CD8B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CD8B_HUMAN
• UniProt AC: P10966
• Protein Name: T-cell surface glycoprotein CD8 beta chain
• Gene Name: CD8B
• Organism: Homo sapiens (Human).
• Sequence Length: 210
• Subcellular Localization: Isoform 1: Cell membrane ; Single-pass type I membrane protein . Requires the partner CD8A for efficient cell surface expression (PubMed:3145196). The heterodimer CD8A/CD8B localizes to lipid rafts due to CD8B cytoplasmic tail palmitoylation.; Isofor
• Protein Description: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. A palmitoylation site in the cytoplasmic tail of CD8B chain contributes to partitioning of CD8 into the plasma membrane lipid rafts where signaling proteins are enriched. Once LCK recruited, it initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). Additionally, plays a critical role in thymic selection of CD8+ T-cells..
• Protein Sequence: MRPRLWLLLAAQLTVLHGNSVLQQTPAYIKVQTNKMVMLSCEAKISLSNMRIYWLRQRQAPSSDSHHEFLALWDSAKGTIHGEEVEQEKIAVFRDASRFILNLTSVKPEDSGIYFCMIVGSPELTFGKGTQLSVVDFLPTTAQPTKKSTLKKRVCRLPRPETQKGPLCSPITLGLLVAGVLVLLVSLGVAIHLCCRRRRARLRFMKQFYK

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
40	Phosphorylation	TNKMVMLSCEAKISL CCCEEEEEEEEEEEC	7.57	-
102	N-linked_Glycosylation	DASRFILNLTSVKPE CHHHHHHCCCCCCCC	36.13	UniProtKB CARBOHYD
140	O-linked_Glycosylation	SVVDFLPTTAQPTKK EEEECCCCCCCCCCC	36.59	12459555
140	Phosphorylation	SVVDFLPTTAQPTKK EEEECCCCCCCCCCC	36.59	30624053
141	O-linked_Glycosylation	VVDFLPTTAQPTKKS EEECCCCCCCCCCCC	22.73	12459555
141	Phosphorylation	VVDFLPTTAQPTKKS EEECCCCCCCCCCCC	22.73	30624053
145	O-linked_Glycosylation	LPTTAQPTKKSTLKK CCCCCCCCCCCHHHH	38.74	12459555
149	O-linked_Glycosylation	AQPTKKSTLKKRVCR CCCCCCCHHHHHHHC	52.02	12459555
194	S-palmitoylation	LGVAIHLCCRRRRAR HHHHHHHHHHHHHHH	0.76	17341584
195	S-palmitoylation	GVAIHLCCRRRRARL HHHHHHHHHHHHHHH	4.82	17341584
209	Phosphorylation	LRFMKQFYK------ HHHHHHHHC------	17.19	-

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

Oops, there are no upstream regulatory protein records of CD8B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CD8B_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 CD8B_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CD8B_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• H00002: Acute lymphoblastic leukemia (ALL) (precursor T lymphoblastic leukemia)
• 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.