ADA1D_HUMAN - dbPTM
ADA1D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADA1D_HUMAN
UniProt AC P25100
Protein Name Alpha-1D adrenergic receptor
Gene Name ADRA1D
Organism Homo sapiens (Human).
Sequence Length 572
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description This alpha-adrenergic receptor mediates its effect through the influx of extracellular calcium..
Protein Sequence MTFRDLLSVSFEGPRPDSSAGGSSAGGGGGSAGGAAPSEGPAVGGVPGGAGGGGGVVGAGSGEDNRSSAGEPGSAGAGGDVNGTAAVGGLVVSAQGVGVGVFLAAFILMAVAGNLLVILSVACNRHLQTVTNYFIVNLAVADLLLSATVLPFSATMEVLGFWAFGRAFCDVWAAVDVLCCTASILSLCTISVDRYVGVRHSLKYPAIMTERKAAAILALLWVVALVVSVGPLLGWKEPVPPDERFCGITEEAGYAVFSSVCSFYLPMAVIVVMYCRVYVVARSTTRSLEAGVKRERGKASEVVLRIHCRGAATGADGAHGMRSAKGHTFRSSLSVRLLKFSREKKAAKTLAIVVGVFVLCWFPFFFVLPLGSLFPQLKPSEGVFKVIFWLGYFNSCVNPLIYPCSSREFKRAFLRLLRCQCRRRRRRRPLWRVYGHHWRASTSGLRQDCAPSSGDAPPGAPLALTALPDPDPEPPGTPEMQAPVASRRKPPSAFREWRLLGPFRRPTTQLRAKVSSLSHKIRAGGAQRAEAACAQRSEVEAVSLGVPHEVAEGATCQAYELADYSNLRETDI
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
2Phosphorylation------MTFRDLLSV
------CCHHHHEEC
27.6423663014
8PhosphorylationMTFRDLLSVSFEGPR
CCHHHHEECCCCCCC
24.0223663014
10PhosphorylationFRDLLSVSFEGPRPD
HHHHEECCCCCCCCC
17.7623663014
65N-linked_GlycosylationGAGSGEDNRSSAGEP
CCCCCCCCCCCCCCC
41.24UniProtKB CARBOHYD
82N-linked_GlycosylationAGAGGDVNGTAAVGG
CCCCCCCCCCCEECC
47.00UniProtKB CARBOHYD
201PhosphorylationRYVGVRHSLKYPAIM
CCCCHHHCCCCCCCC
18.9150563801
228PhosphorylationWVVALVVSVGPLLGW
HHHHHHHHHHHHCCC
17.5568705047
300PhosphorylationKRERGKASEVVLRIH
CCCCCCCCEEEEEEE
34.12-
323PhosphorylationDGAHGMRSAKGHTFR
CCCCCCCCCCCCCCH
25.99-
328PhosphorylationMRSAKGHTFRSSLSV
CCCCCCCCCHHHHHH
29.43-
331PhosphorylationAKGHTFRSSLSVRLL
CCCCCCHHHHHHHHH
31.29-
332PhosphorylationKGHTFRSSLSVRLLK
CCCCCHHHHHHHHHH
22.02-
334PhosphorylationHTFRSSLSVRLLKFS
CCCHHHHHHHHHHHC
13.7224719451
419S-palmitoylationAFLRLLRCQCRRRRR
HHHHHHHHHHHHHHH
4.52-
442PhosphorylationGHHWRASTSGLRQDC
CHHHCCCCCCCCCCC
26.32-
477PhosphorylationPDPEPPGTPEMQAPV
CCCCCCCCHHCCCCH
23.11-
486PhosphorylationEMQAPVASRRKPPSA
HCCCCHHHCCCCCHH
32.62-
492PhosphorylationASRRKPPSAFREWRL
HHCCCCCHHHHHHHH
48.87-
507PhosphorylationLGPFRRPTTQLRAKV
CCCCCCCCHHHHHHH
25.93-
515PhosphorylationTQLRAKVSSLSHKIR
HHHHHHHHHHHHHHH
25.5122468782
516PhosphorylationQLRAKVSSLSHKIRA
HHHHHHHHHHHHHHH
36.56-
518PhosphorylationRAKVSSLSHKIRAGG
HHHHHHHHHHHHHCH
25.36-
543PhosphorylationRSEVEAVSLGVPHEV
CCHHEEEECCCCHHH
26.84-

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
300SPhosphorylationKinaseGRK2P25098
PSP
300SPhosphorylationKinasePKCAP17252
PSP
323SPhosphorylationKinaseGRK2P25098
PSP
323SPhosphorylationKinasePKCAP17252
PSP
332SPhosphorylationKinaseGRK2P25098
PSP
332SPhosphorylationKinasePKCAP17252
PSP
334SPhosphorylationKinaseGRK2P25098
PSP
334SPhosphorylationKinasePKCAP17252
PSP
516SPhosphorylationKinaseGRK2P25098
PSP
516SPhosphorylationKinasePKCAP17252
PSP
518SPhosphorylationKinaseGRK2P25098
PSP
518SPhosphorylationKinasePKCAP17252
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADA1D_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 ADA1D_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTA_HUMANACTA2physical
18468998
AMFR_HUMANAMFRphysical
18468998
CKAP4_HUMANCKAP4physical
18468998
DTNA_HUMANDTNAphysical
18468998
ERLN1_HUMANERLIN1physical
18468998
ERLN2_HUMANERLIN2physical
18468998
GOPC_HUMANGOPCphysical
18468998
SNTB2_HUMANSNTB2physical
18468998
SNTB1_HUMANSNTB1physical
18468998
UTRO_HUMANUTRNphysical
18468998

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADA1D_HUMAN

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Related Literatures of Post-Translational Modification

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