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Q01063

- PDE4D_MOUSE

UniProt

Q01063 - PDE4D_MOUSE

Protein

cAMP-specific 3',5'-cyclic phosphodiesterase 4D

Gene

Pde4d

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      Previous versions | rss
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    Functioni

    Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes.By similarity

    Catalytic activityi

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

    Cofactori

    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.By similarity

    Enzyme regulationi

    Inhibited by rolipram. Activated by phosphatidic acid By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei401 – 4011Proton donorBy similarity
    Metal bindingi405 – 4051Divalent metal cation 1By similarity
    Metal bindingi441 – 4411Divalent metal cation 1By similarity
    Metal bindingi442 – 4421Divalent metal cation 1By similarity
    Metal bindingi442 – 4421Divalent metal cation 2By similarity
    Binding sitei442 – 4421cAMPBy similarity
    Metal bindingi559 – 5591Divalent metal cation 1By similarity
    Sitei562 – 5621Binds AMP, but not cAMPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi401 – 4055cAMPBy similarity

    GO - Molecular functioni

    1. 3',5'-cyclic-AMP phosphodiesterase activity Source: Ensembl
    2. 3',5'-cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
    3. ATPase binding Source: BHF-UCL
    4. cAMP binding Source: Ensembl
    5. drug binding Source: Ensembl
    6. ion channel binding Source: BHF-UCL
    7. metal ion binding Source: UniProtKB-KW
    8. protein binding Source: IntAct

    GO - Biological processi

    1. aging Source: MGI
    2. cAMP catabolic process Source: BHF-UCL
    3. cellular response to cAMP Source: Ensembl
    4. cellular response to epinephrine stimulus Source: BHF-UCL
    5. cellular response to lipopolysaccharide Source: MGI
    6. establishment of endothelial barrier Source: UniProtKB
    7. leukocyte migration Source: MGI
    8. multicellular organism growth Source: MGI
    9. negative regulation of heart contraction Source: BHF-UCL
    10. negative regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    11. negative regulation of relaxation of cardiac muscle Source: BHF-UCL
    12. neutrophil chemotaxis Source: MGI
    13. positive regulation of interferon-gamma production Source: Ensembl
    14. positive regulation of interleukin-2 production Source: Ensembl
    15. positive regulation of interleukin-5 production Source: Ensembl
    16. regulation of cardiac muscle cell contraction Source: BHF-UCL
    17. regulation of cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
    18. regulation of heart rate Source: BHF-UCL
    19. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
    20. regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    21. smooth muscle contraction Source: MGI
    22. T cell receptor signaling pathway Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_203795. DARPP-32 events.
    UniPathwayiUPA00762; UER00747.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    cAMP-specific 3',5'-cyclic phosphodiesterase 4D (EC:3.1.4.53)
    Alternative name(s):
    DPDE3
    Gene namesi
    Name:Pde4d
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:99555. Pde4d.

    Subcellular locationi

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

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. calcium channel complex Source: BHF-UCL
    3. cytosol Source: Ensembl
    4. microtubule organizing center Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 747747cAMP-specific 3',5'-cyclic phosphodiesterase 4DPRO_0000198815Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei238 – 2381PhosphoserineBy similarity
    Modified residuei240 – 2401PhosphoserineBy similarity
    Cross-linki326 – 326Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ01063.
    PRIDEiQ01063.

    PTM databases

    PhosphoSiteiQ01063.

    Expressioni

    Tissue specificityi

    Expressed in brain (at protein level). Isoform 7 is detected in heart, brain, lung, kidney and testis.2 Publications

    Inductioni

    Up-regulated by cAMP and follicle-stimulating hormone.By similarity

    Gene expression databases

    ArrayExpressiQ01063.
    BgeeiQ01063.
    CleanExiMM_PDE4D.
    GenevestigatoriQ01063.

    Interactioni

    Subunit structurei

    Homodimer for the long isoforms. Isoforms with truncated N-termini are monomeric. Binds ARRB2. Interacts with PDE4DIP By similarity. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Interacts (via N-terminal region) with SHANK2 (via proline-rich region); the interaction is increased in a PKA-dependent manner.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Adrb1P349713EBI-7764239,EBI-7764182

    Protein-protein interaction databases

    BioGridi232023. 3 interactions.
    DIPiDIP-29706N.
    IntActiQ01063. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01063.
    SMRiQ01063. Positions 244-678.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG122287.
    GeneTreeiENSGT00740000115148.
    HOGENOMiHOG000236297.
    HOVERGENiHBG108239.
    KOiK01120.
    OMAiQHEVEMP.
    OrthoDBiEOG7HQNBC.
    PhylomeDBiQ01063.

    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 7 (identifier: Q01063-1) [UniParc]FASTAAdd to Basket

    Also known as: PDE4D7

    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

    MERDTCDVLS RSKSASEETL HSCNEEEDPF RGMEPYLVRR LSSRSIQLPP    50
    LAFRQLEQAD LRSESENIPR PTSLPLKILP LIAVTSADSS GFDVDNGTSA 100
    GRSPLDPMTS PGSGLILQAN FVHSQRRESF LYRSDSDYDL SPKSMSRNSS 150
    IASDIHGDDL IVTPFAQVLA SLRTVRNNFA ALTNLQDRAP SKRSPMCNQP 200
    SINKATITEE AYQKLASETL EELDWCLDQL ETLQTRHSVS EMASNKFKRM 250
    LNRELTHLSE MSRSGNQVSE YISNTFLDKQ HEVEIPSPTQ KEKEKKKRPM 300
    SQISGVKKLM HSSSLTNSCI PRFGVKTEQE DVLAKELEDV NKWGLHVFRI 350
    AELSGNRPLT VIMHTIFQER DLLKTFKIPV DTLITYLMTL EDHYHADVAY 400
    HNNIHAADVV QSTHVLLSTP ALEAVFTDLE ILAAIFASAI HDVDHPGVSN 450
    QFLINTNSEL ALMYNDSSVL ENHHLAVGFK LLQEENCDIF QNLTKKQRQS 500
    LRKMVIDIVL ATDMSKHMNL LADLKTMVET KKVTSSGVLL LDNYSDRIQV 550
    LQNMVHCADL SNPTKPLQLY RQWTDRIMEE FFRQGDRERE RGMEISPMCD 600
    KHNASVEKSQ VGFIDYIVHP LWETWADLVH PDAQDILDTL EDNREWYQST 650
    IPQSPSPAPD DQEEGRQGQT EKFQFELTLE EDCESDTEKD SGSQVEEDTS 700
    CSDSKTLCTQ DSESTEIPLD EQVEEEAVAE EESQPETCVP DDCCPDT 747
    Length:747
    Mass (Da):84,563
    Last modified:January 4, 2005 - v2
    Checksum:i68402163664B3676
    GO
    Isoform 9 (identifier: Q01063-2) [UniParc]FASTAAdd to Basket

    Also known as: PDE4D9

    The sequence of this isoform differs from the canonical sequence as follows:
         1-69: Missing.
         70-91: RPTSLPLKILPLIAVTSADSSG → MSIIMKPRSRSTSSLRTTEAVC

    Show »
    Length:678
    Mass (Da):76,817
    Checksum:i51D44F3467C9B71A
    GO
    Isoform 3 (identifier: Q01063-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-163: Missing.
         164-208: PFAQVLASLR...QPSINKATIT → MKEQPSCAGT...TESSFPCLFA

    Show »
    Length:584
    Mass (Da):66,394
    Checksum:iCEDFA3A57387798E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti403 – 4042NI → SR in AAA37368. (PubMed:1326532)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 163163Missing in isoform 3. 1 PublicationVSP_012394Add
    BLAST
    Alternative sequencei1 – 6969Missing in isoform 9. 1 PublicationVSP_012395Add
    BLAST
    Alternative sequencei70 – 9122RPTSL…ADSSG → MSIIMKPRSRSTSSLRTTEA VC in isoform 9. 1 PublicationVSP_012396Add
    BLAST
    Alternative sequencei164 – 20845PFAQV…KATIT → MKEQPSCAGTGHPSMAGYGR MAPFELAGGPVKRLRTESSF PCLFA in isoform 3. 1 PublicationVSP_012397Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF536978 mRNA. Translation: AAN10120.1.
    AY388962 mRNA. Translation: AAQ90406.1.
    AK081466 mRNA. Translation: BAC38226.1.
    CT025605, AC161585, AC163650 Genomic DNA. Translation: CAQ51656.1.
    M94541 mRNA. Translation: AAA37368.1. Different termination.
    CCDSiCCDS49359.1. [Q01063-1]
    RefSeqiNP_035186.1. NM_011056.3. [Q01063-1]
    XP_006517710.1. XM_006517647.1. [Q01063-2]
    UniGeneiMm.434429.

