Skip Header

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

High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B

Gene

PDE8B

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

Functioni

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland.

Catalytic activityi

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.1 Publication

Cofactori

a divalent metal cationBy similarityNote: 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.By similarity

Enzyme regulationi

Inhibited by dipyridimole. Insensitive to selective PDE inhibitors including rolipram and milrinone as well as to the non-selective inhibitor, IBMX. Unaffected by cGMP.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei615 – 6151Proton donorBy similarity
Metal bindingi619 – 6191Divalent metal cation 1By similarity
Metal bindingi655 – 6551Divalent metal cation 1By similarity
Metal bindingi656 – 6561Divalent metal cation 1By similarity
Metal bindingi656 – 6561Divalent metal cation 2By similarity
Metal bindingi781 – 7811Divalent metal cation 1By similarity

GO - Molecular functioni

  1. 3',5'-cyclic-AMP phosphodiesterase activity Source: Ensembl
  2. 3',5'-cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. signal transducer activity Source: InterPro

GO - Biological processi

  1. behavioral fear response Source: Ensembl
  2. cAMP catabolic process Source: UniProtKB-UniPathway
  3. cyclic nucleotide metabolic process Source: UniProtKB
  4. negative regulation of insulin secretion Source: Ensembl
  5. negative regulation of steroid hormone biosynthetic process Source: Ensembl
  6. neuromuscular process controlling balance Source: Ensembl
  7. operant conditioning Source: Ensembl
  8. phosphorelay signal transduction system Source: InterPro
  9. visual learning Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.4.53. 2681.
ReactomeiREACT_19327. G alpha (s) signalling events.
UniPathwayiUPA00762; UER00747.

Names & Taxonomyi

Protein namesi
Recommended name:
High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B (EC:3.1.4.53)
Short name:
HsPDE8B
Alternative name(s):
Cell proliferation-inducing gene 22 protein
Gene namesi
Name:PDE8B
ORF Names:PIG22
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:8794. PDE8B.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Striatal degeneration autosomal dominant (ADSD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA movement disorder affecting the striatal part of the basal ganglia and characterized by bradykinesia, dysarthria and muscle rigidity. These symptoms resemble idiopathic Parkinson disease, but tremor is not present.

See also OMIM:609161
Primary pigmented nodular adrenocortical disease 3 (PPNAD3)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. Adrenal glands show overall normal size and weight, and multiple small yellow-to-dark brown nodules surrounded by a cortex with a uniform appearance. Microscopically, there are moderate diffuse cortical hyperplasia with mostly nonpigmented nodules, multiple capsular deficits and massive circumscribed and infiltrating extra-adrenal cortical excrescences with micronodules. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes.

See also OMIM:614190
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti305 – 3051H → P in PPNAD3; shows significantly higher cyclic AMP levels after transfection with the mutant protein than after transfection with the wild-type, indicating an impaired ability of the mutant protein to degrade cAMP. 1 Publication
VAR_066503

Keywords - Diseasei

Cushing syndrome, Disease mutation

Organism-specific databases

MIMi609161. phenotype.
614190. phenotype.
Orphaneti228169. Autosomal dominant striatal neurodegeneration.
189439. Primary pigmented nodular adrenocortical disease.
PharmGKBiPA33142.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 885885High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8BPRO_0000198840Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei517 – 5171Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95263.
PaxDbiO95263.
PRIDEiO95263.

2D gel databases

UCD-2DPAGEO95263.

PTM databases

PhosphoSiteiO95263.

Expressioni

Tissue specificityi

Abundantly expressed in the thyroid. Also very weakly expressed in brain, spinal cord and placenta. In the thyroid isoform 1 predominates, and isoforms 2 and 6 are also highly expressed. In the placenta isoforms 1 and 2 are expressed equally. In the brain isoform 2 predominates.2 Publications

Gene expression databases

BgeeiO95263.
CleanExiHS_PDE8B.
ExpressionAtlasiO95263. baseline and differential.
GenevestigatoriO95263.

Organism-specific databases

HPAiHPA036912.

Interactioni

Protein-protein interaction databases

BioGridi114177. 1 interaction.
STRINGi9606.ENSP00000264917.

Structurei

3D structure databases

ProteinModelPortaliO95263.
SMRiO95263. Positions 273-383, 541-874.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 33872PASPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni590 – 868279CatalyticBy similarityAdd
BLAST

Domaini

Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain.

Sequence similaritiesi

Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG282089.
GeneTreeiENSGT00760000118889.
HOVERGENiHBG053544.
KOiK18437.
OMAiHLANNYK.
OrthoDBiEOG7X3QQM.
PhylomeDBiO95263.
TreeFamiTF314638.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
InterProiIPR003607. HD/PDEase_dom.
IPR000014. PAS.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
IPR013938. PDEase_PDE8.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF13426. PAS_9. 1 hit.
PF08629. PDE8. 1 hit.
PF00233. PDEase_I. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50112. PAS. 1 hit.
PS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O95263-1) [UniParc]FASTAAdd to basket

Also known as: PDE8B1

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
MGCAPSIHVS QSGVIYCRDS DESSSPRQTT SVSQGPAAPL PGLFVQTDAA
60 70 80 90 100
DAIPPSRASG PPSVARVRRA RTELGSGSSA GSAAPAATTS RGRRRHCCSS
110 120 130 140 150
AEAETQTCYT SVKQVSSAEV RIGPMRLTQD PIQVLLIFAK EDSQSDGFWW
160 170 180 190 200
ACDRAGYRCN IARTPESALE CFLDKHHEII VIDHRQTQNF DAEAVCRSIR
210 220 230 240 250
ATNPSEHTVI LAVVSRVSDD HEEASVLPLL HAGFNRRFME NSSIIACYNE
260 270 280 290 300
LIQIEHGEVR SQFKLRACNS VFTALDHCHE AIEITSDDHV IQYVNPAFER
310 320 330 340 350
MMGYHKGELL GKELADLPKS DKNRADLLDT INTCIKKGKE WQGVYYARRK
360 370 380 390 400
SGDSIQQHVK ITPVIGQGGK IRHFVSLKKL CCTTDNNKQI HKIHRDSGDN
410 420 430 440 450
SQTEPHSFRY KNRRKESIDV KSISSRGSDA PSLQNRRYPS MARIHSMTIE
460 470 480 490 500
APITKVINII NAAQENSPVT VAEALDRVLE ILRTTELYSP QLGTKDEDPH
510 520 530 540 550
TSDLVGGLMT DGLRRLSGNE YVFTKNVHQS HSHLAMPITI NDVPPCISQL
560 570 580 590 600
LDNEESWDFN IFELEAITHK RPLVYLGLKV FSRFGVCEFL NCSETTLRAW
610 620 630 640 650
FQVIEANYHS SNAYHNSTHA ADVLHATAFF LGKERVKGSL DQLDEVAALI
660 670 680 690 700
AATVHDVDHP GRTNSFLCNA GSELAVLYND TAVLESHHTA LAFQLTVKDT
710 720 730 740 750
KCNIFKNIDR NHYRTLRQAI IDMVLATEMT KHFEHVNKFV NSINKPMAAE
760 770 780 790 800
IEGSDCECNP AGKNFPENQI LIKRMMIKCA DVANPCRPLD LCIEWAGRIS
810 820 830 840 850
EEYFAQTDEE KRQGLPVVMP VFDRNTCSIP KSQISFIDYF ITDMFDAWDA
860 870 880
FAHLPALMQH LADNYKHWKT LDDLKCKSLR LPSDS

Note: Major isoform.

Length:885
Mass (Da):98,979
Last modified:August 21, 2003 - v2
Checksum:iDB4F763E51F745A3
GO
Isoform 2 (identifier: O95263-2) [UniParc]FASTAAdd to basket

Also known as: PDE8B2, PDE8B3

The sequence of this isoform differs from the canonical sequence as follows:
     293-389: Missing.

Show »
Length:788
Mass (Da):87,974
Checksum:i816AECACCAE45447
GO
Isoform 3 (identifier: O95263-3) [UniParc]FASTAAdd to basket

Also known as: PDE8B3

The sequence of this isoform differs from the canonical sequence as follows:
     456-510: Missing.

Show »
Length:830
Mass (Da):93,047
Checksum:i5A39ED08E2A877E4
GO
Isoform 4 (identifier: O95263-4) [UniParc]FASTAAdd to basket

Also known as: PDE8B4

The sequence of this isoform differs from the canonical sequence as follows:
     114-133: Missing.

Show »
Length:865
Mass (Da):96,771
Checksum:iDDC83E5525C7E7B7
GO
Isoform 5 (identifier: O95263-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-535: Missing.

Note: No experimental confirmation available.

Show »
Length:350
Mass (Da):39,791
Checksum:iA6D4F19BE26C045F
GO
Isoform 6 (identifier: O95263-6) [UniParc]FASTAAdd to basket

Also known as: PDE8B2

The sequence of this isoform differs from the canonical sequence as follows:
     293-339: Missing.

Show »
Length:838
Mass (Da):93,674
Checksum:i013C790AC0F24F92
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti147 – 1471G → R in CAD38584 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti305 – 3051H → P in PPNAD3; shows significantly higher cyclic AMP levels after transfection with the mutant protein than after transfection with the wild-type, indicating an impaired ability of the mutant protein to degrade cAMP. 1 Publication
VAR_066503

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 535535Missing in isoform 5. 2 PublicationsVSP_008081Add
BLAST
Alternative sequencei114 – 13320Missing in isoform 4. 1 PublicationVSP_008082Add
BLAST
Alternative sequencei293 – 38997Missing in isoform 2. 2 PublicationsVSP_008084Add
BLAST
Alternative sequencei293 – 33947Missing in isoform 6. 1 PublicationVSP_008083Add
BLAST
Alternative sequencei456 – 51055Missing in isoform 3. 1 PublicationVSP_008085Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY129948 mRNA. Translation: AAN71723.1.
AY129949 mRNA. Translation: AAN71724.1.
AY129950 Genomic DNA. Translation: AAN71725.1.
AY129950 Genomic DNA. Translation: AAN71726.1.
AY129950 Genomic DNA. Translation: AAN71727.1.
AB085824 mRNA. Translation: BAC53762.1.
AB085825 mRNA. Translation: BAC53763.1.
AB085826 mRNA. Translation: BAC53764.1.
AB085827 mRNA. Translation: BAC53765.1.
AY423729 mRNA. Translation: AAS00492.1.
CH471084 Genomic DNA. Translation: EAW95803.1.
BC043209 mRNA. No translation available.
AF079529 mRNA. Translation: AAC69564.2.
AL831924 mRNA. Translation: CAD38584.1.
CCDSiCCDS34190.1. [O95263-3]
CCDS34191.1. [O95263-6]
CCDS34192.1. [O95263-2]
CCDS34193.1. [O95263-4]
CCDS4037.1. [O95263-1]
PIRiJE0293.
RefSeqiNP_001025022.1. NM_001029851.2. [O95263-2]
NP_001025023.1. NM_001029852.2. [O95263-3]
NP_001025024.1. NM_001029853.2. [O95263-4]
NP_001025025.1. NM_001029854.2. [O95263-6]
NP_003710.1. NM_003719.3. [O95263-1]
UniGeneiHs.584830.

Genome annotation databases

EnsembliENST00000264917; ENSP00000264917; ENSG00000113231. [O95263-1]
ENST00000333194; ENSP00000331336; ENSG00000113231. [O95263-3]
ENST00000340978; ENSP00000345446; ENSG00000113231. [O95263-6]
ENST00000342343; ENSP00000345646; ENSG00000113231. [O95263-4]
ENST00000346042; ENSP00000330428; ENSG00000113231. [O95263-2]
ENST00000505283; ENSP00000423461; ENSG00000113231. [O95263-5]
GeneIDi8622.
KEGGihsa:8622.
UCSCiuc003kfa.3. human. [O95263-1]
uc003kfb.3. human. [O95263-4]
uc003kfc.3. human. [O95263-3]
uc003kfd.3. human. [O95263-6]
uc003kfe.3. human. [O95263-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY129948 mRNA. Translation: AAN71723.1.
AY129949 mRNA. Translation: AAN71724.1.
AY129950 Genomic DNA. Translation: AAN71725.1.
AY129950 Genomic DNA. Translation: AAN71726.1.
AY129950 Genomic DNA. Translation: AAN71727.1.
AB085824 mRNA. Translation: BAC53762.1.
AB085825 mRNA. Translation: BAC53763.1.
AB085826 mRNA. Translation: BAC53764.1.
AB085827 mRNA. Translation: BAC53765.1.
AY423729 mRNA. Translation: AAS00492.1.
CH471084 Genomic DNA. Translation: EAW95803.1.
BC043209 mRNA. No translation available.
AF079529 mRNA. Translation: AAC69564.2.
AL831924 mRNA. Translation: CAD38584.1.
CCDSiCCDS34190.1. [O95263-3]
CCDS34191.1. [O95263-6]
CCDS34192.1. [O95263-2]
CCDS34193.1. [O95263-4]
CCDS4037.1. [O95263-1]
PIRiJE0293.
RefSeqiNP_001025022.1. NM_001029851.2. [O95263-2]
NP_001025023.1. NM_001029852.2. [O95263-3]
NP_001025024.1. NM_001029853.2. [O95263-4]
NP_001025025.1. NM_001029854.2. [O95263-6]
NP_003710.1. NM_003719.3. [O95263-1]
UniGeneiHs.584830.

3D structure databases

ProteinModelPortaliO95263.
SMRiO95263. Positions 273-383, 541-874.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114177. 1 interaction.
STRINGi9606.ENSP00000264917.

Chemistry

BindingDBiO95263.
ChEMBLiCHEMBL4408.
DrugBankiDB00201. Caffeine.
DB00920. Ketotifen.
GuidetoPHARMACOLOGYi1308.

PTM databases

PhosphoSiteiO95263.

2D gel databases

UCD-2DPAGEO95263.

Proteomic databases

MaxQBiO95263.
PaxDbiO95263.
PRIDEiO95263.

Protocols and materials databases

DNASUi8622.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264917; ENSP00000264917; ENSG00000113231. [O95263-1]
ENST00000333194; ENSP00000331336; ENSG00000113231. [O95263-3]
ENST00000340978; ENSP00000345446; ENSG00000113231. [O95263-6]
ENST00000342343; ENSP00000345646; ENSG00000113231. [O95263-4]
ENST00000346042; ENSP00000330428; ENSG00000113231. [O95263-2]
ENST00000505283; ENSP00000423461; ENSG00000113231. [O95263-5]
GeneIDi8622.
KEGGihsa:8622.
UCSCiuc003kfa.3. human. [O95263-1]
uc003kfb.3. human. [O95263-4]
uc003kfc.3. human. [O95263-3]
uc003kfd.3. human. [O95263-6]
uc003kfe.3. human. [O95263-2]

Organism-specific databases

CTDi8622.
GeneCardsiGC05P076542.
H-InvDBHIX0004971.
HGNCiHGNC:8794. PDE8B.
HPAiHPA036912.
MIMi603390. gene.
609161. phenotype.
614190. phenotype.
neXtProtiNX_O95263.
Orphaneti228169. Autosomal dominant striatal neurodegeneration.
189439. Primary pigmented nodular adrenocortical disease.
PharmGKBiPA33142.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG282089.
GeneTreeiENSGT00760000118889.
HOVERGENiHBG053544.
KOiK18437.
OMAiHLANNYK.
OrthoDBiEOG7X3QQM.
PhylomeDBiO95263.
TreeFamiTF314638.

Enzyme and pathway databases

UniPathwayiUPA00762; UER00747.
BRENDAi3.1.4.53. 2681.
ReactomeiREACT_19327. G alpha (s) signalling events.

Miscellaneous databases

ChiTaRSiPDE8B. human.
GeneWikiiPDE8B.
GenomeRNAii8622.
NextBioi32309.
PROiO95263.
SOURCEiSearch...

Gene expression databases

BgeeiO95263.
CleanExiHS_PDE8B.
ExpressionAtlasiO95263. baseline and differential.
GenevestigatoriO95263.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
InterProiIPR003607. HD/PDEase_dom.
IPR000014. PAS.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
IPR013938. PDEase_PDE8.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
PfamiPF13426. PAS_9. 1 hit.
PF08629. PDE8. 1 hit.
PF00233. PDEase_I. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
SM00091. PAS. 1 hit.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 1 hit.
TIGRFAMsiTIGR00229. sensory_box. 1 hit.
PROSITEiPS50112. PAS. 1 hit.
PS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic organization, chromosomal localization, and alternative splicing of the human phosphodiesterase 8B gene."
    Hayashi M., Shimada Y., Nishimura Y., Hama T., Tanaka T.
    Biochem. Biophys. Res. Commun. 297:1253-1258(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 6), TISSUE SPECIFICITY.
  2. "Comparison of enzymatic characterization and gene organization of cyclic nucleotide phosphodiesterase 8 family in humans."
    Gamanuma M., Yuasa K., Sasaki T., Sakurai N., Kotera J., Omori K.
    Cell. Signal. 15:565-574(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
    Tissue: Thyroid.
  3. "Identification of a human proliferation-inducing gene."
    Kim J.W.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Tissue: Testis.
  6. "Molecular cloning and characterization of human PDE8B, a novel thyroid-specific isozyme of 3',5'-cyclic nucleotide phosphodiesterase."
    Hayashi M., Matsushima K., Ohashi H., Tsunoda H., Murase S., Kawarada Y., Tanaka T.
    Biochem. Biophys. Res. Commun. 250:751-756(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 227-885 (ISOFORM 1).
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-885 (ISOFORM 1).
    Tissue: Amygdala.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: INVOLVEMENT IN ADSD.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "A cAMP-specific phosphodiesterase (PDE8B) that is mutated in adrenal hyperplasia is expressed widely in human and mouse tissues: a novel PDE8B isoform in human adrenal cortex."
    Horvath A., Giatzakis C., Tsang K., Greene E., Osorio P., Boikos S., Libe R., Patronas Y., Robinson-White A., Remmers E., Bertherat J., Nesterova M., Stratakis C.A.
    Eur. J. Hum. Genet. 16:1245-1253(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PPNAD3 PRO-305, CHARACTERIZATION OF VARIANT PPNAD3 PRO-305.

Entry informationi

Entry nameiPDE8B_HUMAN
AccessioniPrimary (citable) accession number: O95263
Secondary accession number(s): Q5J7V7
, Q86XK8, Q8IUJ7, Q8IUJ8, Q8IUJ9, Q8IUK0, Q8N3T2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2000
Last sequence update: August 21, 2003
Last modified: March 31, 2015
This is version 150 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

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