5HT1A_HUMAN - dbPTM
5HT1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 5HT1A_HUMAN
UniProt AC P08908
Protein Name 5-hydroxytryptamine receptor 1A
Gene Name HTR1A
Organism Homo sapiens (Human).
Sequence Length 422
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling inhibits adenylate cyclase activity and activates a phosphatidylinositol-calcium second messenger system that regulates the release of Ca(2+) ions from intracellular stores. Plays a role in the regulation of 5-hydroxytryptamine release and in the regulation of dopamine and 5-hydroxytryptamine metabolism. Plays a role in the regulation of dopamine and 5-hydroxytryptamine levels in the brain, and thereby affects neural activity, mood and behavior. Plays a role in the response to anxiogenic stimuli..
Protein Sequence MDVLSPGQGNNTTSPPAPFETGGNTTGISDVTVSYQVITSLLLGTLIFCAVLGNACVVAAIALERSLQNVANYLIGSLAVTDLMVSVLVLPMAALYQVLNKWTLGQVTCDLFIALDVLCCTSSILHLCAIALDRYWAITDPIDYVNKRTPRRAAALISLTWLIGFLISIPPMLGWRTPEDRSDPDACTISKDHGYTIYSTFGAFYIPLLLMLVLYGRIFRAARFRIRKTVKKVEKTGADTRHGASPAPQPKKSVNGESGSRNWRLGVESKAGGALCANGAVRQGDDGAALEVIEVHRVGNSKEHLPLPSEAGPTPCAPASFERKNERNAEAKRKMALARERKTVKTLGIIMGTFILCWLPFFIVALVLPFCESSCHMPTLLGAIINWLGYSNSLLNPVIYAYFNKDFQNAFKKIIKCKFCRQ
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
10N-linked_GlycosylationVLSPGQGNNTTSPPA
CCCCCCCCCCCCCCC		34.48UniProtKB CARBOHYD
11N-linked_GlycosylationLSPGQGNNTTSPPAP
CCCCCCCCCCCCCCC		52.11UniProtKB CARBOHYD
24N-linked_GlycosylationAPFETGGNTTGISDV
CCCCCCCCCCCCCCC		35.49UniProtKB CARBOHYD
196PhosphorylationISKDHGYTIYSTFGA
ECCCCCCCHHHCCHH		20.3146155755
199PhosphorylationDHGYTIYSTFGAFYI
CCCCCHHHCCHHHHH		17.2646155749
205PhosphorylationYSTFGAFYIPLLLML
HHCCHHHHHHHHHHH		10.9021626883
215PhosphorylationLLLMLVLYGRIFRAA
HHHHHHHHHHHHHHH		9.2521626893
236O-linked_GlycosylationTVKKVEKTGADTRHG
HHHHHHHCCCCCCCC		24.8931492838
240PhosphorylationVEKTGADTRHGASPA
HHHCCCCCCCCCCCC		24.8346155761
240O-linked_GlycosylationVEKTGADTRHGASPA
HHHCCCCCCCCCCCC		24.8331492838
314PhosphorylationLPSEAGPTPCAPASF
CCCCCCCCCCCCHHH		30.04-
324AcetylationAPASFERKNERNAEA
CCHHHCCHHHHCHHH		56.837677601
334UbiquitinationRNAEAKRKMALARER
HCHHHHHHHHHHHHH		28.0217203973
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
314TPhosphorylationKinaseCDK5Q00535
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 5HT1A_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 5HT1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
5HT1D_HUMANHTR1Dphysical
11854302
S1PR3_HUMANS1PR3physical
11854302
GPR26_HUMANGPR26physical
11854302
S1PR1_HUMANS1PR1physical
11854302
FGFR1_HUMANFGFR1physical
22035699
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614674Periodic fever, menstrual cycle-dependent (PFMC)
Kegg Drug
D00283 Clozapine (JAN/USP/INN); Clozaril (TN)
D00679 Ergotamine tartrate (JP16/USP); Ergomar (TN)
D00680 Methylergometrine maleate (JP16); Methylergonovine maleate (USP); Methergine (TN)
D00681 Methysergide maleate (USP); Sansert (TN)
D00702 Buspirone hydrochloride (USP); Buspar (TN)
D01051 Spiperone (JAN/USAN); Spiropitan (TN)
D01163 Ergometrine maleate (JP16); Ergonovine maleate (USP); Ergometrine (TN)
D01164 Aripiprazole (JAN/USAN/INN); Abilify (TN)
D01358 Mianserin hydrochloride (JAN/USAN); Tetramide (TN)
D01462 Lisuride maleate (JAN)
D01992 Tandospirone citrate (JAN/USAN); SM 3997; Sediel (TN)
D02211 Dihydroergotamine mesilate (JP16); Dihydroergotamine mesylate (USP); Migranal (TN)
D02357 Methysergide (USAN/INN)
D02568 Flesinoxan (INN)
D02576 Eptapirone (INN)
D02577 Flibanserin (USAN/INN); Ectris (TN)
D02767 Adatanserin hydrochloride (USAN)
D02995 Asenapine maleate (USAN); Saphris (TN)
D03121 Binospirone mesylate (USAN)
D04314 Gepirone hydrochloride (USAN)
D04533 Indorenate hydrochloride (USAN)
D04611 Ipsapirone hydrochloride (USAN)
D04683 Lecozotan hydrochloride (USAN); Lecozotan SR; SRA 333
D04820 Lurasidone hydrochloride (JAN/USAN); SM 13496; Latuda (TN)
D05523 Pizotyline (USAN); Pizotifen (INN); Sandomigran (TN)
D05804 Sarizotan hydrochloride (USAN); EMD 128130
D06566 Bifeprunox (USAN/INN); OPC-4392
D06567 Bifeprunox mesylate (USAN)
D07218 Metergoline (INN)
D07593 Buspirone (INN); Gen-Buspirone (TN)
D07837 Dihydroergotamine (INN); Neomigran (TN)
D07838 Dihydroergotamine tartrate; Divegal (TN)
D07905 Ergometrine (INN)
D07906 Ergotamine (INN)
D08132 Lisuride (INN)
D08207 Methylergometrine (INN); Ergotyl (TN)
D08216 Mianserin (INN); Tolvon (TN)
D08255 Naratriptan (INN); Naramig (TN)
D08397 Pizotifen malate; Mosegor (TN); Sandomigran (TN)
D08561 Tandospirone (INN)
D09358 Naluzotan (USAN/INN)
D09359 Naluzotan hydrochloride (USAN)
D09366 Pardoprunox hydrochloride (USAN)
D09397 Pardoprunox (USAN/INN)
D09698 Vilazodone (USAN/INN)
D09699 Vilazodone hydrochloride (USAN); Viibryd (TN)
D10184 Vortioxetine (USAN)
D10185 Vortioxetine hydrobromide (USAN)
D10309 Brexpiprazole (USAN/INN)
D10355 Aripiprazole cavoxil (USAN)
D10364 Aripiprazole lauroxil (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 5HT1A_HUMAN

loading...

Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"The proteomic reactor facilitates the analysis of affinity-purifiedproteins by mass spectrometry: application for identifyingubiquitinated proteins in human cells.";
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M.,Haines D.S., Figeys D.;
J. Proteome Res. 6:298-305(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-334, AND MASSSPECTROMETRY.

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