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P17182

- ENOA_MOUSE

UniProt

P17182 - ENOA_MOUSE

Protein

Alpha-enolase

Gene

Eno1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses By similarity. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production By similarity.By similarity

    Catalytic activityi

    2-phospho-D-glycerate = phosphoenolpyruvate + H2O.

    Cofactori

    Magnesium. Binds two Mg2+ per subunit. Required for catalysis and for stabilizing the dimer.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi40 – 401Magnesium 1By similarity
    Binding sitei158 – 1581SubstrateBy similarity
    Binding sitei167 – 1671SubstrateBy similarity
    Active sitei210 – 2101Proton donorBy similarity
    Metal bindingi245 – 2451Magnesium 2By similarity
    Metal bindingi293 – 2931Magnesium 2By similarity
    Binding sitei293 – 2931SubstrateBy similarity
    Metal bindingi318 – 3181Magnesium 2By similarity
    Binding sitei318 – 3181SubstrateBy similarity
    Active sitei343 – 3431Proton acceptorBy similarity
    Binding sitei394 – 3941SubstrateBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphopyruvate hydratase activity Source: MGI

    GO - Biological processi

    1. glycolytic process Source: MGI

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi4.2.1.11. 3474.
    SABIO-RKP17182.
    UniPathwayiUPA00109; UER00187.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-enolase (EC:4.2.1.11)
    Alternative name(s):
    2-phospho-D-glycerate hydro-lyase
    Enolase 1
    Non-neural enolase
    Short name:
    NNE
    Gene namesi
    Name:Eno1
    Synonyms:Eno-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:95393. Eno1.

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity
    Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form By similarity. ENO1 is localized to the M-band.By similarity1 Publication

    GO - Cellular componenti

    1. phosphopyruvate hydratase complex Source: InterPro
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 434433Alpha-enolasePRO_0000134098Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei44 – 441Phosphotyrosine1 Publication
    Modified residuei60 – 601N6-acetyllysine; alternate1 Publication
    Modified residuei60 – 601N6-succinyllysine; alternate1 Publication
    Modified residuei71 – 711N6-acetyllysineBy similarity
    Modified residuei89 – 891N6-acetyllysine; alternate1 Publication
    Modified residuei89 – 891N6-succinyllysine; alternate1 Publication
    Modified residuei92 – 921N6-acetyllysine1 Publication
    Modified residuei126 – 1261N6-acetyllysine1 Publication
    Modified residuei193 – 1931N6-acetyllysine1 Publication
    Modified residuei199 – 1991N6-acetyllysineBy similarity
    Modified residuei202 – 2021N6-acetyllysine1 Publication
    Modified residuei228 – 2281N6-acetyllysine; alternate1 Publication
    Modified residuei228 – 2281N6-succinyllysine; alternate1 Publication
    Modified residuei233 – 2331N6-acetyllysine; alternateBy similarity
    Modified residuei233 – 2331N6-malonyllysine; alternateBy similarity
    Modified residuei254 – 2541PhosphoserineBy similarity
    Modified residuei256 – 2561N6-acetyllysine1 Publication
    Modified residuei263 – 2631PhosphoserineBy similarity
    Modified residuei281 – 2811N6-acetyllysineBy similarity
    Modified residuei287 – 2871PhosphotyrosineBy similarity
    Modified residuei335 – 3351N6-acetyllysine1 Publication
    Modified residuei343 – 3431N6-acetyllysine1 Publication
    Modified residuei406 – 4061N6-acetyllysine1 Publication
    Modified residuei420 – 4201N6-acetyllysine; alternateBy similarity
    Modified residuei420 – 4201N6-malonyllysine; alternateBy similarity
    Modified residuei420 – 4201N6-succinyllysine; alternate1 Publication

    Post-translational modificationi

    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP17182.
    PaxDbiP17182.
    PRIDEiP17182.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00462072.
    P17182.
    SWISS-2DPAGEP17182.
    UCD-2DPAGEP17182.

    PTM databases

    PhosphoSiteiP17182.

    Expressioni

    Tissue specificityi

    The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons. In striated muscle, expression of ENO1 appears to be independent of fiber type.1 Publication

    Developmental stagei

    During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells. In embryonic muscle, ENO1 is highly expressed until E17. Decreased levels from P5.1 Publication

    Gene expression databases

    ArrayExpressiP17182.
    BgeeiP17182.
    GenevestigatoriP17182.

    Interactioni

    Subunit structurei

    Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. ENO1 interacts with PLG in the neuronal plasma membrane and promotes its activation. The C-terminal lysine is required for this binding By similarity. In vitro, interacts with several glycolytic enzymes including PKM, PGM, CKM and aldolase. Also binds troponin, in vitro.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi199451. 16 interactions.
    241069. 8 interactions.
    IntActiP17182. 13 interactions.
    MINTiMINT-4996502.

    Structurei

    3D structure databases

    ProteinModelPortaliP17182.
    SMRiP17182. Positions 2-434.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni370 – 3734Substrate bindingBy similarity
    Regioni405 – 43430Required for interaction with PLGBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the enolase family.Curated

    Phylogenomic databases

    eggNOGiCOG0148.
    HOGENOMiHOG000072174.
    HOVERGENiHBG000067.
    InParanoidiP17182.
    KOiK01689.
    OMAiVSEKSCN.
    OrthoDBiEOG776SQ1.
    PhylomeDBiP17182.
    TreeFamiTF300391.

    Family and domain databases

    Gene3Di3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    HAMAPiMF_00318. Enolase.
    InterProiIPR000941. Enolase.
    IPR020810. Enolase_C.
    IPR029065. Enolase_C-like.
    IPR020809. Enolase_CS.
    IPR020811. Enolase_N.
    IPR029017. Enolase_N_like.
    [Graphical view]
    PANTHERiPTHR11902. PTHR11902. 1 hit.
    PfamiPF00113. Enolase_C. 1 hit.
    PF03952. Enolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001400. Enolase. 1 hit.
    PRINTSiPR00148. ENOLASE.
    SUPFAMiSSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    TIGRFAMsiTIGR01060. eno. 1 hit.
    PROSITEiPS00164. ENOLASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P17182-1 [UniParc]FASTAAdd to Basket

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    MSILRIHARE IFDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR    50
    DNDKTRFMGK GVSQAVEHIN KTIAPALVSK KVNVVEQEKI DKLMIEMDGT 100
    ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN PEVILPVPAF 150
    NVINGGSHAG NKLAMQEFMI LPVGASSFRE AMRIGAEVYH NLKNVIKEKY 200
    GKDATNVGDE GGFAPNILEN KEALELLKTA IAKAGYTDQV VIGMDVAASE 250
    FYRSGKYDLD FKSPDDPSRY ITPDQLADLY KSFVQNYPVV SIEDPFDQDD 300
    WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AASEKSCNCL LLKVNQIGSV 350
    TESLQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR 400
    SERLAKYNQI LRIEEELGSK AKFAGRSFRN PLAK 434
    Length:434
    Mass (Da):47,141
    Last modified:January 23, 2007 - v3
    Checksum:iDBEF6270A70DE3A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti359 – 3591L → P in CAA36605. (PubMed:2362815)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52379 mRNA. Translation: CAA36605.1.
    AK002336 mRNA. Translation: BAB22021.1.
    BC003891 mRNA. Translation: AAH03891.1.
    BC004017 mRNA. Translation: AAH04017.1.
    BC010685 mRNA. Translation: AAH10685.1.
    BC024644 mRNA. Translation: AAH24644.1.
    BC085098 mRNA. Translation: AAH85098.1.
    CCDSiCCDS18971.1.
    PIRiS10246.
    RefSeqiNP_001020559.1. NM_001025388.1.
    NP_075608.2. NM_023119.2.
    UniGeneiMm.372357.
    Mm.372389.
    Mm.70666.

    Genome annotation databases

    EnsembliENSMUST00000076155; ENSMUSP00000075513; ENSMUSG00000059040.
    ENSMUST00000080926; ENSMUSP00000079727; ENSMUSG00000063524.
    GeneIDi13806.
    433182.
    KEGGimmu:13806.
    mmu:433182.
    UCSCiuc008ewh.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52379 mRNA. Translation: CAA36605.1 .
    AK002336 mRNA. Translation: BAB22021.1 .
    BC003891 mRNA. Translation: AAH03891.1 .
    BC004017 mRNA. Translation: AAH04017.1 .
    BC010685 mRNA. Translation: AAH10685.1 .
    BC024644 mRNA. Translation: AAH24644.1 .
    BC085098 mRNA. Translation: AAH85098.1 .
    CCDSi CCDS18971.1.
    PIRi S10246.
    RefSeqi NP_001020559.1. NM_001025388.1.
    NP_075608.2. NM_023119.2.
    UniGenei Mm.372357.
    Mm.372389.
    Mm.70666.

    3D structure databases

    ProteinModelPortali P17182.
    SMRi P17182. Positions 2-434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199451. 16 interactions.
    241069. 8 interactions.
    IntActi P17182. 13 interactions.
    MINTi MINT-4996502.

    PTM databases

    PhosphoSitei P17182.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00462072.
    P17182.
    SWISS-2DPAGE P17182.
    UCD-2DPAGE P17182.

    Proteomic databases

    MaxQBi P17182.
    PaxDbi P17182.
    PRIDEi P17182.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000076155 ; ENSMUSP00000075513 ; ENSMUSG00000059040 .
    ENSMUST00000080926 ; ENSMUSP00000079727 ; ENSMUSG00000063524 .
    GeneIDi 13806.
    433182.
    KEGGi mmu:13806.
    mmu:433182.
    UCSCi uc008ewh.1. mouse.

    Organism-specific databases

    CTDi 2023.
    433182.
    MGIi MGI:95393. Eno1.

    Phylogenomic databases

    eggNOGi COG0148.
    HOGENOMi HOG000072174.
    HOVERGENi HBG000067.
    InParanoidi P17182.
    KOi K01689.
    OMAi VSEKSCN.
    OrthoDBi EOG776SQ1.
    PhylomeDBi P17182.
    TreeFami TF300391.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00187 .
    BRENDAi 4.2.1.11. 3474.
    SABIO-RK P17182.

    Miscellaneous databases

    NextBioi 284584.
    PROi P17182.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17182.
    Bgeei P17182.
    Genevestigatori P17182.

    Family and domain databases

    Gene3Di 3.20.20.120. 1 hit.
    3.30.390.10. 1 hit.
    HAMAPi MF_00318. Enolase.
    InterProi IPR000941. Enolase.
    IPR020810. Enolase_C.
    IPR029065. Enolase_C-like.
    IPR020809. Enolase_CS.
    IPR020811. Enolase_N.
    IPR029017. Enolase_N_like.
    [Graphical view ]
    PANTHERi PTHR11902. PTHR11902. 1 hit.
    Pfami PF00113. Enolase_C. 1 hit.
    PF03952. Enolase_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001400. Enolase. 1 hit.
    PRINTSi PR00148. ENOLASE.
    SUPFAMi SSF51604. SSF51604. 1 hit.
    SSF54826. SSF54826. 1 hit.
    TIGRFAMsi TIGR01060. eno. 1 hit.
    PROSITEi PS00164. ENOLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequences of cDNAs alpha and gamma enolase mRNAs from mouse brain."
      Kaghad M., Dumont X., Chalon P., Lelias J.M., Lamande N., Lucas M., Lazar M., Caput D.
      Nucleic Acids Res. 18:3638-3638(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "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].
      Strain: C57BL/6J.
      Tissue: Kidney.
    3. "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].
      Strain: Czech II and FVB/N.
      Tissue: Mammary gland and Mammary tumor.
    4. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 10-28; 33-50; 61-120; 133-179; 184-193; 203-228; 234-253; 257-262; 270-281; 307-326; 344-358; 373-394 AND 413-420, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    5. "Cholesteryl ester loading of mouse peritoneal macrophages is associated with changes in the expression or modification of specific cellular proteins, including increase in an alpha-enolase isoform."
      Bottalico L.A., Kendrick N.C., Keller A., Li Y., Tabas I.
      Arterioscler. Thromb. 13:264-275(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 60-71; 100-114; 184-198 AND 246-259.
      Tissue: Macrophage.
    6. "Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins."
      Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F., Lazar M., Keller A.
      Biochem. J. 323:791-800(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PKM; PGM; CKM; ALDO AND TROPONIN, DEVELOPMENTAL STAGE.
    7. "Fibre-type distribution and subcellular localisation of alpha and beta enolase in mouse striated muscle."
      Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C., Lucas M., Chatelet F.-P.
      Biol. Cell 92:527-535(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. Cited for: ISGYLATION.
    9. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-89; LYS-92; LYS-126; LYS-193; LYS-202; LYS-228; LYS-256; LYS-335; LYS-343 AND LYS-406, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-89; LYS-228 AND LYS-420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiENOA_MOUSE
    AccessioniPrimary (citable) accession number: P17182
    Secondary accession number(s): Q99KT7, Q9DCY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 157 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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