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Protein

cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A

Gene

PDE10A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate. 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.By similarity1 Publication

Catalytic activityi

Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.
Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.

Cofactori

a divalent metal cation1 PublicationNote: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.1 Publication

Enzyme regulationi

Inhibited by dipyridamole and moderately by IBMX. cAMP acts as an allosteric activator.1 Publication

Kineticsi

  1. KM=56 nM for cAMP1 Publication
  2. KM=4.4 µM for cGMP1 Publication
  1. Vmax=507 nmol/min/mg enzyme for cAMP1 Publication
  2. Vmax=1860 nmol/min/mg enzyme for cGMP1 Publication

Pathwayi: 3',5'-cyclic AMP degradation

This protein is involved in step 1 of the subpathway that synthesizes AMP from 3',5'-cyclic AMP.
Proteins known to be involved in this subpathway in this organism are:
  1. cAMP-specific 3',5'-cyclic phosphodiesterase 4C (PDE4C), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (PDE10A), cAMP-specific 3',5'-cyclic phosphodiesterase 4A (PDE4A), High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (PDE7A), cAMP-specific 3',5'-cyclic phosphodiesterase 7B (PDE7B), cAMP-specific 3',5'-cyclic phosphodiesterase 4D (PDE4D), cAMP-specific 3',5'-cyclic phosphodiesterase 4B (PDE4B), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A (PDE8A), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B (PDE8B)
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.
Proteins known to be involved in this subpathway in this organism are:
  1. cGMP-specific 3',5'-cyclic phosphodiesterase (PDE5A), High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (PDE9A), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (PDE10A)
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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei364Allosteric effector1
Binding sitei383Allosteric effector1
Active sitei515Proton donorBy similarity1
Binding sitei515Substrate1
Metal bindingi519Divalent metal cation 11
Metal bindingi553Divalent metal cation 11
Metal bindingi554Divalent metal cation 11
Metal bindingi554Divalent metal cation 21
Metal bindingi664Divalent metal cation 11
Binding sitei716Substrate1

GO - Molecular functioni

  • 3',5'-cyclic-AMP phosphodiesterase activity Source: Reactome
  • 3',5'-cyclic-GMP phosphodiesterase activity Source: Reactome
  • 3',5'-cyclic-nucleotide phosphodiesterase activity Source: ProtInc
  • cAMP binding Source: UniProtKB
  • cGMP binding Source: UniProtKB
  • cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  • drug binding Source: Ensembl
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, cAMP-binding, cGMP, cGMP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS03586-MONOMER.
BRENDAi3.1.4.17. 2681.
ReactomeiR-HSA-418457. cGMP effects.
R-HSA-418555. G alpha (s) signalling events.
SIGNORiQ9Y233.
UniPathwayiUPA00762; UER00747.
UPA00763; UER00748.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (EC:3.1.4.17, EC:3.1.4.35)
Gene namesi
Name:PDE10A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:8772. PDE10A.

Subcellular locationi

  • Cytoplasm

  • Note: Located mostly to soluble cellular fractions.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Dyskinesia, limb and orofacial, infantile-onset (IOLOD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive, early-onset hyperkinetic movement disorder characterized by axial hypotonia, dyskinesia of the limbs and trunk, orofacial dyskinesia, drooling, and dysarthria. The severity of the hyperkinesis is variable.
See also OMIM:616921
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07679897Y → C in IOLOD; decreased protein abundance. 1 Publication1
Natural variantiVAR_076799106A → P in IOLOD; decreased protein abundance. 1 Publication1
Striatal degeneration, autosomal dominant 2 (ADSD2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by striatal degeneration and dysfunction of basal ganglia, resulting in hyperkinesis.
See also OMIM:616922
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076800290F → 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 Publication1
Natural variantiVAR_076801324F → 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 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi554D → A: Loss of activity and of zinc binding. 1 Publication1
Mutagenesisi554D → N: Reduces activity 1000-fold. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi10846.
MIMi616921. phenotype.
616922. phenotype.
OpenTargetsiENSG00000112541.
PharmGKBiPA33120.

Chemistry databases

ChEMBLiCHEMBL4409.
DrugBankiDB00201. Caffeine.
DB00975. Dipyridamole.
DB01113. Papaverine.
DB08811. Tofisopam.
DB08814. Triflusal.
GuidetoPHARMACOLOGYi1310.

Polymorphism and mutation databases

BioMutaiPDE10A.
DMDMi7993747.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001988431 – 779cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10AAdd BLAST779

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform PDE10A2 (identifier: Q9Y233-2)
Modified residuei16Phosphothreonine1 Publication1

Post-translational modificationi

Isoform PDE10A2: Phosphorylated on Thr-16.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9Y233.
PeptideAtlasiQ9Y233.
PRIDEiQ9Y233.

PTM databases

iPTMnetiQ9Y233.
PhosphoSitePlusiQ9Y233.
SwissPalmiQ9Y233.

Expressioni

Tissue specificityi

Abundant in the putamen and caudate nucleus regions of brain and testis, moderately expressed in the thyroid gland, pituitary gland, thalamus and cerebellum.2 Publications

Gene expression databases

BgeeiENSG00000112541.
CleanExiHS_PDE10A.
ExpressionAtlasiQ9Y233. baseline and differential.
GenevisibleiQ9Y233. HS.

Organism-specific databases

HPAiCAB045998.
HPA047200.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi116057. 2 interactors.
IntActiQ9Y233. 1 interactor.
MINTiMINT-1401257.
STRINGi9606.ENSP00000438284.

Chemistry databases

BindingDBiQ9Y233.

Structurei

Secondary structure

1779
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi247 – 262Combined sources16
Helixi267 – 282Combined sources16
Beta strandi284 – 293Combined sources10
Turni294 – 297Combined sources4
Beta strandi298 – 304Combined sources7
Beta strandi323 – 325Combined sources3
Helixi329 – 337Combined sources9
Beta strandi341 – 344Combined sources4
Helixi346 – 348Combined sources3
Helixi355 – 360Combined sources6
Beta strandi367 – 374Combined sources8
Beta strandi377 – 387Combined sources11
Beta strandi390 – 392Combined sources3
Helixi395 – 419Combined sources25
Helixi443 – 449Combined sources7
Helixi456 – 461Combined sources6
Beta strandi464 – 466Combined sources3
Helixi470 – 475Combined sources6
Helixi476 – 488Combined sources13
Turni490 – 492Combined sources3
Helixi495 – 507Combined sources13
Beta strandi513 – 516Combined sources4
Helixi517 – 532Combined sources16
Helixi533 – 537Combined sources5
Helixi540 – 552Combined sources13
Turni553 – 556Combined sources4
Helixi562 – 567Combined sources6
Helixi571 – 575Combined sources5
Beta strandi577 – 579Combined sources3
Helixi580 – 593Combined sources14
Turni596 – 598Combined sources3
Turni600 – 603Combined sources4
Helixi606 – 622Combined sources17
Helixi625 – 640Combined sources16
Beta strandi646 – 648Combined sources3
Helixi649 – 664Combined sources16
Helixi666 – 669Combined sources4
Helixi672 – 695Combined sources24
Helixi702 – 704Combined sources3
Helixi706 – 711Combined sources6
Helixi712 – 722Combined sources11
Helixi724 – 734Combined sources11
Helixi736 – 738Combined sources3
Helixi739 – 757Combined sources19
Helixi762 – 765Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LRBmodel-A501-757[»]
2OUNX-ray1.56A/B439-766[»]
2OUPX-ray1.56A/B439-766[»]
2OUQX-ray1.90A/B439-766[»]
2OURX-ray1.45A/B439-766[»]
2OUSX-ray1.45A/B439-766[»]
2OUUX-ray1.52A/B439-766[»]
2OUVX-ray1.56A/B439-766[»]
2OUYX-ray1.90A/B439-766[»]
2WEYX-ray2.80A/B439-779[»]
2Y0JX-ray2.43A/B432-764[»]
2ZMFX-ray2.10A/B246-427[»]
3SN7X-ray1.82A/B439-779[»]
3SNIX-ray1.90A/B439-779[»]
3SNLX-ray2.40A/B439-779[»]
3UI7X-ray2.28A/B432-760[»]
3UUOX-ray2.11A/B432-760[»]
3WI2X-ray2.26A/B439-779[»]
3WS8X-ray2.60A/B439-779[»]
3WS9X-ray2.99A/B439-779[»]
3WYKX-ray2.50A/B442-779[»]
3WYLX-ray2.68A/B442-779[»]
3WYMX-ray2.00A/B442-779[»]
4AELX-ray2.20A/B439-779[»]
4AJDX-ray2.30A/D439-764[»]
4AJFX-ray1.90A/D439-764[»]
4AJGX-ray2.30A/D439-764[»]
4AJMX-ray2.40A/D439-764[»]
4BBXX-ray2.50A/B443-769[»]
4DDLX-ray2.07A/B442-779[»]
4DFFX-ray2.11A/B432-779[»]
4FCBX-ray2.10A/B439-779[»]
4FCDX-ray2.02A/B439-779[»]
4HEUX-ray2.00A/B442-759[»]
4HF4X-ray2.00A/B442-759[»]
4LKQX-ray1.62A/B439-779[»]
4LLJX-ray1.56A/B439-779[»]
4LLKX-ray1.55A/B439-779[»]
4LLPX-ray1.75A/B439-779[»]
4LLXX-ray1.75A/B439-779[»]
4LM0X-ray1.66A/B439-779[»]
4LM1X-ray1.60A/B439-779[»]
4LM2X-ray1.55A/B439-779[»]
4LM3X-ray1.49A/B439-779[»]
4LM4X-ray1.48A/B439-779[»]
4MRWX-ray1.96A/B439-779[»]
4MRZX-ray1.58A/B439-779[»]
4MS0X-ray1.79A/B439-779[»]
4MSAX-ray1.62A/B439-779[»]
4MSCX-ray2.47A/B439-779[»]
4MSEX-ray2.81A/B439-779[»]
4MSHX-ray2.30A/B439-779[»]
4MSNX-ray2.30A/B439-779[»]
4MUWX-ray2.64A/B442-779[»]
4MVHX-ray2.50A/B442-779[»]
4P0NX-ray2.08A/B442-779[»]
4P1RX-ray2.24A/B442-779[»]
4PHWX-ray2.50A/B442-779[»]
4TPMX-ray2.77A/B442-779[»]
4TPPX-ray2.65A/B442-779[»]
4WN1X-ray3.13A/B439-779[»]
4XY2X-ray2.03A/B439-779[»]
4YQHX-ray2.31A/B439-759[»]
4YS7X-ray2.50A/B439-759[»]
4ZO5X-ray2.50A/B439-759[»]
5AXPX-ray1.95A/B442-779[»]
5AXQX-ray1.77A/B442-779[»]
5B4KX-ray2.90A/B442-779[»]
5B4LX-ray2.40A/B442-779[»]
5C1WX-ray1.70A/B439-779[»]
5C28X-ray1.56A/B439-779[»]
5C29X-ray2.05A/B439-779[»]
5C2AX-ray2.00A/B439-779[»]
5C2EX-ray2.10A/B439-779[»]
5C2HX-ray2.09A/B439-779[»]
5DH4X-ray2.20A/B439-779[»]
5DH5X-ray2.00A/B439-779[»]
5EDEX-ray2.20A/C/D447-760[»]
B448-760[»]
5EDGX-ray2.30A/B/C/D447-760[»]
5EDHX-ray2.03A/B/C/D448-760[»]
5EDIX-ray2.20A/B/C/D442-760[»]
5I2RX-ray2.50A/B/C/D447-763[»]
5K9RX-ray2.70A/B448-759[»]
ProteinModelPortaliQ9Y233.
SMRiQ9Y233.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y233.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini91 – 234GAF 1Add BLAST144
Domaini266 – 412GAF 2Add BLAST147

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni286 – 287Allosteric effector binding2
Regioni330 – 331Allosteric effector binding2

Domaini

The tandem GAF domains bind cAMP, and regulate enzyme activity. The binding of cAMP stimulates enzyme activity.
Composed of a C-terminal catalytic domain containing two divalent metal sites and an N-terminal regulatory domain which contains one cyclic nucleotide-binding region.

Sequence similaritiesi

Contains 2 GAF domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3689. Eukaryota.
ENOG410XRI7. LUCA.
GeneTreeiENSGT00760000119066.
HOGENOMiHOG000007068.
HOVERGENiHBG082113.
KOiK18438.
OMAiCRFTMSV.
OrthoDBiEOG091G037C.
PhylomeDBiQ9Y233.
TreeFamiTF316499.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom-like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 2 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Isoforms differ in their N-terminal region.
Isoform PDE10A1 (identifier: Q9Y233-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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
Length:779
Mass (Da):88,412
Last modified:November 1, 1999 - v1
Checksum:iC5651BBB524A32B7
GO
Isoform PDE10A2 (identifier: Q9Y233-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MRIEERKSQHLTG → MEDGPSNNASCFRRLTECFLSPS

Show »
Length:789
Mass (Da):89,390
Checksum:i7CC35F16735FB3C2
GO

Sequence cautioni

The sequence AAD32596 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti657G → S in CAG38804 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07679897Y → C in IOLOD; decreased protein abundance. 1 Publication1
Natural variantiVAR_076799106A → P in IOLOD; decreased protein abundance. 1 Publication1
Natural variantiVAR_076800290F → 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 Publication1
Natural variantiVAR_008797303L → P.1
Natural variantiVAR_076801324F → 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 Publication1
Natural variantiVAR_047822706R → K.Corresponds to variant rs2224252dbSNPEnsembl.1
Natural variantiVAR_047823707D → N.Corresponds to variant rs2860112dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0046011 – 13MRIEE…QHLTG → MEDGPSNNASCFRRLTECFL SPS in isoform PDE10A2. 2 PublicationsAdd BLAST13

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, AL136130, AL160160 Genomic DNA. Translation: CAB92797.2.
AL136130, AL117345, AL160160 Genomic DNA. Translation: CAI20436.1.
AL160160, AL117345, AL136130 Genomic DNA. Translation: CAH72023.1.
BC104858 mRNA. Translation: AAI04859.1.
BC104860 mRNA. Translation: AAI04861.1.
AB041798 Genomic DNA. Translation: BAB16383.1.
CCDSiCCDS47513.1. [Q9Y233-2]
CCDS5289.1. [Q9Y233-1]
RefSeqiNP_001124162.1. NM_001130690.2. [Q9Y233-2]
NP_006652.1. NM_006661.3. [Q9Y233-1]
XP_011533690.1. XM_011535388.2. [Q9Y233-1]
UniGeneiHs.348762.

Genome annotation databases

EnsembliENST00000366882; ENSP00000355847; ENSG00000112541. [Q9Y233-1]
ENST00000539869; ENSP00000438284; ENSG00000112541. [Q9Y233-2]
GeneIDi10846.
KEGGihsa:10846.
UCSCiuc003quo.4. human. [Q9Y233-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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, AL136130, AL160160 Genomic DNA. Translation: CAB92797.2.
AL136130, AL117345, AL160160 Genomic DNA. Translation: CAI20436.1.
AL160160, AL117345, AL136130 Genomic DNA. Translation: CAH72023.1.
BC104858 mRNA. Translation: AAI04859.1.
BC104860 mRNA. Translation: AAI04861.1.
AB041798 Genomic DNA. Translation: BAB16383.1.
CCDSiCCDS47513.1. [Q9Y233-2]
CCDS5289.1. [Q9Y233-1]
RefSeqiNP_001124162.1. NM_001130690.2. [Q9Y233-2]
NP_006652.1. NM_006661.3. [Q9Y233-1]
XP_011533690.1. XM_011535388.2. [Q9Y233-1]
UniGeneiHs.348762.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LRBmodel-A501-757[»]
2OUNX-ray1.56A/B439-766[»]
2OUPX-ray1.56A/B439-766[»]
2OUQX-ray1.90A/B439-766[»]
2OURX-ray1.45A/B439-766[»]
2OUSX-ray1.45A/B439-766[»]
2OUUX-ray1.52A/B439-766[»]
2OUVX-ray1.56A/B439-766[»]
2OUYX-ray1.90A/B439-766[»]
2WEYX-ray2.80A/B439-779[»]
2Y0JX-ray2.43A/B432-764[»]
2ZMFX-ray2.10A/B246-427[»]
3SN7X-ray1.82A/B439-779[»]
3SNIX-ray1.90A/B439-779[»]
3SNLX-ray2.40A/B439-779[»]
3UI7X-ray2.28A/B432-760[»]
3UUOX-ray2.11A/B432-760[»]
3WI2X-ray2.26A/B439-779[»]
3WS8X-ray2.60A/B439-779[»]
3WS9X-ray2.99A/B439-779[»]
3WYKX-ray2.50A/B442-779[»]
3WYLX-ray2.68A/B442-779[»]
3WYMX-ray2.00A/B442-779[»]
4AELX-ray2.20A/B439-779[»]
4AJDX-ray2.30A/D439-764[»]
4AJFX-ray1.90A/D439-764[»]
4AJGX-ray2.30A/D439-764[»]
4AJMX-ray2.40A/D439-764[»]
4BBXX-ray2.50A/B443-769[»]
4DDLX-ray2.07A/B442-779[»]
4DFFX-ray2.11A/B432-779[»]
4FCBX-ray2.10A/B439-779[»]
4FCDX-ray2.02A/B439-779[»]
4HEUX-ray2.00A/B442-759[»]
4HF4X-ray2.00A/B442-759[»]
4LKQX-ray1.62A/B439-779[»]
4LLJX-ray1.56A/B439-779[»]
4LLKX-ray1.55A/B439-779[»]
4LLPX-ray1.75A/B439-779[»]
4LLXX-ray1.75A/B439-779[»]
4LM0X-ray1.66A/B439-779[»]
4LM1X-ray1.60A/B439-779[»]
4LM2X-ray1.55A/B439-779[»]
4LM3X-ray1.49A/B439-779[»]
4LM4X-ray1.48A/B439-779[»]
4MRWX-ray1.96A/B439-779[»]
4MRZX-ray1.58A/B439-779[»]
4MS0X-ray1.79A/B439-779[»]
4MSAX-ray1.62A/B439-779[»]
4MSCX-ray2.47A/B439-779[»]
4MSEX-ray2.81A/B439-779[»]
4MSHX-ray2.30A/B439-779[»]
4MSNX-ray2.30A/B439-779[»]
4MUWX-ray2.64A/B442-779[»]
4MVHX-ray2.50A/B442-779[»]
4P0NX-ray2.08A/B442-779[»]
4P1RX-ray2.24A/B442-779[»]
4PHWX-ray2.50A/B442-779[»]
4TPMX-ray2.77A/B442-779[»]
4TPPX-ray2.65A/B442-779[»]
4WN1X-ray3.13A/B439-779[»]
4XY2X-ray2.03A/B439-779[»]
4YQHX-ray2.31A/B439-759[»]
4YS7X-ray2.50A/B439-759[»]
4ZO5X-ray2.50A/B439-759[»]
5AXPX-ray1.95A/B442-779[»]
5AXQX-ray1.77A/B442-779[»]
5B4KX-ray2.90A/B442-779[»]
5B4LX-ray2.40A/B442-779[»]
5C1WX-ray1.70A/B439-779[»]
5C28X-ray1.56A/B439-779[»]
5C29X-ray2.05A/B439-779[»]
5C2AX-ray2.00A/B439-779[»]
5C2EX-ray2.10A/B439-779[»]
5C2HX-ray2.09A/B439-779[»]
5DH4X-ray2.20A/B439-779[»]
5DH5X-ray2.00A/B439-779[»]
5EDEX-ray2.20A/C/D447-760[»]
B448-760[»]
5EDGX-ray2.30A/B/C/D447-760[»]
5EDHX-ray2.03A/B/C/D448-760[»]
5EDIX-ray2.20A/B/C/D442-760[»]
5I2RX-ray2.50A/B/C/D447-763[»]
5K9RX-ray2.70A/B448-759[»]
ProteinModelPortaliQ9Y233.
SMRiQ9Y233.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116057. 2 interactors.
IntActiQ9Y233. 1 interactor.
MINTiMINT-1401257.
STRINGi9606.ENSP00000438284.

Chemistry databases

BindingDBiQ9Y233.
ChEMBLiCHEMBL4409.
DrugBankiDB00201. Caffeine.
DB00975. Dipyridamole.
DB01113. Papaverine.
DB08811. Tofisopam.
DB08814. Triflusal.
GuidetoPHARMACOLOGYi1310.

PTM databases

iPTMnetiQ9Y233.
PhosphoSitePlusiQ9Y233.
SwissPalmiQ9Y233.

Polymorphism and mutation databases

BioMutaiPDE10A.
DMDMi7993747.

Proteomic databases

PaxDbiQ9Y233.
PeptideAtlasiQ9Y233.
PRIDEiQ9Y233.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366882; ENSP00000355847; ENSG00000112541. [Q9Y233-1]
ENST00000539869; ENSP00000438284; ENSG00000112541. [Q9Y233-2]
GeneIDi10846.
KEGGihsa:10846.
UCSCiuc003quo.4. human. [Q9Y233-1]

Organism-specific databases

CTDi10846.
DisGeNETi10846.
GeneCardsiPDE10A.
HGNCiHGNC:8772. PDE10A.
HPAiCAB045998.
HPA047200.
MIMi610652. gene.
616921. phenotype.
616922. phenotype.
neXtProtiNX_Q9Y233.
OpenTargetsiENSG00000112541.
PharmGKBiPA33120.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3689. Eukaryota.
ENOG410XRI7. LUCA.
GeneTreeiENSGT00760000119066.
HOGENOMiHOG000007068.
HOVERGENiHBG082113.
KOiK18438.
OMAiCRFTMSV.
OrthoDBiEOG091G037C.
PhylomeDBiQ9Y233.
TreeFamiTF316499.

Enzyme and pathway databases

UniPathwayiUPA00762; UER00747.
UPA00763; UER00748.
BioCyciZFISH:HS03586-MONOMER.
BRENDAi3.1.4.17. 2681.
ReactomeiR-HSA-418457. cGMP effects.
R-HSA-418555. G alpha (s) signalling events.
SIGNORiQ9Y233.

Miscellaneous databases

EvolutionaryTraceiQ9Y233.
GeneWikiiPDE10A.
GenomeRNAii10846.
PROiQ9Y233.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000112541.
CleanExiHS_PDE10A.
ExpressionAtlasiQ9Y233. baseline and differential.
GenevisibleiQ9Y233. HS.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom-like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 2 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDE10_HUMAN
AccessioniPrimary (citable) accession number: Q9Y233
Secondary accession number(s): Q6FHX1
, Q9HCP9, Q9NTV4, Q9ULW9, Q9Y5T1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.