PDE1C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PDE1C_HUMAN
• UniProt AC: Q14123
• Protein Name: Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
• Gene Name: PDE1C
• Organism: Homo sapiens (Human).
• Sequence Length: 709
• Protein Description: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a high affinity for both cAMP and cGMP..
• Protein Sequence: MESPTKEIEEFESNSLKYLQPEQIEKIWLRLRGLRKYKKTSQRLRSLVKQLERGEASVVDLKKNLEYAATVLESVYIDETRRLLDTEDELSDIQSDAVPSEVRDWLASTFTRQMGMMLRRSDEKPRFKSIVHAVQAGIFVERMYRRTSNMVGLSYPPAVIEALKDVDKWSFDVFSLNEASGDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTVHYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENHHLSAAYRLLQDDEEMNILINLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPEAIEKPKALSLMLHTADISHPAKAWDLHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKSTMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDETSQTGGTGQRRSSLNSISSSDAKRSGVKTSGSEGSAPINNSVISVDYKSFKATWTEVVHINRERWRAKVPKEEKAKKEAEEKARLAAEEQQKEMEAKSQAEEGASGKAEKKTSGETKNQVNGTRANKSDNPRGKNSKAEKSSGEQQQNGDFKDGKNKTDKKDHSNIGNDSKKTDGTKQRSHGSPAPSTSSTCRLTLPVIKPPLRHFKRPAYASSSYAPSVSKKTDEHPARYKMLDQRIKMKKIQNISHNWNRK

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
1	Acetylation	-------MESPTKEI -------CCCCCHHH	11.82	19369195
3	Phosphorylation	-----MESPTKEIEE -----CCCCCHHHHH	36.25	28355574
5	Phosphorylation	---MESPTKEIEEFE ---CCCCCHHHHHHH	51.06	22199227
13	Phosphorylation	KEIEEFESNSLKYLQ HHHHHHHHCCCCCCC	36.72	29514088
15	Phosphorylation	IEEFESNSLKYLQPE HHHHHHCCCCCCCHH	35.20	29514088
18 (in isoform 3)	Phosphorylation	-	18.83	22210691
18	Phosphorylation	FESNSLKYLQPEQIE HHHCCCCCCCHHHHH	18.83	-
20 (in isoform 3)	Phosphorylation	-	36.07	22210691
24 (in isoform 3)	Phosphorylation	-	5.77	22210691
25 (in isoform 3)	Phosphorylation	-	37.88	22210691
46	Phosphorylation	KTSQRLRSLVKQLER HHHHHHHHHHHHHHC	41.95	-
47 (in isoform 3)	Phosphorylation	-	4.51	27251275
49	Phosphorylation	QRLRSLVKQLERGEA HHHHHHHHHHHCCCC	55.23	27251275
49 (in isoform 3)	Phosphorylation	-	55.23	28348404
147	Phosphorylation	VERMYRRTSNMVGLS HHHHCHHCCCCCCCC	18.56	22199227
148	Phosphorylation	ERMYRRTSNMVGLSY HHHCHHCCCCCCCCC	22.55	22199227
154	Phosphorylation	TSNMVGLSYPPAVIE CCCCCCCCCCHHHHH	29.66	22199227
194	Phosphorylation	FIFYELLTRYDLISR HHHHHHHHHHCHHHH	39.55	19835603
196	Phosphorylation	FYELLTRYDLISRFK HHHHHHHHCHHHHCC	15.18	19835603
413	Phosphorylation	AELGLPFSPLCDRKS CHHCCCCCCCCCCCC	18.28	25159151
438	Phosphorylation	IDFIVEPTFTVLTDM CCEEECCCEEEHHHC	20.59	-
451	Phosphorylation	DMTEKIVSPLIDETS HCCHHHHHHHCCCCC	19.91	29514088
457	Phosphorylation	VSPLIDETSQTGGTG HHHHCCCCCCCCCCC	23.53	29514088
458	Phosphorylation	SPLIDETSQTGGTGQ HHHCCCCCCCCCCCC	24.56	29514088
460	Phosphorylation	LIDETSQTGGTGQRR HCCCCCCCCCCCCCH	37.03	29514088
463	Phosphorylation	ETSQTGGTGQRRSSL CCCCCCCCCCCHHHC	31.33	29514088
468	Phosphorylation	GGTGQRRSSLNSISS CCCCCCHHHCCCCCH	41.17	29514088
469	Phosphorylation	GTGQRRSSLNSISSS CCCCCHHHCCCCCHH	29.74	22617229
472	Phosphorylation	QRRSSLNSISSSDAK CCHHHCCCCCHHHHH	29.19	29514088
474	Phosphorylation	RSSLNSISSSDAKRS HHHCCCCCHHHHHHC	24.50	29514088
475	Phosphorylation	SSLNSISSSDAKRSG HHCCCCCHHHHHHCC	30.48	29514088
476	Phosphorylation	SLNSISSSDAKRSGV HCCCCCHHHHHHCCC	34.49	29514088
485	Phosphorylation	AKRSGVKTSGSEGSA HHHCCCCCCCCCCCC	35.59	28348404
486	Phosphorylation	KRSGVKTSGSEGSAP HHCCCCCCCCCCCCC	34.31	24076635
488	Phosphorylation	SGVKTSGSEGSAPIN CCCCCCCCCCCCCCC	38.25	24114839
491	Phosphorylation	KTSGSEGSAPINNSV CCCCCCCCCCCCCCE	27.16	24076635
503	Phosphorylation	NSVISVDYKSFKATW CCEEEEEHHHCEEEE	13.33	-
505	Phosphorylation	VISVDYKSFKATWTE EEEEEHHHCEEEEEE	26.25	-
529	Phosphorylation	RAKVPKEEKAKKEAE HCCCCHHHHHHHHHH	65.52	27251275
626	Phosphorylation	HSNIGNDSKKTDGTK CCCCCCCCCCCCCCC	39.80	30576142
644	Phosphorylation	HGSPAPSTSSTCRLT CCCCCCCCCCCEEEE	26.15	23532336
645	Phosphorylation	GSPAPSTSSTCRLTL CCCCCCCCCCEEEEE	28.17	23532336
667	Phosphorylation	RHFKRPAYASSSYAP CCCCCCCCCCCCCCC	15.08	26434776
669	Phosphorylation	FKRPAYASSSYAPSV CCCCCCCCCCCCCCC	13.72	26434776
670	Phosphorylation	KRPAYASSSYAPSVS CCCCCCCCCCCCCCC	21.13	26434776
675	Phosphorylation	ASSSYAPSVSKKTDE CCCCCCCCCCCCCCC	30.74	26091039
695	Methylation	KMLDQRIKMKKIQNI HHHHHHHHHHHHHCC	47.02	23644510
695	Trimethylation	KMLDQRIKMKKIQNI HHHHHHHHHHHHHCC	47.02	-

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

Oops, there are no upstream regulatory protein records of PDE1C_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PDE1C_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PDE1C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PDE1A_HUMAN	PDE1A	physical	28514442
PDE1B_HUMAN	PDE1B	physical	28514442
ERF3B_HUMAN	GSPT2	physical	28514442

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
• DB00201: Caffeine

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-469, AND MASSSPECTROMETRY.
PubMed: 19369195