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Q9Y233

- PDE10_HUMAN

UniProt

Q9Y233 - PDE10_HUMAN

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
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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

    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

    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

    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

    ArrayExpressiQ9Y233.
    BgeeiQ9Y233.
    CleanExiHS_PDE10A.
    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 – 26216
    Helixi267 – 28216
    Beta strandi284 – 29310
    Turni294 – 2974
    Beta strandi298 – 3047
    Beta strandi323 – 3253
    Helixi329 – 3379
    Beta strandi341 – 3444
    Helixi346 – 3483
    Helixi355 – 3606
    Beta strandi367 – 3748
    Beta strandi377 – 38711
    Beta strandi390 – 3923
    Helixi395 – 41925
    Helixi443 – 4497
    Helixi456 – 4616
    Beta strandi464 – 4663
    Helixi470 – 4756
    Helixi476 – 48813
    Turni490 – 4923
    Helixi495 – 50713
    Beta strandi513 – 5164
    Helixi517 – 53216
    Helixi533 – 5375
    Helixi540 – 55213
    Turni553 – 5564
    Helixi562 – 5676
    Helixi571 – 5755
    Beta strandi577 – 5793
    Helixi580 – 59314
    Turni596 – 5983
    Turni600 – 6034
    Helixi606 – 62217
    Helixi625 – 64016
    Beta strandi646 – 6483
    Helixi649 – 66416
    Helixi666 – 6694
    Helixi672 – 69524
    Helixi702 – 7043
    Helixi706 – 7116
    Helixi712 – 72211
    Helixi724 – 73411
    Helixi736 – 7383
    Helixi739 – 75719

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    ProteinModelPortaliQ9Y233.
    SMRiQ9Y233. Positions 77-765.
    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.
    HOGENOMiHOG000007068.
    HOVERGENiHBG082113.
    KOiK01120.
    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

    MRIEERKSQH LTGLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK    50
    NNKSEDESAP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNQLLLYELS 100
    SIIKIATKAD GFALYFLGEC NNSLCIFTPP GIKEGKPRLI PAGPITQGTT 150
    VSAYVAKSRK TLLVEDILGD ERFPRGTGLE SGTRIQSVLC LPIVTAIGDL 200
    IGILELYRHW GKEAFCLSHQ EVATANLAWA SVAIHQVQVC RGLAKQTELN 250
    DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF QVDHKNKELY 300
    SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP 350
    RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN 400
    FKMFAVFCAL ALHCANMYHR IRHSECIYRV TMEKLSYHSI CTSEEWQGLM 450
    QFTLPVRLCK EIELFHFDIG PFENMWPGIF VYMVHRSCGT SCFELEKLCR 500
    FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI LQNNHTLFTD LERKGLLIAC 550
    LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV SILQLEGHNI 600
    FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLNNQS 650
    HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP 700
    IPMMDRDKKD EVPQGQLGFY NAVAIPCYTT LTQILPPTEP LLKACRDNLS 750
    QWEKVIRGEE TATWISSPSV AQKAAASED 779
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 [» ]
    ProteinModelPortali Q9Y233.
    SMRi Q9Y233. Positions 77-765.
    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 CHEMBL2363066.
    DrugBanki DB00975. Dipyridamole.

    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.
    HOGENOMi HOG000007068.
    HOVERGENi HBG082113.
    KOi K01120.
    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

    ArrayExpressi Q9Y233.
    Bgeei Q9Y233.
    CleanExi HS_PDE10A.
    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

    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: October 1, 2014
    This is version 141 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