PDE9A_HUMAN - dbPTM
PDE9A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDE9A_HUMAN
UniProt AC O76083
Protein Name High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A {ECO:0000305}
Gene Name PDE9A {ECO:0000312|HGNC:HGNC:8795}
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Isoform PDE9A1: Cell projection, ruffle membrane . Cytoplasm, perinuclear region . Golgi apparatus . Endoplasmic reticulum . Cell membrane, sarcolemma .
Isoform PDE9A2: Cell projection, ruffle membrane . Cytoplasm, perinuclear region .
Isoform PDE9A3: C
Protein Description Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes. Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. [PubMed: 9624146]
Protein Sequence MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
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
3Phosphorylation-----MGSGSSSYRP
-----CCCCCCCCCC		33.9223532336
8PhosphorylationMGSGSSSYRPKAIYL
CCCCCCCCCCCEEEE		32.6523532336
27PhosphorylationRIQKVIFSKYCNSSD
CEEHHHHHCCCCHHH		16.1624719451
29PhosphorylationQKVIFSKYCNSSDIM
EHHHHHCCCCHHHHH		8.8217053785
32PhosphorylationIFSKYCNSSDIMDLF
HHHCCCCHHHHHHHH		26.3124719451
36 (in isoform 4)Phosphorylation-4.37-
43PhosphorylationMDLFCIATGLPRNTT
HHHHHHHHCCCCCCE		21.2424719451
62 (in isoform 12)Phosphorylation-14.27-
76PhosphorylationANSERTPYKVRPVAI
CCCCCCCCCCCCCHH		22.85-
77UbiquitinationNSERTPYKVRPVAIK
CCCCCCCCCCCCHHH		32.73-
87PhosphorylationPVAIKQLSAGVEDKR
CCHHHHHCCCCCCCC		22.08-
111 (in isoform 5)Phosphorylation-4.11-
174UbiquitinationAFKINELKAEVANHL
HHHHHHHHHHHHHHH		36.00-
186UbiquitinationNHLAVLEKRVELEGL
HHHHHHHHHHHHCCC		58.54-
194UbiquitinationRVELEGLKVVEIEKC
HHHHCCCEEEEEEEC		55.90-
224UbiquitinationSRTNCPCKYSFLDNH
CCCCCCCCCCCCCCC		29.13-
379PhosphorylationAVRYNDISPLENHHC
EECCCCCCCCCCCCC		26.71-
444PhosphorylationEKMENFDYSNEEHMT
HHHHCCCCCCHHHHH		14.84-
508PhosphorylationFMDRDKVTKATAQIG
CCCHHHCHHHHHHHC		22.24-
511PhosphorylationRDKVTKATAQIGFIK
HHHCHHHHHHHCCEE		22.20-
567PhosphorylationMKELQKKTDSLTSGA
HHHHHHHHHHCCCCC		37.5422817900
569PhosphorylationELQKKTDSLTSGATE
HHHHHHHHCCCCCCH		38.4923312004
571PhosphorylationQKKTDSLTSGATEKS
HHHHHHCCCCCCHHH		29.1222817900
572PhosphorylationKKTDSLTSGATEKSR
HHHHHCCCCCCHHHH		31.5523312004
578PhosphorylationTSGATEKSRERSRDV
CCCCCHHHHHHHHCC		32.8922817900
582PhosphorylationTEKSRERSRDVKNSE
CHHHHHHHHCCCCCC		28.25-
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
-KUbiquitinationE3 ubiquitin ligaseNEURL1O76050
PMID:31068605
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDE9A_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 PDE9A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI32_HUMANTRIM32physical
16189514
PHIPL_HUMANPHYHIPLphysical
16189514
PDE9A_HUMANPDE9Aphysical
16189514
TRI32_HUMANTRIM32physical
19060904
PDE9A_HUMANPDE9Aphysical
25416956
ST1E1_HUMANSULT1E1physical
25416956
LAGE3_HUMANLAGE3physical
25416956
BAG3_HUMANBAG3physical
25416956
TRI32_HUMANTRIM32physical
25416956
GORS2_HUMANGORASP2physical
25416956
TRPV6_HUMANTRPV6physical
25416956
KRA92_HUMANKRTAP9-2physical
25416956
UTP23_HUMANUTP23physical
25416956
LSMD1_HUMANNAA38physical
25416956
PHIPL_HUMANPHYHIPLphysical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
CI106_HUMANC9orf106physical
25416956
TFAP4_HUMANTFAP4physical
21516116
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
DB00201Caffeine
Regulatory Network of PDE9A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND MASSSPECTROMETRY.

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