TGM3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TGM3_HUMAN
• UniProt AC: Q08188
• Protein Name: Protein-glutamine gamma-glutamyltransferase E
• Gene Name: TGM3
• Organism: Homo sapiens (Human).
• Sequence Length: 693
• Subcellular Localization: Cytoplasm .
• Protein Description: Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold (By similarity). In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath..
• Protein Sequence: MAALGVQSINWQTAFNRQAHHTDKFSSQELILRRGQNFQVLMIMNKGLGSNERLEFIVSTGPYPSESAMTKAVFPLSNGSSGGWSAVLQASNGNTLTISISSPASAPIGRYTMALQIFSQGGISSVKLGTFILLFNPWLNVDSVFMGNHAEREEYVQEDAGIIFVGSTNRIGMIGWNFGQFEEDILSICLSILDRSLNFRRDAATDVASRNDPKYVGRVLSAMINSNDDNGVLAGNWSGTYTGGRDPRSWNGSVEILKNWKKSGFSPVRYGQCWVFAGTLNTALRSLGIPSRVITNFNSAHDTDRNLSVDVYYDPMGNPLDKGSDSVWNFHVWNEGWFVRSDLGPSYGGWQVLDATPQERSQGVFQCGPASVIGVREGDVQLNFDMPFIFAEVNADRITWLYDNTTGKQWKNSVNSHTIGRYISTKAVGSNARMDVTDKYKYPEGSDQERQVFQKALGKLKPNTPFAATSSMGLETEEQEPSIIGKLKVAGMLAVGKEVNLVLLLKNLSRDTKTVTVNMTAWTIIYNGTLVHEVWKDSATMSLDPEEEAEHPIKISYAQYEKYLKSDNMIRITAVCKVPDESEVVVERDIILDNPTLTLEVLNEARVRKPVNVQMLFSNPLDEPVRDCVLMVEGSGLLLGNLKIDVPTLGPKEGSRVRFDILPSRSGTKQLLADFSCNKFPAIKAMLSIDVAE

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
2	Acetylation	------MAALGVQSI ------CCCCCCCEE	16.05	-
26	Phosphorylation	AHHTDKFSSQELILR CCCCCCCCHHHHHHH	36.53	28348404
59	Phosphorylation	ERLEFIVSTGPYPSE CCEEEEEECCCCCCH	23.88	20068231
60	Phosphorylation	RLEFIVSTGPYPSES CEEEEEECCCCCCHH	31.14	20068231
65	Phosphorylation	VSTGPYPSESAMTKA EECCCCCCHHHCEEE	38.04	20068231
67	Phosphorylation	TGPYPSESAMTKAVF CCCCCCHHHCEEEEE	27.90	20068231
70	Phosphorylation	YPSESAMTKAVFPLS CCCHHHCEEEEEECC	18.63	20068231
111	Phosphorylation	ASAPIGRYTMALQIF CCCCCCEEEEEEHHH	8.82	25219547
112	Phosphorylation	SAPIGRYTMALQIFS CCCCCEEEEEEHHHH	8.46	8099584
119	Phosphorylation	TMALQIFSQGGISSV EEEEHHHHCCCCCEE	29.55	25219547
124	Phosphorylation	IFSQGGISSVKLGTF HHHCCCCCEEEECCE	32.14	25219547
125	Phosphorylation	FSQGGISSVKLGTFI HHCCCCCEEEECCEE	22.73	25219547
130	Phosphorylation	ISSVKLGTFILLFNP CCEEEECCEEEEECC	20.24	20068231
143	Phosphorylation	NPWLNVDSVFMGNHA CCCCCCCCCCCCCHH	16.99	20068231
191	Phosphorylation	DILSICLSILDRSLN HHHHHHHHHHHHHCC	19.39	24719451
221	Phosphorylation	KYVGRVLSAMINSND HHHHHHHHHHHCCCC	16.97	21406692
226	Phosphorylation	VLSAMINSNDDNGVL HHHHHHCCCCCCCCC	30.61	21406692
238	Phosphorylation	GVLAGNWSGTYTGGR CCCCCCCEEEECCCC	25.84	21406692
240	Phosphorylation	LAGNWSGTYTGGRDP CCCCCEEEECCCCCC	16.64	21406692
241	Phosphorylation	AGNWSGTYTGGRDPR CCCCEEEECCCCCCC	13.60	21406692
242	Phosphorylation	GNWSGTYTGGRDPRS CCCEEEECCCCCCCC	32.76	21406692
249	Phosphorylation	TGGRDPRSWNGSVEI CCCCCCCCCCCCHHH	30.22	23403867
263	Phosphorylation	ILKNWKKSGFSPVRY HHHCHHHCCCCCCEE	41.15	-
266	Phosphorylation	NWKKSGFSPVRYGQC CHHHCCCCCCEEEEE	26.47	-
313	Phosphorylation	NLSVDVYYDPMGNPL CEEEEEEECCCCCCC	17.26	-
424	Phosphorylation	HTIGRYISTKAVGSN HCHHHHEEECCCCCC	18.21	30631047
437	Phosphorylation	SNARMDVTDKYKYPE CCCCCCCCCCCCCCC	23.62	30631047
440	Phosphorylation	RMDVTDKYKYPEGSD CCCCCCCCCCCCCCH	20.68	-
442	Phosphorylation	DVTDKYKYPEGSDQE CCCCCCCCCCCCHHH	11.92	-
470	Phosphorylation	NTPFAATSSMGLETE CCCCCCCCCCCCCCC	17.38	23532336
482	Phosphorylation	ETEEQEPSIIGKLKV CCCCCCCCHHHHHEE	26.53	23532336
497	Acetylation	AGMLAVGKEVNLVLL EEEEECCCEEEHEEE	52.47	30592929
514	Phosphorylation	NLSRDTKTVTVNMTA CCCCCCCEEEEEECE	24.41	25072903
516	Phosphorylation	SRDTKTVTVNMTAWT CCCCCEEEEEECEEE	16.05	25072903
520	Phosphorylation	KTVTVNMTAWTIIYN CEEEEEECEEEEEEC	17.53	25072903
523	Phosphorylation	TVNMTAWTIIYNGTL EEEECEEEEEECCEE	8.60	25072903
526	Phosphorylation	MTAWTIIYNGTLVHE ECEEEEEECCEEEEE	12.04	25072903
529	Phosphorylation	WTIIYNGTLVHEVWK EEEEECCEEEEEEEC	23.20	25072903
565	Acetylation	AQYEKYLKSDNMIRI HHHHHHHCCCCEEEE	53.31	19827501
577	Acetylation	IRITAVCKVPDESEV EEEEEEEECCCCCCE	50.64	21339330
635	Phosphorylation	CVLMVEGSGLLLGNL EEEEEECCCEEECEE	16.86	-
664	Phosphorylation	VRFDILPSRSGTKQL EEEEECCCCCCCCHH	35.32	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TGM3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TGM3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TGM3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPME1_HUMAN	PPME1	physical	28514442

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
• DB00130: L-Glutamine

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-111 AND THR-112, ANDMASS SPECTROMETRY.
PubMed: 19690332