PACR_HUMAN - dbPTM
PACR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PACR_HUMAN
UniProt AC P41586
Protein Name Pituitary adenylate cyclase-activating polypeptide type I receptor
Gene Name ADCYAP1R1
Organism Homo sapiens (Human).
Sequence Length 468
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description This is a receptor for PACAP-27 and PACAP-38. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. May regulate the release of adrenocorticotropin, luteinizing hormone, growth hormone, prolactin, epinephrine, and catecholamine. May play a role in spermatogenesis and sperm motility. Causes smooth muscle relaxation and secretion in the gastrointestinal tract..
Protein Sequence MAGVVHVSLAALLLLPMAPAMHSDCIFKKEQAMCLEKIQRANELMGFNDSSPGCPGMWDNITCWKPAHVGEMVLVSCPELFRIFNPDQVWETETIGESDFGDSNSLDLSDMGVVSRNCTEDGWSEPFPHYFDACGFDEYESETGDQDYYYLSVKALYTVGYSTSLVTLTTAMVILCRFRKLHCTRNFIHMNLFVSFMLRAISVFIKDWILYAEQDSNHCFISTVECKAVMVFFHYCVVSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTVCVTVWATLRLYFDDTGCWDMNDSTALWWVIKGPVVGSIMVNFVLFIGIIVILVQKLQSPDMGGNESSIYLRLARSTLLLIPLFGIHYTVFAFSPENVSKRERLVFELGLGSFQGFVVAVLYCFLNGEVQAEIKRKWRSWKVNRYFAVDFKHRHPSLASSGVNGGTQLSILSKSSSQIRMSGLPADNLAT
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
48N-linked_GlycosylationANELMGFNDSSPGCP
HHHHCCCCCCCCCCC
42.39UniProtKB CARBOHYD
51 (in isoform 5)Phosphorylation-28.3330631047
60N-linked_GlycosylationGCPGMWDNITCWKPA
CCCCCCCCEEEECCC
18.89UniProtKB CARBOHYD
117N-linked_GlycosylationDMGVVSRNCTEDGWS
HCCEEEECCCCCCCC
29.56UniProtKB CARBOHYD
216PhosphorylationILYAEQDSNHCFIST
HHEECCCCCCEEEEE
28.3368707719
300N-linked_GlycosylationDTGCWDMNDSTALWW
CCCCCCCCCCEEEHH
37.29UniProtKB CARBOHYD
337PhosphorylationILVQKLQSPDMGGNE
HHHHHHCCCCCCCCH
33.05-
337 (in isoform 2)Phosphorylation-33.05-
374 (in isoform 4)Phosphorylation-69.9022210691
375N-linked_GlycosylationVFAFSPENVSKRERL
EEEECCCCCCHHHHH
46.90UniProtKB CARBOHYD
384 (in isoform 4)Phosphorylation-8.3122210691
395 (in isoform 2)Phosphorylation-3.2722210691
405 (in isoform 2)Phosphorylation-38.3022210691
434PhosphorylationDFKHRHPSLASSGVN
EECCCCHHHHHCCCC
30.3722210691
437PhosphorylationHRHPSLASSGVNGGT
CCCHHHHHCCCCCCC
32.6824719451
438PhosphorylationRHPSLASSGVNGGTQ
CCHHHHHCCCCCCCE
40.9525332170
444PhosphorylationSSGVNGGTQLSILSK
HCCCCCCCEEEEEEC
27.9522210691
447PhosphorylationVNGGTQLSILSKSSS
CCCCCEEEEEECCCC
16.2124719451
450PhosphorylationGTQLSILSKSSSQIR
CCEEEEEECCCCCEE
28.9025921289
452PhosphorylationQLSILSKSSSQIRMS
EEEEEECCCCCEECC
31.6725921289
453PhosphorylationLSILSKSSSQIRMSG
EEEEECCCCCEECCC
29.9625921289
454PhosphorylationSILSKSSSQIRMSGL
EEEECCCCCEECCCC
36.4025921289
459PhosphorylationSSSQIRMSGLPADNL
CCCCEECCCCCHHHC
27.5931437655
465 (in isoform 2)Phosphorylation-33.4124719451
468PhosphorylationLPADNLAT-------
CCHHHCCC-------
42.1668736991

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 PACR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PACR_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 PACR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLUS_HUMANCLUphysical
25451228

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PACR_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP