NPY1R_HUMAN - dbPTM
NPY1R_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NPY1R_HUMAN
UniProt AC P25929
Protein Name Neuropeptide Y receptor type 1
Gene Name NPY1R
Organism Homo sapiens (Human).
Sequence Length 384
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is NPY > [Pro-34] PYY, PYY and [Leu-31, Pro-34] NPY > NPY (2-36) > [Ile-31, Gln-34] PP and PYY (3-36) > PP > NPY free acid..
Protein Sequence MNSTLFSQVENHSVHSNFSEKNAQLLAFENDDCHLPLAMIFTLALAYGAVIILGVSGNLALIIIILKQKEMRNVTNILIVNLSFSDLLVAIMCLPFTFVYTLMDHWVFGEAMCKLNPFVQCVSITVSIFSLVLIAVERHQLIINPRGWRPNNRHAYVGIAVIWVLAVASSLPFLIYQVMTDEPFQNVTLDAYKDKYVCFDQFPSDSHRLSYTTLLLVLQYFGPLCFIFICYFKIYIRLKRRNNMMDKMRDNKYRSSETKRINIMLLSIVVAFAVCWLPLTIFNTVFDWNHQIIATCNHNLLFLLCHLTAMISTCVNPIFYGFLNKNFQRDLQFFFNFCDFRSRDDDYETIAMSTMHTDVSKTSLKQASPVAFKKINNNDDNEKI
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
2N-linked_Glycosylation------MNSTLFSQV
------CCCCHHHHH
43.64UniProtKB CARBOHYD
11N-linked_GlycosylationTLFSQVENHSVHSNF
CHHHHHCCCCCCCCC
33.60UniProtKB CARBOHYD
17N-linked_GlycosylationENHSVHSNFSEKNAQ
CCCCCCCCCCHHHCE
29.59UniProtKB CARBOHYD
338S-palmitoylationLQFFFNFCDFRSRDD
HHHHHHHCCCCCCCC
5.19-
347PhosphorylationFRSRDDDYETIAMST
CCCCCCCHHHHHHHH
23.2027642862
349PhosphorylationSRDDDYETIAMSTMH
CCCCCHHHHHHHHCC
14.0629759185
353PhosphorylationDYETIAMSTMHTDVS
CHHHHHHHHCCCCCC
17.3528857561
354PhosphorylationYETIAMSTMHTDVSK
HHHHHHHHCCCCCCC
10.4127251275
357PhosphorylationIAMSTMHTDVSKTSL
HHHHHCCCCCCCCCH
27.5527251275
360PhosphorylationSTMHTDVSKTSLKQA
HHCCCCCCCCCHHHC
32.7828857561
362PhosphorylationMHTDVSKTSLKQASP
CCCCCCCCCHHHCCC
31.6128857561
363PhosphorylationHTDVSKTSLKQASPV
CCCCCCCCHHHCCCC
36.9928857561
368PhosphorylationKTSLKQASPVAFKKI
CCCHHHCCCCEEEEC
19.8825849741
383UbiquitinationNNNDDNEKI------
CCCCCCCCC------
61.0333845483

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 NPY1R_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NPY1R_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 NPY1R_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NPY1R_HUMAN !!

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 NPY1R_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND MASSSPECTROMETRY.

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