Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q08499 (PDE4D_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
cAMP-specific 3',5'-cyclic phosphodiesterase 4D

EC=3.1.4.53
Alternative name(s):
DPDE3
PDE43
Gene names
Name:PDE4D
Synonyms:DPDE3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length809 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. Ref.27 Ref.28

Catalytic activity

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 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.27 Ref.28

Enzyme regulation

Inhibited by rolipram. Activated by phosphatidic acid. Ref.13

Pathway

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

Subunit structure

Homodimer for the long isoforms. Isoforms with truncated N-termini are monomeric. Isoform 3 is part of a ternary complex containing PRKAR2A, PRKAR2B and AKAP9. Interacts with PDE4DIP. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1) By similarity. Isoform 5, isoform N3 and isoform 12 bind GNB2L1 via their unique N-terminus. Binds ARRB2. Interacts (via N-terminus region) with SHANK2 (via proline-rich region); the interaction is increased in a PKA-dependent manner. Ref.11 Ref.12 Ref.13 Ref.16 Ref.32

Subcellular location

Apical cell membrane. Cytoplasm By similarity. Membrane By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Found in the soluble fraction, associated with membranes, and associated with the cytoskeleton and the centrosome By similarity. Colocalized with SHANK2 to the apical membrane of colonic crypt cells. Ref.12

Tissue specificity

Expressed in colonic epithelial cells (at protein level). Widespread; most abundant in skeletal muscle. Isoform 6 is detected in brain. Isoform 8 is detected in brain, placenta, lung and kidney. Isoform 7 is detected in heart and skeletal muscle. Ref.6 Ref.16

Post-translational modification

Long isoforms that share a conserved PKA phosphorylation site in the N-terminus are activated by PKA through phosphorylation By similarity. Isoform 3 and isoform 7 are activated by phosphorylation (in vitro), but not isoform 6. Isoform N3 and isoform 12 are phosphorylated on Ser-49, Ser-51, Ser-55 and Ser-59. Ref.6 Ref.13

Sumoylation of long isoforms by PIAS4 augments their activation by PKA phosphorylation and represses their inhibition by ERK phosphorylation. Ref.19

Involvement in disease

Genetic variations in PDE4D might be associated with susceptibility to stroke. Ref.15 states that association with stroke has to be considered with caution.

Acrodysostosis 2, with or without hormone resistance (ACRDYS2) [MIM:614613]: A pleiotropic disorder characterized by skeletal, endocrine, and neurological abnormalities. Skeletal features include brachycephaly, midface hypoplasia with a small upturned nose, brachydactyly, and lumbar spinal stenosis. Endocrine abnormalities include hypothyroidism and hypogonadism in males and irregular menses in females. Developmental disability is a common finding but is variable in severity and can be associated with significant behavioral problems.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.34 Ref.35 Ref.36 Ref.37

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE4 subfamily.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   LigandcAMP
Metal-binding
   Molecular functionHydrolase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell receptor signaling pathway

Inferred from mutant phenotype PubMed 17404263. Source: BHF-UCL

adrenergic receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

adrenergic receptor signaling pathway involved in positive regulation of heart rate

Inferred by curator. Source: BHF-UCL

aging

Inferred from electronic annotation. Source: Ensembl

cAMP catabolic process

Inferred from direct assay PubMed 20819076. Source: BHF-UCL

cAMP-mediated signaling

Non-traceable author statement PubMed 16177794. Source: BHF-UCL

cellular response to cAMP

Inferred from direct assay PubMed 12121997. Source: BHF-UCL

cellular response to epinephrine stimulus

Inferred from direct assay PubMed 12121997. Source: BHF-UCL

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

establishment of endothelial barrier

Inferred from sequence or structural similarity. Source: UniProtKB

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of heart contraction

Inferred from sequence or structural similarity PubMed 21903937. Source: BHF-UCL

negative regulation of peptidyl-serine phosphorylation

Inferred from sequence or structural similarity PubMed 16213210. Source: BHF-UCL

negative regulation of relaxation of cardiac muscle

Inferred from sequence or structural similarity. Source: BHF-UCL

neutrophil chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of interferon-gamma production

Inferred from mutant phenotype PubMed 17404263. Source: BHF-UCL

positive regulation of interleukin-2 production

Inferred from mutant phenotype PubMed 17404263. Source: BHF-UCL

positive regulation of interleukin-5 production

Inferred from mutant phenotype PubMed 17404263. Source: BHF-UCL

regulation of cardiac muscle cell contraction

Inferred from sequence or structural similarity PubMed 21903937. Source: BHF-UCL

regulation of cell communication by electrical coupling involved in cardiac conduction

