UniProt ID | I17RD_HUMAN | |
---|---|---|
UniProt AC | Q8NFM7 | |
Protein Name | Interleukin-17 receptor D | |
Gene Name | IL17RD | |
Organism | Homo sapiens (Human). | |
Sequence Length | 739 | |
Subcellular Localization |
Golgi apparatus membrane Single-pass type I membrane protein . Cell membrane Single-pass type I membrane protein . Predominantly associated with the Golgi apparatus and is partially translocated to the plasma membrane upon stimulation. Isoform 4 |
|
Protein Description | Feedback inhibitor of fibroblast growth factor mediated Ras-MAPK signaling and ERK activation. May inhibit FGF-induced FGFR1 tyrosine phosphorylation. Regulates the nuclear ERK signaling pathway by spatially blocking nuclear translocation of activated ERK without inhibiting cytoplasmic phosphorylation of ERK. Mediates JNK activation and may be involved in apoptosis. Might have a role in the early stages of fate specification of GnRH-secreting neurons (By similarity).. | |
Protein Sequence | MAPWLQLCSVFFTVNACLNGSQLAVAAGGSGRARGADTCGWRGVGPASRNSGLYNITFKYDNCTTYLNPVGKHVIADAQNITISQYACHDQVAVTILWSPGALGIEFLKGFRVILEELKSEGRQCQQLILKDPKQLNSSFKRTGMESQPFLNMKFETDYFVKVVPFPSIKNESNYHPFFFRTRACDLLLQPDNLACKPFWKPRNLNISQHGSDMQVSFDHAPHNFGFRFFYLHYKLKHEGPFKRKTCKQEQTTETTSCLLQNVSPGDYIIELVDDTNTTRKVMHYALKPVHSPWAGPIRAVAITVPLVVISAFATLFTVMCRKKQQENIYSHLDEESSESSTYTAALPRERLRPRPKVFLCYSSKDGQNHMNVVQCFAYFLQDFCGCEVALDLWEDFSLCREGQREWVIQKIHESQFIIVVCSKGMKYFVDKKNYKHKGGGRGSGKGELFLVAVSAIAEKLRQAKQSSSAALSKFIAVYFDYSCEGDVPGILDLSTKYRLMDNLPQLCSHLHSRDHGLQEPGQHTRQGSRRNYFRSKSGRSLYVAICNMHQFIDEEPDWFEKQFVPFHPPPLRYREPVLEKFDSGLVLNDVMCKPGPESDFCLKVEAAVLGATGPADSQHESQHGGLDQDGEARPALDGSAALQPLLHTVKAGSPSDMPRDSGIYDSSVPSSELSLPLMEGLSTDQTETSSLTESVSSSSGLGEEEPPALPSKLLSSGSCKADLGCRSYTDELHAVAPL | |
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 | N-linked_Glycosylation | FTVNACLNGSQLAVA HHHHHHHCCCEEEEC | 48.21 | UniProtKB CARBOHYD | |
38 | Phosphorylation | GRARGADTCGWRGVG CCCCCCCCCCCCCCC | 16.63 | 29978859 | |
48 | Phosphorylation | WRGVGPASRNSGLYN CCCCCCCCCCCCCEE | 34.82 | 29978859 | |
51 | Phosphorylation | VGPASRNSGLYNITF CCCCCCCCCCEEEEE | 29.12 | 29978859 | |
54 | Phosphorylation | ASRNSGLYNITFKYD CCCCCCCEEEEEEEC | 14.19 | 29978859 | |
55 | N-linked_Glycosylation | SRNSGLYNITFKYDN CCCCCCEEEEEEECC | 31.69 | UniProtKB CARBOHYD | |
57 | Phosphorylation | NSGLYNITFKYDNCT CCCCEEEEEEECCEE | 15.50 | 29978859 | |
60 | Phosphorylation | LYNITFKYDNCTTYL CEEEEEEECCEEEEE | 14.27 | 29759185 | |
62 | N-linked_Glycosylation | NITFKYDNCTTYLNP EEEEEECCEEEEECC | 23.19 | UniProtKB CARBOHYD | |
66 | Phosphorylation | KYDNCTTYLNPVGKH EECCEEEEECCCCCE | 6.07 | 29759185 | |
