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Q9WUA5

- EPM2A_MOUSE

UniProt

Q9WUA5 - EPM2A_MOUSE

Protein

Laforin

Gene

Epm2a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    Has been shown to have both dual-specificity protein phosphatase and glucan phosphatase activities and, together with the E3 ubiquitin ligase NHLRC1/malin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. Dephosphorylates phosphotyrosine, phosphoserine and phosphothreonine substrates in vitro. Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway.6 Publications

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei265 – 2651Phosphocysteine intermediate1 PublicationPROSITE-ProRule annotation
    Sitei328 – 3281Required for homodimerizationBy similarity

    GO - Molecular functioni

    1. phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Source: RefGenome
    2. protein binding Source: IntAct
    3. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    4. protein tyrosine phosphatase activity Source: MGI
    5. starch binding Source: InterPro

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW
    2. glycogen metabolic process Source: UniProtKB-KW
    3. habituation Source: MGI
    4. inositol phosphate dephosphorylation Source: RefGenome
    5. nervous system development Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Autophagy, Carbohydrate metabolism, Glycogen metabolism

    Enzyme and pathway databases

    ReactomeiREACT_188939. Glycogen synthesis.
    REACT_203841. Myoclonic epilepsy of Lafora.

    Protein family/group databases

    CAZyiCBM20. Carbohydrate-Binding Module Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laforin (EC:3.1.3.-, EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Glucan phosphatase
    Lafora PTPase
    Short name:
    LAFPTPase
    Gene namesi
    Name:Epm2a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1341085. Epm2a.

    Subcellular locationi

    Cytoplasm 1 Publication. Endoplasmic reticulum 1 Publication
    Note: Under glycogenolytic conditions localizes to the nucleus.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: MGI
    3. endoplasmic reticulum Source: UniProtKB-SubCell
    4. nucleus Source: MGI
    5. polysome Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    Pathology & Biotechi

    Disruption phenotypei

    Impaired behavioral responses, ataxia, spontaneous myoclonic seizures and progressive accumulation of poorly-branched, insoluble forms of glycogen (Lafora bodies) in liver, brain and skeletal muscle tissue. At 3 months of age, overall glycogen levels are normal; by 9 months of age, a 3-fold increase in overall glycogen levels and a 6-fold increase in glycogen phosphate levels is observed. Glycogen synthase (Gys1) and 1,4-alpha-glucan-branching enzyme (Gbe1) activities in brain and muscle tissue are normal. 10 month old mice have neurofibrillary tangles (NFTs, aggregates of hyperphosphorylated Mapt/Tau) in brain and muscle tissue, however NFTs are not observed in 4 and 6 month old mice. 3- and 12- month old mice show reduced numbers of autophagosomes in liver extracts, and 3-month old starved mice have increased levels of the autophagy dysfunction marker Map1lc3b/LC3-II and increased levels of ubiquitinated proteins, suggesting impaired macroautophagy.5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321W → G: Loss of glycogen phosphatase activity. 1 Publication
    Mutagenesisi265 – 2651C → S: Loss of glycogen phosphatase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 330330LaforinPRO_0000094839Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei25 – 251Phosphoserine; by AMPKBy similarity

    Post-translational modificationi

    Polyubiquitinated by NHLRC1/malin.By similarity
    Phosphorylation on Ser-25 by AMPK affects the phosphatase activity of the enzyme and its ability to homodimerize and interact with NHLRC1, PPP1R3C or PRKAA2.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ9WUA5.

    PTM databases

    PhosphoSiteiQ9WUA5.

    Expressioni

    Tissue specificityi

    Widely expressed. Higher levels of expression are found in heart, brain, liver, skeletal muscle and kidney. Found in neuronal dendrites and perikarya, but not in axons.2 Publications

    Developmental stagei

    In the embryo, highly expressed at 17 dpc. Detected in all postnatal stages, but highest expression is found at day 160 after birth.1 Publication

    Gene expression databases

    GenevestigatoriQ9WUA5.

    Interactioni

    Subunit structurei

    Interacts with itself; however no biological function has been identified for the dimer. Interacts with PPP1R3B, PPP1R3C, HIRIP5, and EPM2AIP1. Binds glycogen and Lafora bodies. Interacts with NHLRC1/malin (via the NHL repeats) By similarity. Forms a complex with NHLRC1/malin and HSP70. Interacts with PPP1R3D; in the presence of NHLC1/malin the interaction leads to ubiquitination and autophagic degradation of PPP1R3D. Interacts (via the phosphatase domain) with MAPT/Tau; the interaction dephosphorylates MAPT.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Gsk3bQ9WV602EBI-1040928,EBI-400793
    NHLRC1Q6VVB112EBI-1040928,EBI-6426628From a different organism.

    Protein-protein interaction databases

    IntActiQ9WUA5. 3 interactions.
    MINTiMINT-8374088.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WUA5.
    SMRiQ9WUA5. Positions 8-108, 153-300.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 123123CBM20PROSITE-ProRule annotationAdd
    BLAST
    Domaini242 – 31069Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG243912.
    GeneTreeiENSGT00390000010101.
    HOGENOMiHOG000285975.
    HOVERGENiHBG051493.
    InParanoidiQ9WUA5.
    KOiK14165.
    OMAiHWIEVSG.
    OrthoDBiEOG7RJPRM.
    TreeFamiTF332841.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR013784. Carb-bd-like_fold.
    IPR002044. CBM_fam20.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00686. CBM_20. 1 hit.
    PF00782. DSPc. 1 hit.
    [Graphical view]
    SMARTiSM01065. CBM_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49452. SSF49452. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS51166. CBM20. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9WUA5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLFRFGVVVP PAVAGARQEL LLAGSRPELG RWEPHGAVRL RPAGTAAGAA    50
    ALALQEPGLW LAEVELEAYE EAGGAEPGRV DTFWYKFLQR EPGGELHWEG 100
    NGPHHDRCCT YNEDNLVDGV YCLPVGHWIE ATGHTNEMKH TTDFYFNIAG 150
    HQAMHYSRIL PNIWLGSCPR QLEHVTIKLK HELGVTAVMN FQTEWDIIQN 200
    SSGCNRYPEP MTPDTMMKLY KEEGLSYIWM PTPDMSTEGR VQMLPQAVCL 250
    LHALLENGHT VYVHCNAGVG RSTAAVCGWL HYVIGWNLRK VQYFIMAKRP 300
    AVYIDEDALA QAQQDFSQKF GKVHSSICAL 330
    Length:330
    Mass (Da):36,958
    Last modified:October 3, 2012 - v2
    Checksum:i89B18C64BBBAB02A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti140 – 1401H → R in AAD26336. (PubMed:10092504)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124044 mRNA. Translation: AAD26336.1.
    AC101984 Genomic DNA. No translation available.
    AC157018 Genomic DNA. No translation available.
    CH466562 Genomic DNA. Translation: EDL03516.1.
    AK041609 mRNA. Translation: BAC31004.1.
    CCDSiCCDS23698.1.
    RefSeqiNP_034276.2. NM_010146.2.
    UniGeneiMm.89946.

    Genome annotation databases

    EnsembliENSMUST00000069106; ENSMUSP00000066050; ENSMUSG00000055493.
    GeneIDi13853.
    KEGGimmu:13853.
    UCSCiuc007ejv.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124044 mRNA. Translation: AAD26336.1 .
    AC101984 Genomic DNA. No translation available.
    AC157018 Genomic DNA. No translation available.
    CH466562 Genomic DNA. Translation: EDL03516.1 .
    AK041609 mRNA. Translation: BAC31004.1 .
    CCDSi CCDS23698.1.
    RefSeqi NP_034276.2. NM_010146.2.
    UniGenei Mm.89946.

    3D structure databases

    ProteinModelPortali Q9WUA5.
    SMRi Q9WUA5. Positions 8-108, 153-300.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9WUA5. 3 interactions.
    MINTi MINT-8374088.

    Protein family/group databases

    CAZyi CBM20. Carbohydrate-Binding Module Family 20.

    PTM databases

    PhosphoSitei Q9WUA5.

    Proteomic databases

    PRIDEi Q9WUA5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000069106 ; ENSMUSP00000066050 ; ENSMUSG00000055493 .
    GeneIDi 13853.
    KEGGi mmu:13853.
    UCSCi uc007ejv.1. mouse.

    Organism-specific databases

    CTDi 7957.
    MGIi MGI:1341085. Epm2a.