Inferred by curator PubMed 16213210. Source: BHF-UCL

regulation of heart rate

Inferred from sequence or structural similarity PubMed 16213210. Source: BHF-UCL

regulation of receptor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from sequence or structural similarity PubMed 16213210. Source: BHF-UCL

regulation of ryanodine-sensitive calcium-release channel activity

Inferred from sequence or structural similarity PubMed 16213210. Source: BHF-UCL

smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

calcium channel complex

Inferred from direct assay PubMed 16213210. Source: BHF-UCL

cytosol

Inferred from direct assay Ref.4. Source: BHF-UCL

membrane

Inferred from direct assay Ref.4. Source: BHF-UCL

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

voltage-gated calcium channel complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_function3',5'-cyclic-AMP phosphodiesterase activity

Inferred from direct assay PubMed 17404263Ref.4PubMed 12121997PubMed 20819076. Source: BHF-UCL

3',5'-cyclic-nucleotide phosphodiesterase activity

Non-traceable author statement Ref.5. Source: UniProtKB

ATPase binding

Inferred from physical interaction PubMed 21903937. Source: BHF-UCL

beta-2 adrenergic receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

cAMP binding

Inferred from direct assay PubMed 20819076. Source: BHF-UCL

drug binding

Inferred from physical interaction PubMed 15938621. Source: UniProtKB

enzyme binding

Inferred from sequence or structural similarity PubMed 22975349. Source: BHF-UCL

ion channel binding

Inferred from physical interaction PubMed 16213210. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

scaffold protein binding

Inferred from physical interaction PubMed 15182229PubMed 19372219PubMed 20819076. Source: BHF-UCL

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 19372219. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Adcy2P267693EBI-8095525,EBI-1027877From a different organism.

Alternative products

This entry describes 12 isoforms produced by alternative splicing. [Align] [Select]
Isoform 4 (identifier: Q08499-1)

Also known as: hPDE4D4;

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 3 (identifier: Q08499-2)

Also known as: hPDE4D3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: MEAEGSSAPA...WPSSFQGLRR → MMHVNNFPFRRHSWIC
Note: Contains a phosphoserine at position 53. Activated by phosphorylation at Ser-53. Mutagenesis of Ser-53 abolishes activation.
Isoform 10 (identifier: Q08499-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-205: Missing.
Isoform 1 (identifier: Q08499-4)

Also known as: hPDE4D1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-269: MEAEGSSAPA...QPSINKATIT → MKEQPSCAGT...TESPFPCLFA
Isoform 2 (identifier: Q08499-5)

Also known as: hPDE4D2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-302: Missing.
Isoform 5 (identifier: Q08499-6)

Also known as: hPDE4D5;

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: MEAEGSSAPA...WPSSFQGLRR → MAQQTSPDTL...QRRFTVAHTC
Note: Contains a phosphoserine at position 59. Contains a phosphoserine at position 63.
Isoform N3 (identifier: Q08499-7)

Also known as: PDE4DN3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: MEAEGSSAPA...WPSSFQGLRR → MAQQTSPDTL...QRRFTVAHTC
     270-279: EEAYQKLASE → GLYNGIIAFL
     280-809: Missing.
Note: Contains a phosphoserine at position 59. Contains a phosphoserine at position 63.
Isoform 6 (identifier: Q08499-8)

Also known as: PDE4D6;

The sequence of this isoform differs from the canonical sequence as follows:
     1-291: Missing.
     292-306: ETLQTRHSVSEMASN → MPEANYLLSVSWGYI
Isoform 8 (identifier: Q08499-9)

Also known as: PDE4D8;

The sequence of this isoform differs from the canonical sequence as follows:
     1-122: Missing.
     123-152: RTSYAVETGHRPGLKKSRMSWPSSFQGLRR → MAFVWDPLGATVPGPSTRAKSRLRFSKSYS
Isoform 9 (identifier: Q08499-10)

Also known as: PDE4D9;

The sequence of this isoform differs from the canonical sequence as follows:
     1-130: Missing.
     131-152: GHRPGLKKSRMSWPSSFQGLRR → MSIIMKPRSRSTSSLRTAEAVC
Isoform 7 (identifier: Q08499-11)

Also known as: PDE4D7;

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.
     62-152: PPSPQPQPQC...WPSSFQGLRR → MKRNTCDLLS...IAITSAESSG
Isoform 12 (identifier: Q08499-12)

The sequence of this isoform differs from the canonical sequence as follows:
     1-152: MEAEGSSAPA...WPSSFQGLRR → MAQQTSPDTL...QRRFTVAHTC
     270-283: EEAYQKLASETLEE → GSWMELNPYTLLDM
     284-809: Missing.
Note: Contains a phosphoserine at position 59. Contains a phosphoserine at position 63.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 809809cAMP-specific 3',5'-cyclic phosphodiesterase 4D
PRO_0000198814

Regions

Nucleotide binding462 – 4665cAMP
Compositional bias42 – 8847Pro-rich

Sites

Active site4621Proton donor By similarity
Metal binding4661Divalent metal cation 1
Metal binding5021Divalent metal cation 1
Metal binding5031Divalent metal cation 1
Metal binding5031Divalent metal cation 2
Metal binding6201Divalent metal cation 1
Binding site5031cAMP
Binding site6201cAMP
Binding site6711cAMP
Site6231Binds AMP, but not cAMP

Amino acid modifications

Modified residue2991Phosphoserine Ref.21
Modified residue3011Phosphoserine Ref.21
Cross-link387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.19

Natural variations

Alternative sequence1 – 302302Missing in isoform 2.
VSP_004580
Alternative sequence1 – 291291Missing in isoform 6.
VSP_012383
Alternative sequence1 – 269269MEAEG…KATIT → MKEQPSCAGTGHPMAGYGRM APFELASGPVKRLRTESPFP CLFA in isoform 1.
VSP_004579
Alternative sequence1 – 205205Missing in isoform 10.
VSP_004578
Alternative sequence1 – 152152MEAEG…QGLRR → MMHVNNFPFRRHSWIC in isoform 3.
VSP_004577
Alternative sequence1 – 152152MEAEG…QGLRR → MAQQTSPDTLTVPEVDNPHC PNPWLNEDLVKSLRENLLQH EKSKTARKSVSPKLSPVISP RNSPRLLRRMLLSSNIPKQR RFTVAHTC in isoform 5, isoform N3 and isoform 12.
VSP_012384
Alternative sequence1 – 130130Missing in isoform 9.
VSP_012385
Alternative sequence1 – 122122Missing in isoform 8.
VSP_012386
Alternative sequence1 – 6161Missing in isoform 7.
VSP_012387
Alternative sequence62 – 15291PPSPQ…QGLRR → MKRNTCDLLSRSKSASEETL HSSNEEEDPFRGMEPYLVRR LSCRNIQLPPLAFRQLEQAD LKSESENIQRPTSLPLKILP LIAITSAESSG in isoform 7.
VSP_012388
Alternative sequence123 – 15230RTSYA…QGLRR → MAFVWDPLGATVPGPSTRAK SRLRFSKSYS in isoform 8.
VSP_012389
Alternative sequence131 – 15222GHRPG…QGLRR → MSIIMKPRSRSTSSLRTAEA VC in isoform 9.
VSP_012390
Alternative sequence270 – 28314EEAYQ…ETLEE → GSWMELNPYTLLDM in isoform 12.
VSP_023326
Alternative sequence270 – 27910EEAYQKLASE → GLYNGIIAFL in isoform N3.
VSP_012391
Alternative sequence280 – 809530Missing in isoform N3.
VSP_012392
Alternative sequence284 – 809526Missing in isoform 12.
VSP_023327
Alternative sequence292 – 30615ETLQT…EMASN → MPEANYLLSVSWGYI in isoform 6.
VSP_012393
Natural variant1901S → A in ACRDYS2. Ref.34
VAR_068242
Natural variant2251P → T in ACRDYS2. Ref.34 Ref.37
VAR_068243
Natural variant2261F → S in ACRDYS2. Ref.34
VAR_068244
Natural variant2271A → S in ACRDYS2. Ref.36
VAR_069448
Natural variant2281Q → E in ACRDYS2. Ref.35
VAR_069449
Natural variant3011S → T in ACRDYS2. Ref.37
VAR_069450
Natural variant3041A → V in ACRDYS2. Ref.37
VAR_069451
Natural variant3291V → A in ACRDYS2. Ref.37
VAR_069452
Natural variant5871T → P in ACRDYS2. Ref.34
VAR_068245
Natural variant5901E → A in ACRDYS2. Ref.35 Ref.36
VAR_069453
Natural variant6731G → D in ACRDYS2. Ref.35
VAR_069454
Natural variant6781I → T in ACRDYS2. Ref.37
VAR_069455

Experimental info

Mutagenesis5031D → N: Abolishes catalytic activity.
Mutagenesis5271D → R: Abolishes homodimerization. Ref.22
Mutagenesis5631R → D: Abolishes homodimerization. Ref.22
Sequence conflict5101S → F in AAH36319. Ref.10
Sequence conflict5491D → G in AAN10119. Ref.6
Sequence conflict6441R → P Ref.2
Sequence conflict7691C → R in AAA97890. Ref.3
Sequence conflict7691C → R in AAA97891. Ref.3
Sequence conflict7691C → R in AAA97892. Ref.3

Secondary structure

.......................................................... 809
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 4 (hPDE4D4) [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 7A4773DD3A044F57

FASTA80991,115
        10         20         30         40         50         60 
MEAEGSSAPA RAGSGEGSDS AGGATLKAPK HLWRHEQHHQ YPLRQPQFRL LHPHHHLPPP 

        70         80         90        100        110        120 
PPPSPQPQPQ CPLQPPPPPP LPPPPPPPGA ARGRYASSGA TGRVRHRGYS DTERYLYCRA 

       130        140        150        160        170        180 
MDRTSYAVET GHRPGLKKSR MSWPSSFQGL RRFDVDNGTS AGRSPLDPMT SPGSGLILQA 

       190        200        210        220        230        240 
NFVHSQRRES FLYRSDSDYD LSPKSMSRNS SIASDIHGDD LIVTPFAQVL ASLRTVRNNF 

       250        260        270        280        290        300 
AALTNLQDRA PSKRSPMCNQ PSINKATITE EAYQKLASET LEELDWCLDQ LETLQTRHSV 

       310        320        330        340        350        360 
SEMASNKFKR MLNRELTHLS EMSRSGNQVS EFISNTFLDK QHEVEIPSPT QKEKEKKKRP 

       370        380        390        400        410        420 
MSQISGVKKL MHSSSLTNSS IPRFGVKTEQ EDVLAKELED VNKWGLHVFR IAELSGNRPL 

       430        440        450        460        470        480 
TVIMHTIFQE RDLLKTFKIP VDTLITYLMT LEDHYHADVA YHNNIHAADV VQSTHVLLST 

       490        500        510        520        530        540 
PALEAVFTDL EILAAIFASA IHDVDHPGVS NQFLINTNSE LALMYNDSSV LENHHLAVGF 

       550        560        570        580        590        600 
KLLQEENCDI FQNLTKKQRQ SLRKMVIDIV LATDMSKHMN LLADLKTMVE TKKVTSSGVL 

       610        620        630        640        650        660 
LLDNYSDRIQ VLQNMVHCAD LSNPTKPLQL YRQWTDRIME EFFRQGDRER ERGMEISPMC 

       670        680        690        700        710        720 
DKHNASVEKS QVGFIDYIVH PLWETWADLV HPDAQDILDT LEDNREWYQS TIPQSPSPAP 

       730        740        750        760        770        780 
DDPEEGRQGQ TEKFQFELTL EEDGESDTEK DSGSQVEEDT SCSDSKTLCT QDSESTEIPL 

       790        800 
DEQVEEEAVG EEEESQPEAC VIDDRSPDT 

« Hide

Isoform 3 (hPDE4D3) [UniParc].

Checksum: BDC04171BA91A297
Show »

FASTA67376,467
Isoform 10 [UniParc].

Checksum: 446D0C31C86399AB
Show »

FASTA60468,607
Isoform 1 (hPDE4D1) [UniParc].

Checksum: C1761886FF962102
Show »

FASTA58466,376
Isoform 2 (hPDE4D2) [UniParc].

Checksum: 6C07C949952EE5DF
Show »

FASTA50757,792
Isoform 5 (hPDE4D5) [UniParc].

Checksum: D136AE2B7132DAAC
Show »

FASTA74584,428
Isoform N3 (PDE4DN3) [UniParc].

Checksum: 255EF7985DB75353
Show »

FASTA21523,839
Isoform 6 (PDE4D6) [UniParc].

Checksum: 069F18EB90BAAF4B
Show »

FASTA51859,113
Isoform 8 (PDE4D8) [UniParc].

Checksum: 90B1ED110D7ED77C
Show »

FASTA68777,705
Isoform 9 (PDE4D9) [UniParc].

Checksum: D35B0A2D975C5705
Show »

FASTA67976,816
Isoform 7 (PDE4D7) [UniParc].

Checksum: D10CF5036B1EA7C8
Show »

FASTA74884,662
Isoform 12 [UniParc].

Checksum: 04C84B400D6F7D2C
Show »

FASTA21924,429

References

« Hide 'large scale' references
[1]"A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs."
Bolger G., Michaeli T., Martins T., St John T., Steiner B., Rodgers L., Riggs M., Wigler M., Ferguson K.
Mol. Cell. Biol. 13:6558-6571(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
[2]"Identification of cyclic AMP-phosphodiesterase variants from the PDE4D gene expressed in human peripheral mononuclear cells."
Nemoz G., Zhang R.B., Sette C., Conti M.
FEBS Lett. 384:97-102(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4).
[3]"Isolation of a cDNA encoding a human rolipram-sensitive cyclic AMP phosphodiesterase (PDE IVD)."
Baecker P.A., Obernolte R., Bach C., Yee C., Shelton E.R.
Gene 138:253-256(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10).
Tissue: Heart.
[4]"Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene."
Bolger G.B., Erdogan S., Jones R.E., Loughney K., Scotland G., Hoffmann R., Wilkinson I., Farrell C., Houslay M.D.
Biochem. J. 328:539-548(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 10), SEQUENCE REVISION (ISOFORM 1).
[5]"Phosphodiesterases 4D and 7A splice variants in the response of HUVEC cells to TNF-alpha1."
Miro X., Casacuberta J.M., Gutierrez-Lopez M.D., Landazuri M.O., Puigdomenech P.
Biochem. Biophys. Res. Commun. 274:415-421(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM N3), ALTERNATIVE SPLICING.
Tissue: Umbilical vein endothelial cell.
[6]"Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7."
Wang D., Deng C., Bugaj-Gaweda B., Kwan M., Gunwaldsen C., Leonard C., Xin X., Hu Y., Unterbeck A., De Vivo M.
Cell. Signal. 15:883-891(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 7; 8 AND 9), PHOSPHORYLATION, TISSUE SPECIFICITY.
[7]"The gene encoding phosphodiesterase 4D confers risk of ischemic stroke."
Gretarsdottir S., Thorleifsson G., Reynisdottir S.T., Manolescu A., Jonsdottir S., Jonsdottir T., Gudmundsdottir T., Bjarnadottir S.M., Einarsson O.B., Gudjonsdottir H.M., Hawkins M., Gudmundsson G., Gudmundsdottir H., Andrason H., Gudmundsdottir A.S., Sigurdardottir M., Chou T.T., Nahmias J. expand/collapse author list , Goss S., Sveinbjoernsdottir S., Valdimarsson E.M., Jakobsson F., Agnarsson U., Gudnason V., Thorgeirsson G., Fingerle J., Gurney M., Gudbjartsson D., Frigge M.L., Kong A., Stefansson K., Gulcher J.R.
Nat. Genet. 35:131-138(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7 AND 9), INVOLVEMENT IN SUSCEPTIBILITY TO STROKE.
[8]Erratum
Gretarsdottir S., Thorleifsson G., Reynisdottir S.T., Manolescu A., Jonsdottir S., Jonsdottir T., Gudmundsdottir T., Bjarnadottir S.M., Einarsson O.B., Gudjonsdottir H.M., Hawkins M., Gudmundsson G., Gudmundsdottir H., Andrason H., Gudmundsdottir A.S., Sigurdardottir M., Chou T.T., Nahmias J. expand/collapse author list , Goss S., Sveinbjoernsdottir S., Valdimarsson E.M., Jakobsson F., Agnarsson U., Gudnason V., Thorgeirsson G., Fingerle J., Gurney M., Gudbjartsson D., Frigge M.L., Kong A., Stefansson K., Gulcher J.R.
Nat. Genet. 37:555-555(2005)
[9]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 12).
[10]"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] (ISOFORMS 6 AND 12).
Tissue: Brain and Testis.
[11]"Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5."
Bolger G.B., McCahill A., Yarwood S.J., Steele M.S., Warwicker J., Houslay M.D.
BMC Biochem. 3:24-24(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GNB2L1.
[12]"The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins."
Bolger G.B., McCahill A., Huston E., Cheung Y.F., McSorley T., Baillie G.S., Houslay M.D.
J. Biol. Chem. 278:49230-49238(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2, SUBCELLULAR LOCATION.
[13]"The oligomerization state determines regulatory properties and inhibitor sensitivity of type 4 cAMP-specific phosphodiesterases."
Richter W., Conti M.
J. Biol. Chem. 279:30338-30348(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION OF LONG ISOFORMS, ENZYME REGULATION BY ROLIPRAM AND PHOSPHATIDIC ACID, PHOSPHORYLATION AT SER-53 (ISOFORM 3).
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Many hypotheses but no replication for the association between PDE4D and stroke."
Rosand J., Bayley N., Rost N., de Bakker P.I.W.
Nat. Genet. 38:1091-1092(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISCUSSION OF INVOLVEMENT IN STROKE.
[16]"Dynamic regulation of cystic fibrosis transmembrane conductance regulator by competitive interactions of molecular adaptors."
Lee J.H., Richter W., Namkung W., Kim K.H., Kim E., Conti M., Lee M.G.
J. Biol. Chem. 282:10414-10422(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHANK2, TISSUE SPECIFICITY.
[17]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-63 (ISOFORMS 12; 5 AND N3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Selective SUMO modification of cAMP-specific phosphodiesterase-4D5 (PDE4D5) regulates the functional consequences of phosphorylation by PKA and ERK."
Li X., Vadrevu S., Dunlop A., Day J., Advant N., Troeger J., Klussmann E., Jaffrey E., Hay R.T., Adams D.R., Houslay M.D., Baillie G.S.
Biochem. J. 428:55-65(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-387 BY PIAS4.
[20]"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(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299 AND SER-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Crystal structure of phosphodiesterase 4D and inhibitor complex."
Lee M.E., Markowitz J., Lee J.-O., Lee H.
FEBS Lett. 530:53-58(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 388-715 IN COMPLEX WITH THE INHIBITOR ZARDAVERINE AND DIVALENT METAL IONS, MUTAGENESIS OF ASP-527 AND ARG-563.
[23]"The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterase catalysis."
Huai Q., Colicelli J., Ke H.
Biochemistry 42:13220-13226(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 381-739 IN COMPLEX WITH CAMP AND DIVALENT METAL IONS.
[24]"Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity."
Huai Q., Wang H., Sun Y., Kim H.Y., Liu Y., Ke H.
Structure 11:865-873(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 381-739 IN COMPLEX WITH INHIBITOR.
[25]"Crystal structures of phosphodiesterases 4 and 5 in complex with inhibitor 3-isobutyl-1-methylxanthine suggest a conformation determinant of inhibitor selectivity."
Huai Q., Liu Y., Francis S.H., Corbin J.D., Ke H.
J. Biol. Chem. 279:13095-13101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 381-714 IN COMPLEX WITH METAL IONS AND INHIBITOR.
[26]"Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram."
Xu R.X., Rocque W.J., Lambert M.H., Vanderwall D.E., Luther M.A., Nolte R.T.
J. Mol. Biol. 337:355-365(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 380-756 IN COMPLEX WITH AMP; METAL IONS AND THE INHIBITOR ROLIPRAM.
[27]"A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases."
Zhang K.Y.J., Card G.L., Suzuki Y., Artis D.R., Fong D., Gillette S., Hsieh D., Neiman J., West B.L., Zhang C., Milburn M.V., Kim S.-H., Schlessinger J., Bollag G.
Mol. Cell 15:279-286(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 388-715 IN COMPLEX WITH AMP; METAL IONS AND THE INHIBITOR ROLIPRAM, FUNCTION, COFACTOR.
[28]"Structural basis for the activity of drugs that inhibit phosphodiesterases."
Card G.L., England B.P., Suzuki Y., Fong D., Powell B., Lee B., Luu C., Tabrizizad M., Gillette S., Ibrahim P.N., Artis D.R., Bollag G., Milburn M.V., Kim S.-H., Schlessinger J., Zhang K.Y.J.
Structure 12:2233-2247(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 388-715 IN COMPLEX WITH METAL IONS AND INHIBITORS, FUNCTION, COFACTOR.
[29]"A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design."
Card G.L., Blasdel L., England B.P., Zhang C., Suzuki Y., Gillette S., Fong D., Ibrahim P.N., Artis D.R., Bollag G., Milburn M.V., Kim S.-H., Schlessinger J., Zhang K.Y.J.
Nat. Biotechnol. 23:201-207(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.36 ANGSTROMS) OF 388-715 IN COMPLEX WITH METAL IONS AND INHIBITORS.
[30]"Enantiomer discrimination illustrated by the high resolution crystal structures of type 4 phosphodiesterase."
Huai Q., Sun Y., Wang H., Macdonald D., Aspiotis R., Robinson H., Huang Z., Ke H.
J. Med. Chem. 49:1867-1873(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 381-741 IN COMPLEX WITH METAL IONS AND INHIBITORS.
[31]"Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors."
Wang H., Peng M.-S., Chen Y., Geng J., Robinson H., Houslay M.D., Cai J., Ke H.
Biochem. J. 408:193-201(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 388-715 IN COMPLEX WITH METAL IONS AND THE INHIBITOR NVP.
[32]"1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1."
Smith K.J., Baillie G.S., Hyde E.I., Li X., Houslay T.M., McCahill A., Dunlop A.J., Bolger G.B., Klussmann E., Adams D.R., Houslay M.D.
Cell. Signal. 19:2612-2624(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF N-TERMINUS OF ISOFORM 5/N3/12, INTERACTION WITH GNB2L1.
[33]"The molecular basis for different recognition of substrates by phosphodiesterase families 4 and 10."
Wang H., Robinson H., Ke H.
J. Mol. Biol. 371:302-307(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 388-714 OF MUTANT ASN-503 IN COMPLEX WITH CAMP AND METAL IONS.
[34]"Exome sequencing identifies PDE4D mutations as another cause of acrodysostosis."
Michot C., Le Goff C., Goldenberg A., Abhyankar A., Klein C., Kinning E., Guerrot A.M., Flahaut P., Duncombe A., Baujat G., Lyonnet S., Thalassinos C., Nitschke P., Casanova J.L., Le Merrer M., Munnich A., Cormier-Daire V.
Am. J. Hum. Genet. 90:740-745(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACRDYS2 ALA-190; THR-225; SER-226 AND PRO-587.
[35]"Exome sequencing identifies PDE4D mutations in acrodysostosis."
Lee H., Graham J.M. Jr., Rimoin D.L., Lachman R.S., Krejci P., Tompson S.W., Nelson S.F., Krakow D., Cohn D.H.
Am. J. Hum. Genet. 90:746-751(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACRDYS2 GLU-228; ALA-590 AND ASP-673.
[36]"PRKAR1A and PDE4D mutations cause acrodysostosis but two distinct syndromes with or without GPCR-signaling hormone resistance."
Linglart A., Fryssira H., Hiort O., Holterhus P.M., Perez de Nanclares G., Argente J., Heinrichs C., Kuechler A., Mantovani G., Leheup B., Wicart P., Chassot V., Schmidt D., Rubio-Cabezas O., Richter-Unruh A., Berrade S., Pereda A., Boros E. expand/collapse author list , Munoz-Calvo M.T., Castori M., Gunes Y., Bertrand G., Bougneres P., Clauser E., Silve C.
J. Clin. Endocrinol. Metab. 97:E2328-E2338(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACRDYS2 SER-227 AND ALA-590.
[37]"Identification of novel mutations confirms Pde4d as a major gene causing acrodysostosis."
FORGE Canada Consortium
Lynch D.C., Dyment D.A., Huang L., Nikkel S.M., Lacombe D., Campeau P.M., Lee B., Bacino C.A., Michaud J.L., Bernier F.P., Parboosingh J.S., Innes A.M.
Hum. Mutat. 34:97-102(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACRDYS2 THR-225; THR-301; VAL-304; ALA-329 AND THR-678.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L20970 mRNA. Translation: AAA03592.1.
L20969 mRNA. Translation: AAC00042.1.
U02882 mRNA. Translation: AAC13745.1.
U50157 mRNA. Translation: AAA97890.1.
U50158 mRNA. Translation: AAA97891.1.
U50159 mRNA. Translation: AAA97892.1.
AF012074 mRNA. Translation: AAC00070.1.
AF012073 mRNA. Translation: AAC00069.1.
AJ250854 mRNA. Translation: CAC03757.1.
AF536975 mRNA. Translation: AAN10117.1.
AF536976 mRNA. Translation: AAN10118.1.
AF536977 mRNA. Translation: AAN10119.1.
AY388960 mRNA. Translation: AAQ90404.1.
AY245866 mRNA. Translation: AAP75760.1.
AY245867 mRNA. Translation: AAP75761.1.
BT007398 mRNA. Translation: AAP36062.1.
BC008390 mRNA. Translation: AAH08390.1.
BC036319 mRNA. Translation: AAH36319.1.
PIRI61358.
RefSeqNP_001098101.1. NM_001104631.1.
NP_001159371.1. NM_001165899.1.
NP_001184147.1. NM_001197218.1.
NP_001184148.1. NM_001197219.1.
NP_001184149.1. NM_001197220.1.
NP_001184150.1. NM_001197221.1.
NP_001184151.1. NM_001197222.1.
NP_001184152.1. NM_001197223.1.
NP_006194.2. NM_006203.4.
XP_005248595.1. XM_005248538.2.
XP_005248598.1. XM_005248541.2.
UniGeneHs.117545.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E9KNMR-A-[»]
1MKDX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L388-715[»]
1OYNX-ray2.00A/B/C/D381-740[»]
1PTWX-ray2.30A/B/C/D381-740[»]
1Q9MX-ray2.30A/B/C/D381-740[»]
1TB7X-ray1.63A/B388-715[»]
1TBBX-ray1.60A/B388-715[»]
1XOMX-ray1.55A/B388-715[»]
1XONX-ray1.72A/B388-715[»]
1XOQX-ray1.83A/B388-715[»]
1XORX-ray1.54A/B388-715[»]
1Y2BX-ray1.40A/B388-715[»]
1Y2CX-ray1.67A/B388-715[»]
1Y2DX-ray1.70A/B388-715[»]
1Y2EX-ray2.10A/B388-715[»]
1Y2KX-ray1.36A/B388-715[»]
1ZKNX-ray2.10A/B/C/D381-714[»]
2FM0X-ray2.00A/B/C/D381-741[»]
2FM5X-ray2.03A/B/C/D381-741[»]
2PW3X-ray1.56A/B388-714[»]
2QYNX-ray1.57A/B388-715[»]
3G4GX-ray2.30A/B/C/D299-714[»]
3G4IX-ray1.90A/B/C/D380-753[»]
3G4KX-ray1.95A/B/C/D380-753[»]
3G4LX-ray2.50A/B/C/D380-753[»]
3G58X-ray2.05A/B/C/D380-753[»]
3IADX-ray2.65A/B/C/D326-714[»]
3IAKX-ray2.80A388-715[»]
3K4SX-ray2.05A388-715[»]
3SL3X-ray2.10A/B/C/D381-741[»]
3SL4X-ray1.90A/B/C/D381-741[»]
3SL5X-ray2.65A/B/C/D381-734[»]
3SL6X-ray2.44A/B/C/D381-741[»]
3SL8X-ray2.60A/B/C/D381-741[»]
3V9BX-ray2.10A/B/C/D381-740[»]
ProteinModelPortalQ08499.
SMRQ08499. Positions 327-739.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111170. 31 interactions.
DIPDIP-29709N.
DIP-41115N.
IntActQ08499. 9 interactions.
MINTMINT-92262.

Chemistry

BindingDBQ08499.
ChEMBLCHEMBL2095153.
DrugBankDB00131. Adenosine monophosphate.
DB00651. Dyphylline.
GuidetoPHARMACOLOGY1303.

PTM databases

PhosphoSiteQ08499.

Polymorphism databases

DMDM12644392.

Proteomic databases

PaxDbQ08499.
PRIDEQ08499.

Protocols and materials databases

DNASU5144.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309641; ENSP00000308485; ENSG00000113448. [Q08499-7]
ENST00000317118; ENSP00000321739; ENSG00000113448. [Q08499-8]
ENST00000340635; ENSP00000345502; ENSG00000113448. [Q08499-1]
ENST00000358923; ENSP00000351800; ENSG00000113448. [Q08499-5]
ENST00000360047; ENSP00000353152; ENSG00000113448.
ENST00000405755; ENSP00000384806; ENSG00000113448. [Q08499-9]
ENST00000502484; ENSP00000423094; ENSG00000113448. [Q08499-11]
ENST00000502575; ENSP00000425917; ENSG00000113448. [Q08499-12]
ENST00000503258; ENSP00000425605; ENSG00000113448. [Q08499-10]
ENST00000507116; ENSP00000424852; ENSG00000113448. [Q08499-6]
ENST00000546160; ENSP00000442734; ENSG00000113448. [Q08499-11]
GeneID5144.
KEGGhsa:5144.
UCSCuc003jrs.2. human. [Q08499-8]
uc003jrt.2. human. [Q08499-1]
uc003jru.3. human. [Q08499-4]
uc003jrv.2. human. [Q08499-10]
uc003jrw.2. human. [Q08499-9]
uc003jrz.3. human. [Q08499-6]
uc003jsb.3. human. [Q08499-11]
uc003jsc.3. human. [Q08499-12]

Organism-specific databases

CTD5144.
GeneCardsGC05M058302.
HGNCHGNC:8783. PDE4D.
HPAHPA045895.
MIM600129. gene.
614613. phenotype.
neXtProtNX_Q08499.
Orphanet950. Acrodysostosis.
280651. Acrodysostosis with multiple hormone resistance.
PharmGKBPA33130.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG122287.
HOVERGENHBG108239.
InParanoidQ08499.
KOK01120.
OMAQHEVEMP.
OrthoDBEOG7HQNBC.
PhylomeDBQ08499.
TreeFamTF314638.

Enzyme and pathway databases

BRENDA3.1.4.53. 2681.
ReactomeREACT_111102. Signal Transduction.
SignaLinkQ08499.
UniPathwayUPA00762; UER00747.

Gene expression databases

ArrayExpressQ08499.
BgeeQ08499.
GenevestigatorQ08499.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
InterProIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDE4D. human.
EvolutionaryTraceQ08499.
GeneWikiPDE4D.
GenomeRNAi5144.
NextBio19846.
PROQ08499.
SOURCESearch...

Entry information

Entry namePDE4D_HUMAN
AccessionPrimary (citable) accession number: Q08499
Secondary accession number(s): O43433 expand/collapse secondary AC list , Q13549, Q13550, Q13551, Q7Z2L8, Q8IV84, Q8IVA9, Q8IVD2, Q8IVD3, Q96HL4, Q9HCX7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 155 of the entry and version 2 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 5

Human chromosome 5: entries, gene names and cross-references to MIM