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Q13946

- PDE7A_HUMAN

UniProt

Q13946 - PDE7A_HUMAN

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Protein

High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

Gene

PDE7A

Organism
Homo sapiens (Human)
Status
Reviewed - 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 have a role in muscle signal transduction.1 Publication

Catalytic activityi

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

Cofactori

a divalent metal cation1 PublicationNote: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.1 Publication

Enzyme regulationi

Insensitive to all selective PDE inhibitors.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei212 – 2121Proton donorBy similarity
Metal bindingi216 – 2161Divalent metal cation 1
Metal bindingi252 – 2521Divalent metal cation 1
Metal bindingi253 – 2531Divalent metal cation 1
Metal bindingi253 – 2531Divalent metal cation 2
Metal bindingi362 – 3621Divalent metal cation 1

GO - Molecular functioni

  1. 3',5'-cyclic-AMP phosphodiesterase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cAMP catabolic process Source: UniProtKB-UniPathway
  2. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (EC:3.1.4.53)
Alternative name(s):
HCP1
TM22
Gene namesi
Name:PDE7A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:8791. PDE7A.

Subcellular locationi

Isoform PDE7A1 : Cytoplasmcytosol
Note: PDE7A1 (57 kDa) is located mostly to soluble cellular fractions.
Isoform PDE7A2 : Cytoplasm
Note: PDE7A2 (50 kDa) is located to particulate cellular fractions.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33139.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7APRO_0000198833Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841PhosphoserineSequence Analysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13946.
PaxDbiQ13946.
PRIDEiQ13946.

PTM databases

PhosphoSiteiQ13946.

Expressioni

Tissue specificityi

PDE7A1 is found at high levels in skeletal muscle and at low levels in a variety of tissues including brain and heart. It is expressed as well in two T-cell lines. PDE7A2 is found abundantly in skeletal muscle and at low levels in heart.

Developmental stagei

Developmentally regulated. PDE7A1 and PDE7A2 are found in several fetal tissues, expression is reduced throughout development. It persists strongly only in adult skeletal muscle.

Gene expression databases

BgeeiQ13946.
CleanExiHS_PDE7A.
ExpressionAtlasiQ13946. baseline and differential.
GenevestigatoriQ13946.

Organism-specific databases

HPAiCAB018770.
HPA027340.

Interactioni

Subunit structurei

Interacts with CBFA2T3.3 Publications

Protein-protein interaction databases

BioGridi111176. 4 interactions.
IntActiQ13946. 1 interaction.
STRINGi9606.ENSP00000368730.

Structurei

Secondary structure

1
482
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi140 – 1489Combined sources
Turni149 – 1524Combined sources
Helixi158 – 1647Combined sources
Helixi169 – 18012Combined sources
Helixi183 – 1864Combined sources
Helixi191 – 20313Combined sources
Beta strandi209 – 2135Combined sources
Helixi214 – 22815Combined sources
Helixi231 – 2344Combined sources
Helixi239 – 25113Combined sources
Turni252 – 2554Combined sources
Helixi261 – 2666Combined sources
Helixi270 – 2745Combined sources
Turni275 – 2773Combined sources
Helixi280 – 29617Combined sources
Turni297 – 3015Combined sources
Helixi304 – 31916Combined sources
Helixi323 – 3253Combined sources
Helixi326 – 33914Combined sources
Helixi347 – 36216Combined sources
Helixi365 – 3673Combined sources
Helixi370 – 39324Combined sources
Turni404 – 4063Combined sources
Helixi409 – 41911Combined sources
Helixi421 – 43111Combined sources
Helixi435 – 45319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZKLX-ray1.67A130-482[»]
3G3NX-ray2.40A139-456[»]
ProteinModelPortaliQ13946.
SMRiQ13946. Positions 139-456.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13946.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni187 – 451265CatalyticBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi28 – 336Poly-Ser

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG300643.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000220881.
HOVERGENiHBG053543.
KOiK18436.
OMAiLCDRQTE.
OrthoDBiEOG7M98G3.
PhylomeDBiQ13946.
TreeFamiTF314638.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
InterProiIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform PDE7A1 (identifier: Q13946-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEVCYQLPVL PLDRPVPQHV LSRRGAISFS SSSALFGCPN PRQLSQRRGA
60 70 80 90 100
ISYDSSDQTA LYIRMLGDVR VRSRAGFESE RRGSHPYIDF RIFHSQSEIE
110 120 130 140 150
VSVSARNIRR LLSFQRYLRS SRFFRGTAVS NSLNILDDDY NGQAKCMLEK
160 170 180 190 200
VGNWNFDIFL FDRLTNGNSL VSLTFHLFSL HGLIEYFHLD MMKLRRFLVM
210 220 230 240 250
IQEDYHSQNP YHNAVHAADV TQAMHCYLKE PKLANSVTPW DILLSLIAAA
260 270 280 290 300
THDLDHPGVN QPFLIKTNHY LATLYKNTSV LENHHWRSAV GLLRESGLFS
310 320 330 340 350
HLPLESRQQM ETQIGALILA TDISRQNEYL SLFRSHLDRG DLCLEDTRHR
360 370 380 390 400
HLVLQMALKC ADICNPCRTW ELSKQWSEKV TEEFFHQGDI EKKYHLGVSP
410 420 430 440 450
LCDRHTESIA NIQIGFMTYL VEPLFTEWAR FSNTRLSQTM LGHVGLNKAS
460 470 480
WKGLQREQSS SEDTDAAFEL NSQLLPQENR LS
Length:482
Mass (Da):55,505
Last modified:July 15, 1998 - v2
Checksum:i3B3C8F6E9154F88C
GO
Isoform PDE7A2 (identifier: Q13946-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MEVCYQLPVLPLDRPVPQHVLSRRGAISFSSSSALFGCPNPRQLSQ → MGITLIWCLALVLIKWITSK

Show »
Length:456
Mass (Da):52,725
Checksum:iCAA62B0BFEF074AF
GO
Isoform PDE7A3 (identifier: Q13946-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     416-424: FMTYLVEPL → NYTYLDIAG
     425-482: Missing.

Show »
Length:424
Mass (Da):48,828
Checksum:iA7DBF40D08A7B561
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041D → G in BAF83490. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 761G → E.
Corresponds to variant rs11557049 [ dbSNP | Ensembl ].
VAR_056661

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4646MEVCY…RQLSQ → MGITLIWCLALVLIKWITSK in isoform PDE7A2. 2 PublicationsVSP_004593Add
BLAST
Alternative sequencei416 – 4249FMTYLVEPL → NYTYLDIAG in isoform PDE7A3. 1 PublicationVSP_038645
Alternative sequencei425 – 48258Missing in isoform PDE7A3. 1 PublicationVSP_038646Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12052 mRNA. Translation: AAA35644.2.
U67932 mRNA. Translation: AAB65772.1.
AF332652 mRNA. Translation: AAK57640.1.
AK290801 mRNA. Translation: BAF83490.1.
AK292680 mRNA. Translation: BAF85369.1.
AC055822 Genomic DNA. No translation available.
AC100812 Genomic DNA. No translation available.
BC126360 mRNA. Translation: AAI26361.1.
CCDSiCCDS34901.1. [Q13946-2]
CCDS56538.1. [Q13946-1]
RefSeqiNP_001229247.1. NM_001242318.2. [Q13946-1]
NP_002594.1. NM_002603.3. [Q13946-2]
UniGeneiHs.527119.

Genome annotation databases

EnsembliENST00000379419; ENSP00000368730; ENSG00000205268. [Q13946-2]
ENST00000396642; ENSP00000379881; ENSG00000205268. [Q13946-3]
ENST00000401827; ENSP00000385632; ENSG00000205268. [Q13946-1]
GeneIDi5150.
KEGGihsa:5150.
UCSCiuc003xvp.3. human. [Q13946-2]
uc003xvq.3. human. [Q13946-1]
uc003xvr.3. human. [Q13946-3]

Polymorphism databases

DMDMi3182958.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12052 mRNA. Translation: AAA35644.2 .
U67932 mRNA. Translation: AAB65772.1 .
AF332652 mRNA. Translation: AAK57640.1 .
AK290801 mRNA. Translation: BAF83490.1 .
AK292680 mRNA. Translation: BAF85369.1 .
AC055822 Genomic DNA. No translation available.
AC100812 Genomic DNA. No translation available.
BC126360 mRNA. Translation: AAI26361.1 .
CCDSi CCDS34901.1. [Q13946-2 ]
CCDS56538.1. [Q13946-1 ]
RefSeqi NP_001229247.1. NM_001242318.2. [Q13946-1 ]
NP_002594.1. NM_002603.3. [Q13946-2 ]
UniGenei Hs.527119.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZKL X-ray 1.67 A 130-482 [» ]
3G3N X-ray 2.40 A 139-456 [» ]
ProteinModelPortali Q13946.
SMRi Q13946. Positions 139-456.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111176. 4 interactions.
IntActi Q13946. 1 interaction.
STRINGi 9606.ENSP00000368730.

Chemistry

BindingDBi Q13946.
ChEMBLi CHEMBL2363066.
DrugBanki DB00201. Caffeine.
DB00651. Dyphylline.
DB00920. Ketotifen.
GuidetoPHARMACOLOGYi 1305.

