CRFR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CRFR1_HUMAN
• UniProt AC: P34998
• Protein Name: Corticotropin-releasing factor receptor 1
• Gene Name: CRHR1
• Organism: Homo sapiens (Human).
• Sequence Length: 444
• 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: MGGHPQLRLVKALLLLGLNPVSASLQDQHCESLSLASNISGLQCNASVDLIGTCWPRSPAGQLVVRPCPAFFYGVRYNTTNNGYRECLANGSWAARVNYSECQEILNEEKKSKVHYHVAVIINYLGHCISLVALLVAFVLFLRLRPGCTHWGDQADGALEVGAPWSGAPFQVRRSIRCLRNIIHWNLISAFILRNATWFVVQLTMSPEVHQSNVGWCRLVTAAYNYFHVTNFFWMFGEGCYLHTAIVLTYSTDRLRKWMFICIGWGVPFPIIVAWAIGKLYYDNEKCWFGKRPGVYTDYIYQGPMILVLLINFIFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDEVSRVVFIYFNSFLESFQGFFVSVFYCFLNSEVRSAIRKRWHRWQDKHSIRARVARAMSIPTSPTRVSFHSIKQSTAV

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
38	N-linked_Glycosylation	ESLSLASNISGLQCN HHHHHHHCCCCCCCC	27.17	UniProtKB CARBOHYD
45	N-linked_Glycosylation	NISGLQCNASVDLIG CCCCCCCCCEEEEEE	23.45	UniProtKB CARBOHYD
78	N-linked_Glycosylation	FFYGVRYNTTNNGYR CEEEEEEECCCCCHH	29.84	UniProtKB CARBOHYD
90	N-linked_Glycosylation	GYRECLANGSWAARV CHHHHHHCCCEEEEE	31.89	UniProtKB CARBOHYD
98	N-linked_Glycosylation	GSWAARVNYSECQEI CCEEEEECHHHHHHH	29.12	UniProtKB CARBOHYD
200	Phosphorylation	LRNATWFVVQLTMSP HHCCCEEEEEEECCC	1.70	14657255
330	Phosphorylation	LMTKLRASTTSETIQ HHHHHHCCCCHHHHH	26.28	23863939
331	Phosphorylation	MTKLRASTTSETIQY HHHHHCCCCHHHHHH	33.10	29978859
332	Phosphorylation	TKLRASTTSETIQYR HHHHCCCCHHHHHHH	23.28	29978859
333	Phosphorylation	KLRASTTSETIQYRK HHHCCCCHHHHHHHH	32.60	29978859
335	Phosphorylation	RASTTSETIQYRKAV HCCCCHHHHHHHHHH	17.10	29978859
338	Phosphorylation	TTSETIQYRKAVKAT CCHHHHHHHHHHHHH	15.38	29978859
415	Phosphorylation	HRWQDKHSIRARVAR HHHCCHHHHHHHHHH	21.36	24719451
425	Phosphorylation	ARVARAMSIPTSPTR HHHHHHHCCCCCCCE	25.16	29978859
428	Phosphorylation	ARAMSIPTSPTRVSF HHHHCCCCCCCEEEE	45.74	29978859
429	Phosphorylation	RAMSIPTSPTRVSFH HHHCCCCCCCEEEEE	20.94	24719451
431	Phosphorylation	MSIPTSPTRVSFHSI HCCCCCCCEEEEECC	43.39	29978859
434	Phosphorylation	PTSPTRVSFHSIKQS CCCCCEEEEECCCCC	17.60	29978859
437	Phosphorylation	PTRVSFHSIKQSTAV CCEEEEECCCCCCCC	29.48	29978859
441	Phosphorylation	SFHSIKQSTAV---- EEECCCCCCCC----	17.21	29978859
442	Phosphorylation	FHSIKQSTAV----- EECCCCCCCC-----	29.01	29978859

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
330	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
330	S	Phosphorylation	Phosphorylation at Ser-330 by PKA prevents maximal coupling to Gq-protein, and thereby negatively regulates downstream signaling.	14657255

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CRFR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UCN1_HUMAN	UCN	physical	8612563
GNAQ_HUMAN	GNAQ	physical	10598591
GNAS3_HUMAN	GNAS	physical	10598591
GNAS2_HUMAN	GNAS	physical	10598591
ALEX_HUMAN	GNAS	physical	10598591
GNAS1_HUMAN	GNAS	physical	10598591
GNAO_HUMAN	GNAO1	physical	10598591
GNAI1_HUMAN	GNAI1	physical	10598591
UCN1_RAT	Ucn	physical	11416224
CRF_HUMAN	CRH	physical	19124613

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• D03591: Corticorelin acetate (USAN); Xerecept (TN)
• D03592: Corticorelin ovine triflutate (USAN); Acthrel (TN)
• D03905: Corticorelin (human) (JAN); Xerecept; hCRH (TN)
• D09610: Emicerfont (USAN/INN)
• D09695: Verucerfont (USAN/INN)
• D10022: Pexacerfont (USAN/INN)
• DrugBank
• There are no disease associations of PTM sites.