dbPTM

PDE8A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PDE8A_HUMAN
UniProt AC	O60658
Protein Name	High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
Gene Name	PDE8A
Organism	Homo sapiens (Human).
Sequence Length	829
Subcellular Localization
Protein Description	Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. [PubMed: 18983167 May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development]
Protein Sequence	MGCAPSIHISERLVAEDAPSPAAPPLSSGGPRLPQGQKTAALPRTRGAGLLESELRDGSGKKVAVADVQFGPMRFHQDQLQVLLVFTKEDNQCNGFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRQLDAEALCRSIRSSKLSENTVIVGVVRRVDREELSVMPFISAGFTRRYVENPNIMACYNELLQLEFGEVRSQLKLRACNSVFTALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKAEKISECVQSDTHTDNQTGKHKDRRKGSLDVKAVASRATEVSSQRRHSSMARIHSMTIEAPITKVINIINAAQESSPMPVTEALDRVLEILRTTELYSPQFGAKDDDPHANDLVGGLMSDGLRRLSGNEYVLSTKNTQMVSSNIITPISLDDVPPRIARAMENEEYWDFDIFELEAATHNRPLIYLGLKMFARFGICEFLHCSESTLRSWLQIIEANYHSSNPYHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNAGSELAILYNDTAVLESHHAALAFQLTTGDDKCNIFKNMERNDYRTLRQGIIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKNQEVINTMLRTPENRTLIKRMLIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFVDLPDLMQHLDNNFKYWKGLDEMKLRNLRPPPE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MGCAPSIHISERL --CCCCCCCCHHHCH	14.31	18669648
20	Phosphorylation	LVAEDAPSPAAPPLS HHCCCCCCCCCCCCC	28.97	29255136
21 (in isoform 4)	Ubiquitination	-	31.23	21906983
27	Phosphorylation	SPAAPPLSSGGPRLP CCCCCCCCCCCCCCC	32.48	18691976
39	Phosphorylation	RLPQGQKTAALPRTR CCCCCCCCCCCCCCC	14.85	-
45	Phosphorylation	KTAALPRTRGAGLLE CCCCCCCCCCCCCHH	31.36	-
53	Phosphorylation	RGAGLLESELRDGSG CCCCCHHHCCCCCCC	41.73	30108239
59	Phosphorylation	ESELRDGSGKKVAVA HHCCCCCCCCEEEEE	52.29	25849741
153	Phosphorylation	SIRSSKLSENTVIVG HHHHCCCCCCEEEEE	32.32	-
181	Phosphorylation	PFISAGFTRRYVENP CEECCCCCHHHCCCC	17.20	24260401
239	Phosphorylation	SEDRFIQYANPAFET CHHHCHHHCCCHHHH	11.97	22210691
252	Phosphorylation	ETTMGYQSGELIGKE HHCCCCCCCCCCCCC	26.25	22210691
268 (in isoform 1)	Ubiquitination	-	49.09	21906983
268	Ubiquitination	GEVPINEKKADLLDT CCCCCCHHHHHHHHH	49.09	2190698
269	Ubiquitination	EVPINEKKADLLDTI CCCCCHHHHHHHHHH	40.74	-
284	Ubiquitination	NSCIRIGKEWQGIYY HHHHHHCCHHHCEEE	54.10	-
290	Phosphorylation	GKEWQGIYYAKKKNG CCHHHCEEEEEHHCC	12.28	27642862
291	Phosphorylation	KEWQGIYYAKKKNGD CHHHCEEEEEHHCCC	15.27	-
319	Phosphorylation	QGGKIRHYVSIIRVC CCCCEEEEEEEEEEC	6.00	-
359	Phosphorylation	HKDRRKGSLDVKAVA CCCCCCCCCCHHHHH	25.16	26657352
363	Ubiquitination	RKGSLDVKAVASRAT CCCCCCHHHHHHHHH	36.49	-
367	Phosphorylation	LDVKAVASRATEVSS CCHHHHHHHHHHHHH	18.82	-
370	Phosphorylation	KAVASRATEVSSQRR HHHHHHHHHHHHHHH	35.49	-
373	Phosphorylation	ASRATEVSSQRRHSS HHHHHHHHHHHHHHH	17.96	-
380	Phosphorylation	SSQRRHSSMARIHSM HHHHHHHHCHHHHCC	15.44	29759185
386	Phosphorylation	SSMARIHSMTIEAPI HHCHHHHCCEEECCH	18.43	29255136
388	Phosphorylation	MARIHSMTIEAPITK CHHHHCCEEECCHHH	20.76	29255136
394	Phosphorylation	MTIEAPITKVINIIN CEEECCHHHHHHHHH	20.42	29759185
406	Phosphorylation	IINAAQESSPMPVTE HHHHHHHCCCCCHHH	27.88	22210691
407	Phosphorylation	INAAQESSPMPVTEA HHHHHHCCCCCHHHH	25.19	17192257
412	Phosphorylation	ESSPMPVTEALDRVL HCCCCCHHHHHHHHH	15.07	22210691
428	Phosphorylation	ILRTTELYSPQFGAK HHHHCCCCCCCCCCC	16.45	29978859
429	Phosphorylation	LRTTELYSPQFGAKD HHHCCCCCCCCCCCC	25.50	29978859
435	Ubiquitination	YSPQFGAKDDDPHAN CCCCCCCCCCCCCHH	63.17	-
457	Phosphorylation	SDGLRRLSGNEYVLS HHHHHHHCCCCEEEE	37.45	25159151
461	Phosphorylation	RRLSGNEYVLSTKNT HHHCCCCEEEECCCC	15.64	30266825
464	Phosphorylation	SGNEYVLSTKNTQMV CCCCEEEECCCCEEE	27.56	30266825
465	Phosphorylation	GNEYVLSTKNTQMVS CCCEEEECCCCEEEE	24.93	25850435
468	Phosphorylation	YVLSTKNTQMVSSNI EEEECCCCEEEECCE	21.43	22617229
472	Phosphorylation	TKNTQMVSSNIITPI CCCCEEEECCEECCC	16.60	22617229
473	Phosphorylation	KNTQMVSSNIITPIS CCCEEEECCEECCCC	22.19	22617229
686	Ubiquitination	KFVNSINKPLATLEE HHHHHCCCCCCHHHH	39.47	-
699	Ubiquitination	EENGETDKNQEVINT HHCCCCCCCHHHHHH	68.87	-
706	Phosphorylation	KNQEVINTMLRTPEN CCHHHHHHHHCCCCH	13.37	27174698
710	Phosphorylation	VINTMLRTPENRTLI HHHHHHCCCCHHHHH	30.87	27174698
715	Phosphorylation	LRTPENRTLIKRMLI HCCCCHHHHHHHHHH	44.40	27174698
752	Phosphorylation	SEEYFSQTDEEKQQG CHHHHHCCHHHHHCC	44.15	-
820	Ubiquitination	WKGLDEMKLRNLRPP HCCCCHHCCCCCCCC	42.10	-

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
359	S	Phosphorylation	Kinase	PKACA	P17612	PSP
359	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
359	S	Phosphorylation		22673573
Phosphorylated at Ser-359 by PKA under elevated cAMP conditions, this enhances catalytic activity.

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 PDE8A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PDE8A_HUMAN !!

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
DB00920	Ketotifen

Regulatory Network of PDE8A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386 AND SER-457, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-407 AND SER-457,AND MASS SPECTROMETRY.	18691976 [Abstract]

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