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Q9Y233 (PDE10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A

EC=3.1.4.17
EC=3.1.4.35
Gene names
Name:PDE10A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length779 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Catalytic activity

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

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

Cofactor

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. Ref.11

Enzyme regulation

Inhibited by dipyridamole and moderately by IBMX. cAMP acts as an allosteric activator. Ref.8

Pathway

Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.

Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.

Subunit structure

Homodimer. Ref.12

Subcellular location

Cytoplasm. Note: Located mostly to soluble cellular fractions.

Tissue specificity

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

Domain

The tandem GAF domains bind cAMP, and regulate enzyme activity. The binding of cAMP stimulates enzyme activity. Ref.8 Ref.12

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. Ref.8 Ref.12

Post-translational modification

Isoform PDE10A1:Phosphorylated on Thr-16. Ref.1

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Contains 2 GAF domains.

Biophysicochemical properties

Kinetic parameters:

KM=56 nM for cAMP Ref.11

KM=4.4 µM for cGMP

Vmax=507 nmol/min/mg enzyme for cAMP

Vmax=1860 nmol/min/mg enzyme for cGMP

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandcAMP
cAMP-binding
cGMP
cGMP-binding
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cAMP catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cGMP catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

regulation of cAMP-mediated signaling

Inferred from electronic annotation. Source: Ensembl

regulation of protein kinase A signaling

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_function3',5'-cyclic-GMP phosphodiesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

3',5'-cyclic-nucleotide phosphodiesterase activity

Traceable author statement Ref.2. Source: ProtInc

cAMP binding

Inferred from direct assay PubMed 19689430. Source: UniProtKB

cGMP binding

Non-traceable author statement PubMed 15938621. Source: UniProtKB

cGMP-stimulated cyclic-nucleotide phosphodiesterase activity

Inferred from direct assay PubMed 19689430. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoforms differ in their N-terminal region.
Isoform PDE10A1 (identifier: Q9Y233-1)

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.
Isoform PDE10A2 (identifier: Q9Y233-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MRIEERKSQHLTG → MEDGPSNNASCFRRLTECFLSPS
Note: Contains a phosphothreonine at position 16.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 779779cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
PRO_0000198843

Regions

Domain91 – 234144GAF 1
Domain266 – 412147GAF 2
Region286 – 2872Allosteric effector binding
Region330 – 3312Allosteric effector binding

Sites

Active site5151Proton donor By similarity
Metal binding5191Divalent metal cation 1
Metal binding5531Divalent metal cation 1
Metal binding5541Divalent metal cation 1
Metal binding5541Divalent metal cation 2
Metal binding6641Divalent metal cation 1
Binding site3641Allosteric effector
Binding site3831Allosteric effector
Binding site5151Substrate
Binding site7161Substrate

Natural variations

Alternative sequence1 – 1313MRIEE…QHLTG → MEDGPSNNASCFRRLTECFL SPS in isoform PDE10A2.
VSP_004601
Natural variant3031L → P.
VAR_008797
Natural variant7061R → K.
Corresponds to variant rs2224252 [ dbSNP | Ensembl ].
VAR_047822
Natural variant7071D → N.
Corresponds to variant rs2860112 [ dbSNP | Ensembl ].
VAR_047823

Experimental info

Mutagenesis5541D → A: Loss of activity and of zinc binding. Ref.11
Mutagenesis5541D → N: Reduces activity 1000-fold. Ref.11
Sequence conflict6571G → S in CAG38804. Ref.4

Secondary structure

............................................................................... 779
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform PDE10A1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: C5651BBB524A32B7

FASTA77988,412
        10         20         30         40         50         60 
MRIEERKSQH LTGLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK NNKSEDESAP 

        70         80         90        100        110        120 
KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNQLLLYELS SIIKIATKAD GFALYFLGEC 

       130        140        150        160        170        180 
NNSLCIFTPP GIKEGKPRLI PAGPITQGTT VSAYVAKSRK TLLVEDILGD ERFPRGTGLE 

       190        200        210        220        230        240 
SGTRIQSVLC LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA SVAIHQVQVC 

       250        260        270        280        290        300 
RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF QVDHKNKELY 

       310        320        330        340        350        360 
SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP RFNREVDLYT 

       370        380        390        400        410        420 
GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN FKMFAVFCAL ALHCANMYHR 

       430        440        450        460        470        480 
IRHSECIYRV TMEKLSYHSI CTSEEWQGLM QFTLPVRLCK EIELFHFDIG PFENMWPGIF 

       490        500        510        520        530        540 
VYMVHRSCGT SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI LQNNHTLFTD 

       550        560        570        580        590        600 
LERKGLLIAC LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV SILQLEGHNI 

       610        620        630        640        650        660 
FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLNNQS HRDRVIGLMM 

       670        680        690        700        710        720 
TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP IPMMDRDKKD EVPQGQLGFY 

       730        740        750        760        770 
NAVAIPCYTT LTQILPPTEP LLKACRDNLS QWEKVIRGEE TATWISSPSV AQKAAASED 

« Hide

Isoform PDE10A2 [UniParc].

Checksum: 7CC35F16735FB3C2
Show »

FASTA78989,390

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS47513.1. [Q9Y233-2]
RefSeqNP_001124162.1. NM_001130690.2. [Q9Y233-2]
UniGeneHs.348762.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
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[»]
ProteinModelPortalQ9Y233.
SMRQ9Y233. Positions 77-765.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116057. 2 interactions.
IntActQ9Y233. 1 interaction.
MINTMINT-1401257.
STRING9606.ENSP00000341187.

Chemistry

BindingDBQ9Y233.
ChEMBLCHEMBL2363066.
DrugBankDB00975. Dipyridamole.

PTM databases

PhosphoSiteQ9Y233.

Polymorphism databases

DMDM7993747.

Proteomic databases

MaxQBQ9Y233.
PaxDbQ9Y233.
PRIDEQ9Y233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354448; ENSP00000346435; ENSG00000112541. [Q9Y233-1]
ENST00000366882; ENSP00000355847; ENSG00000112541. [Q9Y233-1]
ENST00000539869; ENSP00000438284; ENSG00000112541. [Q9Y233-2]
GeneID10846.
KEGGhsa:10846.
UCSCuc003qun.3. human. [Q9Y233-1]
uc003quo.3. human. [Q9Y233-2]

Organism-specific databases

CTD10846.
GeneCardsGC06M165714.
HGNCHGNC:8772. PDE10A.
HPACAB045998.
HPA047200.
MIM610652. gene.
neXtProtNX_Q9Y233.
PharmGKBPA33120.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270709.
HOGENOMHOG000007068.
HOVERGENHBG082113.
KOK01120.
OMACRFTMSV.
OrthoDBEOG7WQ7RN.
PhylomeDBQ9Y233.
TreeFamTF316499.

Enzyme and pathway databases

BRENDA3.1.4.17. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
UniPathwayUPA00762; UER00747.
UPA00763; UER00748.

Gene expression databases

ArrayExpressQ9Y233.
BgeeQ9Y233.
CleanExHS_PDE10A.
GenevestigatorQ9Y233.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMSSF55781. SSF55781. 2 hits.
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y233.
GeneWikiPDE10A.
GenomeRNAi10846.
NextBio41178.
PROQ9Y233.
SOURCESearch...

Entry information

Entry namePDE10_HUMAN
AccessionPrimary (citable) accession number: Q9Y233
Secondary accession number(s): Q6FHX1 expand/collapse secondary AC list , Q9HCP9, Q9NTV4, Q9ULW9, Q9Y5T1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM