dbPTM

ANPRA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ANPRA_HUMAN
UniProt AC	P16066
Protein Name	Atrial natriuretic peptide receptor 1
Gene Name	NPR1
Organism	Homo sapiens (Human).
Sequence Length	1061
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand..
Protein Sequence	MPGPRRPAGSRLRLLLLLLLPPLLLLLRGSHAGNLTVAVVLPLANTSYPWSWARVGPAVELALAQVKARPDLLPGWTVRTVLGSSENALGVCSDTAAPLAAVDLKWEHNPAVFLGPGCVYAAAPVGRFTAHWRVPLLTAGAPALGFGVKDEYALTTRAGPSYAKLGDFVAALHRRLGWERQALMLYAYRPGDEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSHYTRLLRTMPRKGRVIYICSSPDAFRTLMLLALEAGLCGEDYVFFHLDIFGQSLQGGQGPAPRRPWERGDGQDVSARQAFQAAKIITYKDPDNPEYLEFLKQLKHLAYEQFNFTMEDGLVNTIPASFHDGLLLYIQAVTETLAHGGTVTDGENITQRMWNRSFQGVTGYLKIDSSGDRETDFSLWDMDPENGAFRVVLNYNGTSQELVAVSGRKLNWPLGYPPPDIPKCGFDNEDPACNQDHLSTLEVLALVGSLSLLGILIVSFFIYRKMQLEKELASELWRVRWEDVEPSSLERHLRSAGSRLTLSGRGSNYGSLLTTEGQFQVFAKTAYYKGNLVAVKRVNRKRIELTRKVLFELKHMRDVQNEHLTRFVGACTDPPNICILTEYCPRGSLQDILENESITLDWMFRYSLTNDIVKGMLFLHNGAICSHGNLKSSNCVVDGRFVLKITDYGLESFRDLDPEQGHTVYAKKLWTAPELLRMASPPVRGSQAGDVYSFGIILQEIALRSGVFHVEGLDLSPKEIIERVTRGEQPPFRPSLALQSHLEELGLLMQRCWAEDPQERPPFQQIRLTLRKFNRENSSNILDNLLSRMEQYANNLEELVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAVIDNFDVYKVETIGDAYMVVSGLPVRNGRLHACEVARMALALLDAVRSFRIRHRPQEQLRLRIGIHTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGEALKIHLSSETKAVLEEFGGFELELRGDVEMKGKGKVRTYWLLGERGSSTRG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	N-linked_Glycosylation	LRGSHAGNLTVAVVL HCCCCCCCEEEEEEE	33.07	UniProtKB CARBOHYD
45	N-linked_Glycosylation	AVVLPLANTSYPWSW EEEEECCCCCCCCCH	36.92	UniProtKB CARBOHYD
67	Ubiquitination	ELALAQVKARPDLLP HHHHHHHHCCCCCCC	26.97	-
149	Ubiquitination	PALGFGVKDEYALTT CCCCCCCCCCCEEEC	45.26	-
212	N-linked_Glycosylation	MRVRDRLNITVDHLE HHHHHHCCCEECCHH	28.87	UniProtKB CARBOHYD
315	Ubiquitination	AAKIITYKDPDNPEY HCEEEEECCCCCHHH	54.88	-
327	Ubiquitination	PEYLEFLKQLKHLAY HHHHHHHHHHHHHHH	59.93	-
338	N-linked_Glycosylation	HLAYEQFNFTMEDGL HHHHHHCCEECCCCC	31.04	UniProtKB CARBOHYD
379	N-linked_Glycosylation	GTVTDGENITQRMWN CCCCCCCCHHHHHHH	48.41	UniProtKB CARBOHYD
386	N-linked_Glycosylation	NITQRMWNRSFQGVT CHHHHHHHHCCCCCC	22.00	UniProtKB CARBOHYD
427	N-linked_Glycosylation	FRVVLNYNGTSQELV EEEEEECCCCCEEEE	46.31	UniProtKB CARBOHYD
505	Phosphorylation	QLEKELASELWRVRW HHHHHHHHHHHCCCH	45.94	22590601
518	Phosphorylation	RWEDVEPSSLERHLR CHHHCCHHHHHHHHH	33.77	20873877
519	Phosphorylation	WEDVEPSSLERHLRS HHHCCHHHHHHHHHH	44.99	20873877
526	Phosphorylation	SLERHLRSAGSRLTL HHHHHHHHCCCCEEE	43.26	20873877
529	Phosphorylation	RHLRSAGSRLTLSGR HHHHHCCCCEEECCC	24.67	20873877
532	Phosphorylation	RSAGSRLTLSGRGSN HHCCCCEEECCCCCC	20.12	20873877
534	Phosphorylation	AGSRLTLSGRGSNYG CCCCEEECCCCCCCC	22.62	20873877
538	Phosphorylation	LTLSGRGSNYGSLLT EEECCCCCCCCCCCC	26.05	23663014
540	Phosphorylation	LSGRGSNYGSLLTTE ECCCCCCCCCCCCCC	15.13	23663014
542	Phosphorylation	GRGSNYGSLLTTEGQ CCCCCCCCCCCCCCE	15.17	23663014
545	Phosphorylation	SNYGSLLTTEGQFQV CCCCCCCCCCCEEEE	28.26	22817900
567	Ubiquitination	KGNLVAVKRVNRKRI CCCEEEEEEECHHHH	40.67	-
698	Ubiquitination	QGHTVYAKKLWTAPE CCCEEEEEEEECHHH	30.61	-
702	Phosphorylation	VYAKKLWTAPELLRM EEEEEEECHHHHHHH	42.65	24719451
711	Phosphorylation	PELLRMASPPVRGSQ HHHHHHCCCCCCCCC	22.01	46164507
749	Ubiquitination	EGLDLSPKEIIERVT ECCCCCHHHHHHHHH	59.16	-
809	Phosphorylation	RKFNRENSSNILDNL HHHCCCCCCCHHHHH	21.73	20873877
810	Phosphorylation	KFNRENSSNILDNLL HHCCCCCCCHHHHHH	39.20	20873877
818	Phosphorylation	NILDNLLSRMEQYAN CHHHHHHHHHHHHHH	32.52	23186163
835	Phosphorylation	EELVEERTQAYLEEK HHHHHHHHHHHHHHH	22.34	-
927	Phosphorylation	VETIGDAYMVVSGLP EEEECCEEEEECCCC	8.65	8391835
1041	Acetylation	LRGDVEMKGKGKVRT EECCEEECCCCEEEE	43.92	19828261
1045	Acetylation	VEMKGKGKVRTYWLL EEECCCCEEEEEEEE	31.84	19828271

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
529	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
529	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
529	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ANPRA_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 ANPRA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANF_HUMAN	NPPA	physical	1660465
ANFB_HUMAN	NPPB	physical	1660465
ANFC_HUMAN	NPPC	physical	1660465

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
D05147	Nesiritide (USAN/INN); Natrecor (TN)
D05148	Nesiritide citrate (USAN)
D10063	Cenderitide (USAN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ANPRA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Mass spectrometric identification of phosphorylation sites inguanylyl cyclase A and B."; Yoder A.R., Stone M.D., Griffin T.J., Potter L.R.; Biochemistry 49:10137-10145(2010). Cited for: PHOSPHORYLATION AT SER-519; SER-529; THR-532; SER-534 AND SER-538.	20977274 [Abstract]