dbPTM

HCN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HCN2_HUMAN
UniProt AC	Q9UL51
Protein Name	Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
Gene Name	HCN2
Organism	Homo sapiens (Human).
Sequence Length	889
Subcellular Localization	Cell membrane Multi-pass membrane protein .
Protein Description	Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current. Modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages (By similarity)..
Protein Sequence	MDARGGGGRPGESPGATPAPGPPPPPPPAPPQQQPPPPPPPAPPPGPGPAPPQHPPRAEALPPEAADEGGPRGRLRSRDSSCGRPGTPGAASTAKGSPNGECGRGEPQCSPAGPEGPARGPKVSFSCRGAASGPAPGPGPAEEAGSEEAGPAGEPRGSQASFMQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPRNCWVSINGMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLNSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPPQVTSAIATLQQAAAMSFCPQVARPLVGPLALGSPRLVRRPPPGPAPAAASPGPPPPASPPGAPASPRAPRTSPYGGLPAAPLAGPALPARRLSRASRPLSASQPSLPHGAPGPAASTRPASSSTPRLGPTPAARAAAPSPDRRDSASPGAAGGLDPQDSARSRLSSNL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
80	Phosphorylation	GRLRSRDSSCGRPGT CCCCCCCCCCCCCCC	26.81	27732954
81	Phosphorylation	RLRSRDSSCGRPGTP CCCCCCCCCCCCCCC	25.53	27732954
87	Phosphorylation	SSCGRPGTPGAASTA CCCCCCCCCCHHHCC	22.64	23312004
92	Phosphorylation	PGTPGAASTAKGSPN CCCCCHHHCCCCCCC	28.50	-
93	Phosphorylation	GTPGAASTAKGSPNG CCCCHHHCCCCCCCC	27.88	17929957
126	Phosphorylation	RGPKVSFSCRGAASG CCCCEEEEECCCCCC	8.73	22210691
132	Phosphorylation	FSCRGAASGPAPGPG EEECCCCCCCCCCCC	44.79	22210691
146	Phosphorylation	GPAEEAGSEEAGPAG CCHHHCCCCCCCCCC	39.03	24076635
158	Phosphorylation	PAGEPRGSQASFMQR CCCCCCCHHHHHHHH	24.69	22210691
161	Phosphorylation	EPRGSQASFMQRQFG CCCCHHHHHHHHHHH	17.39	-
177	Ubiquitination	LLQPGVNKFSLRMFG HHCCCCCHHHHHHHC	33.64	22817900
179	Phosphorylation	QPGVNKFSLRMFGSQ CCCCCHHHHHHHCCH	19.37	25394399
185	Phosphorylation	FSLRMFGSQKAVERE HHHHHHCCHHHHHHH	19.76	-
187	Ubiquitination	LRMFGSQKAVEREQE HHHHCCHHHHHHHHH	56.98	33845483
286	Phosphorylation	PEKIKKKYLRTWFVV HHHHHHHHCHHHHHH	15.42	27251275
289	Phosphorylation	IKKKYLRTWFVVDFV HHHHHCHHHHHHCHH	22.21	27251275
297	Phosphorylation	WFVVDFVSSIPVDYI HHHHCHHHCCCCCEE	23.65	27251275
298	Phosphorylation	FVVDFVSSIPVDYIF HHHCHHHCCCCCEEE	26.13	27251275
303	Phosphorylation	VSSIPVDYIFLIVEK HHCCCCCEEEEEEEC	8.20	27251275
314	Phosphorylation	IVEKGIDSEVYKTAR EEECCCCHHHHHHHH	27.35	27251275
318	Ubiquitination	GIDSEVYKTARALRI CCCHHHHHHHHHHHH	40.67	33845483
407	N-linked_Glycosylation	VSINGMVNHSWSELY EEECHHCCCCHHHHH	18.00	UniProtKB CARBOHYD
476	Phosphorylation	LDSSRRQYQEKYKQV HHHHHHHHHHHHHHH	19.48	-
480	Phosphorylation	RRQYQEKYKQVEQYM HHHHHHHHHHHHHHH	13.10	17977941
486	Phosphorylation	KYKQVEQYMSFHKLP HHHHHHHHHHHCCCC	4.92	-
576	Phosphorylation	DYIIREGTIGKKMYF CEEEEECCCCCEEEE	23.08	22817900
582	Phosphorylation	GTIGKKMYFIQHGVV CCCCCEEEEEECCEE	13.35	22817900
602	Phosphorylation	GNKEMKLSDGSYFGE CCCEEECCCCCCCCE	34.11	24719451
606	Phosphorylation	MKLSDGSYFGEICLL EECCCCCCCCEEEEE	22.57	24719451
614	Phosphorylation	FGEICLLTRGRRTAS CCEEEEEECCCCCEE	20.37	24719451
668	Phosphorylation	DRIGKKNSILLHKVQ HHHCCCCCHHHHHCC	24.40	-
697	Phosphorylation	IIQEIVKYDREMVQQ HHHHHHHHCHHHHHH	14.89	-
754	Phosphorylation	VGPLALGSPRLVRRP CCCHHCCCCCEECCC	14.01	29255136
756	Methylation	PLALGSPRLVRRPPP CHHCCCCCEECCCCC	47.73	-
771	Phosphorylation	GPAPAAASPGPPPPA CCCCCCCCCCCCCCC	26.18	21712546
779	Phosphorylation	PGPPPPASPPGAPAS CCCCCCCCCCCCCCC	37.08	21712546
786	Phosphorylation	SPPGAPASPRAPRTS CCCCCCCCCCCCCCC	17.54	27732954
792	Phosphorylation	ASPRAPRTSPYGGLP CCCCCCCCCCCCCCC	32.75	18669648
792	O-linked_Glycosylation	ASPRAPRTSPYGGLP CCCCCCCCCCCCCCC	32.75	28657654
793	Phosphorylation	SPRAPRTSPYGGLPA CCCCCCCCCCCCCCC	19.87	25332170
795	Phosphorylation	RAPRTSPYGGLPAAP CCCCCCCCCCCCCCC	24.48	18669648
826	Phosphorylation	PLSASQPSLPHGAPG CCCCCCCCCCCCCCC	47.07	25332170
837	Phosphorylation	GAPGPAASTRPASSS CCCCCCHHCCCCCCC	27.36	25332170
842	Phosphorylation	AASTRPASSSTPRLG CHHCCCCCCCCCCCC	27.75	25332170
851	Phosphorylation	STPRLGPTPAARAAA CCCCCCCCHHHHHCC	24.62	24275569
860	Phosphorylation	AARAAAPSPDRRDSA HHHHCCCCCCCCCCC	34.40	23312004
866	Phosphorylation	PSPDRRDSASPGAAG CCCCCCCCCCCCCCC	28.91	24076635
868	Phosphorylation	PDRRDSASPGAAGGL CCCCCCCCCCCCCCC	28.02	28555341
880	Phosphorylation	GGLDPQDSARSRLSS CCCCHHHHHHHHHHH	21.97	30243723

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
668	S	Phosphorylation	Kinase	PRKG2	Q13237	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
668	S	Phosphorylation		-
Phosphorylation at Ser-668 by PRKG2 shifts the voltage-dependence to more negative voltages, hence counteracting the stimulatory effect of cGMP on gating.

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 HCN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HCN4_HUMAN	HCN4	physical	12928435
HCN2_HUMAN	HCN2	physical	12034718
HCN1_HUMAN	HCN1	physical	12034718

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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HCN2_HUMAN

Related Literatures of Post-Translational Modification

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