CD209_HUMAN - dbPTM
CD209_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD209_HUMAN
UniProt AC Q9NNX6
Protein Name CD209 antigen
Gene Name CD209
Organism Homo sapiens (Human).
Sequence Length 404
Subcellular Localization Isoform 1: Cell membrane
Single-pass type II membrane protein .
Isoform 2: Cell membrane
Single-pass type II membrane protein .
Isoform 3: Cell membrane
Single-pass type II membrane protein .
Isoform 4: Cell membrane
Single-pass type II membran
Protein Description Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response.; On DCs it is a high affinity receptor for ICAM2 and ICAM3 by binding to mannose-like carbohydrates. May act as a DC rolling receptor that mediates transendothelial migration of DC presursors from blood to tissues by binding endothelial ICAM2. Seems to regulate DC-induced T-cell proliferation by binding to ICAM3 on T-cells in the immunological synapse formed between DC and T-cells.; (Microbial infection) Acts as an attachment receptor for HIV-1 and HIV-2.; (Microbial infection) Acts as an attachment receptor for Ebolavirus.; (Microbial infection) Acts as an attachment receptor for Cytomegalovirus.; (Microbial infection) Acts as an attachment receptor for HCV.; (Microbial infection) Acts as an attachment receptor for Dengue virus.; (Microbial infection) Acts as an attachment receptor for Measles virus.; (Microbial infection) Acts as an attachment receptor for Herpes simplex virus 1.; (Microbial infection) Acts as an attachment receptor for Influenzavirus A.; (Microbial infection) Acts as an attachment receptor for SARS coronavirus.; (Microbial infection) Acts as an attachment receptor for Japanese encephalitis virus.; (Microbial infection) Acts as an attachment receptor for Lassa virus. [PubMed: 23966408 Acts as an attachment receptor for Marburg virusn.; (Microbial infection) Acts as an attachment receptor for Respiratory syncytial virus.; (Microbial infection) Acts as an attachment receptor for Rift valley fever virus and uukuniemi virus.; (Microbial infection) Acts as an attachment receptor for West-nile virus.; (Microbial infection) Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of bacterial pathogen antigens, including Leishmania pifanoi LPG, Lewis-x antigen in Helicobacter pylori LPS, mannose in Klebsiella pneumonae LPS, di-mannose and tri-mannose in Mycobacterium tuberculosis ManLAM and Lewis-x antigen in Schistosoma mansoni SEA]
Protein Sequence MSDSKEPRLQQLGLLEEEQLRGLGFRQTRGYKSLAGCLGHGPLVLQLLSFTLLAGLLVQVSKVPSSISQEQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTWLKAAVGELPEKSKMQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTQLKAAVERLCHPCPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLLPSFKQYWNRGEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA
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 Orthologous
Protein Cluster
17 (in isoform 8)Phosphorylation-51.52-
17 (in isoform 7)Phosphorylation-51.52-
21 (in isoform 8)Phosphorylation-37.68-
21 (in isoform 7)Phosphorylation-37.68-
22 (in isoform 8)Phosphorylation-38.45-
22 (in isoform 7)Phosphorylation-38.45-
48 (in isoform 10)Phosphorylation-2.2622210691
48 (in isoform 6)Phosphorylation-2.2622210691
48 (in isoform 12)Phosphorylation-2.2622210691
48 (in isoform 11)Phosphorylation-2.2622210691
