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Q9EPB4

- ASC_MOUSE

UniProt

Q9EPB4 - ASC_MOUSE

Protein

Apoptosis-associated speck-like protein containing a CARD

Gene

Pycard

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.4 Publications

    GO - Molecular functioni

    1. peptidase activator activity involved in apoptotic process Source: MGI
    2. protein binding Source: MGI
    3. protein homodimerization activity Source: HGNC
    4. Pyrin domain binding Source: HGNC

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    2. activation of innate immune response Source: UniProtKB
    3. apoptotic process Source: MGI
    4. cellular response to interleukin-1 Source: Ensembl
    5. cellular response to lipopolysaccharide Source: Ensembl
    6. defense response to Gram-negative bacterium Source: Ensembl
    7. defense response to virus Source: Ensembl
    8. inflammatory response Source: MGI
    9. innate immune response Source: UniProtKB-KW
    10. interleukin-1 beta production Source: MGI
    11. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: Ensembl
    12. macropinocytosis Source: UniProtKB
    13. myeloid dendritic cell activation involved in immune response Source: UniProtKB
    14. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    15. negative regulation of interferon-beta production Source: Ensembl
    16. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
    17. negative regulation of protein serine/threonine kinase activity Source: Ensembl
    18. positive regulation of actin filament polymerization Source: UniProtKB
    19. positive regulation of activated T cell proliferation Source: UniProtKB
    20. positive regulation of adaptive immune response Source: Ensembl
    21. positive regulation of antigen processing and presentation of peptide antigen via MHC class II Source: UniProtKB
    22. positive regulation of apoptotic process Source: Ensembl
    23. positive regulation of chemokine secretion Source: UniProtKB
    24. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
    25. positive regulation of defense response to virus by host Source: UniProtKB
    26. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    27. positive regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    28. positive regulation of interferon-gamma production Source: UniProtKB
    29. positive regulation of interleukin-10 secretion Source: Ensembl
    30. positive regulation of interleukin-1 beta secretion Source: UniProtKB
    31. positive regulation of interleukin-6 production Source: UniProtKB
    32. positive regulation of interleukin-6 secretion Source: Ensembl
    33. positive regulation of interleukin-8 secretion Source: Ensembl
    34. positive regulation of JNK cascade Source: Ensembl
    35. positive regulation of NF-kappaB transcription factor activity Source: Ensembl
    36. positive regulation of phagocytosis Source: UniProtKB
    37. positive regulation of release of cytochrome c from mitochondria Source: Ensembl
    38. positive regulation of T cell migration Source: UniProtKB
    39. positive regulation of tumor necrosis factor production Source: Ensembl
    40. regulation of apoptotic process Source: MGI
    41. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    42. regulation of inflammatory response Source: MGI
    43. regulation of intrinsic apoptotic signaling pathway Source: Ensembl
    44. regulation of protein stability Source: UniProtKB
    45. regulation of Rac GTPase activity Source: UniProtKB
    46. regulation of tumor necrosis factor-mediated signaling pathway Source: Ensembl
    47. tumor necrosis factor-mediated signaling pathway Source: Ensembl

    Keywords - Biological processi

    Apoptosis, Immunity, Inflammatory response, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_198662. The AIM2 inflammasome.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Apoptosis-associated speck-like protein containing a CARD
    Short name:
    mASC
    Alternative name(s):
    PYD and CARD domain-containing protein
    Gene namesi
    Name:Pycard
    Synonyms:Asc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1931465. Pycard.

    Subcellular locationi

    Cytoplasm 2 Publications. Endoplasmic reticulum By similarity. Mitochondrion By similarity. Nucleus By similarity
    Note: Upstream of caspase activation, a redistribution from the cytoplasm to the aggregates occurs. These appear as hollow, perinuclear spherical, ball-like structures. Upon NLRP3 inflammasome activation redistributes to the perinuclear space localizing to endoplasmic reticulum and mitochondria. Localized primarily to the nucleus in resting monocytes/macrophages and rapidly redistributed to the cytoplasm upon pathogen infection By similarity. Localized to large cytoplasmic aggregate appearing as a speck containing AIM2, PYCARD, CASP8 and bacterial DNA after infection with Francisella tularensis.By similarity

    GO - Cellular componenti

    1. AIM2 inflammasome complex Source: UniProtKB
    2. cytoplasm Source: HGNC
    3. cytosol Source: MGI
    4. endoplasmic reticulum Source: UniProtKB-SubCell
    5. extracellular region Source: MGI
    6. mitochondrion Source: UniProtKB-SubCell
    7. neuronal cell body Source: Ensembl
    8. NLRP1 inflammasome complex Source: Ensembl
    9. NLRP3 inflammasome complex Source: UniProtKB
    10. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Increased resistance to endotoxic shock and severe defects in caspase-1 activation and interleukin-1 beta and interleukin-18 production in macrophages in response to several pro-inflammatory molecules.2 Publications

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 193193Apoptosis-associated speck-like protein containing a CARDPRO_0000064693Add
    BLAST

    Post-translational modificationi

    Phosphorylated.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9EPB4.
    PaxDbiQ9EPB4.
    PRIDEiQ9EPB4.

    PTM databases

    PhosphoSiteiQ9EPB4.

    Expressioni

    Tissue specificityi

    Expressed in small intestine, colon, thymus, spleen, brain, heart, skeletal muscle, kidney, lung and liver.

    Developmental stagei

    Strongly expressed at E9.5 in the telencephalon, thalamic areas of the diencephalon, heart and liver.

    Gene expression databases

    ArrayExpressiQ9EPB4.
    BgeeiQ9EPB4.
    CleanExiMM_PYCARD.
    GenevestigatoriQ9EPB4.

    Interactioni

    Subunit structurei

    Self-associates; enforced oligomerization induces apoptosis, NF-kappa-B regulation and interleukin-1 beta seceretion. Homooligomers can form disk-like particles of approximately 12 nm diameter and approximately 1 nm height. Component of several inflammasomes containing one pattern recognition receptor/sensor, such as NLRP1, NLRP2, NLRP3, AIM2, MEFV or NOD2, and probably NLRC4, NLRP12 or IFI16. Major component of the ASC pyroptosome, a 1-2 um supramolecular assembly (one per macrophage cell) which consists of oligomerized PYCARD dimers and CASP1. Interacts with CASP1 (precursor form); the interaction induces activation of CASP1 leading to the processing of interleukin-1 beta; PYCARD competes with RIPK2 for binding to CASP1. Interacts with NLRP3; the interaction requires the homooligomerization of NLRP3. Interacts with NLRP2, NLRC4, MEFV, CARD16, AIM2, IFI16, NOD2, DDX58, RIPK2, PYDC1, PYDC2, NLRP10, CASP8, CHUK, IKBKB and BAX.1 Publication

    Protein-protein interaction databases

    DIPiDIP-27619N.
    IntActiQ9EPB4. 3 interactions.
    STRINGi10090.ENSMUSP00000033056.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EPB4.
    SMRiQ9EPB4. Positions 1-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9191DAPINPROSITE-ProRule annotationAdd
    BLAST
    Domaini105 – 19389CARDPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The DAPIN domain mediates homotypic interactions with DAPIN domains of proteins such as of NLRP3, PYDC1 and AIM2.By similarity
    The CARD domain mediates interaction with CASP1 and NLRC4.By similarity

    Sequence similaritiesi

    Contains 1 CARD domain.PROSITE-ProRule annotation
    Contains 1 DAPIN domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG39139.
    GeneTreeiENSGT00440000033973.
    HOGENOMiHOG000034090.
    HOVERGENiHBG018739.
    InParanoidiQ9EPB4.
    KOiK12799.
    OMAiPMDAVDL.
    OrthoDBiEOG786H4P.
    PhylomeDBiQ9EPB4.
    TreeFamiTF337882.

    Family and domain databases

    Gene3Di1.10.533.10. 2 hits.
    InterProiIPR001315. CARD.
    IPR004020. DAPIN.
    IPR011029. DEATH-like_dom.
    [Graphical view]
    PfamiPF00619. CARD. 1 hit.
    PF02758. PYRIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 2 hits.
    PROSITEiPS50209. CARD. 1 hit.
    PS50824. DAPIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9EPB4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRARDAILD ALENLSGDEL KKFKMKLLTV QLREGYGRIP RGALLQMDAI    50
    DLTDKLVSYY LESYGLELTM TVLRDMGLQE LAEQLQTTKE ESGAVAAAAS 100
    VPAQSTARTG HFVDQHRQAL IARVTEVDGV LDALHGSVLT EGQYQAVRAE 150
    TTSQDKMRKL FSFVPSWNLT CKDSLLQALK EIHPYLVMDL EQS 193
    Length:193
    Mass (Da):21,459
    Last modified:March 1, 2001 - v1
    Checksum:i2A4EA40194870B31
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti159 – 1591K → E in BAB31341. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB032249 mRNA. Translation: BAB16609.1.
    AF310104 mRNA. Translation: AAG30287.1.
    AK009852 mRNA. Translation: BAB26543.1.
    AK007742 mRNA. Translation: BAB25229.1.
    AK018682 mRNA. Translation: BAB31341.1.
    BC008252 mRNA. Translation: AAH08252.1.
    CCDSiCCDS21888.1.
    RefSeqiNP_075747.3. NM_023258.4.
    UniGeneiMm.24163.

    Genome annotation databases

    EnsembliENSMUST00000033056; ENSMUSP00000033056; ENSMUSG00000030793.
    GeneIDi66824.
    KEGGimmu:66824.
    UCSCiuc009jxu.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB032249 mRNA. Translation: BAB16609.1 .
    AF310104 mRNA. Translation: AAG30287.1 .
    AK009852 mRNA. Translation: BAB26543.1 .
    AK007742 mRNA. Translation: BAB25229.1 .
    AK018682 mRNA. Translation: BAB31341.1 .
    BC008252 mRNA. Translation: AAH08252.1 .
    CCDSi CCDS21888.1.
    RefSeqi NP_075747.3. NM_023258.4.
    UniGenei Mm.24163.

    3D structure databases

    ProteinModelPortali Q9EPB4.
    SMRi Q9EPB4. Positions 1-193.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-27619N.
    IntActi Q9EPB4. 3 interactions.
    STRINGi 10090.ENSMUSP00000033056.

    PTM databases

    PhosphoSitei Q9EPB4.

    Proteomic databases

    MaxQBi Q9EPB4.
    PaxDbi Q9EPB4.
    PRIDEi Q9EPB4.

    Protocols and materials databases

    DNASUi 66824.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033056 ; ENSMUSP00000033056 ; ENSMUSG00000030793 .
    GeneIDi 66824.
    KEGGi mmu:66824.
    UCSCi uc009jxu.2. mouse.

    Organism-specific databases

    CTDi 29108.
    MGIi MGI:1931465. Pycard.

    Phylogenomic databases

    eggNOGi NOG39139.
    GeneTreei ENSGT00440000033973.
    HOGENOMi HOG000034090.
    HOVERGENi HBG018739.
    InParanoidi Q9EPB4.
    KOi K12799.
    OMAi PMDAVDL.
    OrthoDBi EOG786H4P.
    PhylomeDBi Q9EPB4.
    TreeFami TF337882.

    Enzyme and pathway databases

    Reactomei REACT_198662. The AIM2 inflammasome.

    Miscellaneous databases

    NextBioi 322743.
    PROi Q9EPB4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9EPB4.
    Bgeei Q9EPB4.
    CleanExi MM_PYCARD.
    Genevestigatori Q9EPB4.

    Family and domain databases

    Gene3Di 1.10.533.10. 2 hits.
    InterProi IPR001315. CARD.
    IPR004020. DAPIN.
    IPR011029. DEATH-like_dom.
    [Graphical view ]
    Pfami PF00619. CARD. 1 hit.
    PF02758. PYRIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 2 hits.
    PROSITEi PS50209. CARD. 1 hit.
    PS50824. DAPIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Murine ortholog of ASC, a CARD-containing protein, self-associates and exhibits restricted distribution in developing mouse embryos."
      Masumoto J., Taniguchi S., Nakayama K., Ayukawa K., Sagara J.
      Exp. Cell Res. 262:128-133(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Thymus.
    2. "Pycard a PYD and CARD containing molecule."
      Martinon F., Hofmann K., Tschopp J.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    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].
      Strain: C57BL/6J.
      Tissue: Pancreas and Tongue.
    4. "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].
    5. "ASC is essential for LPS-induced activation of procaspase-1 independently of TLR-associated signal adaptor molecules."
      Yamamoto M., Yaginuma K., Tsutsui H., Sagara J., Guan X., Seki E., Yasuda K., Yamamoto M., Akira S., Nakanishi K., Noda T., Taniguchi S.
      Genes Cells 9:1055-1067(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    6. "Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf."
      Mariathasan S., Newton K., Monack D.M., Vucic D., French D.M., Lee W.P., Roose-Girma M., Erickson S., Dixit V.M.
      Nature 430:213-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "The inflammasome adaptor ASC regulates the function of adaptive immune cells by controlling Dock2-mediated Rac activation and actin polymerization."
      Ippagunta S.K., Malireddi R.K., Shaw P.J., Neale G.A., Walle L.V., Green D.R., Fukui Y., Lamkanfi M., Kanneganti T.D.
      Nat. Immunol. 12:1010-1016(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages."
      Pierini R., Juruj C., Perret M., Jones C.L., Mangeot P., Weiss D.S., Henry T.
      Cell Death Differ. 19:1709-1721(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CASP8.

    Entry informationi

    Entry nameiASC_MOUSE
    AccessioniPrimary (citable) accession number: Q9EPB4
    Secondary accession number(s): Q9D2W9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 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