PDE4D_HUMAN - dbPTM
PDE4D_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDE4D_HUMAN
UniProt AC Q08499
Protein Name cAMP-specific 3',5'-cyclic phosphodiesterase 4D
Gene Name PDE4D
Organism Homo sapiens (Human).
Sequence Length 809
Subcellular Localization Apical cell membrane . Cytoplasm. Membrane. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Found in the soluble fraction, associated with membranes, and associated with the cytoskeleton and the centrosome
Protein Description Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes..
Protein Sequence MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPPPPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRAMDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQANFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNFAALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRPMSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAPDDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPLDEQVEEEAVGEEEESQPEACVIDDRSPDT
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
2 (in isoform 10)Phosphorylation-56.2624719451
5 (in isoform 12)Phosphorylation-33.6729116813
5 (in isoform 6)Phosphorylation-33.6729116813
5 (in isoform 7)Phosphorylation-33.6729116813
6Phosphorylation--MEAEGSSAPARAG
--CCCCCCCCCCCCC		18.1620363803
6 (in isoform 12)Phosphorylation-18.1624719451
6 (in isoform 6)Phosphorylation-18.1624719451
6 (in isoform 7)Phosphorylation-18.1624719451
9 (in isoform 10)Phosphorylation-24.9930243723
9 (in isoform 12)Phosphorylation-24.9929116813
9 (in isoform 6)Phosphorylation-24.9929116813
9 (in isoform 7)Phosphorylation-24.9929116813
11 (in isoform 10)Phosphorylation-38.1226657352
11 (in isoform 12)Phosphorylation-38.1229116813
11 (in isoform 6)Phosphorylation-38.1229116813
11 (in isoform 7)Phosphorylation-38.1229116813
12 (in isoform 11)Phosphorylation-20.7124719451
13 (in isoform 2)Phosphorylation-30.5422617229
14PhosphorylationSAPARAGSGEGSDSA
CCCCCCCCCCCCCCC		32.4620363803
14 (in isoform 11)Phosphorylation-32.4628450419
16 (in isoform 11)Phosphorylation-58.1628450419
18PhosphorylationRAGSGEGSDSAGGAT
CCCCCCCCCCCCCCE		24.8820363803
19 (in isoform 11)Phosphorylation-54.0528348404
20PhosphorylationGSGEGSDSAGGATLK
CCCCCCCCCCCCEEC		30.4320363803
25PhosphorylationSDSAGGATLKAPKHL
CCCCCCCEECCCHHH		31.8722817900
28 (in isoform 9)Phosphorylation-22.8328450419
30 (in isoform 9)Phosphorylation-57.0724719451
48 (in isoform 6)Ubiquitination-8.27-
49 (in isoform 12)Phosphorylation-30.9622167270
49 (in isoform 6)Phosphorylation-30.9622167270
49 (in isoform 7)Phosphorylation-30.9622167270
51 (in isoform 12)Phosphorylation-5.2822167270
51 (in isoform 6)Phosphorylation-5.2822167270
51 (in isoform 7)Phosphorylation-5.2822167270
53 (in isoform 6)Ubiquitination-28.60-
54 (in isoform 2)Phosphorylation-15.3915131123
55 (in isoform 12)Phosphorylation-28.7322167270
55 (in isoform 6)Phosphorylation-28.7322167270
55 (in isoform 7)Phosphorylation-28.7322167270
59 (in isoform 12)Phosphorylation-61.4622167270
59 (in isoform 6)Phosphorylation-61.4622167270
59 (in isoform 7)Phosphorylation-61.4622167270
63 (in isoform 12)Phosphorylation-65.5022777824
63 (in isoform 6)Phosphorylation-65.5022777824
