CLC7A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CLC7A_HUMAN
• UniProt AC: Q9BXN2
• Protein Name: C-type lectin domain family 7 member A
• Gene Name: CLEC7A
• Organism: Homo sapiens (Human).
• Sequence Length: 247
• Subcellular Localization: Cell membrane ; Single-pass type II membrane protein .; Isoform 5: Cytoplasm.; Isoform 6: Cytoplasm .; Isoform 7: Cytoplasm .
• Protein Description: Lectin that functions as pattern receptor specific for beta-1,3-linked and beta-1,6-linked glucans, such as cell wall constituents from pathogenic bacteria and fungi. Necessary for the TLR2-mediated inflammatory response and for TLR2-mediated activation of NF-kappa-B. Enhances cytokine production in macrophages and dendritic cells. Mediates production of reactive oxygen species in the cell. Mediates phagocytosis of C.albicans conidia. Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation (By similarity)..
• Protein Sequence: MEYHPDLENLDEDGYTQLHFDSQSNTRIAVVSEKGSCAASPPWRLIAVILGILCLVILVIAVVLGTMAIWRSNSGSNTLENGYFLSRNKENHSQPTQSSLEDSVTPTKAVKTTGVLSSPCPPNWIIYEKSCYLFSMSLNSWDGSKRQCWQLGSNLLKIDSSNELGFIVKQVSSQPDNSFWIGLSRPQTEVPWLWEDGSTFSSNLFQIRTTATQENPSPNCVWIHVSVIYDQLCSVPSYSICEKKFSM

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
16	Phosphorylation	NLDEDGYTQLHFDSQ CCCCCCCEEEEEECC	30.13	27486199
22	Phosphorylation	YTQLHFDSQSNTRIA CEEEEEECCCCCEEE	34.27	27486199
24	Phosphorylation	QLHFDSQSNTRIAVV EEEEECCCCCEEEEE	44.09	24719451
26	Phosphorylation	HFDSQSNTRIAVVSE EEECCCCCEEEEEEC	28.79	27486199
32	Phosphorylation	NTRIAVVSEKGSCAA CCEEEEEECCCCCCC	27.30	22673903
66 (in isoform 9)	Phosphorylation	-	10.16	-
78 (in isoform 5)	Ubiquitination	-	36.83	21906983
91	N-linked_Glycosylation	FLSRNKENHSQPTQS ECCCCCCCCCCCCCC	41.54	UniProtKB CARBOHYD
103	Phosphorylation	TQSSLEDSVTPTKAV CCCHHCCCCCCCCCE	20.65	23312004
105	Phosphorylation	SSLEDSVTPTKAVKT CHHCCCCCCCCCEEE	29.23	21406692
111 (in isoform 2)	Ubiquitination	-	45.27	21906983
111	Ubiquitination	VTPTKAVKTTGVLSS CCCCCCEEECCCCCC	45.27	-
112	O-linked_Glycosylation	TPTKAVKTTGVLSSP CCCCCEEECCCCCCC	23.37	OGP
114 (in isoform 7)	Phosphorylation	-	24.49	-
115 (in isoform 7)	Phosphorylation	-	4.38	-
125 (in isoform 7)	Phosphorylation	-	2.82	-
132	Phosphorylation	IIYEKSCYLFSMSLN EEEECEEEEEEEECC	20.20	22817900
153	Phosphorylation	RQCWQLGSNLLKIDS HHHHHCCCCEEECCC	32.66	29978859
157	Ubiquitination	QLGSNLLKIDSSNEL HCCCCEEECCCCCCC	47.86	2190698
157 (in isoform 1)	Ubiquitination	-	47.86	21906983
160	Phosphorylation	SNLLKIDSSNELGFI CCEEECCCCCCCEEE	38.24	22817900
160 (in isoform 3)	Phosphorylation	-	38.24	-
161 (in isoform 3)	Phosphorylation	-	30.49	-
169	Ubiquitination	NELGFIVKQVSSQPD CCCEEEEEECCCCCC	39.92	-
171 (in isoform 3)	Phosphorylation	-	5.01	-
178	Phosphorylation	VSSQPDNSFWIGLSR CCCCCCCEEEEEECC	29.36	28787133

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

Oops, there are no upstream regulatory protein records of CLC7A_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CLC7A_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 CLC7A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CH60_HUMAN	HSPD1	physical	21988832
RANB9_HUMAN	RANBP9	physical	21988832
CLC7A_HUMAN	CLEC7A	physical	25416956
ADA33_HUMAN	ADAM33	physical	25416956
TMM79_HUMAN	TMEM79	physical	25416956
JAGN1_HUMAN	JAGN1	physical	25416956
SMIM3_HUMAN	SMIM3	physical	25416956
SYNE4_HUMAN	SYNE4	physical	25416956
BNI3L_HUMAN	BNIP3L	physical	21516116

Drug and Disease Associations

• Kegg Disease
• H01109: Chronic mucocutaneous candidiasis (CMC); Familial candidiasis (CANDF)
• OMIM Disease
• 613108: Candidiasis, familial, 4 (CANDF4)
• 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

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND MASSSPECTROMETRY.
PubMed: 18187866