TGM2_HUMAN - dbPTM
TGM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TGM2_HUMAN
UniProt AC P21980
Protein Name Protein-glutamine gamma-glutamyltransferase 2
Gene Name TGM2
Organism Homo sapiens (Human).
Sequence Length 687
Subcellular Localization
Protein Description Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins..
Protein Sequence MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNYEASVDSLTFSVVTGPAPSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLEASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEERQEYVLTQQGFIYQGSAKFIKNIPWNFGQFEDGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGRWDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPTPQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNADVVDWIQQDDGSVHKSINRSLIVGLKISTKSVGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVGQSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLNLEPFSEKSVPLCILYEKYRDCLTESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQKRKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPDPVEAGEEVKVRMDLLPLHMGLHKLVVNFESDKLKAVKGFRNVIIGPA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAEELVLER
------CCHHHHHHH		20.9722814378
10S-nitrosocysteineEELVLERCDLELETN
HHHHHHHCCEEEECC		5.24-
10S-nitrosylationEELVLERCDLELETN
HHHHHHHCCEEEECC		5.2422178444
27S-nitrosocysteineDHHTADLCREKLVVR
CCCHHHHHHCEEEEE		5.63-
27S-nitrosylationDHHTADLCREKLVVR
CCCHHHHHHCEEEEE		5.6322178444
53PhosphorylationEGRNYEASVDSLTFS
CCCCEEEEEEEEEEE		17.9524275569
56PhosphorylationNYEASVDSLTFSVVT
CEEEEEEEEEEEEEE		27.4424275569
60PhosphorylationSVDSLTFSVVTGPAP
EEEEEEEEEEECCCC		15.5024275569
98S-nitrosocysteineTVVDQQDCTLSLQLT
EEECCCCCEEEEEEE		3.42-
98S-nitrosylationTVVDQQDCTLSLQLT
EEECCCCCEEEEEEE		3.4222178444
143S-nitrosylationILLFNAWCPADAVYL
HHHHEECCCCCEEEE		1.5322178444
143S-nitrosocysteineILLFNAWCPADAVYL
HHHHEECCCCCEEEE		1.53-
159PhosphorylationSEEERQEYVLTQQGF
CHHHHHHHEEEECCE		7.75-
202AcetylationILLDVNPKFLKNAGR
HHHCCCHHHHHHCCC		59.1130592923
205AcetylationDVNPKFLKNAGRDCS
CCCHHHHHHCCCCCC		48.1322424773
205MalonylationDVNPKFLKNAGRDCS
CCCHHHHHHCCCCCC		48.1326320211
212PhosphorylationKNAGRDCSRRSSPVY
HHCCCCCCCCCCCEE		34.7122142843
215PhosphorylationGRDCSRRSSPVYVGR
CCCCCCCCCCEEECE		37.5723403867
216PhosphorylationRDCSRRSSPVYVGRV
CCCCCCCCCEEECEE		19.3028355574
219PhosphorylationSRRSSPVYVGRVVSG
CCCCCCEEECEEEEC		10.6923403867
230S-nitrosylationVVSGMVNCNDDQGVL
EEECCEECCCCCCEE		3.9322178444
230S-nitrosocysteineVVSGMVNCNDDQGVL
EEECCEECCCCCCEE		3.93-
245PhosphorylationLGRWDNNYGDGVSPM
EEEECCCCCCCCCCC		23.89-
250PhosphorylationNNYGDGVSPMSWIGS
CCCCCCCCCCHHHCH		22.03-