80 | N-linked_Glycosylation | HVIADAQNITISQYA EEEECCCCEEEEEEC | 34.78 | UniProtKB CARBOHYD | |
137 | N-linked_Glycosylation | LKDPKQLNSSFKRTG HCCHHHHCHHHHHCC | 32.87 | UniProtKB CARBOHYD | |
147 | Phosphorylation | FKRTGMESQPFLNMK HHHCCCCCCCCCCCE | 33.97 | 27251275 | |
157 | Phosphorylation | FLNMKFETDYFVKVV CCCCEEECCEEEEEE | 38.85 | 27251275 | |
159 | Phosphorylation | NMKFETDYFVKVVPF CCEEECCEEEEEEEC | 20.07 | 27251275 | |
168 | Phosphorylation | VKVVPFPSIKNESNY EEEEECCCCCCCCCC | 46.72 | 29083192 | |
171 | N-linked_Glycosylation | VPFPSIKNESNYHPF EECCCCCCCCCCCCC | 57.15 | UniProtKB CARBOHYD | |
173 | Phosphorylation | FPSIKNESNYHPFFF CCCCCCCCCCCCCEE | 52.67 | 30266825 | |
175 | Phosphorylation | SIKNESNYHPFFFRT CCCCCCCCCCCEEEC | 21.83 | 30266825 | |
182 | Phosphorylation | YHPFFFRTRACDLLL CCCCEEECCCHHHHC | 19.91 | 30266825 | |
206 | N-linked_Glycosylation | FWKPRNLNISQHGSD CCCCCCCCCCCCCCC | 35.10 | UniProtKB CARBOHYD | |
268 | Phosphorylation | QNVSPGDYIIELVDD CCCCCCCEEEEEECC | 15.09 | - | |
277 | N-linked_Glycosylation | IELVDDTNTTRKVMH EEEECCCCCHHHHHH | 46.58 | UniProtKB CARBOHYD | |
304 | Phosphorylation | PIRAVAITVPLVVIS CCHHEEEHHHHHHHH | 13.31 | - | |
415 | Phosphorylation | VIQKIHESQFIIVVC HHHHHHHCCEEEEEE | 19.07 | - | |
423 | Phosphorylation | QFIIVVCSKGMKYFV CEEEEEECCCCEEEE | 22.19 | - | |
435 | Phosphorylation | YFVDKKNYKHKGGGR EEEECCCCCCCCCCC | 24.29 | 22817900 | |
467 | Phosphorylation | KLRQAKQSSSAALSK HHHHHHHCCHHHHHH | 26.08 | - | |
529 | Phosphorylation | GQHTRQGSRRNYFRS CCCCCCCCCCCCEEC | 21.52 | 28165663 | |
654 | Phosphorylation | LHTVKAGSPSDMPRD HHHHCCCCCCCCCCC | 26.53 | 27732954 | |
656 | Phosphorylation | TVKAGSPSDMPRDSG HHCCCCCCCCCCCCC | 48.52 | 27732954 | |
712 | Phosphorylation | EEPPALPSKLLSSGS CCCCCCCHHHHCCCC | 36.46 | 24719451 | |
729 | Phosphorylation | ADLGCRSYTDELHAV CCCCCCCCCCCEEEE | 10.00 | 24173317 | |
730 | Phosphorylation | DLGCRSYTDELHAVA CCCCCCCCCCEEEEC | 25.01 | - |
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 I17RD_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of I17RD_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 I17RD_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
M3K7_HUMAN | MAP3K7 | physical | 23770285 | |
FBW1A_HUMAN | BTRC | physical | 28514442 | |
FBW1B_HUMAN | FBXW11 | physical | 28514442 | |
PTPRD_HUMAN | PTPRD | physical | 28514442 | |
TR19L_HUMAN | RELT | physical | 28514442 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
615267 | Hypogonadotropic hypogonadism 18 with or without anosmia (HH18) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...