63 (in isoform 7)Phosphorylation-65.5022777824
73 (in isoform 12)Phosphorylation-18.3628674419
73 (in isoform 6)Phosphorylation-18.3628674419
73 (in isoform 7)Phosphorylation-18.3628674419
74 (in isoform 12)Phosphorylation-33.3325690035
74 (in isoform 6)Phosphorylation-33.3325690035
74 (in isoform 7)Phosphorylation-33.3325690035
78 (in isoform 6)Ubiquitination-49.25-
140 (in isoform 6)Ubiquitination-31.84-
142PhosphorylationGLKKSRMSWPSSFQG
CCCCCCCCCCCCCCC		34.4227499020
164PhosphorylationNGTSAGRSPLDPMTS
CCCCCCCCCCCCCCC		28.9726425664
170PhosphorylationRSPLDPMTSPGSGLI
CCCCCCCCCCCCEEE		36.8429632367
171PhosphorylationSPLDPMTSPGSGLIL
CCCCCCCCCCCEEEE		22.4729632367
174PhosphorylationDPMTSPGSGLILQAN
CCCCCCCCEEEEEEE		33.5329632367
185PhosphorylationLQANFVHSQRRESFL
EEEEECCCCCCHHHE		21.7830175587
190PhosphorylationVHSQRRESFLYRSDS
CCCCCCHHHEECCCC		20.8123927012
193PhosphorylationQRRESFLYRSDSDYD
CCCHHHEECCCCCCC		13.1723403867
195PhosphorylationRESFLYRSDSDYDLS
CHHHEECCCCCCCCC		28.1022167270
197PhosphorylationSFLYRSDSDYDLSPK
HHEECCCCCCCCCHH		39.0422167270
199PhosphorylationLYRSDSDYDLSPKSM
EECCCCCCCCCHHHH		23.8023927012
202PhosphorylationSDSDYDLSPKSMSRN
CCCCCCCCHHHHCCC		27.6416964243
205PhosphorylationDYDLSPKSMSRNSSI
CCCCCHHHHCCCCCC		25.9422817900
207PhosphorylationDLSPKSMSRNSSIAS
CCCHHHHCCCCCCCC		35.0922817900
210PhosphorylationPKSMSRNSSIASDIH
HHHHCCCCCCCCCCC		23.2420068231
211PhosphorylationKSMSRNSSIASDIHG
HHHCCCCCCCCCCCC		26.2329496963
214PhosphorylationSRNSSIASDIHGDDL
CCCCCCCCCCCCCCE		35.1120068231
224PhosphorylationHGDDLIVTPFAQVLA
CCCCEEECCHHHHHH		13.0022673903
232PhosphorylationPFAQVLASLRTVRNN
CHHHHHHHHHHHHHH		17.7724719451
239 (in isoform 2)Phosphorylation-19.85-
252PhosphorylationNLQDRAPSKRSPMCN
CCHHCCCCCCCCCCC		39.4530576142
255PhosphorylationDRAPSKRSPMCNQPS
HCCCCCCCCCCCCCC		22.2622167270
262PhosphorylationSPMCNQPSINKATIT
CCCCCCCCCCCCCCC		29.0929396449
267PhosphorylationQPSINKATITEEAYQ
CCCCCCCCCCHHHHH		30.0026330541
269PhosphorylationSINKATITEEAYQKL
CCCCCCCCHHHHHHH		24.3426330541
273PhosphorylationATITEEAYQKLASET
CCCCHHHHHHHHHHH		14.9526330541
278PhosphorylationEAYQKLASETLEELD
HHHHHHHHHHHHHHH		41.3624260401
299PhosphorylationETLQTRHSVSEMASN
HHHHHHHHHHHHHHH		24.8521406692
301PhosphorylationLQTRHSVSEMASNKF
HHHHHHHHHHHHHHH		25.3521406692
305PhosphorylationHSVSEMASNKFKRML
HHHHHHHHHHHHHHH		38.9630619164
307UbiquitinationVSEMASNKFKRMLNR
HHHHHHHHHHHHHHH		50.17-
309MethylationEMASNKFKRMLNREL
HHHHHHHHHHHHHHH		38.21-
317PhosphorylationRMLNRELTHLSEMSR
HHHHHHHHHHHHHHC		18.9323186163
323PhosphorylationLTHLSEMSRSGNQVS
HHHHHHHHCCCCHHH		21.1728555341
323 (in isoform 6)Sumoylation-21.17-
325PhosphorylationHLSEMSRSGNQVSEF
HHHHHHCCCCHHHHH		34.4921712546
330PhosphorylationSRSGNQVSEFISNTF
HCCCCHHHHHHHHHC		19.6121712546
334PhosphorylationNQVSEFISNTFLDKQ
CHHHHHHHHHCCCCC		34.8321712546
336PhosphorylationVSEFISNTFLDKQHE
HHHHHHHHCCCCCCC		20.8423312004
340UbiquitinationISNTFLDKQHEVEIP
HHHHCCCCCCCCCCC		56.56-
348PhosphorylationQHEVEIPSPTQKEKE
CCCCCCCCCCHHHHH		46.3629255136
350PhosphorylationEVEIPSPTQKEKEKK
CCCCCCCCHHHHHHH		57.5229255136
358UbiquitinationQKEKEKKKRPMSQIS
HHHHHHHCCCHHHHH		73.19-
362PhosphorylationEKKKRPMSQISGVKK
HHHCCCHHHHHHHHH		27.3529978859
