CD28_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CD28_HUMAN
• UniProt AC: P10747
• Protein Name: T-cell-specific surface glycoprotein CD28
• Gene Name: CD28
• Organism: Homo sapiens (Human).
• Sequence Length: 220
• Subcellular Localization: Membrane; Single-pass type I membrane protein.; Isoform 3: Cell surface .
• Protein Description: Involved in T-cell activation, the induction of cell proliferation and cytokine production and promotion of T-cell survival. Enhances the production of IL4 and IL10 in T-cells in conjunction with TCR/CD3 ligation and CD40L costimulation. [PubMed: 8617933 Isoform 3 enhances CD40L-mediated activation of NF-kappa-B and kinases MAPK8 and PAK2 in T-cells]
• Protein Sequence: MLRLLLALNLFPSIQVTGNKILVKQSPMLVAYDNAVNLSCKYSYNLFSREFRASLHKGLDSAVEVCVVYGNYSQQLQVYSKTGFNCDGKLGNESVTFYLQNLYVNQTDIYFCKIEVMYPPPYLDNEKSNGTIIHVKGKHLCPSPLFPGPSKPFWVLVVVGGVLACYSLLVTVAFIIFWVRSKRSRLLHSDYMNMTPRRPGPTRKHYQPYAPPRDFAAYRS

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
37	N-linked_Glycosylation	VAYDNAVNLSCKYSY EEECCCCCCEEECCH	24.67	15696168
71	N-linked_Glycosylation	EVCVVYGNYSQQLQV EEEEEECCHHHEEEE	18.65	19349973
71	N-linked_Glycosylation	EVCVVYGNYSQQLQV EEEEEECCHHHEEEE	18.65	19349973
92	N-linked_Glycosylation	NCDGKLGNESVTFYL CCCCCCCCCEEEEEE	49.13	19349973
92	N-linked_Glycosylation	NCDGKLGNESVTFYL CCCCCCCCCEEEEEE	49.13	19349973
105	N-linked_Glycosylation	YLQNLYVNQTDIYFC EEEEEECCCCEEEEE	26.02	15696168
129	N-linked_Glycosylation	YLDNEKSNGTIIHVK CCCCCCCCCEEEEEC	63.80	19349973
129	N-linked_Glycosylation	YLDNEKSNGTIIHVK CCCCCCCCCEEEEEC	63.80	19349973
136	Ubiquitination	NGTIIHVKGKHLCPS CCEEEEECCCCCCCC	48.34	-
138	Ubiquitination	TIIHVKGKHLCPSPL EEEEECCCCCCCCCC	27.90	-
152	Ubiquitination	LFPGPSKPFWVLVVV CCCCCCCCCEEEEEC	32.44	-
189	Phosphorylation	KRSRLLHSDYMNMTP HHHHHHCCCCCCCCC	30.33	21082442
191	Phosphorylation	SRLLHSDYMNMTPRR HHHHCCCCCCCCCCC	8.06	21082442
195	Phosphorylation	HSDYMNMTPRRPGPT CCCCCCCCCCCCCCC	14.51	28796482
204	Ubiquitination	RRPGPTRKHYQPYAP CCCCCCCCCCCCCCC	49.49	-
206	Phosphorylation	PGPTRKHYQPYAPPR CCCCCCCCCCCCCCC	17.76	20368329
209	Phosphorylation	TRKHYQPYAPPRDFA CCCCCCCCCCCCCCH	19.06	21964608
218	Phosphorylation	PPRDFAAYRS----- CCCCCHHHCC-----	14.14	16493040
218	Ubiquitination	PPRDFAAYRS----- CCCCCHHHCC-----	14.14	-
220	Phosphorylation	RDFAAYRS------- CCCHHHCC-------	31.71	28796482

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
191	Y	Phosphorylation	Kinase	ITK	Q08881	PhosphoELM
191	Y	Phosphorylation	Kinase	LCK	P06239	PhosphoELM
209	Y	Phosphorylation	Kinase	ITK	Q08881	PhosphoELM
218	Y	Phosphorylation	Kinase	ITK	Q08881	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CD28_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 CD28_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CD80_HUMAN	CD80	physical	7545666
GRAP2_HUMAN	GRAP2	physical	10820259
GRB2_HUMAN	GRB2	physical	8576157
P85A_HUMAN	PIK3R1	physical	8621607
DUS14_HUMAN	DUSP14	physical	11123293
P85A_HUMAN	PIK3R1	physical	19190244
P85B_HUMAN	PIK3R2	physical	19190244
PK3CA_HUMAN	PIK3CA	physical	9915850
DOK1_HUMAN	DOK1	physical	9620604
VAV_HUMAN	VAV1	physical	9620604
CD80_HUMAN	CD80	physical	1847722
P85A_HUMAN	PIK3R1	physical	11526404

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

N-linked Glycosylation

"Crystal structure of a soluble CD28-Fab complex.";
Evans E.J., Esnouf R.M., Manso-Sancho R., Gilbert R.J., James J.R.,Yu C., Fennelly J.A., Vowles C., Hanke T., Walse B., Hunig T.,Sorensen P., Stuart D.I., Davis S.J.;
Nat. Immunol. 6:271-279(2005).
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 17-152 IN COMPLEX WITH THEFAB FRAGMENT OF A MITOGENIC ANTIBODY, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-37 AND ASN-105.
PubMed: 15696168

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71 AND ASN-129, AND MASSSPECTROMETRY.
PubMed: 19349973

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-189; TYR-191 ANDTYR-218, AND MASS SPECTROMETRY.
PubMed: 19690332

"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-191 AND TYR-209, ANDMASS SPECTROMETRY.
PubMed: 16094384

"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-209, AND MASSSPECTROMETRY.
PubMed: 15592455