dbPTM

CD244_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CD244_HUMAN
UniProt AC	Q9BZW8
Protein Name	Natural killer cell receptor 2B4
Gene Name	CD244
Organism	Homo sapiens (Human).
Sequence Length	370
Subcellular Localization	Membrane Single-pass type I membrane protein . Cell membrane . Receptor engagement results in a recruitment to lipid drafts essential for the subsequent tyrosine phosphorylation of the ITSMs.
Protein Description	Heterophilic receptor of the signaling lymphocytic activation molecule (SLAM) family; its ligand is CD48. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Acts as activating natural killer (NK) cell receptor. [PubMed: 10359122]
Protein Sequence	MLGQVVTLILLLLLKVYQGKGCQGSADHVVSISGVPLQLQPNSIQTKVDSIAWKKLLPSQNGFHHILKWENGSLPSNTSNDRFSFIVKNLSLLIKAAQQQDSGLYCLEVTSISGKVQTATFQVFVFESLLPDKVEKPRLQGQGKILDRGRCQVALSCLVSRDGNVSYAWYRGSKLIQTAGNLTYLDEEVDINGTHTYTCNVSNPVSWESHTLNLTQDCQNAHQEFRFWPFLVIIVILSALFLGTLACFCVWRRKRKEKQSETSPKEFLTIYEDVKDLKTRRNHEQEQTFPGGGSTIYSMIQSQSSAPTSQEPAYTLYSLIQPSRKSGSRKRNHSPSFNSTIYEVIGKSQPKAQNPARLSRKELENFDVYS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
71	N-linked_Glycosylation	HHILKWENGSLPSNT CEEEEECCCCCCCCC	44.21	19349973
71	N-linked_Glycosylation	HHILKWENGSLPSNT CEEEEECCCCCCCCC	44.21	19349973
76	Phosphorylation	WENGSLPSNTSNDRF ECCCCCCCCCCCCHH	59.02	-
77	N-linked_Glycosylation	ENGSLPSNTSNDRFS CCCCCCCCCCCCHHH	45.66	19349973
77	N-linked_Glycosylation	ENGSLPSNTSNDRFS CCCCCCCCCCCCHHH	45.66	19349973
89	N-linked_Glycosylation	RFSFIVKNLSLLIKA HHHHHHHHHHHHHHH	24.78	21606496
164	N-linked_Glycosylation	CLVSRDGNVSYAWYR EEECCCCCEEEEEEE	24.69	UniProtKB CARBOHYD
164	N-linked_Glycosylation	CLVSRDGNVSYAWYR EEECCCCCEEEEEEE	24.69	19349973
168	Ubiquitination	RDGNVSYAWYRGSKL CCCCEEEEEEECCEE	6.85	32142685
181	N-linked_Glycosylation	KLIQTAGNLTYLDEE EEEEECCCCEEECCE	27.09	UniProtKB CARBOHYD
192	N-linked_Glycosylation	LDEEVDINGTHTYTC ECCEECCCCCEEEEE	44.86	UniProtKB CARBOHYD
200	N-linked_Glycosylation	GTHTYTCNVSNPVSW CCEEEEEECCCCCEE	32.24	UniProtKB CARBOHYD
213	N-linked_Glycosylation	SWESHTLNLTQDCQN EEEEEEEEECHHHHH	42.04	UniProtKB CARBOHYD
260	Ubiquitination	RKRKEKQSETSPKEF HHHHHHCCCCCHHHH	54.64	32142685
265	Ubiquitination	KQSETSPKEFLTIYE HCCCCCHHHHHHHHH	61.95	32142685
269	Phosphorylation	TSPKEFLTIYEDVKD CCHHHHHHHHHHHHH	27.17	28176486
271	Phosphorylation	PKEFLTIYEDVKDLK HHHHHHHHHHHHHHH	10.80	15713798
288	Phosphorylation	RNHEQEQTFPGGGST CCCCCCCCCCCCCHH	30.92	22210691
297	Phosphorylation	PGGGSTIYSMIQSQS CCCCHHHHHHHHCCC	7.71	15713798
317	Phosphorylation	QEPAYTLYSLIQPSR CCCCCHHHHHHCCCC	8.14	15713798
334	Phosphorylation	GSRKRNHSPSFNSTI CCCCCCCCCCCCHHH	26.28	23401153
336	Phosphorylation	RKRNHSPSFNSTIYE CCCCCCCCCCHHHHH	39.82	23401153
339	Phosphorylation	NHSPSFNSTIYEVIG CCCCCCCHHHHHHHC	17.74	28450419
340	Phosphorylation	HSPSFNSTIYEVIGK CCCCCCHHHHHHHCC	28.78	28450419
342	Phosphorylation	PSFNSTIYEVIGKSQ CCCCHHHHHHHCCCC	12.30	10556801
348	Phosphorylation	IYEVIGKSQPKAQNP HHHHHCCCCCCCCCH	46.64	-
359	Phosphorylation	AQNPARLSRKELENF CCCHHHCCHHHHCCC	35.43	29978859
369	Phosphorylation	ELENFDVYS------ HHCCCCCCC------	15.54	21552520