54 (in isoform 6)Phosphorylation-15.0822210691
54 (in isoform 12)Phosphorylation-15.0822210691
54 (in isoform 11)Phosphorylation-15.0822210691
54 (in isoform 10)Phosphorylation-15.0822210691
65PhosphorylationVQVSKVPSSISQEQS
HHHHCCCCCCCHHHH		43.2029978859
66PhosphorylationQVSKVPSSISQEQSR
HHHCCCCCCCHHHHH		21.8629978859
68PhosphorylationSKVPSSISQEQSRQD
HCCCCCCCHHHHHHH		29.6124043423
72PhosphorylationSSISQEQSRQDAIYQ
CCCCHHHHHHHHHHH		31.0224043423
78PhosphorylationQSRQDAIYQNLTQLK
HHHHHHHHHHHHHHH		7.9629978859
80N-linked_GlycosylationRQDAIYQNLTQLKAA
HHHHHHHHHHHHHHH		28.25UniProtKB CARBOHYD
82PhosphorylationDAIYQNLTQLKAAVG
HHHHHHHHHHHHHHH		39.1329978859
92PhosphorylationKAAVGELSEKSKLQE
HHHHHHHCHHHHHHH		38.3822210691
95PhosphorylationVGELSEKSKLQEIYQ
HHHHCHHHHHHHHHH		34.25-
101PhosphorylationKSKLQEIYQELTQLK
HHHHHHHHHHHHHHH		8.65-
108AcetylationYQELTQLKAAVGELP
HHHHHHHHHHHCCCC		25.207432115
118PhosphorylationVGELPEKSKLQEIYQ
HCCCCCHHHHHHHHH		36.62-
124PhosphorylationKSKLQEIYQELTRLK
HHHHHHHHHHHHHHH		8.65-
131AcetylationYQELTRLKAAVGELP
HHHHHHHHHHHCCCC		30.897432123
141PhosphorylationVGELPEKSKLQEIYQ
HCCCCCHHHHHHHHH		36.62-
154AcetylationYQELTWLKAAVGELP
HHHHHHHHHHHCCCC		26.347432131
164PhosphorylationVGELPEKSKMQEIYQ
HCCCCCHHHHHHHHH		31.53-
170PhosphorylationKSKMQEIYQELTRLK
HHHHHHHHHHHHHHH		8.6524043423
174PhosphorylationQEIYQELTRLKAAVG
HHHHHHHHHHHHHHC		32.9524043423
177AcetylationYQELTRLKAAVGELP
HHHHHHHHHHHCCCC		30.897432139
187PhosphorylationVGELPEKSKQQEIYQ
HCCCCHHHHHHHHHH		33.7525690035
193PhosphorylationKSKQQEIYQELTRLK
HHHHHHHHHHHHHHH		8.6525690035
197PhosphorylationQEIYQELTRLKAAVG
HHHHHHHHHHHHHHC		32.9524043423
200AcetylationYQELTRLKAAVGELP
HHHHHHHHHHHCCCC		30.897432147
210PhosphorylationVGELPEKSKQQEIYQ
HCCCCHHHHHHHHHH		33.7525690035
216PhosphorylationKSKQQEIYQELTRLK
HHHHHHHHHHHHHHH		8.6525690035
220PhosphorylationQEIYQELTRLKAAVG
HHHHHHHHHHHHHHC		32.9524043423
223AcetylationYQELTRLKAAVGELP
HHHHHHHHHHHCCCC		30.897432155
233PhosphorylationVGELPEKSKQQEIYQ
HCCCCHHHHHHHHHH		33.75-
239PhosphorylationKSKQQEIYQELTQLK
HHHHHHHHHHHHHHH		8.6520736484
338PhosphorylationDGSPLLPSFKQYWNR
CCCCCCHHHHHHHHC		45.0724719451
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

Oops, there are no upstream regulatory protein records of CD209_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD209_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 CD209_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD209_HUMANCD209physical
11739956
CD209_HUMANCD209physical
11384997
CLC4M_HUMANCLEC4Mphysical
11384997
LG3BP_HUMANLGALS3BPphysical
21515679
CEAM5_HUMANCEACAM5physical
21515679
LSP1_HUMANLSP1physical
24867235
CYLD_HUMANCYLDphysical
24867235
IKKE_HUMANIKBKEphysical
24867235
VAC14_HUMANVAC14physical
25416956
CLC4M_HUMANCLEC4Mphysical
26186194
ZN703_HUMANZNF703physical
26186194
HMDH_HUMANHMGCRphysical
26186194
5HT1B_HUMANHTR1Bphysical
26186194
KLH26_HUMANKLHL26physical
26186194
CLC4M_HUMANCLEC4Mphysical
28514442
5HT1B_HUMANHTR1Bphysical
28514442
HMDH_HUMANHMGCRphysical
28514442
ZN703_HUMANZNF703physical
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 CD209_HUMAN

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Related Literatures of Post-Translational Modification

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