PDE8B_HUMAN - dbPTM
PDE8B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDE8B_HUMAN
UniProt AC O95263
Protein Name High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
Gene Name PDE8B
Organism Homo sapiens (Human).
Sequence Length 885
Subcellular Localization
Protein Description Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland..
Protein Sequence MGCAPSIHVSQSGVIYCRDSDESSSPRQTTSVSQGPAAPLPGLFVQTDAADAIPPSRASGPPSVARVRRARTELGSGSSAGSAAPAATTSRGRRRHCCSSAEAETQTCYTSVKQVSSAEVRIGPMRLTQDPIQVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASVLPLLHAGFNRRFMENSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGKIRHFVSLKKLCCTTDNNKQIHKIHRDSGDNSQTEPHSFRYKNRRKESIDVKSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLEILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHQSHSHLAMPITINDVPPCISQLLDNEESWDFNIFELEAITHKRPLVYLGLKVFSRFGVCEFLNCSETTLRAWFQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPMAAEIEGSDCECNPAGKNFPENQILIKRMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKSLRLPSDS
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
72PhosphorylationARVRRARTELGSGSS
HHHHHHHHCCCCCCC		34.2821712546
78PhosphorylationRTELGSGSSAGSAAP
HHCCCCCCCCCCCCC		20.7930576142
79PhosphorylationTELGSGSSAGSAAPA
HCCCCCCCCCCCCCC		39.9330576142
82PhosphorylationGSGSSAGSAAPAATT
CCCCCCCCCCCCCCC		22.4522210691
89PhosphorylationSAAPAATTSRGRRRH
CCCCCCCCCCCCCCC		16.2321712546
143PhosphorylationLIFAKEDSQSDGFWW
EEEECCCCCCCCCEE		32.45-
312UbiquitinationHKGELLGKELADLPK
CHHHHCCHHHHCCCC		49.91-
319UbiquitinationKELADLPKSDKNRAD
HHHHCCCCCCCCHHH		77.81-
336UbiquitinationDTINTCIKKGKEWQG
HHHHHHHHHCCCCCE		58.58-
350UbiquitinationGVYYARRKSGDSIQQ
EEEEEECCCCCCHHH		53.92-
351PhosphorylationVYYARRKSGDSIQQH
EEEEECCCCCCHHHH		46.1225159151
354PhosphorylationARRKSGDSIQQHVKI
EECCCCCCHHHHEEE		26.3120068231
360UbiquitinationDSIQQHVKITPVIGQ
CCHHHHEEEEEEECC		38.44-
362PhosphorylationIQQHVKITPVIGQGG
HHHHEEEEEEECCCC		13.0422817900
370UbiquitinationPVIGQGGKIRHFVSL
EEECCCCEEEEEEEE		43.31-
378UbiquitinationIRHFVSLKKLCCTTD
EEEEEEEECEEEECC		35.87-
388UbiquitinationCCTTDNNKQIHKIHR
EEECCCCCEEEEEEC		57.81-
392UbiquitinationDNNKQIHKIHRDSGD
CCCCEEEEEECCCCC		41.66-
397PhosphorylationIHKIHRDSGDNSQTE
EEEEECCCCCCCCCC		48.2629116813
401PhosphorylationHRDSGDNSQTEPHSF
ECCCCCCCCCCCCCC		43.1323312004
407PhosphorylationNSQTEPHSFRYKNRR
CCCCCCCCCCCCCCC		23.3329116813
410PhosphorylationTEPHSFRYKNRRKES
CCCCCCCCCCCCCCC		15.5928555341
421UbiquitinationRKESIDVKSISSRGS
CCCCCCCEECCCCCC		38.02-
428PhosphorylationKSISSRGSDAPSLQN
EECCCCCCCCHHHHC		29.5021130716
438 (in isoform 3)Phosphorylation-9.0927251275
438PhosphorylationPSLQNRRYPSMARIH
HHHHCCCCCCCCCCE		9.0929116813
440 (in isoform 3)Phosphorylation-19.0127251275
446PhosphorylationPSMARIHSMTIEAPI
CCCCCCEEEEEECCH		18.4329255136
