EDNRB_HUMAN - dbPTM
EDNRB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EDNRB_HUMAN
UniProt AC P24530
Protein Name Endothelin receptor type B {ECO:0000305}
Gene Name EDNRB {ECO:0000312|HGNC:HGNC:3180}
Organism Homo sapiens (Human).
Sequence Length 442
Subcellular Localization Cell membrane
Multi-pass membrane protein. internalized after activation by endothelins.
Protein Description Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system..
Protein Sequence MQPPPSLCGRALVALVLACGLSRIWGEERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCQGPIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIVIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDIITMDYKGSYLRICLLHPVQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTLYNQNDPNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS
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
5 (in isoform 3)Phosphorylation-46.7624719451
12 (in isoform 3)Phosphorylation-1.9224719451
14 (in isoform 3)Phosphorylation-7.8724719451
52PhosphorylationIMTPPTKTLWPKGSN
ECCCCCCCCCCCCCC		36.21-
59N-linked_GlycosylationTLWPKGSNASLARSL
CCCCCCCCHHHHHHC		42.06UniProtKB CARBOHYD
80PhosphorylationKGDRTAGSPPRTISP
CCCCCCCCCCCCCCC		29.30-
200PhosphorylationCALSIDRYRAVASWS
HHHHCHHHHHHHHHH		10.1214636059
205PhosphorylationDRYRAVASWSRIKGI
HHHHHHHHHHHCCCC		20.9814636059
305PhosphorylationCEMLRKKSGMQIALN
HHHHHHHCCCCHHHC		42.4014636059
400S-palmitoylationFKNCFKSCLCCWCQS
HHHHHHHHHHHHHHC		3.3011606208
402S-palmitoylationNCFKSCLCCWCQSFE
HHHHHHHHHHHHCHH		1.6711606208
403S-palmitoylationCFKSCLCCWCQSFEE
HHHHHHHHHHHCHHH		2.3511606208
405S-palmitoylationKSCLCCWCQSFEEKQ
HHHHHHHHHCHHHHC		1.1911606208
407PhosphorylationCLCCWCQSFEEKQSL
HHHHHHHCHHHHCCH		31.3329802988
413PhosphorylationQSFEEKQSLEEKQSC
HCHHHHCCHHHHHHH		49.1414636059
419PhosphorylationQSLEEKQSCLKFKAN
CCHHHHHHHHHHHCC		32.2714636059
430PhosphorylationFKANDHGYDNFRSSN
HHCCCCCCCCCCCCC		12.3224927040
435PhosphorylationHGYDNFRSSNKYSSS
CCCCCCCCCCCCCCC		33.8414636059
436PhosphorylationGYDNFRSSNKYSSS-
CCCCCCCCCCCCCC-		32.8429507054
439PhosphorylationNFRSSNKYSSS----
CCCCCCCCCCC----		20.3114636059
440PhosphorylationFRSSNKYSSS-----
CCCCCCCCCC-----		26.2214636059
441PhosphorylationRSSNKYSSS------
CCCCCCCCC------		36.6614636059
442PhosphorylationSSNKYSSS-------
CCCCCCCC-------		38.0014636059
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 EDNRB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
402CPalmitoylation

9261180
403CPalmitoylation

9261180
405CPalmitoylation

9261180
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 EDNRB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARBK1_HUMANADRBK1physical
9211925
CSN5_HUMANCOPS5physical
20034471
EDN3_HUMANEDN3physical
7509919
VPS8_HUMANVPS8physical
28514442
CA112_HUMANC1orf112physical
28514442
LCAP_HUMANLNPEPphysical
28514442
PXK_HUMANPXKphysical
28514442
EXOC2_HUMANEXOC2physical
28514442
ATM_HUMANATMphysical
28514442
INT12_HUMANINTS12physical
28514442
BIG1_HUMANARFGEF1physical
28514442
KNTC1_HUMANKNTC1physical
28514442
THADA_HUMANTHADAphysical
28514442
TYW1B_HUMANTYW1Bphysical
28514442
PDXD1_HUMANPDXDC1physical
28514442
TNPO2_HUMANTNPO2physical
28514442
ECM29_HUMANKIAA0368physical
28514442
BIG2_HUMANARFGEF2physical
28514442
BTAF1_HUMANBTAF1physical
28514442
XPO7_HUMANXPO7physical
28514442
EXOC5_HUMANEXOC5physical
28514442
AT2B2_HUMANATP2B2physical
28514442
EXOC1_HUMANEXOC1physical
28514442
CIP2A_HUMANKIAA1524physical
28514442
NRP1_HUMANNRP1physical
28514442
Drug and Disease Associations
Kegg Disease
H00054 Nasopharyngeal cancer
H00759 Waardenburg syndrome (WS)
H00823 ABCD syndrome
H00910 Hirschsprung disease (HD)
OMIM Disease
277580Waardenburg syndrome 4A (WS4A)
600155Hirschsprung disease 2 (HSCR2)
600501ABCD syndrome (ABCDS)
Kegg Drug
D01227 Bosentan hydrate (JAN); Bosentan (USAN); Tracleer (TN)
D07171 Sitaxentan (USAN/INN)
D07538 Bosentan (INN)
D08517 Sitaxentan sodium (USAN); Thelin (TN)
D10135 Macitentan (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EDNRB_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Palmitoylation of human endothelinB. Its critical role in G proteincoupling and a differential requirement for the cytoplasmic tail by Gprotein subtypes.";
Okamoto Y., Ninomiya H., Tanioka M., Sakamoto A., Miwa S., Masaki T.;
J. Biol. Chem. 272:21589-21596(1997).
Cited for: PALMITOYLATION AT CYS-402; CYS-403 AND CYS-405, AND MUTAGENESIS OFCYS-402; CYS-403 AND CYS-405.

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