2652-HydroxyisobutyrylationVDILRRWKNHGCQRV
HHHHHHHHHCCCCEE		36.94-
269S-nitrosylationRRWKNHGCQRVKYGQ
HHHHHCCCCEEEECH		1.4922178444
269S-nitrosocysteineRRWKNHGCQRVKYGQ
HHHHHCCCCEEEECH		1.49-
277S-nitrosocysteineQRVKYGQCWVFAAVA
CEEEECHHHHHHHHH		2.65-
277S-nitrosylationQRVKYGQCWVFAAVA
CEEEECHHHHHHHHH		2.6522178444
285S-nitrosylationWVFAAVACTVLRCLG
HHHHHHHHHHHHHHC		1.8622178444
285S-nitrosocysteineWVFAAVACTVLRCLG
HHHHHHHHHHHHHHC		1.86-
315PhosphorylationNSNLLIEYFRNEFGE
CCCHHHHHHHHHCCC		10.80-
336S-nitrosylationEMIWNFHCWVESWMT
HEEEEEEEEEEHHCC		3.6822178444
336S-nitrosocysteineEMIWNFHCWVESWMT
HEEEEEEEEEEHHCC		3.68-
365PhosphorylationDPTPQEKSEGTYCCG
CCCCCCCCCCEEECC		40.2726356563
368PhosphorylationPQEKSEGTYCCGPVP
CCCCCCCEEECCCEE		14.8828152594
369PhosphorylationQEKSEGTYCCGPVPV
CCCCCCEEECCCEEE		9.1521082442
370S-nitrosocysteineEKSEGTYCCGPVPVR
CCCCCEEECCCEEEC		1.86-
370S-nitrosylationEKSEGTYCCGPVPVR
CCCCCEEECCCEEEC		1.8622178444
371S-nitrosocysteineKSEGTYCCGPVPVRA
CCCCEEECCCEEECE		4.93-
371S-nitrosylationKSEGTYCCGPVPVRA
CCCCEEECCCEEECE		4.9322178444
385PhosphorylationAIKEGDLSTKYDAPF
EEEECCCCCCCCCCE		27.8224275569
415PhosphorylationDDGSVHKSINRSLIV
CCCCEECEECHHHEE		15.3723403867
419PhosphorylationVHKSINRSLIVGLKI
EECEECHHHEEEEEE		20.2623403867
427PhosphorylationLIVGLKISTKSVGRD
HEEEEEEEECCCCCC		28.3518187866
4292-HydroxyisobutyrylationVGLKISTKSVGRDER
EEEEEEECCCCCCCC		36.03-
449PhosphorylationTYKYPEGSSEEREAF
EEECCCCCHHHHHHH		32.6828857561
450PhosphorylationYKYPEGSSEEREAFT
EECCCCCHHHHHHHH		55.0928857561
464UbiquitinationTRANHLNKLAEKEET
HHHHHHHHHHHHHHH		56.27-
468AcetylationHLNKLAEKEETGMAM
HHHHHHHHHHHCCEE		56.07-
4682-HydroxyisobutyrylationHLNKLAEKEETGMAM
HHHHHHHHHHHCCEE		56.07-
483SulfoxidationRIRVGQSMNMGSDFD
EEECCCCCCCCCCCE		2.8430846556
485SulfoxidationRVGQSMNMGSDFDVF
ECCCCCCCCCCCEEE		3.9930846556
524S-nitrosylationNGILGPECGTKYLLN
CCEECCCCCCEEEEE		10.6422178444
524S-nitrosocysteineNGILGPECGTKYLLN
CCEECCCCCCEEEEE		10.64-
538PhosphorylationNLNLEPFSEKSVPLC
ECCCCCCCCCCCCEE		55.6321712546
541PhosphorylationLEPFSEKSVPLCILY
CCCCCCCCCCEEEHH		25.5621712546
545S-nitrosylationSEKSVPLCILYEKYR
CCCCCCEEEHHHHHH		1.3222178444
545S-nitrosocysteineSEKSVPLCILYEKYR
CCCCCCEEEHHHHHH		1.32-
554S-palmitoylationLYEKYRDCLTESNLI
HHHHHHHHCCCCCCC		3.6126865113
554S-nitrosylationLYEKYRDCLTESNLI
HHHHHHHHCCCCCCC		3.612212679
5622-HydroxyisobutyrylationLTESNLIKVRALLVE
CCCCCCCCHHHHHHH		28.91-
575PhosphorylationVEPVINSYLLAERDL
HHHHHHHHHHHHCCC		10.97-
583PhosphorylationLLAERDLYLENPEIK
HHHHCCCCCCCCCCE		19.09-
5902-HydroxyisobutyrylationYLENPEIKIRILGEP
CCCCCCCEEEECCCH		25.03-
