSLQ NPLPVALEGC TFTVEGAGLT EEQKTVEIPD PVEAGEEVKV
660 670 680
RMDLLPLHMG LHKLVVNFES DKLKAVKGFR NVIIGPA
Length:687
Mass (Da):77,329
Last modified:January 23, 2002 - v2
Checksum:i7DA33FF335DE7B37
GO
Isoform 2 (identifier: P21980-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     539-548: EKSVPLCILY → GKALCSWSIC
     549-687: Missing.

Show »
Length:548
Mass (Da):61,678
Checksum:i8C2F43A4D1029AC2
GO
Isoform 3 (identifier: P21980-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:349
Mass (Da):38,671
Checksum:i37E1EE27C243CCC5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511E → Q in AAA63261. (PubMed:1670766)Curated
Sequence conflicti186 – 1861E → Q in AAA63261. (PubMed:1670766)Curated
Sequence conflicti224 – 2241V → G in AAA63261. (PubMed:1670766)Curated
Sequence conflicti533 – 5331N → T in AAA63261. (PubMed:1670766)Curated
Sequence conflicti655 – 6551L → V in AAA63261. (PubMed:1670766)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761R → H.1 Publication
Corresponds to variant rs41274720 [ dbSNP | Ensembl ].
VAR_052553
Natural varianti214 – 2141R → H.1 Publication
Corresponds to variant rs45530133 [ dbSNP | Ensembl ].
VAR_055357
Natural varianti324 – 3241Q → R.1 Publication
Corresponds to variant rs45567334 [ dbSNP | Ensembl ].
VAR_055358
Natural varianti330 – 3301M → R in patients with early-onset diabetes type 2; pathological significance unknown. 1 Publication
VAR_037998
Natural varianti331 – 3311I → N in patients with early-onset diabetes type 2; pathological significance unknown. 1 Publication
VAR_037999
Natural varianti436 – 4361R → W.1 Publication
Corresponds to variant rs45629036 [ dbSNP | Ensembl ].
VAR_055359
Natural varianti536 – 5361P → S.1 Publication
Corresponds to variant rs45556333 [ dbSNP | Ensembl ].
VAR_052554
Natural varianti660 – 6601G → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036554

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei287 – 34963VLRCL…PDLQP → GELHAGMWVMSPGRGHEEHW SRNQDIPALVLPPATNTLNA LCGLEPVTTLSGPLSNSHPS SGC in isoform 3. 1 PublicationVSP_006413Add
BLAST
Alternative sequencei350 – 687338Missing in isoform 3. 1 PublicationVSP_006414Add
BLAST
Alternative sequencei539 – 54810EKSVPLCILY → GKALCSWSIC in isoform 2. 2 PublicationsVSP_006411
Alternative sequencei549 – 687139Missing in isoform 2. 2 PublicationsVSP_006412Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS13302.1. [P21980-1]
PIRiA39045.
A44302.
S68092.
RefSeqiNP_004604.2. NM_004613.2. [P21980-1]
NP_945189.1. NM_198951.1. [P21980-2]
UniGeneiHs.517033.

Genome annotation databases

EnsembliENST00000361475; ENSP00000355330; ENSG00000198959. [P21980-1]
GeneIDi7052.
KEGGihsa:7052.
UCSCiuc002xhr.3. human. [P21980-1]
uc002xht.3. human. [P21980-2]
uc002xhu.3. human. [P21980-3]

Polymorphism databases

DMDMi20141877.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Tissue transglutaminase entry

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS13302.1. [P21980-1 ]
PIRi A39045.
A44302.
S68092.
RefSeqi NP_004604.2. NM_004613.2. [P21980-1 ]
NP_945189.1. NM_198951.1. [P21980-2 ]
UniGenei Hs.517033.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P21980.
SMRi P21980. Positions 4-687.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112910. 65 interactions.
DIPi DIP-33557N.
IntActi P21980. 40 interactions.
MINTi MINT-88880.
STRINGi 9606.ENSP00000355330.

Chemistry

BindingDBi P21980.
ChEMBLi CHEMBL2730.
DrugBanki DB00130. L-Glutamine.

PTM databases

PhosphoSitei P21980.

Polymorphism databases

DMDMi 20141877.

Proteomic databases

MaxQBi P21980.
PaxDbi P21980.
PeptideAtlasi P21980.
PRIDEi P21980.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361475 ; ENSP00000355330 ; ENSG00000198959 . [P21980-1 ]
GeneIDi 7052.
KEGGi hsa:7052.
UCSCi uc002xhr.3. human. [P21980-1 ]
uc002xht.3. human. [P21980-2 ]
uc002xhu.3. human. [P21980-3 ]

Organism-specific databases

CTDi 7052.
GeneCardsi GC20M036756.
HGNCi HGNC:11778. TGM2.
HPAi CAB002598.
HPA021019.
HPA029518.
MIMi 190196. gene.
neXtProti NX_P21980.
PharmGKBi PA36491.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG80379.
HOGENOMi HOG000231695.
HOVERGENi HBG004342.
InParanoidi P21980.
KOi K05625.
OMAi ANGRDHH.
OrthoDBi EOG7WT40M.
PhylomeDBi P21980.
TreeFami TF324278.

Enzyme and pathway databases

SignaLinki P21980.

Miscellaneous databases

ChiTaRSi TGM2. human.
EvolutionaryTracei P21980.
GeneWikii Tissue_transglutaminase.
GenomeRNAii 7052.
NextBioi 27573.
PMAP-CutDB P21980.
PROi P21980.
SOURCEi Search...

Gene expression databases

Bgeei P21980.
CleanExi HS_TGM2.
ExpressionAtlasi P21980. baseline and differential.
Genevestigatori P21980.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
3.90.260.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR11590. PTHR11590. 1 hit.
Pfami PF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000459. TGM_EBP42. 1 hit.
SMARTi SM00460. TGc. 1 hit.
[Graphical view ]
SUPFAMi SSF49309. SSF49309. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEi PS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-660.
  15. Cited for: VARIANTS ARG-330 AND ASN-331.

Entry informationi

Entry nameiTGM2_HUMAN
AccessioniPrimary (citable) accession number: P21980
Secondary accession number(s): E1P5V9
, Q16436, Q6B838, Q9BTN7, Q9UH35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2002
Last modified: October 29, 2014
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3