PDE12_HUMAN - dbPTM
PDE12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDE12_HUMAN
UniProt AC Q6L8Q7
Protein Name 2',5'-phosphodiesterase 12
Gene Name PDE12
Organism Homo sapiens (Human).
Sequence Length 609
Subcellular Localization Mitochondrion matrix .
Protein Description Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. This enzyme degraded triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a negative regulator of the The 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferons (IFNs). Suppression of this enzyme induces reduction of viral replication in Hela cells, thus counteracting the antiviral pathway probably by inhibiting the 2-5A system..
Protein Sequence MWRLPGARAALRVIRTAVEKLSRAEAGSQTAAGAMERAVVRCVPSEPKLSLSFALADGSHKNMQRDQSEPLGRVLSRIATNALKGHAKAAAAKKSRKSRPNASGGAACSGPGPEPAVFCEPVVKLYYREEAVAEDVLNVDAWQDGAVLQIGDVKYKVERNPPAFTELQLPRYIMAGFPVCPKLSLEFGDPASSLFRWYKEAKPGAAEPEVGVPSSLSPSSPSSSWTETDVEERVYTPSNADIGLRLKLHCTPGDGQRFGHSRELESVCVVEAGPGTCTFDHRHLYTKKVTEDALIRTVSYNILADTYAQTEFSRTVLYPYCAPYALELDYRQNLIQKELTGYNADVICLQEVDRAVFSDSLVPALEAFGLEGVFRIKQHEGLATFYRKSKFSLLSQHDISFYEALESDPLHKELLEKLVLYPSAQEKVLQRSSVLQVSVLQSTKDSSKRICVANTHLYWHPKGGYIRLIQMAVALAHIRHVSCDLYPGIPVIFCGDFNSTPSTGMYHFVINGSIPEDHEDWASNGEEERCNMSLTHFFKLKSACGEPAYTNYVGGFHGCLDYIFIDLNALEVEQVIPLPSHEEVTTHQALPSVSHPSDHIALVCDLKWK
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
16PhosphorylationAALRVIRTAVEKLSR
HHHHHHHHHHHHHHH		24.7520068231
22PhosphorylationRTAVEKLSRAEAGSQ
HHHHHHHHHHHHCCC		40.2820068231
28PhosphorylationLSRAEAGSQTAAGAM
HHHHHHCCCCHHHHH		31.2620068231
30PhosphorylationRAEAGSQTAAGAMER
HHHHCCCCHHHHHHH		21.8520068231
45PhosphorylationAVVRCVPSEPKLSLS
HEEECCCCCCCEEEE		46.2422210691
50PhosphorylationVPSEPKLSLSFALAD
CCCCCCEEEEEEECC		28.2620068231
52PhosphorylationSEPKLSLSFALADGS
CCCCEEEEEEECCCC		12.7120068231
59PhosphorylationSFALADGSHKNMQRD
EEEECCCCCCCCCCC		31.6620068231
61UbiquitinationALADGSHKNMQRDQS
EECCCCCCCCCCCCC		56.6721890473
61 (in isoform 2)Ubiquitination-56.6721890473
61 (in isoform 1)Ubiquitination-56.6721890473
61MalonylationALADGSHKNMQRDQS
EECCCCCCCCCCCCC		56.6726320211
68PhosphorylationKNMQRDQSEPLGRVL
CCCCCCCCCCHHHHH		45.5321406692
76PhosphorylationEPLGRVLSRIATNAL
CCHHHHHHHHHHHHH		20.8427282143
80PhosphorylationRVLSRIATNALKGHA
HHHHHHHHHHHHHHH		20.7529083192
84UbiquitinationRIATNALKGHAKAAA
HHHHHHHHHHHHHHH		46.36-
84 (in isoform 2)Ubiquitination-46.36-
97UbiquitinationAAAKKSRKSRPNASG
HHHHHHHCCCCCCCC		58.89-
98PhosphorylationAAKKSRKSRPNASGG
HHHHHHCCCCCCCCC		52.4322199227
103PhosphorylationRKSRPNASGGAACSG
HCCCCCCCCCCCCCC		44.3822199227
109PhosphorylationASGGAACSGPGPEPA
CCCCCCCCCCCCCCC		43.2128348404
193PhosphorylationEFGDPASSLFRWYKE
CCCCCHHHHHHHHHH		33.3624719451
198PhosphorylationASSLFRWYKEAKPGA
HHHHHHHHHHCCCCC		8.4923312004
199UbiquitinationSSLFRWYKEAKPGAA
HHHHHHHHHCCCCCC		44.21-
202 (in isoform 2)Ubiquitination-45.1121890473
202UbiquitinationFRWYKEAKPGAAEPE
HHHHHHCCCCCCCCC		45.1121906983
202 (in isoform 1)Ubiquitination-45.1121890473
214PhosphorylationEPEVGVPSSLSPSSP
CCCCCCCCCCCCCCC		41.3225159151
215PhosphorylationPEVGVPSSLSPSSPS
CCCCCCCCCCCCCCC		27.1425159151
217PhosphorylationVGVPSSLSPSSPSSS
CCCCCCCCCCCCCCC		25.3623401153
219PhosphorylationVPSSLSPSSPSSSWT
CCCCCCCCCCCCCCC		52.0522167270
220PhosphorylationPSSLSPSSPSSSWTE
CCCCCCCCCCCCCCC		31.9922167270
222PhosphorylationSLSPSSPSSSWTETD
CCCCCCCCCCCCCCC		38.6622167270
223PhosphorylationLSPSSPSSSWTETDV
CCCCCCCCCCCCCCC		33.0222167270
224PhosphorylationSPSSPSSSWTETDVE
CCCCCCCCCCCCCCH		42.2122167270
226PhosphorylationSSPSSSWTETDVEER
CCCCCCCCCCCCHHC		30.8423927012
228PhosphorylationPSSSWTETDVEERVY
CCCCCCCCCCHHCEE		37.6623927012
235PhosphorylationTDVEERVYTPSNADI
CCCHHCEECCCCCCE		21.1023312004
236PhosphorylationDVEERVYTPSNADIG
CCHHCEECCCCCCEE		19.8623312004
245MethylationSNADIGLRLKLHCTP
CCCCEEEEEEEEECC		25.27115486763
247AcetylationADIGLRLKLHCTPGD
CCEEEEEEEEECCCC		29.7425953088
247UbiquitinationADIGLRLKLHCTPGD
CCEEEEEEEEECCCC		29.74-
290PhosphorylationHLYTKKVTEDALIRT
CCCCCCCCHHHHHHH		36.7127174698
297PhosphorylationTEDALIRTVSYNILA
CHHHHHHHHHHHHHH		13.5526356563
299PhosphorylationDALIRTVSYNILADT
HHHHHHHHHHHHHCC		16.3226356563
300PhosphorylationALIRTVSYNILADTY
HHHHHHHHHHHHCCC		11.2426356563
306PhosphorylationSYNILADTYAQTEFS
HHHHHHCCCCCCCCC		18.3626356563
307PhosphorylationYNILADTYAQTEFSR
HHHHHCCCCCCCCCE		9.3926356563
310PhosphorylationLADTYAQTEFSRTVL
HHCCCCCCCCCEECC		30.7226356563
313PhosphorylationTYAQTEFSRTVLYPY
CCCCCCCCEECCCCC		22.3226356563
377UbiquitinationLEGVFRIKQHEGLAT
CCEEEEEEECCCCCE		41.15-
377SuccinylationLEGVFRIKQHEGLAT
CCEEEEEEECCCCCE		41.1527452117
412UbiquitinationLESDPLHKELLEKLV
HHCCHHHHHHHHHHC		58.71-
417 (in isoform 1)Ubiquitination-43.8121890473
417UbiquitinationLHKELLEKLVLYPSA
HHHHHHHHHCCCHHH		43.8121906983
417 (in isoform 2)Ubiquitination-43.8121890473
427 (in isoform 2)Ubiquitination-35.8421890473
427UbiquitinationLYPSAQEKVLQRSSV
CCHHHHHHHHHHCCE		35.8421890473
427AcetylationLYPSAQEKVLQRSSV
CCHHHHHHHHHHCCE		35.8423749302
427 (in isoform 1)Ubiquitination-35.8421890473
432PhosphorylationQEKVLQRSSVLQVSV
HHHHHHHCCEEEEEE		16.3121955146
433PhosphorylationEKVLQRSSVLQVSVL
HHHHHHCCEEEEEEE		29.0921955146
438PhosphorylationRSSVLQVSVLQSTKD
HCCEEEEEEEECCCC		12.2621955146
442PhosphorylationLQVSVLQSTKDSSKR
EEEEEEECCCCCCCC		33.0121955146
443PhosphorylationQVSVLQSTKDSSKRI
EEEEEECCCCCCCCE		26.3821955146
462UbiquitinationTHLYWHPKGGYIRLI
EEEEECCCCHHHHHH		52.67-
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 PDE12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDE12_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 PDE12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PUR8_HUMANADSLphysical
22863883
PGTB1_HUMANPGGT1Bphysical
22863883
WDR4_HUMANWDR4physical
22863883
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
There are no disease associations of PTM sites.
Regulatory Network of PDE12_HUMAN

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Related Literatures of Post-Translational Modification

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