UniProtKB - Q9Y233 (PDE10_HUMAN)
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
PDE10A
Functioni
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides (PubMed:10373451, PubMed:10393245, PubMed:16330539, PubMed:27058447, PubMed:17389385).
Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate (PubMed:10373451, PubMed:10393245, PubMed:27058447, PubMed:17389385).
May play a critical role in regulating cAMP and cGMP levels in the striatum, a region of the brain that contributes to the control of movement and cognition (PubMed:27058447).
5 PublicationsCatalytic activityi
- EC:3.1.4.174 Publications
Cofactori
Activity regulationi
Kineticsi
- KM=0.26 µM for cAMP1 Publication
- KM=7.2 µM for cGMP1 Publication
- KM=56 nM for cAMP1 Publication
- KM=4.4 µM for cGMP1 Publication
- Vmax=507 nmol/min/mg enzyme for cAMP1 Publication
- Vmax=1860 nmol/min/mg enzyme for cGMP1 Publication
: 3',5'-cyclic AMP degradation Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes AMP from 3',5'-cyclic AMP.5 Publications This subpathway is part of the pathway 3',5'-cyclic AMP degradation, which is itself part of Purine metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from 3',5'-cyclic AMP, the pathway 3',5'-cyclic AMP degradation and in Purine metabolism.
Pathwayi: 3',5'-cyclic GMP degradation
This protein is involved in step 1 of the subpathway that synthesizes GMP from 3',5'-cyclic GMP.4 Publications This subpathway is part of the pathway 3',5'-cyclic GMP degradation, which is itself part of Purine metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes GMP from 3',5'-cyclic GMP, the pathway 3',5'-cyclic GMP degradation and in Purine metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 364 | 3',5'-cAMPCombined sources1 Publication | 1 | |
Binding sitei | 383 | 3',5'-cAMPCombined sources1 Publication | 1 | |
Active sitei | 515 | Proton donorBy similarity | 1 | |
Binding sitei | 515 | 3',5'-cAMP1 Publication | 1 | |
Binding sitei | 515 | 3',5'-cGMP1 Publication | 1 | |
Metal bindingi | 519 | Divalent metal cation 11 Publication | 1 | |
Metal bindingi | 553 | Divalent metal cation 11 Publication | 1 | |
Metal bindingi | 554 | Divalent metal cation 11 Publication | 1 | |
Metal bindingi | 554 | Divalent metal cation 21 Publication | 1 | |
Metal bindingi | 664 | Divalent metal cation 11 Publication | 1 | |
Binding sitei | 716 | 3',5'-cAMP1 Publication | 1 | |
Binding sitei | 716 | 3',5'-cGMP1 Publication | 1 |
GO - Molecular functioni
- 3',5'-cyclic-AMP phosphodiesterase activity Source: RHEA
- 3',5'-cyclic-GMP phosphodiesterase activity Source: RHEA
- 3',5'-cyclic-nucleotide phosphodiesterase activity Source: GO_Central
- cAMP binding Source: UniProtKB
- cGMP binding Source: UniProtKB
- cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- cAMP catabolic process Source: UniProtKB-UniPathway
- cGMP catabolic process Source: UniProtKB-UniPathway
- negative regulation of cGMP-mediated signaling Source: GO_Central
- signal transduction Source: GO_Central
Keywordsi
Molecular function | Allosteric enzyme, Hydrolase |
Ligand | cAMP, cAMP-binding, cGMP, cGMP-binding, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 3.1.4.17, 2681 |
PathwayCommonsi | Q9Y233 |
Reactomei | R-HSA-418457, cGMP effects R-HSA-418555, G alpha (s) signalling events |
SABIO-RKi | Q9Y233 |
SignaLinki | Q9Y233 |
SIGNORi | Q9Y233 |
UniPathwayi | UPA00762;UER00747 UPA00763;UER00748 |
Names & Taxonomyi
Protein namesi | Recommended name: cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (EC:3.1.4.174 Publications) |
Gene namesi | Name:PDE10A |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:8772, PDE10A |
MIMi | 610652, gene |
neXtProti | NX_Q9Y233 |
VEuPathDBi | HostDB:ENSG00000112541 |
Subcellular locationi
Cytoplasm and Cytosol
- cytosol 2 Publications
Cytosol
- cytosol Source: Reactome
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Involvement in diseasei
Dyskinesia, limb and orofacial, infantile-onset (IOLOD)1 Publication
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_076798 | 97 | Y → C in IOLOD; decreased protein abundance. 1 PublicationCorresponds to variant dbSNP:rs778899140Ensembl. | 1 | |
Natural variantiVAR_076799 | 106 | A → P in IOLOD; decreased protein abundance. 1 PublicationCorresponds to variant dbSNP:rs875989839Ensembl. | 1 |
Striatal degeneration, autosomal dominant 2 (ADSD2)1 Publication
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_076800 | 290 | F → L in ADSD2; no effect on basal 3',5'-cyclic-nucleotide phosphodiesterase activity; the mutation severely disrupts the stimulatory effect on the enzyme activity mediated by cAMP binding. 1 PublicationCorresponds to variant dbSNP:rs875989841Ensembl. | 1 | |
Natural variantiVAR_076801 | 324 | F → L in ADSD2; no effect on basal 3',5'-cyclic-nucleotide phosphodiesterase activity; the mutation severely disrupts the stimulatory effect on the enzyme activity mediated by cAMP binding. 1 PublicationCorresponds to variant dbSNP:rs875989840Ensembl. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 554 | D → A: Loss of activity and of zinc binding. 1 Publication | 1 | |
Mutagenesisi | 554 | D → N: Reduces activity 1000-fold. 1 Publication | 1 |
Keywords - Diseasei
Disease variantOrganism-specific databases
DisGeNETi | 10846 |
MalaCardsi | PDE10A |
MIMi | 616921, phenotype 616922, phenotype |
OpenTargetsi | ENSG00000112541 |
Orphaneti | 494541, Childhood-onset benign chorea with striatal involvement 494526, Infantile-onset generalized dyskinesia with orofacial involvement |
PharmGKBi | PA33120 |
Miscellaneous databases
Pharosi | Q9Y233, Tclin |
Chemistry databases
ChEMBLi | CHEMBL4409 |
DrugBanki | DB08384, 2-({4-[4-(pyridin-4-ylmethyl)-1H-pyrazol-3-yl]phenoxy}methyl)quinoline DB08386, 2-{[4-(4-pyridin-4-yl-1H-pyrazol-3-yl)phenoxy]methyl}quinoline DB08383, 4,5-bis(4-methoxyphenyl)-2-thiophen-2-yl-1H-imidazole DB08389, 6,7-DIMETHOXY-4-[(3R)-3-(2-NAPHTHYLOXY)PYRROLIDIN-1-YL]QUINAZOLINE DB00201, Caffeine DB00975, Dipyridamole DB08387, Mardepodect DB01113, Papaverine DB08391, PQ-10 DB08811, Tofisopam DB09283, Trapidil DB08814, Triflusal |
DrugCentrali | Q9Y233 |
GuidetoPHARMACOLOGYi | 1310 |
Genetic variation databases
BioMutai | PDE10A |
DMDMi | 7993747 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000198843 | 1 – 779 | cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10AAdd BLAST | 779 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
---|---|---|---|---|---|
Isoform PDE10A2 (identifier: Q9Y233-2) | |||||
Modified residuei | 16 | Phosphothreonine1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
PhosphoproteinProteomic databases
EPDi | Q9Y233 |
jPOSTi | Q9Y233 |
MassIVEi | Q9Y233 |
MaxQBi | Q9Y233 |
PaxDbi | Q9Y233 |
PeptideAtlasi | Q9Y233 |
PRIDEi | Q9Y233 |
ProteomicsDBi | 85625 [Q9Y233-1] 85626 [Q9Y233-2] |
PTM databases
GlyGeni | Q9Y233, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | Q9Y233 |
PhosphoSitePlusi | Q9Y233 |
SwissPalmi | Q9Y233 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000112541, Expressed in caudate nucleus and 175 other tissues |
ExpressionAtlasi | Q9Y233, baseline and differential |
Genevisiblei | Q9Y233, HS |
Organism-specific databases
HPAi | ENSG00000112541, Tissue enriched (brain) |
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 116057, 7 interactors |
IntActi | Q9Y233, 2 interactors |
STRINGi | 9606.ENSP00000438284 |
Chemistry databases
BindingDBi | Q9Y233 |
Miscellaneous databases
RNActi | Q9Y233, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q9Y233 |
SMRi | Q9Y233 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9Y233 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 91 – 234 | GAF 1Add BLAST | 144 | |
Domaini | 266 – 412 | GAF 2Add BLAST | 147 | |
Domaini | 442 – 759 | PDEasePROSITE-ProRule annotationAdd BLAST | 318 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 286 – 287 | 3',5'-cAMP bindingCombined sources1 Publication | 2 | |
Regioni | 330 – 331 | 3',5'-cAMP bindingCombined sources1 Publication | 2 |
Domaini
Sequence similaritiesi
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG3689, Eukaryota |
GeneTreei | ENSGT00940000156543 |
HOGENOMi | CLU_006980_1_0_1 |
OrthoDBi | 904682at2759 |
PhylomeDBi | Q9Y233 |
TreeFami | TF316499 |
Family and domain databases
CDDi | cd00077, HDc, 1 hit |
Gene3Di | 1.10.1300.10, 1 hit 3.30.450.40, 2 hits |
InterProi | View protein in InterPro IPR003018, GAF IPR029016, GAF-like_dom_sf IPR003607, HD/PDEase_dom IPR023088, PDEase IPR002073, PDEase_catalytic_dom IPR036971, PDEase_catalytic_dom_sf IPR023174, PDEase_CS |
Pfami | View protein in Pfam PF01590, GAF, 2 hits PF00233, PDEase_I, 1 hit |
PRINTSi | PR00387, PDIESTERASE1 |
SMARTi | View protein in SMART SM00065, GAF, 2 hits SM00471, HDc, 1 hit |
PROSITEi | View protein in PROSITE PS00126, PDEASE_I_1, 1 hit PS51845, PDEASE_I_2, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 15 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MRIEERKSQH LTGLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK
60 70 80 90 100
NNKSEDESAP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNQLLLYELS
110 120 130 140 150
SIIKIATKAD GFALYFLGEC NNSLCIFTPP GIKEGKPRLI PAGPITQGTT
160 170 180 190 200
VSAYVAKSRK TLLVEDILGD ERFPRGTGLE SGTRIQSVLC LPIVTAIGDL
210 220 230 240 250
IGILELYRHW GKEAFCLSHQ EVATANLAWA SVAIHQVQVC RGLAKQTELN
260 270 280 290 300
DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF QVDHKNKELY
310 320 330 340 350
SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP
360 370 380 390 400
RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN
410 420 430 440 450
FKMFAVFCAL ALHCANMYHR IRHSECIYRV TMEKLSYHSI CTSEEWQGLM
460 470 480 490 500
QFTLPVRLCK EIELFHFDIG PFENMWPGIF VYMVHRSCGT SCFELEKLCR
510 520 530 540 550
FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI LQNNHTLFTD LERKGLLIAC
560 570 580 590 600
LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV SILQLEGHNI
610 620 630 640 650
FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLNNQS
660 670 680 690 700
HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP
710 720 730 740 750
IPMMDRDKKD EVPQGQLGFY NAVAIPCYTT LTQILPPTEP LLKACRDNLS
760 770
QWEKVIRGEE TATWISSPSV AQKAAASED
The sequence of this isoform differs from the canonical sequence as follows:
1-13: MRIEERKSQHLTG → MEDGPSNNASCFRRLTECFLSPS
Computationally mapped potential isoform sequencesi
There are 15 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A3B3ISJ6 | A0A3B3ISJ6_HUMAN | Phosphodiesterase | PDE10A PDE10A19 | 791 | Annotation score: | ||
A0A3B3ITT8 | A0A3B3ITT8_HUMAN | Phosphodiesterase | PDE10A | 847 | Annotation score: | ||
A0A3F2YP58 | A0A3F2YP58_HUMAN | Phosphodiesterase | PDE10A | 1,055 | Annotation score: | ||
A0A5F9ZHF9 | A0A5F9ZHF9_HUMAN | Phosphodiesterase | PDE10A | 820 | Annotation score: | ||
A0A5F9ZI67 | A0A5F9ZI67_HUMAN | Phosphodiesterase | PDE10A | 806 | Annotation score: | ||
A0A7I2YQV2 | A0A7I2YQV2_HUMAN | Phosphodiesterase | PDE10A | 802 | Annotation score: | ||
A0A1B1UZQ1 | A0A1B1UZQ1_HUMAN | Phosphodiesterase | PDE10A | 709 | Annotation score: | ||
A0A3B3IRU7 | A0A3B3IRU7_HUMAN | Phosphodiesterase | PDE10A | 772 | Annotation score: | ||
A0A3B3IT18 | A0A3B3IT18_HUMAN | cAMP and cAMP-inhibited cGMP 3',5'-... | PDE10A | 93 | Annotation score: | ||
A0A087WUD0 | A0A087WUD0_HUMAN | cAMP and cAMP-inhibited cGMP 3',5'-... | PDE10A | 183 | Annotation score: | ||
There are more potential isoformsShow all |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 657 | G → S in CAG38804 (Ref. 4) Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_076798 | 97 | Y → C in IOLOD; decreased protein abundance. 1 PublicationCorresponds to variant dbSNP:rs778899140Ensembl. | 1 | |
Natural variantiVAR_076799 | 106 | A → P in IOLOD; decreased protein abundance. 1 PublicationCorresponds to variant dbSNP:rs875989839Ensembl. | 1 | |
Natural variantiVAR_076800 | 290 | F → L in ADSD2; no effect on basal 3',5'-cyclic-nucleotide phosphodiesterase activity; the mutation severely disrupts the stimulatory effect on the enzyme activity mediated by cAMP binding. 1 PublicationCorresponds to variant dbSNP:rs875989841Ensembl. | 1 | |
Natural variantiVAR_008797 | 303 | L → P. | 1 | |
Natural variantiVAR_076801 | 324 | F → L in ADSD2; no effect on basal 3',5'-cyclic-nucleotide phosphodiesterase activity; the mutation severely disrupts the stimulatory effect on the enzyme activity mediated by cAMP binding. 1 PublicationCorresponds to variant dbSNP:rs875989840Ensembl. | 1 | |
Natural variantiVAR_047822 | 706 | R → K. Corresponds to variant dbSNP:rs2224252Ensembl. | 1 | |
Natural variantiVAR_047823 | 707 | D → N. Corresponds to variant dbSNP:rs2860112Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_004601 | 1 – 13 | MRIEE…QHLTG → MEDGPSNNASCFRRLTECFL SPS in isoform PDE10A2. 2 PublicationsAdd BLAST | 13 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB026816 mRNA Translation: BAA84467.1 AB020593 mRNA Translation: BAA78034.1 AF127479 mRNA Translation: AAD32595.1 AF127480 mRNA Translation: AAD32596.1 Different initiation. CR536567 mRNA Translation: CAG38804.1 AL117345 Genomic DNA No translation available. AL136130 Genomic DNA No translation available. AL160160 Genomic DNA No translation available. BC104858 mRNA Translation: AAI04859.1 BC104860 mRNA Translation: AAI04861.1 AB041798 Genomic DNA Translation: BAB16383.1 |
CCDSi | CCDS47513.1 [Q9Y233-2] CCDS5289.1 [Q9Y233-1] |
RefSeqi | NP_001124162.1, NM_001130690.2 [Q9Y233-2] NP_006652.1, NM_006661.3 [Q9Y233-1] XP_011533690.1, XM_011535388.2 [Q9Y233-1] |
Genome annotation databases
Ensembli | ENST00000366882.7; ENSP00000355847.3; ENSG00000112541.19 |
GeneIDi | 10846 |
KEGGi | hsa:10846 |
UCSCi | uc003quo.4, human [Q9Y233-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB026816 mRNA Translation: BAA84467.1 AB020593 mRNA Translation: BAA78034.1 AF127479 mRNA Translation: AAD32595.1 AF127480 mRNA Translation: AAD32596.1 Different initiation. CR536567 mRNA Translation: CAG38804.1 AL117345 Genomic DNA No translation available. AL136130 Genomic DNA No translation available. AL160160 Genomic DNA No translation available. BC104858 mRNA Translation: AAI04859.1 BC104860 mRNA Translation: AAI04861.1 AB041798 Genomic DNA Translation: BAB16383.1 |
CCDSi | CCDS47513.1 [Q9Y233-2] CCDS5289.1 [Q9Y233-1] |
RefSeqi | NP_001124162.1, NM_001130690.2 [Q9Y233-2] NP_006652.1, NM_006661.3 [Q9Y233-1] XP_011533690.1, XM_011535388.2 [Q9Y233-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2OUN | X-ray | 1.56 | A/B | 439-766 | [»] | |
2OUP | X-ray | 1.56 | A/B | 439-766 | [»] | |
2OUQ | X-ray | 1.90 | A/B | 439-766 | [»] | |
2OUR | X-ray | 1.45 | A/B | 439-766 | [»] | |
2OUS | X-ray | 1.45 | A/B | 439-766 | [»] | |
2OUU | X-ray | 1.52 | A/B | 439-766 | [»] | |
2OUV | X-ray | 1.56 | A/B | 439-766 | [»] | |
2OUY | X-ray | 1.90 | A/B | 439-766 | [»] | |
2WEY | X-ray | 2.80 | A/B | 439-779 | [»] | |
2Y0J | X-ray | 2.43 | A/B | 432-764 | [»] | |
2ZMF | X-ray | 2.10 | A/B | 246-427 | [»] | |
3SN7 | X-ray | 1.82 | A/B | 439-779 | [»] | |
3SNI | X-ray | 1.90 | A/B | 439-779 | [»] | |
3SNL | X-ray | 2.40 | A/B | 439-779 | [»] | |
3UI7 | X-ray | 2.28 | A/B | 432-760 | [»] | |
3UUO | X-ray | 2.11 | A/B | 432-760 | [»] | |
3WI2 | X-ray | 2.26 | A/B | 439-779 | [»] | |
3WS8 | X-ray | 2.60 | A/B | 439-779 | [»] | |
3WS9 | X-ray | 2.99 | A/B | 439-779 | [»] | |
3WYK | X-ray | 2.50 | A/B | 442-779 | [»] | |
3WYL | X-ray | 2.68 | A/B | 442-779 | [»] | |
3WYM | X-ray | 2.00 | A/B | 442-779 | [»] | |
4AEL | X-ray | 2.20 | A/B | 439-779 | [»] | |
4AJD | X-ray | 2.30 | A/D | 439-764 | [»] | |
4AJF | X-ray | 1.90 | A/D | 439-764 | [»] | |
4AJG | X-ray | 2.30 | A/D | 439-764 | [»] | |
4AJM | X-ray | 2.40 | A/D | 439-764 | [»] | |
4BBX | X-ray | 2.50 | A/B | 443-769 | [»] | |
4DDL | X-ray | 2.07 | A/B | 442-779 | [»] | |
4DFF | X-ray | 2.11 | A/B | 432-779 | [»] | |
4FCB | X-ray | 2.10 | A/B | 439-779 | [»] | |
4FCD | X-ray | 2.02 | A/B | 439-779 | [»] | |
4HEU | X-ray | 2.00 | A/B | 442-759 | [»] | |
4HF4 | X-ray | 2.00 | A/B | 442-759 | [»] | |
4LKQ | X-ray | 1.62 | A/B | 439-779 | [»] | |
4LLJ | X-ray | 1.56 | A/B | 439-779 | [»] | |
4LLK | X-ray | 1.55 | A/B | 439-779 | [»] | |
4LLP | X-ray | 1.75 | A/B | 439-779 | [»] | |
4LLX | X-ray | 1.75 | A/B | 439-779 | [»] | |
4LM0 | X-ray | 1.66 | A/B | 439-779 | [»] | |
4LM1 | X-ray | 1.60 | A/B | 439-779 | [»] | |
4LM2 | X-ray | 1.55 | A/B | 439-779 | [»] | |
4LM3 | X-ray | 1.49 | A/B | 439-779 | [»] | |
4LM4 | X-ray | 1.48 | A/B | 439-779 | [»] | |
4MRW | X-ray | 1.96 | A/B | 439-779 | [»] | |
4MRZ | X-ray | 1.58 | A/B | 439-779 | [»] | |
4MS0 | X-ray | 1.79 | A/B | 439-779 | [»] | |
4MSA | X-ray | 1.62 | A/B | 439-779 | [»] | |
4MSC | X-ray | 2.47 | A/B | 439-779 | [»] | |
4MSE | X-ray | 2.81 | A/B | 439-779 | [»] | |
4MSH | X-ray | 2.30 | A/B | 439-779 | [»] | |
4MSN | X-ray | 2.30 | A/B | 439-779 | [»] | |
4MUW | X-ray | 2.64 | A/B | 442-779 | [»] | |
4MVH | X-ray | 2.50 | A/B | 442-779 | [»] | |
4P0N | X-ray | 2.08 | A/B | 442-779 | [»] | |
4P1R | X-ray | 2.24 | A/B | 442-779 | [»] | |
4PHW | X-ray | 2.50 | A/B | 442-779 | [»] | |
4TPM | X-ray | 2.77 | A/B | 442-779 | [»] | |
4TPP | X-ray | 2.65 | A/B | 442-779 | [»] | |
4WN1 | X-ray | 3.13 | A/B | 439-779 | [»] | |
4XY2 | X-ray | 2.03 | A/B | 439-779 | [»] | |
4YQH | X-ray | 2.31 | A/B | 439-759 | [»] | |
4YS7 | X-ray | 2.50 | A/B | 439-759 | [»] | |
4ZO5 | X-ray | 2.50 | A/B | 439-759 | [»] | |
5AXP | X-ray | 1.95 | A/B | 442-779 | [»] | |
5AXQ | X-ray | 1.77 | A/B | 442-779 | [»] | |
5B4K | X-ray | 2.90 | A/B | 442-779 | [»] | |
5B4L | X-ray | 2.40 | A/B | 442-779 | [»] | |
5C1W | X-ray | 1.70 | A/B | 439-779 | [»] | |
5C28 | X-ray | 1.56 | A/B | 439-779 | [»] | |
5C29 | X-ray | 2.05 | A/B | 439-779 | [»] | |
5C2A | X-ray | 2.00 | A/B | 439-779 | [»] | |
5C2E | X-ray | 2.10 | A/B | 439-779 | [»] | |
5C2H | X-ray | 2.09 | A/B | 439-779 | [»] | |
5DH4 | X-ray | 2.20 | A/B | 439-779 | [»] | |
5DH5 | X-ray | 2.00 | A/B | 439-779 | [»] | |
5EDE | X-ray | 2.20 | A/C/D | 447-760 | [»] | |
B | 448-760 | [»] | ||||
5EDG | X-ray | 2.30 | A/B/C/D | 447-760 | [»] | |
5EDH | X-ray | 2.03 | A/B/C/D | 448-760 | [»] | |
5EDI | X-ray | 2.20 | A/B/C/D | 442-760 | [»] | |
5I2R | X-ray | 2.50 | A/B/C/D | 447-763 | [»] | |
5K9R | X-ray | 2.70 | A/B | 448-759 | [»] | |
5UWF | X-ray | 1.87 | C/D | 439-779 | [»] | |
5XUI | X-ray | 2.77 | A/B | 439-779 | [»] | |
5XUJ | X-ray | 2.44 | A/B | 439-779 | [»] | |
5ZNL | X-ray | 2.80 | A/B | 439-760 | [»] | |
6IJH | X-ray | 2.60 | A/B | 439-779 | [»] | |
6IJI | X-ray | 2.70 | A/B | 439-760 | [»] | |
6KDX | X-ray | 2.44 | A/B | 439-779 | [»] | |
6KDZ | X-ray | 3.10 | A/B | 439-779 | [»] | |
6KE0 | X-ray | 2.95 | A/B | 439-779 | [»] | |
6KO0 | X-ray | 2.60 | A/B | 439-759 | [»] | |
6KO1 | X-ray | 2.70 | A/B | 439-759 | [»] | |
6KZE | X-ray | 2.50 | A/B | 439-760 | [»] | |
6MSA | X-ray | 2.06 | A/B | 439-766 | [»] | |
6MSC | X-ray | 2.36 | A/B | 439-766 | [»] | |
7BPI | X-ray | 2.40 | A/B | 439-760 | [»] | |
AlphaFoldDBi | Q9Y233 | |||||
SMRi | Q9Y233 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 116057, 7 interactors |
IntActi | Q9Y233, 2 interactors |
STRINGi | 9606.ENSP00000438284 |
Chemistry databases
BindingDBi | Q9Y233 |
ChEMBLi | CHEMBL4409 |
DrugBanki | DB08384, 2-({4-[4-(pyridin-4-ylmethyl)-1H-pyrazol-3-yl]phenoxy}methyl)quinoline DB08386, 2-{[4-(4-pyridin-4-yl-1H-pyrazol-3-yl)phenoxy]methyl}quinoline DB08383, 4,5-bis(4-methoxyphenyl)-2-thiophen-2-yl-1H-imidazole DB08389, 6,7-DIMETHOXY-4-[(3R)-3-(2-NAPHTHYLOXY)PYRROLIDIN-1-YL]QUINAZOLINE DB00201, Caffeine DB00975, Dipyridamole DB08387, Mardepodect DB01113, Papaverine DB08391, PQ-10 DB08811, Tofisopam DB09283, Trapidil DB08814, Triflusal |
DrugCentrali | Q9Y233 |
GuidetoPHARMACOLOGYi | 1310 |
PTM databases
GlyGeni | Q9Y233, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | Q9Y233 |
PhosphoSitePlusi | Q9Y233 |
SwissPalmi | Q9Y233 |
Genetic variation databases
BioMutai | PDE10A |
DMDMi | 7993747 |
Proteomic databases
EPDi | Q9Y233 |
jPOSTi | Q9Y233 |
MassIVEi | Q9Y233 |
MaxQBi | Q9Y233 |
PaxDbi | Q9Y233 |
PeptideAtlasi | Q9Y233 |
PRIDEi | Q9Y233 |
ProteomicsDBi | 85625 [Q9Y233-1] 85626 [Q9Y233-2] |
Protocols and materials databases
Antibodypediai | 33512, 217 antibodies from 27 providers |
DNASUi | 10846 |
Genome annotation databases
Ensembli | ENST00000366882.7; ENSP00000355847.3; ENSG00000112541.19 |
GeneIDi | 10846 |
KEGGi | hsa:10846 |
UCSCi | uc003quo.4, human [Q9Y233-1] |
Organism-specific databases
CTDi | 10846 |
DisGeNETi | 10846 |
GeneCardsi | PDE10A |
HGNCi | HGNC:8772, PDE10A |
HPAi | ENSG00000112541, Tissue enriched (brain) |
MalaCardsi | PDE10A |
MIMi | 610652, gene 616921, phenotype 616922, phenotype |
neXtProti | NX_Q9Y233 |
OpenTargetsi | ENSG00000112541 |
Orphaneti | 494541, Childhood-onset benign chorea with striatal involvement 494526, Infantile-onset generalized dyskinesia with orofacial involvement |
PharmGKBi | PA33120 |
VEuPathDBi | HostDB:ENSG00000112541 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3689, Eukaryota |
GeneTreei | ENSGT00940000156543 |
HOGENOMi | CLU_006980_1_0_1 |
OrthoDBi | 904682at2759 |
PhylomeDBi | Q9Y233 |
TreeFami | TF316499 |
Enzyme and pathway databases
UniPathwayi | UPA00762;UER00747 UPA00763;UER00748 |
BRENDAi | 3.1.4.17, 2681 |
PathwayCommonsi | Q9Y233 |
Reactomei | R-HSA-418457, cGMP effects R-HSA-418555, G alpha (s) signalling events |
SABIO-RKi | Q9Y233 |
SignaLinki | Q9Y233 |
SIGNORi | Q9Y233 |
Miscellaneous databases
BioGRID-ORCSi | 10846, 7 hits in 1071 CRISPR screens |
ChiTaRSi | PDE10A, human |
EvolutionaryTracei | Q9Y233 |
GeneWikii | PDE10A |
GenomeRNAii | 10846 |
Pharosi | Q9Y233, Tclin |
PROi | PR:Q9Y233 |
RNActi | Q9Y233, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000112541, Expressed in caudate nucleus and 175 other tissues |
ExpressionAtlasi | Q9Y233, baseline and differential |
Genevisiblei | Q9Y233, HS |
Family and domain databases
CDDi | cd00077, HDc, 1 hit |
Gene3Di | 1.10.1300.10, 1 hit 3.30.450.40, 2 hits |
InterProi | View protein in InterPro IPR003018, GAF IPR029016, GAF-like_dom_sf IPR003607, HD/PDEase_dom IPR023088, PDEase IPR002073, PDEase_catalytic_dom IPR036971, PDEase_catalytic_dom_sf IPR023174, PDEase_CS |
Pfami | View protein in Pfam PF01590, GAF, 2 hits PF00233, PDEase_I, 1 hit |
PRINTSi | PR00387, PDIESTERASE1 |
SMARTi | View protein in SMART SM00065, GAF, 2 hits SM00471, HDc, 1 hit |
PROSITEi | View protein in PROSITE PS00126, PDEASE_I_1, 1 hit PS51845, PDEASE_I_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PDE10_HUMAN | |
Accessioni | Q9Y233Primary (citable) accession number: Q9Y233 Secondary accession number(s): Q6FHX1 Q9Y5T1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | November 1, 1999 | |
Last modified: | May 25, 2022 | |
This is version 201 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families