    Genome annotation databases

    EnsembliENSMUST00000074103; ENSMUSP00000073742; ENSMUSG00000021699. [Q01063-2]
    ENSMUST00000120664; ENSMUSP00000113024; ENSMUSG00000021699. [Q01063-3]
    ENSMUST00000122041; ENSMUSP00000113488; ENSMUSG00000021699. [Q01063-1]
    ENSMUST00000177907; ENSMUSP00000136485; ENSMUSG00000021699. [Q01063-1]
    GeneIDi238871.
    KEGGimmu:238871.
    UCSCiuc007rvg.2. mouse. [Q01063-1]
    uc007rvj.2. mouse. [Q01063-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF536978 mRNA. Translation: AAN10120.1 .
    AY388962 mRNA. Translation: AAQ90406.1 .
    AK081466 mRNA. Translation: BAC38226.1 .
    CT025605 , AC161585 , AC163650 Genomic DNA. Translation: CAQ51656.1 .
    M94541 mRNA. Translation: AAA37368.1 . Different termination.
    CCDSi CCDS49359.1. [Q01063-1 ]
    RefSeqi NP_035186.1. NM_011056.3. [Q01063-1 ]
    XP_006517710.1. XM_006517647.1. [Q01063-2 ]
    UniGenei Mm.434429.

    3D structure databases

    ProteinModelPortali Q01063.
    SMRi Q01063. Positions 244-678.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 232023. 3 interactions.
    DIPi DIP-29706N.
    IntActi Q01063. 2 interactions.

    Chemistry

    BindingDBi Q01063.
    ChEMBLi CHEMBL2111373.
    DrugBanki DB00131. Adenosine monophosphate.

    PTM databases

    PhosphoSitei Q01063.

    Proteomic databases

    PaxDbi Q01063.
    PRIDEi Q01063.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000074103 ; ENSMUSP00000073742 ; ENSMUSG00000021699 . [Q01063-2 ]
    ENSMUST00000120664 ; ENSMUSP00000113024 ; ENSMUSG00000021699 . [Q01063-3 ]
    ENSMUST00000122041 ; ENSMUSP00000113488 ; ENSMUSG00000021699 . [Q01063-1 ]
    ENSMUST00000177907 ; ENSMUSP00000136485 ; ENSMUSG00000021699 . [Q01063-1 ]
    GeneIDi 238871.
    KEGGi mmu:238871.
    UCSCi uc007rvg.2. mouse. [Q01063-1 ]
    uc007rvj.2. mouse. [Q01063-2 ]

    Organism-specific databases

    CTDi 5144.
    MGIi MGI:99555. Pde4d.

    Phylogenomic databases

    eggNOGi NOG122287.
    GeneTreei ENSGT00740000115148.
    HOGENOMi HOG000236297.
    HOVERGENi HBG108239.
    KOi K01120.
    OMAi QHEVEMP.
    OrthoDBi EOG7HQNBC.
    PhylomeDBi Q01063.

    Enzyme and pathway databases

    UniPathwayi UPA00762 ; UER00747 .
    Reactomei REACT_203795. DARPP-32 events.

    Miscellaneous databases

    NextBioi 383911.
    PROi Q01063.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01063.
    Bgeei Q01063.
    CleanExi MM_PDE4D.
    Genevestigatori Q01063.

    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

    1. "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] (ISOFORM 7), TISSUE SPECIFICITY.
      Strain: BALB/c.
    2. Chai H., Gaweda B., De Vivo M., Wang D.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Strain: C57BL/6J.
      Tissue: Head.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding the 63-kDa calmodulin-dependent phosphodiesterase."
      Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.
      J. Biol. Chem. 267:18683-18688(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 400-514.
    6. "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.
    7. "Remodeling of ryanodine receptor complex causes 'leaky' channels: a molecular mechanism for decreased exercise capacity."
      Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.
      Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH RYR1; FKBP1A; PKA AND PP1.

    Entry informationi

    Entry nameiPDE4D_MOUSE
    AccessioniPrimary (citable) accession number: Q01063
    Secondary accession number(s): B2KF58
    , Q6TRH9, Q8C4Q7, Q8CG05
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3