TMIG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TMIG2_HUMAN
• UniProt AC: Q96BF3
• Protein Name: Transmembrane and immunoglobulin domain-containing protein 2
• Gene Name: TMIGD2
• Organism: Homo sapiens (Human).
• Sequence Length: 282
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein .
• Protein Description: Plays a role in cell-cell interaction, cell migration, and angiogenesis. Through interaction with HHLA2, costimulates T-cells in the context of TCR-mediated activation. Enhances T-cell proliferation and cytokine production via an AKT-dependent signaling cascade..
• Protein Sequence: MGSPGMVLGLLVQIWALQEASSLSVQQGPNLLQVRQGSQATLVCQVDQATAWERLRVKWTKDGAILCQPYITNGSLSLGVCGPQGRLSWQAPSHLTLQLDPVSLNHSGAYVCWAAVEIPELEEAEGNITRLFVDPDDPTQNRNRIASFPGFLFVLLGVGSMGVAAIVWGAWFWGRRSCQQRDSGNSPGNAFYSNVLYRPRGAPKKSEDCSGEGKDQRGQSIYSTSFPQPAPRQPHLASRPCPSPRPCPSPRPGHPVSMVRVSPRPSPTQQPRPKGFPKVGEE

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
73	N-linked_Glycosylation	LCQPYITNGSLSLGV EEECEEECCCEEEEE	28.62	UniProtKB CARBOHYD
105	N-linked_Glycosylation	QLDPVSLNHSGAYVC EECCEECCCCCCEEE	21.55	UniProtKB CARBOHYD
127	N-linked_Glycosylation	ELEEAEGNITRLFVD CHHHCCCCEEEEEEC	24.78	UniProtKB CARBOHYD
183 (in isoform 2)	Phosphorylation	-	41.90	-
186	Phosphorylation	QQRDSGNSPGNAFYS HCCCCCCCCCCCCEE	37.40	-
188 (in isoform 2)	Phosphorylation	-	37.61	25839225
189 (in isoform 2)	Phosphorylation	-	30.20	28796482
192	Phosphorylation	NSPGNAFYSNVLYRP CCCCCCCEECCCCCC	9.27	25884760
193 (in isoform 2)	Phosphorylation	-	17.63	28796482
193	Phosphorylation	SPGNAFYSNVLYRPR CCCCCCEECCCCCCC	17.63	28796482
197	Phosphorylation	AFYSNVLYRPRGAPK CCEECCCCCCCCCCC	17.81	28796482
220	Phosphorylation	GKDQRGQSIYSTSFP CCCCCCCCEEECCCC	26.73	23401153
222	Phosphorylation	DQRGQSIYSTSFPQP CCCCCCEEECCCCCC	15.90	25884760
223	Phosphorylation	QRGQSIYSTSFPQPA CCCCCEEECCCCCCC	18.86	26074081
224	O-linked_Glycosylation	RGQSIYSTSFPQPAP CCCCEEECCCCCCCC	19.88	OGP
224	Phosphorylation	RGQSIYSTSFPQPAP CCCCEEECCCCCCCC	19.88	28796482
225	Phosphorylation	GQSIYSTSFPQPAPR CCCEEECCCCCCCCC	29.05	26074081
238	Phosphorylation	PRQPHLASRPCPSPR CCCCCCCCCCCCCCC	43.02	-
243	Phosphorylation	LASRPCPSPRPCPSP CCCCCCCCCCCCCCC	40.01	27732954
249	Phosphorylation	PSPRPCPSPRPGHPV CCCCCCCCCCCCCCC	40.01	27732954
262	Phosphorylation	PVSMVRVSPRPSPTQ CCEEEEEECCCCCCC	12.48	23401153
266	Phosphorylation	VRVSPRPSPTQQPRP EEEECCCCCCCCCCC	41.69	23401153
268	Phosphorylation	VSPRPSPTQQPRPKG EECCCCCCCCCCCCC	44.14	23684312

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
220	S	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TMIG2_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 TMIG2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of TMIG2_HUMAN !!

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
• There are no disease associations of PTM sites.

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 SER-220, AND MASSSPECTROMETRY.
PubMed: 19690332