Q9Y233 (PDE10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	779 AA.
Sequence status	Complete.
Protein existence	Evidence 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
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 component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Metal-binding Nucleotide-binding cAMP cAMP-binding cGMP cGMP-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Allosteric enzyme Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood 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: Compara regulation of protein kinase A signaling cascade Inferred from electronic annotation. Source: Compara signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	3',5'-cyclic-GMP phosphodiesterase activity Inferred from electronic annotation. Source: EC 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: Phosphorylated at Thr-16 by PKA.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 779

779

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

PRO_0000198843

Regions

Domain

91 – 234

144

GAF 1

Domain

266 – 412

147

GAF 2

Region

286 – 287

2

Allosteric effector binding

Region

330 – 331

2

Allosteric effector binding

Sites

Active site

515

1

Proton donor By similarity

Metal binding

519

1

Divalent metal cation 1

Metal binding

553

1

Divalent metal cation 1

Metal binding

554

1

Divalent metal cation 1

Metal binding

554

1

Divalent metal cation 2

Metal binding

664

1

Divalent metal cation 1

Binding site

364

1

Allosteric effector

Binding site

383

1

Allosteric effector

Binding site

515

1

Substrate

Binding site

716

1

Substrate

Natural variations

Alternative sequence

1 – 13

13

MRIEE…QHLTG → MEDGPSNNASCFRRLTECFL SPS in isoform PDE10A2.

VSP_004601

Natural variant

303

1

L → P.

VAR_008797

Natural variant

706

1

R → K.
Corresponds to variant rs2224252 [ dbSNP | Ensembl ].

VAR_047822

Natural variant

707

1

D → N.
Corresponds to variant rs2860112 [ dbSNP | Ensembl ].

VAR_047823

Experimental info

Mutagenesis

554

1

D → A: Loss of activity and of zinc binding. Ref.11

Mutagenesis

554

1

D → N: Reduces activity 1000-fold. Ref.11

Sequence conflict

657

1

G → S in CAG38804. Ref.4

Secondary structure

1

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779

Helix Strand Turn

Details...

Helix

247 – 262

16

Helix

267 – 282

16

Beta strand

284 – 293

10

Turn

294 – 297

4

Beta strand

298 – 304

7

Beta strand

323 – 325

3

Helix

329 – 337

9

Beta strand

341 – 344

4

Helix

346 – 348

3

Helix

355 – 360

6

Beta strand

367 – 374

8

Beta strand

377 – 387

11

Beta strand

390 – 392

3

Helix

395 – 419

25

Helix

443 – 449

7

Helix

456 – 461

6

Beta strand

464 – 466

3

Helix

470 – 475

6

Helix

476 – 488

13

Turn

490 – 492

3

Helix

495 – 507

13

Beta strand

513 – 516

4

Helix

517 – 532

16

Helix

533 – 537

5

Helix

540 – 552

13

Turn

553 – 556

4

Helix

562 – 567

6

Helix

571 – 575

5

Beta strand

577 – 579

3

Helix

580 – 593

14

Turn

596 – 598

3

Turn

600 – 603

4

Helix

606 – 622

17

Helix

625 – 640

16

Helix

649 – 664

16

Helix

666 – 669

4

Helix

672 – 695

24

Helix

702 – 704

3

Helix

706 – 711

6

Helix

712 – 722

11

Helix

724 – 734

11

Helix

736 – 738

3

Helix

739 – 757

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform PDE10A1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: C5651BBB524A32B7	FASTA	779	88,412
	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
	Isoform PDE10A2 [UniParc]. Checksum: 7CC35F16735FB3C2	FASTA	789	89,390
	10 20 30 40 50 60 MEDGPSNNAS CFRRLTECFL SPSLTDEKVK AYLSLHPQVL DEFVSESVSA ETVEKWLKRK 70 80 90 100 110 120 NNKSEDESAP KEVSRYQDTN MQGVVYELNS YIEQRLDTGG DNQLLLYELS SIIKIATKAD 130 140 150 160 170 180 GFALYFLGEC NNSLCIFTPP GIKEGKPRLI PAGPITQGTT VSAYVAKSRK TLLVEDILGD 190 200 210 220 230 240 ERFPRGTGLE SGTRIQSVLC LPIVTAIGDL IGILELYRHW GKEAFCLSHQ EVATANLAWA 250 260 270 280 290 300 SVAIHQVQVC RGLAKQTELN DFLLDVSKTY FDNIVAIDSL LEHIMIYAKN LVNADRCALF 310 320 330 340 350 360 QVDHKNKELY SDLFDIGEEK EGKPVFKKTK EIRFSIEKGI AGQVARTGEV LNIPDAYADP 370 380 390 400 410 420 RFNREVDLYT GYTTRNILCM PIVSRGSVIG VVQMVNKISG SAFSKTDENN FKMFAVFCAL 430 440 450 460 470 480 ALHCANMYHR IRHSECIYRV TMEKLSYHSI CTSEEWQGLM QFTLPVRLCK EIELFHFDIG 490 500 510 520 530 540 PFENMWPGIF VYMVHRSCGT SCFELEKLCR FIMSVKKNYR RVPYHNWKHA VTVAHCMYAI 550 560 570 580 590 600 LQNNHTLFTD LERKGLLIAC LCHDLDHRGF SNSYLQKFDH PLAALYSTST MEQHHFSQTV 610 620 630 640 650 660 SILQLEGHNI FSTLSSSEYE QVLEIIRKAI IATDLALYFG NRKQLEEMYQ TGSLNLNNQS 670 680 690 700 710 720 HRDRVIGLMM TACDLCSVTK LWPVTKLTAN DIYAEFWAEG DEMKKLGIQP IPMMDRDKKD 730 740 750 760 770 780 EVPQGQLGFY NAVAIPCYTT LTQILPPTEP LLKACRDNLS QWEKVIRGEE TATWISSPSV AQKAAASED

References

	« Hide 'large scale' referencesShow '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 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]	"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.

IPI

IPI00297440.
IPI00939904.

RefSeq

NP_001124162.1. NM_001130690.2.

UniGene

Hs.348762.

3D structure databases

PDBe
RCSB PDB
PDBj

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	439-760	[»]
3UUO	X-ray	2.11	A/B	439-760	[»]
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	[»]
4DDL	X-ray	2.07	A/B	442-779	[»]
4DFF	X-ray	2.11	A/B	439-779	[»]
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	[»]

ProteinModelPortal

Q9Y233.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y233. 1 interaction.

MINT

MINT-1401257.

STRING

9606.ENSP00000341187.

PTM databases

PhosphoSite

Q9Y233.

Polymorphism databases

DMDM

7993747.

Proteomic databases

PaxDb

Q9Y233.

PRIDE

Q9Y233.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000354448; ENSP00000346435; ENSG00000112541.
ENST00000366882; ENSP00000355847; ENSG00000112541.
ENST00000539869; ENSP00000438284; ENSG00000112541.

GeneID

10846.

KEGG

hsa:10846.

UCSC

uc003qun.3. human.

Organism-specific databases

CTD

10846.

GeneCards

GC06M165714.

HGNC

HGNC:8772. PDE10A.

HPA

CAB045998.
HPA047200.

MIM

610652. gene.

neXtProt

NX_Q9Y233.

PharmGKB

PA33120.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG270709.

HOGENOM

HOG000007068.

HOVERGEN

HBG082113.

KO

K01120.

OrthoDB

EOG4MCWZN.

Enzyme and pathway databases

BRENDA

3.1.4.17. 2681.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

UniPathway

UPA00762; UER00747.
UPA00763; UER00748.

Gene expression databases

ArrayExpress

Q9Y233.

Bgee

Q9Y233.

CleanEx

HS_PDE10A.

Genevestigator

Q9Y233.

GermOnline

ENSG00000112541. Homo sapiens.

Family and domain databases

Gene3D

1.10.1300.10. 1 hit.

InterPro

IPR003018. GAF.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]

Pfam

PF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]

PRINTS

PR00387. PDIESTERASE1.

SMART

SM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]

PROSITE

PS00126. PDEASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9Y233.

ChEMBL

CHEMBL4409.

DrugBank

DB00975. Dipyridamole.

EvolutionaryTrace

Q9Y233.

GenomeRNAi

10846.

NextBio

41178.

SOURCE

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Entry information

Entry name

PDE10_HUMAN

Accession

Primary (citable) accession number: Q9Y233
Secondary accession number(s): Q6FHX1 , Q9HCP9, Q9NTV4, Q9ULW9, Q9Y5T1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.