365PhosphorylationKRPMSQISGVKKLMH
CCCHHHHHHHHHHHC		29.8729978859
373PhosphorylationGVKKLMHSSSLTNSS
HHHHHHCCCCCCCCC		13.9926657352
374PhosphorylationVKKLMHSSSLTNSSI
HHHHHCCCCCCCCCC		18.0625159151
375PhosphorylationKKLMHSSSLTNSSIP
HHHHCCCCCCCCCCC		42.0825159151
377PhosphorylationLMHSSSLTNSSIPRF
HHCCCCCCCCCCCCC		34.6928450419
379PhosphorylationHSSSLTNSSIPRFGV
CCCCCCCCCCCCCCC		25.1429978859
380PhosphorylationSSSLTNSSIPRFGVK
CCCCCCCCCCCCCCC		38.3920068231
387SumoylationSIPRFGVKTEQEDVL
CCCCCCCCCHHHHHH		46.88-
387SumoylationSIPRFGVKTEQEDVL
CCCCCCCCCHHHHHH		46.88-
387UbiquitinationSIPRFGVKTEQEDVL
CCCCCCCCCHHHHHH		46.88-
396UbiquitinationEQEDVLAKELEDVNK
HHHHHHHHHHHHHHH		59.68-
529PhosphorylationALMYNDSSVLENHHL
EEEECCCCHHHHCHH		33.3217081983
556UbiquitinationDIFQNLTKKQRQSLR
HHHHCCCHHHHHHHH		50.50-
576PhosphorylationIVLATDMSKHMNLLA
HHHHCCHHHHHHHHH		23.40-
579 (in isoform 2)Phosphorylation-4.31-
595PhosphorylationMVETKKVTSSGVLLL
HHHCCCCCCCCEEEE		26.5120068231
596PhosphorylationVETKKVTSSGVLLLD
HHCCCCCCCCEEEEC		28.2521815630
597PhosphorylationETKKVTSSGVLLLDN
HCCCCCCCCEEEECC		24.4520068231
606PhosphorylationVLLLDNYSDRIQVLQ
EEEECCHHHHHHHHH		27.02-
622PhosphorylationMVHCADLSNPTKPLQ
HHHHHCCCCCCCCHH		41.1129978859
625PhosphorylationCADLSNPTKPLQLYR
HHCCCCCCCCHHHHH		49.9329978859
657PhosphorylationRERGMEISPMCDKHN
HHHCCCCCCCCCCCC		8.0221815630
666PhosphorylationMCDKHNASVEKSQVG
CCCCCCCCCCHHHCC		35.8124719451
708PhosphorylationLEDNREWYQSTIPQS
HHHHHHHHHHCCCCC		6.4522167270
710PhosphorylationDNREWYQSTIPQSPS
HHHHHHHHCCCCCCC		16.7721815630
711PhosphorylationNREWYQSTIPQSPSP
HHHHHHHCCCCCCCC		22.5826657352
715PhosphorylationYQSTIPQSPSPAPDD
HHHCCCCCCCCCCCC		23.2226657352
717PhosphorylationSTIPQSPSPAPDDPE
HCCCCCCCCCCCCHH		38.6522167270
746PhosphorylationTLEEDGESDTEKDSG
EEEECCCCCCCCCCC		56.1926657352
748PhosphorylationEEDGESDTEKDSGSQ
EECCCCCCCCCCCCC		54.9729743597
752PhosphorylationESDTEKDSGSQVEED
CCCCCCCCCCCCCCC		51.9525849741
754PhosphorylationDTEKDSGSQVEEDTS
CCCCCCCCCCCCCCC		34.7023927012
760PhosphorylationGSQVEEDTSCSDSKT
CCCCCCCCCCCCCCE		34.6125159151
761PhosphorylationSQVEEDTSCSDSKTL
CCCCCCCCCCCCCEE		24.7621815630
763PhosphorylationVEEDTSCSDSKTLCT
CCCCCCCCCCCEEEE		44.6923927012
765PhosphorylationEDTSCSDSKTLCTQD
CCCCCCCCCEEEECC		15.9621955146
806PhosphorylationACVIDDRSPDT----
CEEECCCCCCC----		33.8422468782
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
12SPhosphorylationKinasePKA-FAMILY-GPS
13SPhosphorylationKinasePRKACAP17612
GPS
54SPhosphorylationKinasePRKACAP17612
GPS
126SPhosphorylationKinasePRKACAP17612
GPS
126SPhosphorylationKinasePRKACAP17612
GPS
126SPhosphorylationKinasePKA-FAMILY-GPS
150SPhosphorylationKinasePKA-FAMILY-GPS
191SPhosphorylationKinasePKA-FAMILY-GPS
578SPhosphorylationKinaseERK-SUBFAMILY-GPS
579SPhosphorylationKinaseMAPK1P28482
GPS
579SPhosphorylationKinaseMAPK3P27361
GPS
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:19372219
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
49SPhosphorylation

-
51SPhosphorylation

-
55SPhosphorylation

-
59SPhosphorylation

18669648
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 PDE4D_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDE4D_HUMANPDE4Dphysical
12387865
