CD3G_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CD3G_HUMAN
• UniProt AC: P09693
• Protein Name: T-cell surface glycoprotein CD3 gamma chain
• Gene Name: CD3G
• Organism: Homo sapiens (Human).
• Sequence Length: 182
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein.
• Protein Description: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. [PubMed: 2470098 In addition to this role of signal transduction in T-cell activation, CD3G plays an essential role in the dynamic regulation of TCR expression at the cell surface]
• Protein Sequence: MEQGKGLAVLILAIILLQGTLAQSIKGNHLVKVYDYQEDGSVLLTCDAEAKNITWFKDGKMIGFLTEDKKKWNLGSNAKDPRGMYQCKGSQNKSKPLQVYYRMCQNCIELNAATISGFLFAEIVSIFVLAVGVYFIAGQDGVRQSRASDKQTLLPNDQLYQPLKDREDDQYSHLQGNQLRRN

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
32	Ubiquitination	IKGNHLVKVYDYQED HCCCCEEEEEEECCC	41.24	-
51	Ubiquitination	LTCDAEAKNITWFKD EEEECCCCCEEEEEC	40.15	-
52	N-linked_Glycosylation	TCDAEAKNITWFKDG EEECCCCCEEEEECC	43.92	8636209
52	N-linked_Glycosylation	TCDAEAKNITWFKDG EEECCCCCEEEEECC	43.92	8636209
57	Ubiquitination	AKNITWFKDGKMIGF CCCEEEEECCEEEEE	58.07	-
60	Ubiquitination	ITWFKDGKMIGFLTE EEEEECCEEEEEEEC	37.16	-
69	Ubiquitination	IGFLTEDKKKWNLGS EEEEECCHHHCCCCC	50.44	-
70	Ubiquitination	GFLTEDKKKWNLGSN EEEECCHHHCCCCCC	75.29	-
71	Ubiquitination	FLTEDKKKWNLGSNA EEECCHHHCCCCCCC	47.24	-
76	Phosphorylation	KKKWNLGSNAKDPRG HHHCCCCCCCCCCCC	36.46	-
79	Ubiquitination	WNLGSNAKDPRGMYQ CCCCCCCCCCCCCEE	72.94	-
88	Ubiquitination	PRGMYQCKGSQNKSK CCCCEECCCCCCCCC	46.18	-
92	N-linked_Glycosylation	YQCKGSQNKSKPLQV EECCCCCCCCCCHHH	52.87	8636209
92	N-linked_Glycosylation	YQCKGSQNKSKPLQV EECCCCCCCCCCHHH	52.87	8636209
94	Phosphorylation	CKGSQNKSKPLQVYY CCCCCCCCCCHHHHH	47.24	24719451
95	Ubiquitination	KGSQNKSKPLQVYYR CCCCCCCCCHHHHHH	51.89	-
100	Phosphorylation	KSKPLQVYYRMCQNC CCCCHHHHHHHHHHH	3.41	26657352
101	Phosphorylation	SKPLQVYYRMCQNCI CCCHHHHHHHHHHHH	7.94	26657352
145	Phosphorylation	GQDGVRQSRASDKQT CCCCCCCCCCCCCCC	21.17	22817900
148	Phosphorylation	GVRQSRASDKQTLLP CCCCCCCCCCCCCCC	44.20	23401153
150	Ubiquitination	RQSRASDKQTLLPND CCCCCCCCCCCCCCC	42.56	-
152	Phosphorylation	SRASDKQTLLPNDQL CCCCCCCCCCCCCCC	35.68	26657352
160	Phosphorylation	LLPNDQLYQPLKDRE CCCCCCCCCCCCCCC	11.49	19605366
164	Ubiquitination	DQLYQPLKDREDDQY CCCCCCCCCCCCHHH	62.51	-
171	Phosphorylation	KDREDDQYSHLQGNQ CCCCCHHHHHHCHHC	12.68	19605366
172	Phosphorylation	DREDDQYSHLQGNQL CCCCHHHHHHCHHCC	16.46	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
145	S	Phosphorylation	Kinase	PRKCA	P04409	GPS
148	S	Phosphorylation	Kinase	PKCA	P04409	PSP
148	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
148	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
148	S	Phosphorylation	Kinase	PKC	-	Uniprot
148	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CD3G_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 CD3G_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GCR_HUMAN	NR3C1	physical	16888650
FYN_HUMAN	FYN	physical	16888650

Drug and Disease Associations

• Kegg Disease
• H00002: Acute lymphoblastic leukemia (ALL) (precursor T lymphoblastic leukemia)
• OMIM Disease
• 615607: Immunodeficiency 17 (IMD17)
• Kegg Drug
• D05092: Muromonab-CD3 (JAN/USAN/INN); Orthoclone okt3 (TN)
• D06314: Visilizumab (USAN/INN); Nuvion (TN)
• D08959: Otelixizumab (USAN)
• D09013: Teplizumab (USAN/INN)
• D09207: Catumaxomab (INN)
• D09325: Blinatumomab (USAN/INN)
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"The human T3 gamma chain is phosphorylated at serine 126 in responseto T lymphocyte activation.";
Davies A.A., Cantrell D.A., Hexham J.M., Parker P.J., Rothbard J.,Crumpton M.J.;
J. Biol. Chem. 262:10918-10921(1987).
Cited for: PHOSPHORYLATION AT SER-145 AND SER-148.
PubMed: 3112151

"Dephosphorylation of the human T lymphocyte CD3 antigen.";
Alexander D., Goris J., Marais R., Rothbard J., Merlevede W.,Crumpton M.J.;
Eur. J. Biochem. 181:55-65(1989).
Cited for: PROTEIN SEQUENCE OF 139-182, AND PHOSPHORYLATION AT SER-145 ANDSER-148.
PubMed: 2540970

"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-160 AND TYR-171, ANDMASS SPECTROMETRY.
PubMed: 16094384