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Protein Page:
TGM2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
TGM2 an enzyme of the transglutaminase family that catalyzes the crosslinking of proteins and the conjugation of polyamines to proteins. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. . Is the autoantigen in coeliac disease and plays a role in apoptosis, cellular differentiation and matrix stabilisation. Three alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Transferase; EC 2.3.2.13
Chromosomal Location of Human Ortholog: 20q12
Cellular Component: cytosol; focal adhesion; intrinsic to plasma membrane; mitochondrion
Molecular Function: protein binding; protein-glutamine gamma-glutamyltransferase activity
Biological Process: apoptotic cell clearance; elevation of mitochondrial calcium ion concentration; positive regulation of apoptosis; positive regulation of cell adhesion; reduction of endoplasmic reticulum calcium ion concentration
Reference #:  P21980 (UniProtKB)
Alt. Names/Synonyms: C polypeptide; G-ALPHA-h; GNAH; Protein-glutamine gamma-glutamyltransferase 2; protein-glutamine-gamma-glutamyltransferase; TG(C); TG2; TGase C; TGase H; TGase-2; TGase-H; TGC; TGM2; Tissue transglutaminase; transglutaminase 2 (C polypeptide, protein-glutamine-gamma-glutamyltransferase); Transglutaminase C; Transglutaminase H; Transglutaminase-2
Gene Symbols: TGM2
Molecular weight: 77,329 Da
Basal Isoelectric point: 5.11  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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TGM2

Protein Structure Not Found.
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Sites Implicated In
molecular association, regulation: S215‑p, S216‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 4 H44 QPFWLTLHFEGRNYE
0 1 S56‑p NYEASVDsLTFsVVT
0 1 T58 EASVDsLTFsVVTGP
0 1 S60‑p SVDsLTFsVVTGPAP
0 1 S68 VVTGPAPSQEAGTKA
0 1 K74 PSQEAGTKARFPLRD
0 1 Y159‑p SEEERQEyVLTQQGF
0 3 K202‑ac ILLDVNPkFLKNAGR
1 0 S212‑p KNAGRDCsRRssPVy
1 1 S215‑p GRDCsRRssPVyVGR
3 5 S216‑p RDCsRRssPVyVGRV
0 8 Y219‑p sRRssPVyVGRVVSG
0 1 Y245‑p LGRWDNNyGDGVsPM
0 1 S250‑p NNyGDGVsPMSWIGS
0 1 Y315‑p NSNLLIEyFRNEFGE
0 1 G325 NEFGEIQGDKSEMIW
0 8 T368‑p PQEKSEGtyCCGPVP
0 612 Y369‑p QEKSEGtyCCGPVPV
0 1 K380 PVPVRAIKEGDLSTK
0 2 K414 QDDGSVHKSINRsLI
0 1 S419‑p VHKSINRsLIVGLKI
0 3 K425 RsLIVGLKIsTKSVG
0 1 S427‑p LIVGLKIsTKSVGRD
0 1 S449 TYKYPEGSSEEREAF
0 1 R458 EEREAFTRANHLNKL
0 1 S538‑p NLNLEPFsEKsVPLC
0 1 S541‑p LEPFsEKsVPLCILY
0 1 Y575‑p VEPVINSyLLAERDL
0 1 Y583‑p LLAERDLyLENPEIK
0 2 K590 yLENPEIKIRILGEP
0 1 K590 yLENPEIKIRILGEP
0 1 K602 GEPKQKRKLVAEVsL
0 1 S608‑p RKLVAEVsLQNPLPV
0 10 E618 NPLPVALEGCTFTVE
0 2 K649 VEAGEEVKVRMDLLP
0 1 K649 VEAGEEVKVRMDLLP
0 1 K672‑ac VVNFESDkLKAVKGF
  mouse

 
Y44 QRFRLTLYFEGRGYE
S56 GYEASVDSLTFGAVT
T58 EASVDSLTFGAVTGP
G60 SVDSLTFGAVTGPDP
S68 AVTGPDPSEEAGTKA
K74 PSEEAGTKARFSLSD
Y159 SEEERREYVLTQQGF
K202 MLLDMNPKFLKNRSR
S212 KNRSRDCSRRSsPIy
S215 SRDCSRRSsPIyVGR
S216‑p RDCSRRSsPIyVGRV
Y219‑p SRRSsPIyVGRVVSA
Y245 LGRWDNNYGDGISPM
S250 NNYGDGISPMAWIGS
Y315 NSNLLIEYFRNEFGE
S325‑p NEFGELEsNKSEMIW
T368 PQEKSEGTyCCGPVS
Y369‑p QEKSEGTyCCGPVSV
K380 PVSVRAIKEGDLSTK
K414‑ac QEDGSVLkSINRSLV
S419 VLkSINRSLVVGQkI
K425‑ub RSLVVGQkISTKSVG
S427 LVVGQkISTKSVGRD
S449 TYKYPEGSPEEREVF
K458‑ub EEREVFTkANHLNKL
S537 NLTLDPYSENSIPLR
S540 LDPYSENSIPLRILY
Y574 IEPAANSYLLAERDL
Y582 LLAERDLYLENPEIk
K589‑ac YLENPEIkIRVLGEP
K589‑ub YLENPEIkIRVLGEP
K601 GEPKQNRKLVAEVSL
S607 RKLVAEVSLKNPLSD
Y617‑p NPLSDPLyDCIFTVE
K648‑ac VPAGDLVkARVDLFP
K648‑ub VPAGDLVkARVDLFP
K671 VVNFQCDKLKSVKGY
  rat

 
Y44‑p QRFRLTLyFEGRGYE
R56 GYEASVDRLtFGAVT
T58‑p EASVDRLtFGAVTGP
G60 SVDRLtFGAVTGPDP
S68‑p AVTGPDPsEEAGTkA
K74‑ac PsEEAGTkARFSLSD
Y159 SEAERREYVLTQQGF
K202 MLLDVNPKFLKDRSR
S212 KDRSRDCSRRSSPIY
S215 SRDCSRRSSPIYVGR
S216 RDCSRRSSPIYVGRV
Y219 SRRSSPIYVGRVVSG
Y245 LGRWDNNYGDGISPM
S250 NNYGDGISPMAWIGS
Y315 NSNLLIEYFRNEYGE
S325 NEYGELESNKSEMIW
T368 PQEKSEGTyCCGPVS
Y369‑p QEKSEGTyCCGPVSV
K380‑ac PVSVRAIkEGDLSTK
K414‑ac QSDGSVLkSINNSLV
S419 VLkSINNSLVVGQKI
K425 NSLVVGQKISTKSVG
S427 LVVGQKISTKSVGRD
S449‑p TYKYPEGsPEEREVF
R458 EEREVFTRANHLNKL
S537 NLTLDPYSENSIPLR
S540 LDPYSENSIPLRILY
Y574 VEPAANSYLLAERDL
Y582 LLAERDLYLENPEIk
K589‑ac YLENPEIkIRILGEP
K589 YLENPEIKIRILGEP
K601‑ac GEPKQNRkLVAEVSL
S607 RkLVAEVSLKNPLSD
Y617 NPLSDSLYDCVFTVE
K648‑ac VPAGDAVkVRVDLFP
K648 VPAGDAVKVRVDLFP
K671 VVNFQCDKLKSVKGY
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