446 (in isoform 3)Phosphorylation-18.4319276368
448PhosphorylationMARIHSMTIEAPITK
CCCCEEEEEECCHHH		20.7629255136
448 (in isoform 3)Phosphorylation-20.7627251275
454PhosphorylationMTIEAPITKVINIIN
EEEECCHHHHHHHHH		20.4224275569
454 (in isoform 3)Phosphorylation-20.4229116813
455UbiquitinationTIEAPITKVINIINA
EEECCHHHHHHHHHH		41.66-
462 (in isoform 3)Phosphorylation-10.5018691976
466 (in isoform 3)Phosphorylation-39.2629116813
467PhosphorylationINAAQENSPVTVAEA
HHHHHHCCCCCHHHH		21.7220068231
469 (in isoform 3)Phosphorylation-7.2527251275
470PhosphorylationAQENSPVTVAEALDR
HHHCCCCCHHHHHHH		19.8620068231
489PhosphorylationLRTTELYSPQLGTKD
HHHCCCCCCCCCCCC		20.8521130716
495UbiquitinationYSPQLGTKDEDPHTS
CCCCCCCCCCCCCCC		58.27-
502PhosphorylationKDEDPHTSDLVGGLM
CCCCCCCCHHHHHHH		26.3924719451
517PhosphorylationTDGLRRLSGNEYVFT
CCCHHHCCCCCEEEE		37.4525159151
521PhosphorylationRRLSGNEYVFTKNVH
HHCCCCCEEEECCCC		12.5925159151
637UbiquitinationFLGKERVKGSLDQLD
HHCHHHHCCCHHHHH		49.34-
701UbiquitinationQLTVKDTKCNIFKNI
EEEECCCCCCCCCCC		35.10-
713PhosphorylationKNIDRNHYRTLRQAI
CCCCCHHHHHHHHHH		14.6129978859
715PhosphorylationIDRNHYRTLRQAIID
CCCHHHHHHHHHHHH		21.0829978859
727PhosphorylationIIDMVLATEMTKHFE
HHHHHHHHHHHHHHH		23.3322210691
730PhosphorylationMVLATEMTKHFEHVN
HHHHHHHHHHHHHHH		18.3522210691
738UbiquitinationKHFEHVNKFVNSINK
HHHHHHHHHHHHCCC		49.99-
745UbiquitinationKFVNSINKPMAAEIE
HHHHHCCCCCCEEEC		34.20-
754PhosphorylationMAAEIEGSDCECNPA
CCEEECCCCCCCCCC		26.7125159151
773UbiquitinationPENQILIKRMMIKCA
CHHHHHHHHHHHHHH		30.69-
811UbiquitinationFAQTDEEKRQGLPVV
HHCCHHHHHCCCCEE		48.23-
869UbiquitinationADNYKHWKTLDDLKC
HHHHCCCCCHHHHCC		38.64-
870PhosphorylationDNYKHWKTLDDLKCK
HHHCCCCCHHHHCCC		30.17-
875UbiquitinationWKTLDDLKCKSLRLP
CCCHHHHCCCCCCCC		46.76-
878PhosphorylationLDDLKCKSLRLPSDS
HHHHCCCCCCCCCCC		28.3527251275
883PhosphorylationCKSLRLPSDS-----
CCCCCCCCCC-----		55.8930576142
885PhosphorylationSLRLPSDS-------
CCCCCCCC-------		46.5921712546
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

Oops, there are no upstream regulatory protein records of PDE8B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDE8B_HUMAN !!
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 PDE8B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PDE8B_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609161Striatal degeneration autosomal dominant (ADSD)
614190Primary pigmented nodular adrenocortical disease 3 (PPNAD3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00201Caffeine
DB00920Ketotifen
Regulatory Network of PDE8B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-517, AND MASSSPECTROMETRY.
"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-517, AND MASSSPECTROMETRY.

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