PILRA_HUMAN - dbPTM
PILRA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PILRA_HUMAN
UniProt AC Q9UKJ1
Protein Name Paired immunoglobulin-like type 2 receptor alpha
Gene Name PILRA
Organism Homo sapiens (Human).
Sequence Length 303
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein .
Isoform 2: Cell membrane
Single-pass type I membrane protein .
Isoform 3: Secreted .
Isoform 4: Secreted .
Protein Description Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. PILRA is thought to act as a cellular signaling inhibitory receptor by recruiting cytoplasmic phosphatases like PTPN6/SHP-1 and PTPN11/SHP-2 via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules. Receptor for PIANP..
Protein Sequence MGRPLLLPLLPLLLPPAFLQPSGSTGSGPSYLYGVTQPKHLSASMGGSVEIPFSFYYPWELATAPDVRISWRRGHFHRQSFYSTRPPSIHKDYVNRLFLNWTEGQKSGFLRISNLQKQDQSVYFCRVELDTRSSGRQQWQSIEGTKLSITQAVTTTTQRPSSMTTTWRLSSTTTTTGLRVTQGKRRSDSWHISLETAVGVAVAVTVLGIMILGLICLLRWRRRKGQQRTKATTPAREPFQNTEEPYENIRNEGQNTDPKLNPKDDGIVYASLALSSSTSPRAPPSHRPLKSPQNETLYSVLKA
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
70PhosphorylationTAPDVRISWRRGHFH
ECCCEEEEEECCCCC		12.1724719451
83PhosphorylationFHRQSFYSTRPPSIH
CCCCCCCCCCCCCCC		18.87-
84PhosphorylationHRQSFYSTRPPSIHK
CCCCCCCCCCCCCCH		35.50-
88PhosphorylationFYSTRPPSIHKDYVN
CCCCCCCCCCHHHHH		39.75-
100N-linked_GlycosylationYVNRLFLNWTEGQKS
HHHHHCCCCCCCCCC		35.9719159218
100N-linked_GlycosylationYVNRLFLNWTEGQKS
HHHHHCCCCCCCCCC		35.9719349973
145PhosphorylationQWQSIEGTKLSITQA
EEEEEECEEEEEEEE		18.93-
187PhosphorylationVTQGKRRSDSWHISL
EEECCCCCCCEEEEH		39.7822210691
205PhosphorylationVGVAVAVTVLGIMIL
HHHHHHHHHHHHHHH		10.5622210691
242O-linked_GlycosylationAREPFQNTEEPYENI
CCCCCCCCCCCCHHH		30.83OGP
256PhosphorylationIRNEGQNTDPKLNPK
HHCCCCCCCCCCCCC		45.88-
269PhosphorylationPKDDGIVYASLALSS
CCCCCEEEEEEEECC		6.6410660620
271PhosphorylationDDGIVYASLALSSST
CCCEEEEEEEECCCC		9.1123663014
275PhosphorylationVYASLALSSSTSPRA
EEEEEEECCCCCCCC		19.3523663014
276PhosphorylationYASLALSSSTSPRAP
EEEEEECCCCCCCCC		38.1923663014
277PhosphorylationASLALSSSTSPRAPP
EEEEECCCCCCCCCC		29.5423663014
278PhosphorylationSLALSSSTSPRAPPS
EEEECCCCCCCCCCC		44.7023663014
279PhosphorylationLALSSSTSPRAPPSH
EEECCCCCCCCCCCC		17.8423663014
296PhosphorylationLKSPQNETLYSVLKA
CCCCCCHHHHHHHCC		38.2528176486
298PhosphorylationSPQNETLYSVLKA--
CCCCHHHHHHHCC--		12.2628176486
299PhosphorylationPQNETLYSVLKA---
CCCHHHHHHHCC---		24.8828176486
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 PILRA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PILRA_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 PILRA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTN6_HUMANPTPN6physical
10903717
PTN11_HUMANPTPN11physical
10903717
PTN6_HUMANPTPN6physical
10660620
SRBS1_HUMANSORBS1physical
21988832
K319L_HUMANKIAA0319Lphysical
26186194
PODXL_HUMANPODXLphysical
26186194
NID2_HUMANNID2physical
26186194
TRI68_HUMANTRIM68physical
26186194
SAR1B_HUMANSAR1Bphysical
26186194
LRRT4_HUMANLRRTM4physical
26186194
B4GN3_HUMANB4GALNT3physical
26186194
B4GN4_HUMANB4GALNT4physical
26186194
LAMA4_HUMANLAMA4physical
26186194
PILRB_HUMANPILRBphysical
26186194
B4GN4_HUMANB4GALNT4physical
28514442
NID2_HUMANNID2physical
28514442
PILRB_HUMANPILRBphysical
28514442
TRI68_HUMANTRIM68physical
28514442
LAMA4_HUMANLAMA4physical
28514442
B4GN3_HUMANB4GALNT3physical
28514442
K319L_HUMANKIAA0319Lphysical
28514442
LRRT4_HUMANLRRTM4physical
28514442
PODXL_HUMANPODXLphysical
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 PILRA_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-100, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory