DRD1_HUMAN - dbPTM
DRD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DRD1_HUMAN
UniProt AC P21728
Protein Name D(1A) dopamine receptor
Gene Name DRD1
Organism Homo sapiens (Human).
Sequence Length 446
Subcellular Localization Cell membrane
Multi-pass membrane protein. Endoplasmic reticulum membrane
Multi-pass membrane protein. Transport from the endoplasmic reticulum to the cell surface is regulated by interaction with DNAJC14..
Protein Description Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase..
Protein Sequence MRTLNTSAMDGTGLVVERDFSVRILTACFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVAEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPKAAFILISVAWTLSVLISFIPVQLSWHKAKPTSPSDGNATSLAETIDNCDSSLSRTYAISSSVISFYIPVAIMIVTYTRIYRIAQKQIRRIAALERAAVHAKNCQTTTGNGKPVECSQPESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFILNCILPFCGSGETQPFCIDSNTFDVFVWFGWANSSLNPIIYAFNADFRKAFSTLLGCYRLCPATNNAIETVSINNNGAAMFSSHHEPRGSISKECNLVYLIPHAVGSSEDLKKEEAAGIARPLEKLSPALSVILDYDTDVSLEKIQPITQNGQHPT
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
3Phosphorylation-----MRTLNTSAMD
-----CCCCCCCCCC		24.0626552605
5N-linked_Glycosylation---MRTLNTSAMDGT
---CCCCCCCCCCCC		31.23UniProtKB CARBOHYD
6Phosphorylation--MRTLNTSAMDGTG
--CCCCCCCCCCCCC		22.4526552605
7Phosphorylation-MRTLNTSAMDGTGL
-CCCCCCCCCCCCCE		22.1126552605
12PhosphorylationNTSAMDGTGLVVERD
CCCCCCCCCEEEECC		24.0726552605
56PhosphorylationIRFRHLRSKVTNFFV
HHHHHHHHHCCCCHH		37.53-
136PhosphorylationFRYERKMTPKAAFIL
CCCCCCCCHHHHHHH		25.36-
193PhosphorylationCDSSLSRTYAISSSV
CCHHHHHHHHCCHHH		17.5822210691
194PhosphorylationDSSLSRTYAISSSVI
CHHHHHHHHCCHHHH		10.7922210691
197PhosphorylationLSRTYAISSSVISFY
HHHHHHCCHHHHHHH		14.3722210691
223UbiquitinationRIYRIAQKQIRRIAA
HHHHHHHHHHHHHHH		38.38-
244PhosphorylationHAKNCQTTTGNGKPV
HHHCCCCCCCCCCCC		13.56-
245PhosphorylationAKNCQTTTGNGKPVE
HHCCCCCCCCCCCCC		31.85-
254PhosphorylationNGKPVECSQPESSFK
CCCCCCCCCCCCCCC		34.95-
258PhosphorylationVECSQPESSFKMSFK
CCCCCCCCCCCCCCH		48.00-
259PhosphorylationECSQPESSFKMSFKR
CCCCCCCCCCCCCHH		27.50-
263PhosphorylationPESSFKMSFKRETKV
CCCCCCCCCHHHHHH		28.36-
347S-palmitoylationAFSTLLGCYRLCPAT
HHHHHHHHHHHCCCC		1.4810618483
351S-palmitoylationLLGCYRLCPATNNAI
HHHHHHHCCCCCCEE		1.2710618483
360PhosphorylationATNNAIETVSINNNG
CCCCEEEEEEECCCC		17.2822817900
389PhosphorylationSKECNLVYLIPHAVG
CCCCCEEEEECCCCC		11.3327642862
428PhosphorylationSVILDYDTDVSLEKI
HHHHCCCCCCCHHHC		31.88-
431PhosphorylationLDYDTDVSLEKIQPI
HCCCCCCCHHHCCCC		33.35-
439PhosphorylationLEKIQPITQNGQHPT
HHHCCCCCCCCCCCC		23.75-
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
380SPhosphorylationKinasePKA-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DRD1_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 DRD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPG1_HUMANCOPG1physical
11893085
COPG2_HUMANCOPG2physical
11893085
HRH3_HUMANHRH3physical
19413572
RANB9_HUMANRANBP9physical
20395553
RBP10_HUMANRANBP10physical
20395553
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
D00059 Levodopa (JP16/USP/INN); Dopar (TN)
D00374 Tiotixene (JAN); Thiothixene (USP); Navane (TN)
D00502 Pergolide mesilate (JAN); Pergolide mesylate (USP); Permax (TN)
D00613 Fenoldopam mesylate (USP); Corlopam (TN)
D00633 Dopamine hydrochloride (JP16/USP); Actopamin (TN); Intropin (TN)
D01044 Flupentixol (INN); Flupenthixol; Depixol (TN)
D01742 Clebopride malate (JP16); Clast (TN)
D02004 Apomorphine hydrochloride hydrate (JAN); Apomorphine hydrochloride (USP); Apokyn (TN); Ixense (TN);
D02236 Flupentixol dihydrochloride (JAN)
D02612 Thiothixene hydrochloride (USP); Thiothixene dihydrochloride dihydrate; Tiotixene dihydrochloride; T
D02613 Clopenthixol (USAN)
D02641 Butaclamol hydrochloride (USAN)
D02676 Oxiperomide (USAN/INN)
D02775 Adrogolide hydrochloride (USAN)
D03494 Ciladopa hydrochloride (USAN); Tremerase (TN)
D03534 Clebopride (USAN); Cleboril (TN)
D03556 Zuclopenthixol (INN); Clopixol (TN)
D03891 Dopexamine (USAN/INN)
D03937 Ecopipam hydrochloride (USAN)
D04488 Ibopamine (USAN/INN)
D07460 Apomorphine (BAN); Uprima (TN)
D07870 Dopamine (INN); Medopa (TN)
D07976 Flupentixol decanoate; Fluanxol depot (TN)
D08057 Ibopamine hydrochloride; Scandine (TN)
D08339 Pergolide (INN); Permax (TN)
D08691 Zuclopenthixol acetate; Cisordinol-acutard (TN)
D08692 Zuclopenthixol decanoate; Clopixol depot (TN)
D08693 Zuclopenthixol dihydrochloride; Clopixol (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DRD1_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Palmitoylation occurs at cysteine 347 and cysteine 351 of thedopamine D(1) receptor.";
Jin H., Xie Z., George S.R., O'Dowd B.F.;
Eur. J. Pharmacol. 386:305-312(1999).
Cited for: PALMITOYLATION AT CYS-347 AND CYS-351.

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