UniProt ID | WNT2B_HUMAN | |
---|---|---|
UniProt AC | Q93097 | |
Protein Name | Protein Wnt-2b | |
Gene Name | WNT2B | |
Organism | Homo sapiens (Human). | |
Sequence Length | 391 | |
Subcellular Localization | Secreted, extracellular space, extracellular matrix . Secreted . | |
Protein Description | Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt/beta-catenin signaling pathway. Plays a redundant role in embryonic lung development.. | |
Protein Sequence | MLRPGGAEEAAQLPLRRASAPVPVPSPAAPDGSRASARLGLACLLLLLLLTLPARVDTSWWYIGALGARVICDNIPGLVSRQRQLCQRYPDIMRSVGEGAREWIRECQHQFRHHRWNCTTLDRDHTVFGRVMLRSSREAAFVYAISSAGVVHAITRACSQGELSVCSCDPYTRGRHHDQRGDFDWGGCSDNIHYGVRFAKAFVDAKEKRLKDARALMNLHNNRCGRTAVRRFLKLECKCHGVSGSCTLRTCWRALSDFRRTGDYLRRRYDGAVQVMATQDGANFTAARQGYRRATRTDLVYFDNSPDYCVLDKAAGSLGTAGRVCSKTSKGTDGCEIMCCGRGYDTTRVTRVTQCECKFHWCCAVRCKECRNTVDVHTCKAPKKAEWLDQT | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
19 | Phosphorylation | QLPLRRASAPVPVPS CCCCCCCCCCCCCCC | 31.15 | 23312004 | |
117 | N-linked_Glycosylation | QFRHHRWNCTTLDRD HHHHCCCCCEECCCC | 17.14 | 18780401 | |
243 | O-palmitoleoylation | ECKCHGVSGSCTLRT EEEECCCCCCCHHHH | 29.58 | - | |
269 | Phosphorylation | GDYLRRRYDGAVQVM HHHHHHHCCCCEEEE | 19.54 | 24043423 | |
278 | Phosphorylation | GAVQVMATQDGANFT CCEEEEEECCCCCCH | 14.75 | 24043423 | |
283 | N-linked_Glycosylation | MATQDGANFTAARQG EEECCCCCCHHHHHH | 40.09 | 18780401 | |
283 | N-linked_Glycosylation | MATQDGANFTAARQG EEECCCCCCHHHHHH | 40.09 | 18780401 | |
285 | Phosphorylation | TQDGANFTAARQGYR ECCCCCCHHHHHHHH | 21.15 | 24043423 |
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 WNT2B_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of WNT2B_HUMAN !! |
* 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 WNT2B_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of WNT2B_HUMAN !! |
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. |
loading...
N-linked Glycosylation | |
Reference | PubMed |
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry."; Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; Proteomics 8:3833-3847(2008). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-117 AND ASN-283, AND MASSSPECTROMETRY. |