HCN3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HCN3_MOUSE
• UniProt AC: O88705
• Protein Name: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3
• Gene Name: Hcn3
• Organism: Mus musculus (Mouse).
• Sequence Length: 779
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• Protein Description: Hyperpolarization-activated potassium channel. May also facilitate the permeation of sodium ions..
• Protein Sequence: MEEEARPAAGAGEAATPARETPPAAPAQARAASGGVPESAPEPKRRQLGTLLQPTVNKFSLRVFGSHKAVEIEQERVKSAGAWIIHPYSDFRFYWDLIMLLLMVGNLIVLPVGITFFKEENSPPWIVFNVLSDTFFLLDLVLNFRTGIVVEEGAEILLAPRAIRTRYLRTWFLVDLISSIPVDYIFLVVELEPRLDAEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPMLQDFPSDCWVSMNRMVNHSWGRQYSHALFKAMSHMLCIGYGQQAPVGMPDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADTRQRIHEYYEHRYQGKMFDEESILGELSEPLREEIINFTCRGLVAHMPLFAHADPSFVTAVLTKLRFEVFQPGDLVVREGSVGRKMYFIQHGLLSVLARGARDTRLTDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDHFNAVLEEFPMMRRAFETVAMDRLRRIGKKNSILQRKRSEPSPGSSGGVMEQHLVQHDRDMARGVRGLAPGTGARLSGKPVLWEPLVHAPLQAAAVTSNVAIALTHQRGPLPLSPDSPATLLARSARRSAGSPASPLVPVRAGPLLARGPWASTSRLPAPPARTLHASLSRTGRSQVSLLGPPPGGGARRLGPRGRPLSASQPSLPQRATGDGSPRRKGSGSERLPPSGLLAKPPGTVQPPRSSVPEPVTPRGPQISANM

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
33	Phosphorylation	PAQARAASGGVPESA CHHHHHHCCCCCCCC	34.79	29899451
290	N-linked_Glycosylation	VSMNRMVNHSWGRQY EHHHHHCCCCHHHHH	17.71	-
369	Phosphorylation	KYKQVEQYMSFHKLP HHHHHHHHHHHCCCC	4.92	-
465	Phosphorylation	GSVGRKMYFIQHGLL CCCCCEEHHHHHCHH	10.68	28059163
473	Phosphorylation	FIQHGLLSVLARGAR HHHHCHHHHHHHCCC	21.81	28059163
514	Phosphorylation	ADTYCRLYSLSVDHF CCCHHHHEEECHHHH	6.55	27357545
517	Phosphorylation	YCRLYSLSVDHFNAV HHHHEEECHHHHHHH	21.40	27357545
551	Phosphorylation	RRIGKKNSILQRKRS HHHCHHCCHHHHCCC	33.29	22324799
558	Phosphorylation	SILQRKRSEPSPGSS CHHHHCCCCCCCCCC	57.82	29899451
561	Phosphorylation	QRKRSEPSPGSSGGV HHCCCCCCCCCCCCH	37.53	29899451
565	Phosphorylation	SEPSPGSSGGVMEQH CCCCCCCCCCHHHHH	45.54	29899451
633	Phosphorylation	QRGPLPLSPDSPATL CCCCCCCCCCCHHHH	25.40	25521595
636	Phosphorylation	PLPLSPDSPATLLAR CCCCCCCCHHHHHHH	21.59	22324799
639	Phosphorylation	LSPDSPATLLARSAR CCCCCHHHHHHHHHH	26.20	29899451
648	Phosphorylation	LARSARRSAGSPASP HHHHHHHCCCCCCCC	31.28	22807455
651	Phosphorylation	SARRSAGSPASPLVP HHHHCCCCCCCCCCC	19.60	22817900
654	Phosphorylation	RSAGSPASPLVPVRA HCCCCCCCCCCCCCC	23.35	22817900
683	Phosphorylation	LPAPPARTLHASLSR CCCCCCCHHHEECCC	25.63	26026062
687	Phosphorylation	PARTLHASLSRTGRS CCCHHHEECCCCCCC	19.01	22817900
691	Phosphorylation	LHASLSRTGRSQVSL HHEECCCCCCCCEEE	33.30	26026062
718	Phosphorylation	GPRGRPLSASQPSLP CCCCCCCCCCCCCCC	28.67	20415495
720	Phosphorylation	RGRPLSASQPSLPQR CCCCCCCCCCCCCCC	38.97	20415495
723	Phosphorylation	PLSASQPSLPQRATG CCCCCCCCCCCCCCC	45.07	20415495
769	Phosphorylation	SSVPEPVTPRGPQIS CCCCCCCCCCCCCCC	20.27	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of HCN3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HCN3_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of HCN3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KCTD3_MOUSE	Kctd3	physical	23382386
PEX5R_MOUSE	Pex5l	physical	23382386

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633, AND MASSSPECTROMETRY.
PubMed: 17114649