    Phylogenomic databases

    eggNOGi NOG243912.
    GeneTreei ENSGT00390000010101.
    HOGENOMi HOG000285975.
    HOVERGENi HBG051493.
    InParanoidi Q9WUA5.
    KOi K14165.
    OMAi HWIEVSG.
    OrthoDBi EOG7RJPRM.
    TreeFami TF332841.

    Enzyme and pathway databases

    Reactomei REACT_188939. Glycogen synthesis.
    REACT_203841. Myoclonic epilepsy of Lafora.

    Miscellaneous databases

    NextBioi 284714.
    PROi Q9WUA5.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori Q9WUA5.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR013784. Carb-bd-like_fold.
    IPR002044. CBM_fam20.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR013783. Ig-like_fold.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    Pfami PF00686. CBM_20. 1 hit.
    PF00782. DSPc. 1 hit.
    [Graphical view ]
    SMARTi SM01065. CBM_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49452. SSF49452. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEi PS51166. CBM20. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of mouse homologue for the human epilepsy gene, EPM2A."
      Ganesh S., Amano K., Delgado-Escueta A.V., Yamakawa K.
      Biochem. Biophys. Res. Commun. 257:24-28(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Strain: ICR.
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] OF 10-137.
      Strain: C57BL/6J.
      Tissue: Thymus.
    5. "Regional and developmental expression of Epm2a gene and its evolutionary conservation."
      Ganesh S., Agarwala K.L., Amano K., Suzuki T., Delgado-Escueta A.V., Yamakawa K.
      Biochem. Biophys. Res. Commun. 283:1046-1053(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    6. "Laforin preferentially binds the neurotoxic starch-like polyglucosans, which form in its absence in progressive myoclonus epilepsy."
      Chan E.M., Ackerley C.A., Lohi H., Ianzano L., Cortez M.A., Shannon P., Scherer S.W., Minassian B.A.
      Hum. Mol. Genet. 13:1117-1129(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH POLYGLUCOSANS AND GLYCOGEN.
    7. "Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo."
      Tagliabracci V.S., Turnbull J., Wang W., Girard J.M., Zhao X., Skurat A.V., Delgado-Escueta A.V., Minassian B.A., Depaoli-Roach A.A., Roach P.J.
      Proc. Natl. Acad. Sci. U.S.A. 104:19262-19266(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A GLUCAN PHOSPHATASE, DISRUPTION PHENOTYPE, ACTIVE SITE, MUTAGENESIS OF TRP-32 AND CYS-265.
    8. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    9. "The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system."
      Garyali P., Siwach P., Singh P.K., Puri R., Mittal S., Sengupta S., Parihar R., Ganesh S.
      Hum. Mol. Genet. 18:688-700(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COMPLEX FORMATION WITH NHLRC1 AND HSP70.
    10. "Hyperphosphorylation and aggregation of Tau in laforin-deficient mice, an animal model for Lafora disease."
      Puri R., Suzuki T., Yamakawa K., Ganesh S.
      J. Biol. Chem. 284:22657-22663(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAPT, DISRUPTION PHENOTYPE.
    11. "Laforin, the most common protein mutated in Lafora disease, regulates autophagy."
      Aguado C., Sarkar S., Korolchuk V.I., Criado O., Vernia S., Boya P., Sanz P., de Cordoba S.R., Knecht E., Rubinsztein D.C.
      Hum. Mol. Genet. 19:2867-2876(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    12. "Increased laforin and laforin binding to glycogen underlie Lafora body formation in malin-deficient Lafora disease."
      Tiberia E., Turnbull J., Wang T., Ruggieri A., Zhao X.C., Pencea N., Israelian J., Wang Y., Ackerley C.A., Wang P., Liu Y., Minassian B.A.
      J. Biol. Chem. 287:25650-25659(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    13. "Glycogenic activity of R6, a protein phosphatase 1 regulatory subunit, is modulated by the laforin-malin complex."
      Rubio-Villena C., Garcia-Gimeno M.A., Sanz P.
      Int. J. Biochem. Cell Biol. 45:1479-1488(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R3D.

    Entry informationi

    Entry nameiEPM2A_MOUSE
    AccessioniPrimary (citable) accession number: Q9WUA5
    Secondary accession number(s): G5E8E2, Q8BY80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 109 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3