AKAP6_HUMANAKAP6physical
11296225
RACK1_HUMANGNB2L1physical
10329691
MDM2_HUMANMDM2physical
19372219
RACK1_HUMANGNB2L1physical
19372219
LIS1_HUMANPAFAH1B1physical
21652625
A4_HUMANAPPphysical
21832049
ARRB2_HUMANARRB2physical
14500724
ARRB1_HUMANARRB1physical
14500724
LYN_HUMANLYNphysical
10571082
BIN1_HUMANBIN1physical
22863883
HDGR2_HUMANHDGFRP2physical
22863883
TRAF1_HUMANTRAF1physical
25416956
COIL_HUMANCOILphysical
25416956
AKA12_HUMANAKAP12physical
16642035
PDE4B_HUMANPDE4Bphysical
28514442
RACK1_HUMANGNB2L1physical
12193273
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
17006457 states that association with stroke has to be considered with caution.Note=Genetic variations in PDE4D might be associated with susceptibility to stroke. PubMed
614613
Kegg Drug
D00227 Aminophylline (USP/INN); Somophyllin (TN); Theophylline ethylenediamine (TN)
D00371 Theophylline (JP16); Elixophyllin (TN); Quibron-t (TN); Theo-24 (TN); Theodur G (TN); Theolair (TN);
D00528 Anhydrous caffeine (JP16); Caffeine (USP); Anhydrous caffeine (TN)
D00718 Flavoxate hydrochloride (JP16/USAN); Urispas (TN)
D01220 Trapidil (JP16/INN); Rocornal (TN)
D01385 Ibudilast (JP16/INN); Ketas (TN)
D01453 Caffeine hydrate (JP16); Caffeine monohydrate; Caffeine (TN)
D01630 Propentofylline (JAN/INN)
D01704 Cilomilast (JAN/USAN/INN); Ariflo (TN)
D01712 Theophylline sodium acetate (JAN)
D01771 Proxyphylline (JAN/INN); Monophyllin (TN)
D01783 Rolipram (JAN/USAN/INN)
D02017 Choline theophylline (JAN); Oxtriphylline (USP); Choline theophyllinate (INN); Theophyline - choline
D02218 Papaverine hydrochloride (JP16/USP); Pavabid (TN)
D02985 Arofylline (USAN/INN)
D03898 Doxofylline (USAN/INN); Maxivent (TN)
D04185 Filaminast (USAN/INN)
D05429 Aminophylline hydrate (JP16)
D05474 Piclamilast (USAN/INN)
D05744 Roflumilast (JAN/USAN/INN); Daliresp (TN)
D06103 Theophylline (USP); Theophylline monohydrate; Accurbron (TN)
D06104 Theophylline sodium glycinate (USP); Asbron (TN)
D06132 Tibenelast sodium (USAN)
D06575 Catramilast (USAN/INN)
D07089 Moxaverine (INN)
D07425 Papaverine (BAN); Mesotina (TN)
D07439 Papaverine sulfate; Papaverine SAD (TN)
D07603 Caffeine citrate (USP); Cafcit (TN)
D07961 Flavoxate (INN); Bladuril (TN)
D08238 Moxaverine hydrochloride; Certonal (TN)
D08860 Apremilast (USAN)
D09020 Tofimilast (INN/USAN)
DrugBank
DB00131Adenosine monophosphate
DB00201Caffeine
DB00651Dyphylline
DB05266Ibudilast
DB01088Iloprost
DB00920Ketotifen
DB01656Roflumilast
Regulatory Network of PDE4D_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-348, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-20, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND THR-25, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-202, ANDMASS SPECTROMETRY.
Sumoylation
ReferencePubMed
"Selective SUMO modification of cAMP-specific phosphodiesterase-4D5(PDE4D5) regulates the functional consequences of phosphorylation byPKA and ERK.";
Li X., Vadrevu S., Dunlop A., Day J., Advant N., Troeger J.,Klussmann E., Jaffrey E., Hay R.T., Adams D.R., Houslay M.D.,Baillie G.S.;
Biochem. J. 428:55-65(2010).
Cited for: SUMOYLATION AT LYS-387 BY PIAS4.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory