PDE3B_HUMAN - dbPTM
PDE3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDE3B_HUMAN
UniProt AC Q13370
Protein Name cGMP-inhibited 3',5'-cyclic phosphodiesterase B
Gene Name PDE3B
Organism Homo sapiens (Human).
Sequence Length 1112
Subcellular Localization Membrane
Multi-pass membrane protein .
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. May play a role in fat metabolism. Regulates cAMP binding of RAPGEF3. Through simultaneous binding to RAPGEF3 and PIK3R6 assembles a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis..
Protein Sequence MRRDERDAKAMRSLQPPDGAGSPPESLRNGYVKSCVSPLRQDPPRGFFFHLCRFCNVELRPPPASPQQPRRCSPFCRARLSLGALAAFVLALLLGAEPESWAAGAAWLRTLLSVCSHSLSPLFSIACAFFFLTCFLTRTKRGPGPGRSCGSWWLLALPACCYLGDFLVWQWWSWPWGDGDAGSAAPHTPPEAAAGRLLLVLSCVGLLLTLAHPLRLRHCVLVLLLASFVWWVSFTSLGSLPSALRPLLSGLVGGAGCLLALGLDHFFQIREAPLHPRLSSAAEEKVPVIRPRRRSSCVSLGETAASYYGSCKIFRRPSLPCISREQMILWDWDLKQWYKPHYQNSGGGNGVDLSVLNEARNMVSDLLTDPSLPPQVISSLRSISSLMGAFSGSCRPKINPLTPFPGFYPCSEIEDPAEKGDRKLNKGLNRNSLPTPQLRRSSGTSGLLPVEQSSRWDRNNGKRPHQEFGISSQGCYLNGPFNSNLLTIPKQRSSSVSLTHHVGLRRAGVLSSLSPVNSSNHGPVSTGSLTNRSPIEFPDTADFLNKPSVILQRSLGNAPNTPDFYQQLRNSDSNLCNSCGHQMLKYVSTSESDGTDCCSGKSGEEENIFSKESFKLMETQQEEETEKKDSRKLFQEGDKWLTEEAQSEQQTNIEQEVSLDLILVEEYDSLIEKMSNWNFPIFELVEKMGEKSGRILSQVMYTLFQDTGLLEIFKIPTQQFMNYFRALENGYRDIPYHNRIHATDVLHAVWYLTTRPVPGLQQIHNGCGTGNETDSDGRINHGRIAYISSKSCSNPDESYGCLSSNIPALELMALYVAAAMHDYDHPGRTNAFLVATNAPQAVLYNDRSVLENHHAASAWNLYLSRPEYNFLLHLDHVEFKRFRFLVIEAILATDLKKHFDFLAEFNAKANDVNSNGIEWSNENDRLLVCQVCIKLADINGPAKVRDLHLKWTEGIVNEFYEQGDEEANLGLPISPFMDRSSPQLAKLQESFITHIVGPLCNSYDAAGLLPGQWLEAEEDNDTESGDDEDGEELDTEDEEMENNLNPKPPRRKSRRRIFCQLMHHLTENHKIWKEIVEEEEKCKADGNKLQVENSSLPQADEIQVIEEADEEE
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
13PhosphorylationRDAKAMRSLQPPDGA
HHHHHHHHCCCCCCC		20.47-
22PhosphorylationQPPDGAGSPPESLRN
CCCCCCCCCCHHHHC		36.4321815630
26PhosphorylationGAGSPPESLRNGYVK
CCCCCCHHHHCCCCC		38.1026462736
33UbiquitinationSLRNGYVKSCVSPLR
HHHCCCCCCCCCCHH		29.65-
33UbiquitinationSLRNGYVKSCVSPLR
HHHCCCCCCCCCCHH		29.65-
34PhosphorylationLRNGYVKSCVSPLRQ
HHCCCCCCCCCCHHC		15.0924719451
37PhosphorylationGYVKSCVSPLRQDPP
CCCCCCCCCHHCCCC		23.6521815630
65PhosphorylationELRPPPASPQQPRRC
EECCCCCCCCCCCCC		29.0828450419
73PhosphorylationPQQPRRCSPFCRARL
CCCCCCCCHHHHHHH		21.1417255105
279PhosphorylationAPLHPRLSSAAEEKV
CCCCHHCCCHHHHCC		21.1423312004
280PhosphorylationPLHPRLSSAAEEKVP
CCCHHCCCHHHHCCC		35.7729116813
285UbiquitinationLSSAAEEKVPVIRPR
CCCHHHHCCCCCCCC		43.26-
285UbiquitinationLSSAAEEKVPVIRPR
CCCHHHHCCCCCCCC		43.26-
295PhosphorylationVIRPRRRSSCVSLGE
CCCCCCCCCCCCCCC		26.6923401153
296PhosphorylationIRPRRRSSCVSLGET
CCCCCCCCCCCCCCH		19.4127273156
299PhosphorylationRRRSSCVSLGETAAS
CCCCCCCCCCCHHHH		34.6830631047
303PhosphorylationSCVSLGETAASYYGS
CCCCCCCHHHHHHCC		26.2330576142
306PhosphorylationSLGETAASYYGSCKI
CCCCHHHHHHCCCCE		19.2023312004
307PhosphorylationLGETAASYYGSCKIF
CCCHHHHHHCCCCEE		13.7123312004
308PhosphorylationGETAASYYGSCKIFR
CCHHHHHHCCCCEEC		10.4829759185
310PhosphorylationTAASYYGSCKIFRRP
HHHHHHCCCCEECCC		8.9823312004
312UbiquitinationASYYGSCKIFRRPSL
HHHHCCCCEECCCCC		46.72-
312UbiquitinationASYYGSCKIFRRPSL
HHHHCCCCEECCCCC		46.72-
318PhosphorylationCKIFRRPSLPCISRE
CCEECCCCCCCCCHH		43.0330266825
323PhosphorylationRPSLPCISREQMILW
CCCCCCCCHHHEEEE		36.1630266825
339UbiquitinationWDLKQWYKPHYQNSG
CCHHHHCCCHHCCCC		23.5121890473
339UbiquitinationWDLKQWYKPHYQNSG
CCHHHHCCCHHCCCC		23.5121890473
339UbiquitinationWDLKQWYKPHYQNSG
CCHHHHCCCHHCCCC		23.5121890473
371PhosphorylationSDLLTDPSLPPQVIS
HHHHHCCCCCHHHHH		57.21-
378PhosphorylationSLPPQVISSLRSISS
CCCHHHHHHHHHHHH		25.1830301811
379PhosphorylationLPPQVISSLRSISSL
CCHHHHHHHHHHHHH		19.3725954137
390 (in isoform 2)Phosphorylation-7.6225849741
393PhosphorylationLMGAFSGSCRPKINP
HHHHHCCCCCCCCCC		13.02-
419UbiquitinationEIEDPAEKGDRKLNK
HCCCHHHHCCHHCHH		69.12-
426UbiquitinationKGDRKLNKGLNRNSL
HCCHHCHHCCCCCCC		75.18-
432PhosphorylationNKGLNRNSLPTPQLR
HHCCCCCCCCCHHHH		32.2723882029
435PhosphorylationLNRNSLPTPQLRRSS
CCCCCCCCHHHHHCC		29.0330576142
441PhosphorylationPTPQLRRSSGTSGLL
CCHHHHHCCCCCCCC		27.0424972180
442PhosphorylationTPQLRRSSGTSGLLP
CHHHHHCCCCCCCCC		44.2523911959
444PhosphorylationQLRRSSGTSGLLPVE
HHHHCCCCCCCCCHH		22.9023911959
445PhosphorylationLRRSSGTSGLLPVEQ
HHHCCCCCCCCCHHH		30.8523882029
453PhosphorylationGLLPVEQSSRWDRNN
CCCCHHHCCCCCCCC		14.3623882029
454PhosphorylationLLPVEQSSRWDRNNG
CCCHHHCCCCCCCCC		36.7623882029
487PhosphorylationPFNSNLLTIPKQRSS
CCCCCCCCCCCCCCC		38.10-
493PhosphorylationLTIPKQRSSSVSLTH
CCCCCCCCCCCCCCC		25.1929255136
494PhosphorylationTIPKQRSSSVSLTHH
CCCCCCCCCCCCCCC		36.6329255136
495UbiquitinationIPKQRSSSVSLTHHV
CCCCCCCCCCCCCCH		19.57-
495PhosphorylationIPKQRSSSVSLTHHV
CCCCCCCCCCCCCCH		19.5723401153
497PhosphorylationKQRSSSVSLTHHVGL
CCCCCCCCCCCCHHH		29.5129255136
499PhosphorylationRSSSVSLTHHVGLRR
CCCCCCCCCCHHHHC		11.4829255136
511PhosphorylationLRRAGVLSSLSPVNS
HHCCCCHHHCCCCCC		27.1627174698
512PhosphorylationRRAGVLSSLSPVNSS
HCCCCHHHCCCCCCC		28.8027174698
514PhosphorylationAGVLSSLSPVNSSNH
CCCHHHCCCCCCCCC		28.8428450419
518PhosphorylationSSLSPVNSSNHGPVS
HHCCCCCCCCCCCCC		32.5228450419
519PhosphorylationSLSPVNSSNHGPVST
HCCCCCCCCCCCCCC		27.8728450419
525PhosphorylationSSNHGPVSTGSLTNR
CCCCCCCCCCCCCCC		30.1328450419
526PhosphorylationSNHGPVSTGSLTNRS
CCCCCCCCCCCCCCC		30.9028450419
528PhosphorylationHGPVSTGSLTNRSPI
CCCCCCCCCCCCCCC		31.9122468782
530PhosphorylationPVSTGSLTNRSPIEF
CCCCCCCCCCCCCCC		30.2226074081
533PhosphorylationTGSLTNRSPIEFPDT
CCCCCCCCCCCCCCH		32.0926074081
534UbiquitinationGSLTNRSPIEFPDTA
CCCCCCCCCCCCCHH		27.22-
546UbiquitinationDTADFLNKPSVILQR
CHHHHCCCCCEEHHH		40.59-
550UbiquitinationFLNKPSVILQRSLGN
HCCCCCEEHHHHCCC		2.96-
554PhosphorylationPSVILQRSLGNAPNT
CCEEHHHHCCCCCCC		27.8928450419
560UbiquitinationRSLGNAPNTPDFYQQ
HHCCCCCCCHHHHHH		62.93-
561PhosphorylationSLGNAPNTPDFYQQL
HCCCCCCCHHHHHHH		24.1528796482
565PhosphorylationAPNTPDFYQQLRNSD
CCCCHHHHHHHHCCC		11.6128796482
571PhosphorylationFYQQLRNSDSNLCNS
HHHHHHCCCCCCHHH		35.6630576142
573PhosphorylationQQLRNSDSNLCNSCG
HHHHCCCCCCHHHCC		31.36-
576UbiquitinationRNSDSNLCNSCGHQM
HCCCCCCHHHCCCHH		4.05-
577UbiquitinationNSDSNLCNSCGHQML
CCCCCCHHHCCCHHH		43.43-
578PhosphorylationSDSNLCNSCGHQMLK
CCCCCHHHCCCHHHH		22.0825159151
585UbiquitinationSCGHQMLKYVSTSES
HCCCHHHHHHHCCCC		37.96-
586PhosphorylationCGHQMLKYVSTSESD
CCCHHHHHHHCCCCC		8.82-
588PhosphorylationHQMLKYVSTSESDGT
CHHHHHHHCCCCCCC		24.1128450419
589PhosphorylationQMLKYVSTSESDGTD
HHHHHHHCCCCCCCC		26.8628450419
590PhosphorylationMLKYVSTSESDGTDC
HHHHHHCCCCCCCCC		27.8328450419
592PhosphorylationKYVSTSESDGTDCCS
HHHHCCCCCCCCCCC		40.9028450419
601UbiquitinationGTDCCSGKSGEEENI
CCCCCCCCCCCCCCC		38.71-
602PhosphorylationTDCCSGKSGEEENIF
CCCCCCCCCCCCCCC		55.7721815630
610PhosphorylationGEEENIFSKESFKLM
CCCCCCCCHHHHHHH		31.5524719451
611UbiquitinationEEENIFSKESFKLME
CCCCCCCHHHHHHHH		46.78-
613PhosphorylationENIFSKESFKLMETQ
CCCCCHHHHHHHHHH		31.2728555341
627UbiquitinationQQEEETEKKDSRKLF
HCHHHHHHHHHHHHH		70.11-
628UbiquitinationQEEETEKKDSRKLFQ
CHHHHHHHHHHHHHH		55.49-
632UbiquitinationTEKKDSRKLFQEGDK
HHHHHHHHHHHHHHH		58.57-
669PhosphorylationILVEEYDSLIEKMSN
EEHHHHHHHHHHHHC		30.2824719451
675PhosphorylationDSLIEKMSNWNFPIF
HHHHHHHHCCCCCHH		50.1623879269
751PhosphorylationDVLHAVWYLTTRPVP
HHHHHHHHHCCCCCC		6.38-
769PhosphorylationQIHNGCGTGNETDSD
HCCCCCCCCCCCCCC		40.69-
773PhosphorylationGCGTGNETDSDGRIN
CCCCCCCCCCCCCCC		44.81-
892UbiquitinationLVIEAILATDLKKHF
HHHHHHHHHCHHHHH		7.92-
943UbiquitinationADINGPAKVRDLHLK
HHCCCCCEEEEEHHH		40.72-
980PhosphorylationISPFMDRSSPQLAKL
CCCCCCCCCHHHHHH		41.9527251275
981PhosphorylationSPFMDRSSPQLAKLQ
CCCCCCCCHHHHHHH		19.9828985074
1030UbiquitinationESGDDEDGEELDTED
CCCCCCCCCCCCCCC		28.38-
1073UbiquitinationTENHKIWKEIVEEEE
HHCCHHHHHHHHHHH		40.82-
1081UbiquitinationEIVEEEEKCKADGNK
HHHHHHHHHCCCCCC		44.29-
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
73SPhosphorylationKinasePRKACAP17612
GPS
295SPhosphorylationKinaseAKT1P31749
Uniprot
295SPhosphorylationKinaseAKT2P31751
Uniprot
296SPhosphorylationKinasePRKACAP17612
GPS
318SPhosphorylationKinasePRKACAP17612
GPS
318SPhosphorylationKinasePKA-FAMILY-GPS
318SPhosphorylationKinasePKA_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDE3B_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 PDE3B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PDE3B_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
D00227 Aminophylline (USP/INN); Somophyllin (TN); Theophylline ethylenediamine (TN)
D00231 Amrinone (JAN/INN); Inamrinone (USP); Amcoral (TN)
D00371 Theophylline (JP16); Elixophyllin (TN); Quibron-t (TN); Theo-24 (TN); Theodur G (TN); Theolair (TN);
D00417 Milrinone (JAN/USP/INN); Milrila (TN)
D00528 Anhydrous caffeine (JP16); Caffeine (USP); Anhydrous caffeine (TN)
D00718 Flavoxate hydrochloride (JP16/USAN); Urispas (TN)
D01133 Pimobendan (JAN/USAN/INN); Acardi (TN)
D01198 Toborinone (JAN/USAN/INN)
D01220 Trapidil (JP16/INN); Rocornal (TN)
D01385 Ibudilast (JP16/INN); Ketas (TN)
D01453 Caffeine hydrate (JP16); Caffeine monohydrate; Caffeine (TN)
D01630 Propentofylline (JAN/INN)
D01690 Vesnarinone (JAN/USAN/INN); Arkin Z (TN)
D01712 Theophylline sodium acetate (JAN)
D01771 Proxyphylline (JAN/INN); Monophyllin (TN)
D01896 Cilostazol (JP16/USAN/INN); Pletal (TN)
D02017 Choline theophylline (JAN); Oxtriphylline (USP); Choline theophyllinate (INN); Theophyline - choline
D02042 Olprinone hydrochloride hydrate (JAN); Coretec (TN)
D02084 Inamrinone lactate; Inocor (TN)
D02085 Milrinone lactate; Primacor (TN)
D02218 Papaverine hydrochloride (JP16/USP); Pavabid (TN)
D02933 Anagrelide hydrochloride (USAN); Agrylin (TN)
D04004 Enoximone (USAN/INN); Perfan (TN)
D04508 Imazodan hydrochloride (USAN)
D04529 Indolidan (USAN/INN)
D04628 Isomazole hydrochloride (USAN)
D04720 Levosimendan (USAN/INN); Simdax (TN)
D04751 Lixazinone sulfate (USAN)
D05429 Aminophylline hydrate (JP16)
D06103 Theophylline (USP); Theophylline monohydrate; Accurbron (TN)
D06104 Theophylline sodium glycinate (USP); Asbron (TN)
D06132 Tibenelast sodium (USAN)
D07089 Moxaverine (INN)
D07425 Papaverine (BAN); Mesotina (TN)
D07439 Papaverine sulfate; Papaverine SAD (TN)
D07455 Anagrelide (INN/BAN)
D07603 Caffeine citrate (USP); Cafcit (TN)
D07961 Flavoxate (INN); Bladuril (TN)
D08238 Moxaverine hydrochloride; Certonal (TN)
D08294 Olprinone (INN)
D09843 Beradilol monoethyl maleate (JAN); TZC-5665
D10255 Anagrelide hydrochloride hydrate (JAN); Anagrelide hydrochloride monohydrate
DrugBank
DB00201Caffeine
Regulatory Network of PDE3B_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-442, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442 AND THR-444, ANDMASS SPECTROMETRY.

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