590AcetylationYLENPEIKIRILGEP
CCCCCCCEEEECCCH		25.0323236377
590UbiquitinationYLENPEIKIRILGEP
CCCCCCCEEEECCCH		25.03-
5982-HydroxyisobutyrylationIRILGEPKQKRKLVA
EEECCCHHHHCEEEE		65.24-
608PhosphorylationRKLVAEVSLQNPLPV
CEEEEEEECCCCCCC		18.7524275569
620S-nitrosocysteineLPVALEGCTFTVEGA
CCCEEECCEEEEECC		1.75-
620S-nitrosylationLPVALEGCTFTVEGA
CCCEEECCEEEEECC		1.7522178444
6492-HydroxyisobutyrylationVEAGEEVKVRMDLLP
CCCCCCEEEEEEEEE		27.66-
649AcetylationVEAGEEVKVRMDLLP
CCCCCCEEEEEEEEE		27.6623236377
649UbiquitinationVEAGEEVKVRMDLLP
CCCCCCEEEEEEEEE		27.66-
6722-HydroxyisobutyrylationVVNFESDKLKAVKGF
EEECCCHHHHHCCCC		62.25-
672AcetylationVVNFESDKLKAVKGF
EEECCCHHHHHCCCC		62.2525825284
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
215SPhosphorylationKinasePRKACAP17612
GPS
216SPhosphorylationKinasePRKACAP17612
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TGM2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TGM2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB_HUMANRB1physical
9315663
FINC_HUMANFN1physical
11829448
TGM2_HUMANTGM2physical
11867708
PLCD1_HUMANPLCD1physical
9512491
H31T_HUMANHIST3H3physical
20665636
PIAS4_HUMANPIAS4physical
19625650
PAK1_HUMANPAK1physical
21900206
SQSTM_HUMANSQSTM1physical
22322858
A4_HUMANAPPphysical
21832049
VHL_HUMANVHLphysical
21625219
TGM2_HUMANTGM2physical
21988832
T176A_HUMANTMEM176Aphysical
21988832
G6PD_HUMANG6PDphysical
22863883
LDHB_HUMANLDHBphysical
22863883
6PGD_HUMANPGDphysical
22863883
KS6A3_HUMANRPS6KA3physical
22863883
TXND5_HUMANTXNDC5physical
22863883
UBFD1_HUMANUBFD1physical
22863883
1433G_HUMANYWHAGphysical
22863883
1433T_HUMANYWHAQphysical
22863883
1433Z_HUMANYWHAZphysical
22863883
ANCHR_HUMANZFYVE19physical
22863883
PINK1_HUMANPINK1physical
25557247
CD11B_HUMANCDK11Bphysical
26496610
CO5A1_HUMANCOL5A1physical
26496610
CO5A2_HUMANCOL5A2physical
26496610
MRCKA_HUMANCDC42BPAphysical
26496610
PLOD3_HUMANPLOD3physical
26496610
SRGP3_HUMANSRGAP3physical
26496610
MVP_HUMANMVPphysical
26496610
SF3B4_HUMANSF3B4physical
26496610
ENOPH_HUMANENOPH1physical
26496610
RBM25_HUMANRBM25physical
26496610
GT251_HUMANCOLGALT1physical
26496610
T126A_HUMANTMEM126Aphysical
26496610
RPA43_HUMANTWISTNBphysical
26496610
P53_HUMANTP53physical
27031960
SQSTM_HUMANSQSTM1physical
27031960
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00130L-Glutamine
Regulatory Network of TGM2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-219 AND TYR-369, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-369, AND MASSSPECTROMETRY.

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