HCN2_MOUSE - dbPTM
HCN2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HCN2_MOUSE
UniProt AC O88703
Protein Name Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
Gene Name Hcn2
Organism Mus musculus (Mouse).
Sequence Length 863
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..
Protein Sequence MDARGGGGRPGDSPGTTPAPGPPPPPPPPAPPQPQPPPAPPPNPTTPSHPESADEPGPRARLCSRDSACTPGAAKGGANGECGRGEPQCSPEGPARGPKVSFSCRGAASGPSAAEEAGSEEAGPAGEPRGSQASFLQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPSDCWVSINNMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLSSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPQVTSAIATLQQAVAMSFCPQVARPLVGPLALGSPRLVRRAPPGPLPPAASPGPPAASPPAAPSSPRAPRTSPYGVPGSPATRVGPALPARRLSRASRPLSASQPSLPHGVPAPSPAASARPASSSTPRLGPAPTARTAAPSPDRRDSASPGAASGLDPLDSARSRLSSNL
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
63S-palmitoylationPGPRARLCSRDSACT
CCCCCCCCCCCCCCC
2.3326546007
64PhosphorylationGPRARLCSRDSACTP
CCCCCCCCCCCCCCC
43.6525521595
67PhosphorylationARLCSRDSACTPGAA
CCCCCCCCCCCCCCC
24.9222324799
69S-palmitoylationLCSRDSACTPGAAKG
CCCCCCCCCCCCCCC
5.6626546007
70PhosphorylationCSRDSACTPGAAKGG
CCCCCCCCCCCCCCC
25.1922817900
82S-palmitoylationKGGANGECGRGEPQC
CCCCCCCCCCCCCCC
4.8326546007
89S-palmitoylationCGRGEPQCSPEGPAR
CCCCCCCCCCCCCCC
12.2526546007
90PhosphorylationGRGEPQCSPEGPARG
CCCCCCCCCCCCCCC
22.2725521595
99UbiquitinationEGPARGPKVSFSCRG
CCCCCCCCEEEEECC
54.02-
101PhosphorylationPARGPKVSFSCRGAA
CCCCCCEEEEECCCC
19.9829899451
103PhosphorylationRGPKVSFSCRGAASG
CCCCEEEEECCCCCC
8.7322324799
104S-palmitoylationGPKVSFSCRGAASGP
CCCEEEEECCCCCCC
4.3626546007
109PhosphorylationFSCRGAASGPSAAEE
EEECCCCCCCCHHHH
51.1824925903
112PhosphorylationRGAASGPSAAEEAGS
CCCCCCCCHHHHHCC
43.5722324799
119PhosphorylationSAAEEAGSEEAGPAG
CHHHHHCCCCCCCCC
39.0325521595
131PhosphorylationPAGEPRGSQASFLQR
CCCCCCCHHHHHHHH
24.6925159016
134PhosphorylationEPRGSQASFLQRQFG
CCCCHHHHHHHHHHH
20.8925159016
150UbiquitinationLLQPGVNKFSLRMFG
HHCCCCCHHHHHHHC
33.64-
152PhosphorylationQPGVNKFSLRMFGSQ
CCCCCHHHHHHHCCH
19.3729899451
160UbiquitinationLRMFGSQKAVEREQE
HHHHCCHHHHHHHHH
56.9827667366
291UbiquitinationGIDSEVYKTARALRI
CCCHHHHHHHHHHHH
40.6727667366
380N-linked_GlycosylationVSINNMVNHSWSELY
EEHHHHCCCCHHHHH
16.83-
459PhosphorylationKYKQVEQYMSFHKLP
HHHHHHHHHHHCCCC
4.92-
464UbiquitinationEQYMSFHKLPADFRQ
HHHHHHCCCCHHHHH
54.90-
472UbiquitinationLPADFRQKIHDYYEH
CCHHHHHHHHHHHHH
37.4427667366
476PhosphorylationFRQKIHDYYEHRYQG
HHHHHHHHHHHHHCC
9.1522817900
510UbiquitinationIVNFNCRKLVASMPL
HCCCCCCHHHHHCCC
49.90-
514PhosphorylationNCRKLVASMPLFANA
CCCHHHHHCCCCCCC
17.2926160508
527PhosphorylationNADPNFVTAMLTKLK
CCCCCHHHHHHHHCE
11.3826160508
531PhosphorylationNFVTAMLTKLKFEVF
CHHHHHHHHCEEEEE
22.6526160508
639UbiquitinationRLDRIGKKNSILLHK
HHHHHCCCCCCCEEE
51.1927667366
641PhosphorylationDRIGKKNSILLHKVQ
HHHCCCCCCCEEECC
24.4022324799
652PhosphorylationHKVQHDLSSGVFNNQ
EECCCCCCCCCCCCH
30.9729899451
653PhosphorylationKVQHDLSSGVFNNQE
ECCCCCCCCCCCCHH
46.3929899451
726PhosphorylationVGPLALGSPRLVRRA
CCCHHCCCCCCCCCC
14.0122817900
728MethylationPLALGSPRLVRRAPP
CHHCCCCCCCCCCCC
47.7324129315
743PhosphorylationGPLPPAASPGPPAAS
CCCCCCCCCCCCCCC
32.2824925903
750PhosphorylationSPGPPAASPPAAPSS
CCCCCCCCCCCCCCC
33.2625521595
756PhosphorylationASPPAAPSSPRAPRT
CCCCCCCCCCCCCCC
48.5325521595
757PhosphorylationSPPAAPSSPRAPRTS
CCCCCCCCCCCCCCC
19.8325521595
763PhosphorylationSSPRAPRTSPYGVPG
CCCCCCCCCCCCCCC
32.7520047950
764PhosphorylationSPRAPRTSPYGVPGS
CCCCCCCCCCCCCCC
19.8725521595
766PhosphorylationRAPRTSPYGVPGSPA
CCCCCCCCCCCCCCC
30.4424925903
771PhosphorylationSPYGVPGSPATRVGP
CCCCCCCCCCCCCCC
12.8025521595
774PhosphorylationGVPGSPATRVGPALP
CCCCCCCCCCCCCCC
29.3124925903
789PhosphorylationARRLSRASRPLSASQ
HHHHHCCCCCCCCCC
33.0629899451
793PhosphorylationSRASRPLSASQPSLP
HCCCCCCCCCCCCCC
28.6729899451
795PhosphorylationASRPLSASQPSLPHG
CCCCCCCCCCCCCCC
38.9720047950
798PhosphorylationPLSASQPSLPHGVPA
CCCCCCCCCCCCCCC
47.0729899451
807PhosphorylationPHGVPAPSPAASARP
CCCCCCCCCCHHCCC
29.3119060867
811PhosphorylationPAPSPAASARPASSS
CCCCCCHHCCCCCCC
27.2420415495
816PhosphorylationAASARPASSSTPRLG
CHHCCCCCCCCCCCC
27.7529899451
817PhosphorylationASARPASSSTPRLGP
HHCCCCCCCCCCCCC
40.1022324799
818PhosphorylationSARPASSSTPRLGPA
HCCCCCCCCCCCCCC
39.6822324799
819PhosphorylationARPASSSTPRLGPAP
CCCCCCCCCCCCCCC
17.8629899451
827PhosphorylationPRLGPAPTARTAAPS
CCCCCCCCCCCCCCC
30.7729899451
830PhosphorylationGPAPTARTAAPSPDR
CCCCCCCCCCCCCCC
25.3822324799
834PhosphorylationTARTAAPSPDRRDSA
CCCCCCCCCCCCCCC
34.4025521595
840PhosphorylationPSPDRRDSASPGAAS
CCCCCCCCCCCCHHC
28.9125521595
842PhosphorylationPDRRDSASPGAASGL
CCCCCCCCCCHHCCC
28.0225521595
847PhosphorylationSASPGAASGLDPLDS
CCCCCHHCCCCHHHH
39.0825521595
860PhosphorylationDSARSRLSSNL----
HHHHHHHHHCC----
18.9722807455

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
476YPhosphorylationKinaseSRCP12931
PSP
641SPhosphorylationKinasePRKG2Q13237
GPS
641SPhosphorylationKinasePRKG2Q61410
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
641SPhosphorylation

21347269

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HCN1_MOUSEHcn1physical
12928435

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HCN2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-119; SER-750 ANDSER-771, AND MASS SPECTROMETRY.

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