I17RA_HUMAN - dbPTM
I17RA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID I17RA_HUMAN
UniProt AC Q96F46
Protein Name Interleukin-17 receptor A
Gene Name IL17RA
Organism Homo sapiens (Human).
Sequence Length 866
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein .
Isoform 2: Secreted .
Protein Description Receptor for IL17A. [PubMed: 17911633]
Protein Sequence MGAARSPPSAVPGPLLGLLLLLLGVLAPGGASLRLLDHRALVCSQPGLNCTVKNSTCLDDSWIHPRNLTPSSPKDLQIQLHFAHTQQGDLFPVAHIEWTLQTDASILYLEGAELSVLQLNTNERLCVRFEFLSKLRHHHRRWRFTFSHFVVDPDQEYEVTVHHLPKPIPDGDPNHQSKNFLVPDCEHARMKVTTPCMSSGSLWDPNITVETLEAHQLRVSFTLWNESTHYQILLTSFPHMENHSCFEHMHHIPAPRPEEFHQRSNVTLTLRNLKGCCRHQVQIQPFFSSCLNDCLRHSATVSCPEMPDTPEPIPDYMPLWVYWFITGISILLVGSVILLIVCMTWRLAGPGSEKYSDDTKYTDGLPAADLIPPPLKPRKVWIIYSADHPLYVDVVLKFAQFLLTACGTEVALDLLEEQAISEAGVMTWVGRQKQEMVESNSKIIVLCSRGTRAKWQALLGRGAPVRLRCDHGKPVGDLFTAAMNMILPDFKRPACFGTYVVCYFSEVSCDGDVPDLFGAAPRYPLMDRFEEVYFRIQDLEMFQPGRMHRVGELSGDNYLRSPGGRQLRAALDRFRDWQVRCPDWFECENLYSADDQDAPSLDEEVFEEPLLPPGTGIVKRAPLVREPGSQACLAIDPLVGEEGGAAVAKLEPHLQPRGQPAPQPLHTLVLAAEEGALVAAVEPGPLADGAAVRLALAGEGEACPLLGSPGAGRNSVLFLPVDPEDSPLGSSTPMASPDLLPEDVREHLEGLMLSLFEQSLSCQAQGGCSRPAMVLTDPHTPYEEEQRQSVQSDQGYISRSSPQPPEGLTEMEEEEEEEQDPGKPALPLSPEDLESLRSLQRQLLFRQLQKNSGWDTMGSESEGPSA
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
49N-linked_GlycosylationVCSQPGLNCTVKNST
EECCCCCCCEECCCC
25.9019838198
54N-linked_GlycosylationGLNCTVKNSTCLDDS
CCCCEECCCCCCCCC
37.9119838198
67N-linked_GlycosylationDSWIHPRNLTPSSPK
CCCCCCCCCCCCCCC
53.3619838198
134UbiquitinationVRFEFLSKLRHHHRR
HHHHHHHHHCHHHHH
52.25-
206N-linked_GlycosylationSGSLWDPNITVETLE
CCCCCCCCEEEEEEE
39.84UniProtKB CARBOHYD
225N-linked_GlycosylationRVSFTLWNESTHYQI
EEEEEEECCCCCEEE
36.1319838198
242N-linked_GlycosylationTSFPHMENHSCFEHM
ECCCCCCCCCCHHHH
25.46UniProtKB CARBOHYD
264PhosphorylationPEEFHQRSNVTLTLR
HHHHHHHCCEEEEEC
29.14-
265N-linked_GlycosylationEEFHQRSNVTLTLRN
HHHHHHCCEEEEECC
32.7417660510
354UbiquitinationLAGPGSEKYSDDTKY
HHCCCCCCCCCCCCC
52.3233845483
360UbiquitinationEKYSDDTKYTDGLPA
CCCCCCCCCCCCCCH
53.8233845483
554PhosphorylationMHRVGELSGDNYLRS
CEECEECCCCCCCCC
39.54-
561PhosphorylationSGDNYLRSPGGRQLR
CCCCCCCCCCHHHHH
25.8724300666
629PhosphorylationPLVREPGSQACLAID
CCCCCCCCCEEEEEC
25.8923401153
708PhosphorylationEACPLLGSPGAGRNS
CCCCCCCCCCCCCCC
21.8229255136
726PhosphorylationLPVDPEDSPLGSSTP
EECCCCCCCCCCCCC
21.9928270605
730PhosphorylationPEDSPLGSSTPMASP
CCCCCCCCCCCCCCC
38.4328270605
731PhosphorylationEDSPLGSSTPMASPD
CCCCCCCCCCCCCCC
34.4328270605
732PhosphorylationDSPLGSSTPMASPDL
CCCCCCCCCCCCCCC
20.8428270605
736PhosphorylationGSSTPMASPDLLPED
CCCCCCCCCCCCCHH
16.8228270605
776PhosphorylationSRPAMVLTDPHTPYE
CCCEEEECCCCCCCH
35.7528796482
780PhosphorylationMVLTDPHTPYEEEQR
EEECCCCCCCHHHHH
32.7128796482
782PhosphorylationLTDPHTPYEEEQRQS
ECCCCCCCHHHHHHH
36.8128796482
792PhosphorylationEQRQSVQSDQGYISR
HHHHHHHCCCCCCCC
29.7327732954
796PhosphorylationSVQSDQGYISRSSPQ
HHHCCCCCCCCCCCC
7.0627732954
798PhosphorylationQSDQGYISRSSPQPP
HCCCCCCCCCCCCCC
20.0227732954
800PhosphorylationDQGYISRSSPQPPEG
CCCCCCCCCCCCCCC
39.3128450419
801PhosphorylationQGYISRSSPQPPEGL
CCCCCCCCCCCCCCC
26.8326657352
809PhosphorylationPQPPEGLTEMEEEEE
CCCCCCCCCHHHHHH
44.1128450419
829PhosphorylationGKPALPLSPEDLESL
CCCCCCCCHHHHHHH
25.0520639409
835PhosphorylationLSPEDLESLRSLQRQ
CCHHHHHHHHHHHHH
36.0620639409

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
780TPhosphorylationKinaseGSK3AP49840
PSP
780TPhosphorylationKinaseGSK3BP49841
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of I17RA_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 I17RA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF6_HUMANTRAF6physical
17346928
TRAF6_HUMANTRAF6physical
17277779
M3K7_HUMANMAP3K7physical
17277779
TALD3_HUMANKIAA0586physical
28514442
KS6A3_HUMANRPS6KA3physical
28514442
KS6A2_HUMANRPS6KA2physical
28514442
KS6A1_HUMANRPS6KA1physical
28514442
TBB1_HUMANTUBB1physical
28514442
DDX11_HUMANDDX11physical
28514442
SIK2_HUMANSIK2physical
28514442
PLCH1_HUMANPLCH1physical
28514442
PKHA5_HUMANPLEKHA5physical
28514442
ZN318_HUMANZNF318physical
28514442
RICTR_HUMANRICTORphysical
28514442
FANCJ_HUMANBRIP1physical
28514442
TRPS1_HUMANTRPS1physical
28514442
K1671_HUMANKIAA1671physical
28514442
CE034_HUMANC5orf34physical
28514442
GCR_HUMANNR3C1physical
28514442
ACD11_HUMANACAD11physical
28514442
GTSE1_HUMANGTSE1physical
28514442
VIP2_HUMANPPIP5K2physical
28514442
SMG8_HUMANSMG8physical
28514442
NCOR1_HUMANNCOR1physical
28514442
MCM8_HUMANMCM8physical
28514442
MAP7_HUMANMAP7physical
28514442
TBL1X_HUMANTBL1Xphysical
28514442
HASP_HUMANGSG2physical
28514442
UBP54_HUMANUSP54physical
28514442
BCOR_HUMANBCORphysical
28514442
ICE2_HUMANICE2physical
28514442
ANKH1_HUMANANKHD1physical
28514442
HAUS5_HUMANHAUS5physical
28514442
MA7D2_HUMANMAP7D2physical
28514442
BCAS3_HUMANBCAS3physical
28514442
IF4E2_HUMANEIF4E2physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
HD_HUMANHTTphysical
28514442
GRDN_HUMANCCDC88Aphysical
28514442
ZN644_HUMANZNF644physical
28514442
MKS1_HUMANMKS1physical
28514442
BCD1_HUMANZNHIT6physical
28514442
PKN3_HUMANPKN3physical
28514442
CN080_HUMANC14orf80physical
28514442
TBCD_HUMANTBCDphysical
28514442
LRIF1_HUMANLRIF1physical
28514442
CBWD1_HUMANCBWD1physical
28514442
TASOR_HUMANFAM208Aphysical
28514442
TBL1R_HUMANTBL1XR1physical
28514442
SIMC1_HUMANSIMC1physical
28514442
HDAC3_HUMANHDAC3physical
28514442
CO039_HUMANC15orf39physical
28514442
IQGA3_HUMANIQGAP3physical
28514442
DYHC2_HUMANDYNC2H1physical
28514442
YETS2_HUMANYEATS2physical
28514442
ESPL1_HUMANESPL1physical
28514442
TTF2_HUMANTTF2physical
28514442
KAISO_HUMANZBTB33physical
28514442
TRAF3_HUMANTRAF3physical
28219902
CIKS_HUMANTRAF3IP2physical
28219902

Drug and Disease Associations
Kegg Disease
H00363 Candidiasis
H01109 Chronic mucocutaneous candidiasis (CMC); Familial candidiasis (CANDF)
OMIM Disease
613953Candidiasis, familial, 5 (CANDF5)
Kegg Drug
D10061 Brodalumab (USAN)
D10071 Ixekizumab (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of I17RA_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural basis of receptor sharing by interleukin 17 cytokines.";
Ely L.K., Fischer S., Garcia K.C.;
Nat. Immunol. 10:1245-1251(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 32-317 IN COMPLEX WITH IL17F,GLYCOSYLATION AT ASN-49; ASN-54; ASN-67; ASN-225 AND ASN-265,FUNCTION, AND DISULFIDE BONDS.

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