PTM databases

PhosphoSitei Q13946.

Polymorphism databases

DMDMi 3182958.

Proteomic databases

MaxQBi Q13946.
PaxDbi Q13946.
PRIDEi Q13946.

Protocols and materials databases

DNASUi 5150.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379419 ; ENSP00000368730 ; ENSG00000205268 . [Q13946-2 ]
ENST00000396642 ; ENSP00000379881 ; ENSG00000205268 . [Q13946-3 ]
ENST00000401827 ; ENSP00000385632 ; ENSG00000205268 . [Q13946-1 ]
GeneIDi 5150.
KEGGi hsa:5150.
UCSCi uc003xvp.3. human. [Q13946-2 ]
uc003xvq.3. human. [Q13946-1 ]
uc003xvr.3. human. [Q13946-3 ]

Organism-specific databases

CTDi 5150.
GeneCardsi GC08M066629.
HGNCi HGNC:8791. PDE7A.
HPAi CAB018770.
HPA027340.
MIMi 171885. gene.
neXtProti NX_Q13946.
PharmGKBi PA33139.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG300643.
GeneTreei ENSGT00760000118889.
HOGENOMi HOG000220881.
HOVERGENi HBG053543.
KOi K18436.
OMAi LCDRQTE.
OrthoDBi EOG7M98G3.
PhylomeDBi Q13946.
TreeFami TF314638.

Enzyme and pathway databases

UniPathwayi UPA00762 ; UER00747 .
Reactomei REACT_19327. G alpha (s) signalling events.

Miscellaneous databases

ChiTaRSi PDE7A. human.
EvolutionaryTracei Q13946.
GeneWikii PDE7A.
GenomeRNAii 5150.
NextBioi 19872.
PROi Q13946.
SOURCEi Search...

Gene expression databases

Bgeei Q13946.
CleanExi HS_PDE7A.
ExpressionAtlasi Q13946. baseline and differential.
Genevestigatori Q13946.

Family and domain databases

Gene3Di 1.10.1300.10. 1 hit.
InterProi IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view ]
Pfami PF00233. PDEase_I. 1 hit.
[Graphical view ]
PRINTSi PR00387. PDIESTERASE1.
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a previously undetected human cAMP phosphodiesterase by complementation of cAMP phosphodiesterase-deficient Saccharomyces cerevisiae."
    Michaeli T., Bloom T.J., Martins T., Loughney K., Ferguson K., Riggs M., Rodgers L., Beavo J.A., Wigler M.
    J. Biol. Chem. 268:12925-12932(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE7A1).
  2. "Alternative splicing of the high affinity cAMP-specific phosphodiesterase (PDE7A) mRNA in human skeletal muscle and heart."
    Han P., Zhu X., Michaeli T.
    J. Biol. Chem. 272:16152-16157(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE7A2).
    Tissue: Skeletal muscle.
  3. "T cell activation up-regulates cyclic nucleotide phosphodiesterases 8A1 and 7A3."
    Glavas N.A., Ostenson C., Schaefer J.B., Vasta V., Beavo J.A.
    Proc. Natl. Acad. Sci. U.S.A. 98:6319-6324(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE7A3).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE7A1).
    Tissue: Kidney and Thymus.
  5. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [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 PDE7A2).
  7. "A-kinase anchoring proteins interact with phosphodiesterases in T lymphocyte cell lines."
    Asirvatham A.L., Galligan S.G., Schillace R.V., Davey M.P., Vasta V., Beavo J.A., Carr D.W.
    J. Immunol. 173:4806-4814(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBFA2T3.
  8. "Multiple elements jointly determine inhibitor selectivity of cyclic nucleotide phosphodiesterases 4 and 7."
    Wang H., Liu Y., Chen Y., Robinson H., Ke H.
    J. Biol. Chem. 280:30949-30955(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 130-482 IN COMPLEX WITH METAL IONS AND THE INHIBITOR IBMX.
  9. "Synthesis, structural analysis, and biological evaluation of thioxoquinazoline derivatives as phosphodiesterase 7 inhibitors."
    Castano T., Wang H., Campillo N.E., Ballester S., Gonzalez-Garcia C., Hernandez J., Perez C., Cuenca J., Perez-Castillo A., Martinez A., Huertas O., Gelpi J.L., Luque F.J., Ke H., Gil C.
    ChemMedChem 4:866-876(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 139-456 IN COMPLEX WITH METAL IONS, FUNCTION, COFACTOR.

Entry informationi

Entry nameiPDE7A_HUMAN
AccessioniPrimary (citable) accession number: Q13946
Secondary accession number(s): A0AVH6
, A8K436, A8K9G5, O15380, Q96T72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 26, 2014
This is version 142 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3