CRFR1_RAT - dbPTM
CRFR1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRFR1_RAT
UniProt AC P35353
Protein Name Corticotropin-releasing factor receptor 1
Gene Name Crhr1
Organism Rattus norvegicus (Rat).
Sequence Length 415
Subcellular Localization Cell membrane
Multi-pass membrane protein. Endosome. Agonist-binding promotes endocytosis..
Protein Description G-protein coupled receptor for CRH (corticotropin-releasing factor) and UCN (urocortin). Has high affinity for CRH and UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels. Inhibits the activity of the calcium channel CACNA1H. Required for normal embryonic development of the adrenal gland and for normal hormonal responses to stress. Plays a role in the response to anxiogenic stimuli..
Protein Sequence MGRRPQLRLVKALLLLGLNPVSTSLQDQRCENLSLTSNVSGLQCNASVDLIGTCWPRSPAGQLVVRPCPAFFYGVRYNTTNNGYRECLANGSWAARVNYSECQEILNEEKKSKVHYHVAVIINYLGHCISLVALLVAFVLFLRLRSIRCLRNIIHWNLISAFILRNATWFVVQLTVSPEVHQSNVAWCRLVTAAYNYFHVTNFFWMFGEGCYLHTAIVLTYSTDRLRKWMFVCIGWGVPFPIIVAWAIGKLHYDNEKCWFGKRPGVYTDYIYQGPMILVLLINFIFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDEVSRVVFIYFNSFLESFQGFFVSVFYCFLNSEVRSAIRKRWRRWQDKHSIRARVARAMSIPTSPTRVSFHSIKQSTAV
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
38N-linked_GlycosylationENLSLTSNVSGLQCN
CCCCCCCCCCCCCCC
27.0911567096
45N-linked_GlycosylationNVSGLQCNASVDLIG
CCCCCCCCCEEEEEE
23.4511567096
78N-linked_GlycosylationFFYGVRYNTTNNGYR
CEEEEEEECCCCCHH
29.8411567096
90N-linked_GlycosylationGYRECLANGSWAARV
CHHHHHHCCCEEEEE
31.8911567096
98N-linked_GlycosylationGSWAARVNYSECQEI
CCEEEEECHHHHHHH
29.1211567096
301PhosphorylationLMTKLRASTTSETIQ
HHHHHHCCCCHHHHH
26.28-
396PhosphorylationARVARAMSIPTSPTR
HHHHHHHCCCCCCCE
25.1628432305
399PhosphorylationARAMSIPTSPTRVSF
HHHHCCCCCCCEEEE
45.7428432305
400PhosphorylationRAMSIPTSPTRVSFH
HHHCCCCCCCEEEEE
20.9428432305
402PhosphorylationMSIPTSPTRVSFHSI
HCCCCCCCEEEEECC
43.3928432305
405PhosphorylationPTSPTRVSFHSIKQS
CCCCCEEEEECCCCC
17.6028432305
408PhosphorylationPTRVSFHSIKQSTAV
CCEEEEECCCCCCCC
29.4817913459

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
301SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
301SPhosphorylation

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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 CRFR1_RAT !!

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

Oops, there are no PPI records of CRFR1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRFR1_RAT

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Functional and protein chemical characterization of the N-terminaldomain of the rat corticotropin-releasing factor receptor 1.";
Hofmann B.A., Sydow S., Jahn O., van Werven L., Liepold T., Eckart K.,Spiess J.;
Protein Sci. 10:2050-2062(2001).
Cited for: DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-38; ASN-45; ASN-78; ASN-90AND ASN-98.

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