Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y233

- PDE10_HUMAN

UniProt

Q9Y233 - PDE10_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

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

Gene

PDE10A

Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 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

Vmax=507 nmol/min/mg enzyme for cAMP1 Publication

Vmax=1860 nmol/min/mg enzyme for cGMP1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei364 – 3641Allosteric effector
Binding sitei383 – 3831Allosteric effector
Active sitei515 – 5151Proton donorBy similarity
Binding sitei515 – 5151Substrate
Metal bindingi519 – 5191Divalent metal cation 1
Metal bindingi553 – 5531Divalent metal cation 1
Metal bindingi554 – 5541Divalent metal cation 1
Metal bindingi554 – 5541Divalent metal cation 2
Metal bindingi664 – 6641Divalent metal cation 1
Binding sitei716 – 7161Substrate

GO - Molecular functioni

  1. 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB-EC
  2. 3',5'-cyclic-nucleotide phosphodiesterase activity Source: ProtInc
  3. cAMP binding Source: UniProtKB
  4. cGMP binding Source: UniProtKB
  5. cGMP-stimulated cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  6. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cAMP catabolic process Source: UniProtKB-UniPathway
  3. cGMP catabolic process Source: UniProtKB-UniPathway
  4. regulation of cAMP-mediated signaling Source: Ensembl
  5. regulation of protein kinase A signaling Source: Ensembl
  6. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi3.1.4.17. 2681.
ReactomeiREACT_19327. G alpha (s) signalling events.
REACT_23767. cGMP effects.
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
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:8772. PDE10A.

Subcellular locationi

Cytoplasm
Note: Located mostly to soluble cellular fractions.

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi554 – 5541D → A: Loss of activity and of zinc binding. 1 Publication
Mutagenesisi554 – 5541D → N: Reduces activity 1000-fold. 1 Publication

Organism-specific databases

PharmGKBiPA33120.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 779779cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10APRO_0000198843Add
BLAST

Post-translational modificationi

Isoform PDE10A1: Phosphorylated on Thr-16.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y233.
PaxDbiQ9Y233.
PRIDEiQ9Y233.

PTM databases

PhosphoSiteiQ9Y233.

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.

Gene expression databases

BgeeiQ9Y233.
CleanExiHS_PDE10A.
ExpressionAtlasiQ9Y233. baseline and differential.
GenevestigatoriQ9Y233.

Organism-specific databases

HPAiCAB045998.
HPA047200.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi116057. 2 interactions.
IntActiQ9Y233. 1 interaction.
MINTiMINT-1401257.
STRINGi9606.ENSP00000341187.

Structurei

Secondary structure

1
779
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi247 – 26216Combined sources
Helixi267 – 28216Combined sources
Beta strandi284 – 29310Combined sources
Turni294 – 2974Combined sources
Beta strandi298 – 3047Combined sources
Beta strandi323 – 3253Combined sources
Helixi329 – 3379Combined sources
Beta strandi341 – 3444Combined sources
Helixi346 – 3483Combined sources
Helixi355 – 3606Combined sources
Beta strandi367 – 3748Combined sources
Beta strandi377 – 38711Combined sources
Beta strandi390 – 3923Combined sources
Helixi395 – 41925Combined sources
Helixi443 – 4497Combined sources
Helixi456 – 4616Combined sources
Beta strandi464 – 4663Combined sources
Helixi470 – 4756Combined sources
Helixi476 – 48813Combined sources
Turni490 – 4923Combined sources
Helixi495 – 50713Combined sources
Beta strandi513 – 5164Combined sources
Helixi517 – 53216Combined sources
Helixi533 – 5375Combined sources
Helixi540 – 55213Combined sources
Turni553 – 5564Combined sources
Helixi562 – 5676Combined sources
Helixi571 – 5755Combined sources
Beta strandi577 – 5793Combined sources
Helixi580 – 59314Combined sources
Turni596 – 5983Combined sources
Turni600 – 6034Combined sources
Helixi606 – 62217Combined sources
Helixi625 – 64016Combined sources
Beta strandi646 – 6483Combined sources
Helixi649 – 66416Combined sources
Helixi666 – 6694Combined sources
Helixi672 – 69524Combined sources
Helixi702 – 7043Combined sources
Helixi706 – 7116Combined sources
Helixi712 – 72211Combined sources
Helixi724 – 73411Combined sources
Helixi736 – 7383Combined sources
Helixi739 – 75719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
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[»]
ProteinModelPortaliQ9Y233.
SMRiQ9Y233. Positions 144-765.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y233.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 234144GAF 1Add
BLAST
Domaini266 – 412147GAF 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni286 – 2872Allosteric effector binding
Regioni330 – 3312Allosteric effector binding

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

eggNOGiNOG270709.
GeneTreeiENSGT00760000119066.
HOGENOMiHOG000007068.
HOVERGENiHBG082113.
KOiK18438.
OMAiCRFTMSV.
OrthoDBiEOG7WQ7RN.
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. Align

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

Note: Contains a phosphothreonine at position 16.

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

Sequence cautioni

The sequence AAD32596.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti657 – 6571G → S in CAG38804. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031L → P.
VAR_008797
Natural varianti706 – 7061R → K.
Corresponds to variant rs2224252 [ dbSNP | Ensembl ].
VAR_047822
Natural varianti707 – 7071D → N.
Corresponds to variant rs2860112 [ dbSNP | Ensembl ].
VAR_047823

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1313MRIEE…QHLTG → MEDGPSNNASCFRRLTECFL SPS in isoform PDE10A2. 2 PublicationsVSP_004601Add
BLAST

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]
RefSeqiNP_001124162.1. NM_001130690.2. [Q9Y233-2]
UniGeneiHs.348762.

Genome annotation databases

EnsembliENST00000366882; ENSP00000355847; ENSG00000112541. [Q9Y233-1]
ENST00000539869; ENSP00000438284; ENSG00000112541. [Q9Y233-2]
GeneIDi10846.
KEGGihsa:10846.
UCSCiuc003qun.3. human. [Q9Y233-1]
uc003quo.3. human. [Q9Y233-2]

Polymorphism databases

DMDMi7993747.

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 .
CCDSi CCDS47513.1. [Q9Y233-2 ]
RefSeqi NP_001124162.1. NM_001130690.2. [Q9Y233-2 ]
UniGenei Hs.348762.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LRB model - A 501-757 [» ]
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 [» ]
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 [» ]
ProteinModelPortali Q9Y233.
SMRi Q9Y233. Positions 144-765.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116057. 2 interactions.
IntActi Q9Y233. 1 interaction.
MINTi MINT-1401257.
STRINGi 9606.ENSP00000341187.

Chemistry

BindingDBi Q9Y233.
ChEMBLi CHEMBL4409.
DrugBanki DB00201. Caffeine.
DB00975. Dipyridamole.
DB01113. Papaverine.
DB08811. Tofisopam.
DB08814. Triflusal.

PTM databases

PhosphoSitei Q9Y233.

Polymorphism databases

DMDMi 7993747.

Proteomic databases

MaxQBi Q9Y233.
PaxDbi Q9Y233.
PRIDEi Q9Y233.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366882 ; ENSP00000355847 ; ENSG00000112541 . [Q9Y233-1 ]
ENST00000539869 ; ENSP00000438284 ; ENSG00000112541 . [Q9Y233-2 ]
GeneIDi 10846.
KEGGi hsa:10846.
UCSCi uc003qun.3. human. [Q9Y233-1 ]
uc003quo.3. human. [Q9Y233-2 ]

Organism-specific databases

CTDi 10846.
GeneCardsi GC06M165714.
HGNCi HGNC:8772. PDE10A.
HPAi CAB045998.
HPA047200.
MIMi 610652. gene.
neXtProti NX_Q9Y233.
PharmGKBi PA33120.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG270709.
GeneTreei ENSGT00760000119066.
HOGENOMi HOG000007068.
HOVERGENi HBG082113.
KOi K18438.
OMAi CRFTMSV.
OrthoDBi EOG7WQ7RN.
PhylomeDBi Q9Y233.
TreeFami TF316499.

Enzyme and pathway databases

UniPathwayi UPA00762 ; UER00747 .
UPA00763 ; UER00748 .
BRENDAi 3.1.4.17. 2681.
Reactomei REACT_19327. G alpha (s) signalling events.
REACT_23767. cGMP effects.

Miscellaneous databases

EvolutionaryTracei Q9Y233.
GeneWikii PDE10A.
GenomeRNAii 10846.
NextBioi 41178.
PROi Q9Y233.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y233.
CleanExi HS_PDE10A.
ExpressionAtlasi Q9Y233. baseline and differential.
Genevestigatori Q9Y233.

Family and domain databases

Gene3Di 1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProi IPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view ]
Pfami PF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view ]
PRINTSi PR00387. PDIESTERASE1.
SMARTi SM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view ]
SUPFAMi SSF55781. SSF55781. 2 hits.
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and phosphorylation of PDE10A2, a novel alternative splice variant of human phosphodiesterase that hydrolyzes cAMP and cGMP."
    Kotera J., Fujishige K., Yuasa K., Omori K.
    Biochem. Biophys. Res. Commun. 261:551-557(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE10A2), PHOSPHORYLATION AT THR-16 (ISOFORM PDE10A2) BY PKA.
    Tissue: Fetal lung.
  2. "Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A)."
    Fujishige K., Kotera J., Michibata H., Yuasa K., Takebayashi S., Okumura K., Omori K.
    J. Biol. Chem. 274:18438-18445(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE10A1).
    Tissue: Fetal lung.
  3. "Isolation and characterization of PDE10A, a novel human 3',5'-cyclic nucleotide phosphodiesterase."
    Loughney K., Snyder P.B., Uher L., Rosman G.J., Ferguson K., Florio V.A.
    Gene 234:109-117(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PDE10A1 AND PDE10A2).
    Tissue: Fetal brain.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE10A1).
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE10A1).
    Tissue: Colon.
  7. "The human phosphodiesterase PDE10A gene genomic organization and evolutionary relatedness with other PDEs containing GAF domains."
    Fujishige K., Kotera J., Yuasa K., Omori K.
    Eur. J. Biochem. 267:5943-5951(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-779, ALTERNATIVE SPLICING.
  8. "cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11."
    Gross-Langenhoff M., Hofbauer K., Weber J., Schultz A., Schultz J.E.
    J. Biol. Chem. 281:2841-2846(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, ENZYME REGULATION.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural insight into substrate specificity of phosphodiesterase 10."
    Wang H., Liu Y., Hou J., Zheng M., Robinson H., Ke H.
    Proc. Natl. Acad. Sci. U.S.A. 104:5782-5787(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 436-766 IN COMPLEXES WITH AMP; CAMP; GMP; CGMP AND MAGNESIUM, MUTAGENESIS OF ASP-554, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
  12. "Crystal structure of the GAF-B domain from human phosphodiesterase 10A complexed with its ligand, cAMP."
    Handa N., Mizohata E., Kishishita S., Toyama M., Morita S., Uchikubo-Kamo T., Akasaka R., Omori K., Kotera J., Terada T., Shirouzu M., Yokoyama S.
    J. Biol. Chem. 283:19657-19664(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 242-427 IN COMPLEX WITH CAMP, DOMAIN, SUBUNIT.

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 26, 2014
This is version 143 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

External Data

Dasty 3