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
297	Y	Phosphorylation	Kinase	FYN	P06241	Uniprot
342	Y	Phosphorylation	Kinase	FYN	P06241	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CD244_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CD244_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SH21A_HUMAN	SH2D1A	physical	15169881
FYN_HUMAN	FYN	physical	15169881
MIC60_HUMAN	IMMT	physical	26186194
CAND2_HUMAN	CAND2	physical	26186194
HEAT1_HUMAN	HEATR1	physical	26186194
HEAT6_HUMAN	HEATR6	physical	26186194
PDXD1_HUMAN	PDXDC1	physical	26186194
BIG1_HUMAN	ARFGEF1	physical	26186194
BIG2_HUMAN	ARFGEF2	physical	26186194
MTOR_HUMAN	MTOR	physical	26186194
POMT2_HUMAN	POMT2	physical	26186194
POMT1_HUMAN	POMT1	physical	26186194
P85A_HUMAN	PIK3R1	physical	26186194
UFSP2_HUMAN	UFSP2	physical	26186194
LTN1_HUMAN	LTN1	physical	26186194
RN213_HUMAN	RNF213	physical	26186194
MTX2_HUMAN	MTX2	physical	26186194
MTX3_HUMAN	MTX3	physical	26186194
ST7_HUMAN	ST7	physical	26186194
MYADM_HUMAN	MYADM	physical	26186194
CAR19_HUMAN	C9orf89	physical	26186194
RIMB1_HUMAN	BZRAP1	physical	26186194
CAR19_HUMAN	C9orf89	physical	28514442
POMT2_HUMAN	POMT2	physical	28514442
POMT1_HUMAN	POMT1	physical	28514442
PDXD1_HUMAN	PDXDC1	physical	28514442
MYADM_HUMAN	MYADM	physical	28514442
MTX3_HUMAN	MTX3	physical	28514442
MTOR_HUMAN	MTOR	physical	28514442
MTX2_HUMAN	MTX2	physical	28514442
RN213_HUMAN	RNF213	physical	28514442
MIC60_HUMAN	IMMT	physical	28514442
CAND2_HUMAN	CAND2	physical	28514442
BIG2_HUMAN	ARFGEF2	physical	28514442
RIMB1_HUMAN	BZRAP1	physical	28514442
LTN1_HUMAN	LTN1	physical	28514442
ST7_HUMAN	ST7	physical	28514442
MIC25_HUMAN	CHCHD6	physical	28514442
HEAT6_HUMAN	HEATR6	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
There are no disease associations of PTM sites.

Regulatory Network of CD244_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-271, AND MASSSPECTROMETRY.	18083107 [Abstract]