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P08228

- SODC_MOUSE

UniProt

P08228 - SODC_MOUSE

Protein

Superoxide dismutase [Cu-Zn]

Gene

Sod1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

    Catalytic activityi

    2 superoxide + 2 H+ = O2 + H2O2.

    Cofactori

    Binds 1 copper ion per subunit.By similarity
    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi47 – 471Copper; catalyticBy similarity
    Metal bindingi49 – 491Copper; catalyticBy similarity
    Metal bindingi64 – 641Copper; catalyticBy similarity
    Metal bindingi64 – 641Zinc; via pros nitrogen1 Publication
    Metal bindingi72 – 721Zinc; via pros nitrogen1 Publication
    Metal bindingi81 – 811Zinc; via pros nitrogen1 Publication
    Metal bindingi84 – 841Zinc; structural1 Publication
    Metal bindingi121 – 1211Copper; catalyticBy similarity

    GO - Molecular functioni

    1. chaperone binding Source: UniProtKB
    2. copper ion binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein phosphatase 2B binding Source: UniProtKB
    5. superoxide dismutase activity Source: MGI
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. activation of MAPK activity Source: MGI
    2. aging Source: MGI
    3. anterograde axon cargo transport Source: BHF-UCL
    4. auditory receptor cell stereocilium organization Source: MGI
    5. cell aging Source: Ensembl
    6. cellular iron ion homeostasis Source: MGI
    7. embryo implantation Source: MGI
    8. glutathione metabolic process Source: MGI
    9. heart contraction Source: MGI
    10. hydrogen peroxide biosynthetic process Source: MGI
    11. locomotory behavior Source: MGI
    12. muscle cell cellular homeostasis Source: MGI
    13. myeloid cell homeostasis Source: MGI
    14. negative regulation of apoptotic process Source: MGI
    15. negative regulation of cholesterol biosynthetic process Source: UniProtKB
    16. negative regulation of neuron apoptotic process Source: MGI
    17. neurofilament cytoskeleton organization Source: MGI
    18. ovarian follicle development Source: MGI
    19. peripheral nervous system myelin maintenance Source: MGI
    20. positive regulation of catalytic activity Source: UniProtKB
    21. positive regulation of cytokine production Source: UniProtKB
    22. positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
    23. positive regulation of superoxide anion generation Source: Ensembl
    24. reactive oxygen species metabolic process Source: UniProtKB
    25. regulation of blood pressure Source: MGI
    26. regulation of mitochondrial membrane potential Source: UniProtKB
    27. regulation of multicellular organism growth Source: MGI
    28. regulation of protein kinase activity Source: UniProtKB
    29. regulation of Rac GTPase activity Source: Ensembl
    30. relaxation of vascular smooth muscle Source: MGI
    31. removal of superoxide radicals Source: MGI
    32. response to amphetamine Source: Ensembl
    33. response to axon injury Source: MGI
    34. response to copper ion Source: Ensembl
    35. response to drug Source: MGI
    36. response to ethanol Source: MGI
    37. response to heat Source: MGI
    38. response to hydrogen peroxide Source: MGI
    39. response to nutrient levels Source: Ensembl
    40. response to organic substance Source: UniProtKB
    41. response to oxidative stress Source: MGI
    42. response to reactive oxygen species Source: MGI
    43. response to superoxide Source: MGI
    44. retina homeostasis Source: MGI
    45. retrograde axon cargo transport Source: BHF-UCL
    46. sensory perception of sound Source: MGI
    47. spermatogenesis Source: MGI
    48. superoxide anion generation Source: MGI
    49. superoxide metabolic process Source: MGI
    50. transmission of nerve impulse Source: MGI

    Keywords - Molecular functioni

    Antioxidant, Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Superoxide dismutase [Cu-Zn] (EC:1.15.1.1)
    Gene namesi
    Name:Sod1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:98351. Sod1.

    Subcellular locationi

    Cytoplasm. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic vesicle Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. dendrite cytoplasm Source: UniProtKB
    5. extracellular matrix Source: UniProtKB
    6. extracellular space Source: UniProtKB
    7. mitochondrion Source: UniProtKB
    8. neuronal cell body Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. peroxisome Source: Ensembl
    11. plasma membrane Source: Ensembl
    12. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    40% reduction in hepatic GPX1 activity.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 154153Superoxide dismutase [Cu-Zn]PRO_0000164062Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei4 – 41N6-succinyllysine1 Publication
    Lipidationi7 – 71S-palmitoyl cysteineBy similarity
    Modified residuei10 – 101N6-succinyllysine1 Publication
    Disulfide bondi58 ↔ 147By similarity
    Modified residuei92 – 921N6-succinyllysine1 Publication
    Modified residuei99 – 991PhosphoserineBy similarity
    Modified residuei123 – 1231N6-acetyllysine; alternate1 Publication
    Modified residuei123 – 1231N6-succinyllysine; alternate1 Publication
    Modified residuei137 – 1371N6-acetyllysine; alternate1 Publication
    Modified residuei137 – 1371N6-succinyllysine; alternate1 Publication

    Post-translational modificationi

    Palmitoylation helps nuclear targeting and decreases catalytic activity.By similarity
    Succinylation, adjacent to copper catalytic site probably inhibit activity. Desuccinylated by SIRT5, enhancing activity By similarity.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP08228.
    PaxDbiP08228.
    PRIDEiP08228.

    2D gel databases

    DOSAC-COBS-2DPAGEP08228.
    REPRODUCTION-2DPAGEIPI00130589.
    P08228.
    SWISS-2DPAGEP08228.
    UCD-2DPAGEP08228.

    PTM databases

    PhosphoSiteiP08228.

    Expressioni

    Gene expression databases

    BgeeiP08228.
    CleanExiMM_SOD1.
    GenevestigatoriP08228.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Rac1P630014EBI-1635090,EBI-413646

    Protein-protein interaction databases

    BioGridi203387. 9 interactions.
    DIPiDIP-48691N.
    IntActiP08228. 11 interactions.
    MINTiMINT-1869618.
    STRINGi10090.ENSMUSP00000023707.

    Structurei

    Secondary structure

    1
    154
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 108
    Beta strandi12 – 143
    Beta strandi16 – 2510
    Beta strandi30 – 389
    Beta strandi41 – 5010
    Turni55 – 584
    Helixi59 – 613
    Beta strandi77 – 793
    Beta strandi84 – 907
    Beta strandi96 – 10914
    Beta strandi116 – 1238
    Beta strandi130 – 1323
    Helixi133 – 1386
    Beta strandi143 – 1497

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GTTX-ray2.40A/B/C/D/E/F2-154[»]
    3GTVX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L82-154[»]
    3LTVX-ray2.45A/B/C/D/E/F2-154[»]
    ProteinModelPortaliP08228.
    SMRiP08228. Positions 2-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08228.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Cu-Zn superoxide dismutase family.Curated

    Phylogenomic databases

    eggNOGiCOG2032.
    GeneTreeiENSGT00530000063226.
    HOGENOMiHOG000263447.
    HOVERGENiHBG000062.
    InParanoidiP08228.
    KOiK04565.
    OMAiNDPNAKR.
    OrthoDBiEOG776SR4.
    PhylomeDBiP08228.
    TreeFamiTF105131.

    Family and domain databases

    Gene3Di2.60.40.200. 1 hit.
    InterProiIPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view]
    PfamiPF00080. Sod_Cu. 1 hit.
    [Graphical view]
    PRINTSiPR00068. CUZNDISMTASE.
    SUPFAMiSSF49329. SSF49329. 1 hit.
    PROSITEiPS00087. SOD_CU_ZN_1. 1 hit.
    PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08228-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ    50
    YGDNTQGCTS AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI 100
    EDRVISLSGE HSIIGRTMVV HEKQDDLGKG GNEESTKTGN AGSRLACGVI 150
    GIAQ 154
    Length:154
    Mass (Da):15,943
    Last modified:January 23, 2007 - v2
    Checksum:iCAE548C66043BAC4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021D → H in AAA40121. (PubMed:2022332)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06683 mRNA. Translation: CAA29880.1.
    M60798
    , M60794, M60795, M60796, M60797 Genomic DNA. Translation: AAA40121.1.
    M35725 mRNA. Translation: AAA37518.1.
    AK020624 mRNA. Translation: BAB32154.1.
    AK077284 mRNA. Translation: BAC36730.1.
    BC002066 mRNA. Translation: AAH02066.1.
    BC048874 mRNA. Translation: AAH48874.1.
    BC086886 mRNA. Translation: AAH86886.1.
    CCDSiCCDS37395.1.
    PIRiJQ0915.
    RefSeqiNP_035564.1. NM_011434.1.
    UniGeneiMm.276325.
    Mm.466779.

    Genome annotation databases

    EnsembliENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982.
    GeneIDi20655.
    KEGGimmu:20655.
    UCSCiuc007zvz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06683 mRNA. Translation: CAA29880.1 .
    M60798
    , M60794 , M60795 , M60796 , M60797 Genomic DNA. Translation: AAA40121.1 .
    M35725 mRNA. Translation: AAA37518.1 .
    AK020624 mRNA. Translation: BAB32154.1 .
    AK077284 mRNA. Translation: BAC36730.1 .
    BC002066 mRNA. Translation: AAH02066.1 .
    BC048874 mRNA. Translation: AAH48874.1 .
    BC086886 mRNA. Translation: AAH86886.1 .
    CCDSi CCDS37395.1.
    PIRi JQ0915.
    RefSeqi NP_035564.1. NM_011434.1.
    UniGenei Mm.276325.
    Mm.466779.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GTT X-ray 2.40 A/B/C/D/E/F 2-154 [» ]
    3GTV X-ray 2.20 A/B/C/D/E/F/G/H/I/J/K/L 82-154 [» ]
    3LTV X-ray 2.45 A/B/C/D/E/F 2-154 [» ]
    ProteinModelPortali P08228.
    SMRi P08228. Positions 2-154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203387. 9 interactions.
    DIPi DIP-48691N.
    IntActi P08228. 11 interactions.
    MINTi MINT-1869618.
    STRINGi 10090.ENSMUSP00000023707.

    PTM databases

    PhosphoSitei P08228.

    2D gel databases

    DOSAC-COBS-2DPAGE P08228.
    REPRODUCTION-2DPAGE IPI00130589.
    P08228.
    SWISS-2DPAGE P08228.
    UCD-2DPAGE P08228.

    Proteomic databases

    MaxQBi P08228.
    PaxDbi P08228.
    PRIDEi P08228.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023707 ; ENSMUSP00000023707 ; ENSMUSG00000022982 .
    GeneIDi 20655.
    KEGGi mmu:20655.
    UCSCi uc007zvz.1. mouse.

    Organism-specific databases

    CTDi 6647.
    MGIi MGI:98351. Sod1.

    Phylogenomic databases

    eggNOGi COG2032.
    GeneTreei ENSGT00530000063226.
    HOGENOMi HOG000263447.
    HOVERGENi HBG000062.
    InParanoidi P08228.
    KOi K04565.
    OMAi NDPNAKR.
    OrthoDBi EOG776SR4.
    PhylomeDBi P08228.
    TreeFami TF105131.

    Enzyme and pathway databases

    Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi SOD1. mouse.
    EvolutionaryTracei P08228.
    NextBioi 299081.
    PROi P08228.
    SOURCEi Search...

    Gene expression databases

    Bgeei P08228.
    CleanExi MM_SOD1.
    Genevestigatori P08228.

    Family and domain databases

    Gene3Di 2.60.40.200. 1 hit.
    InterProi IPR018152. SOD_Cu/Zn_BS.
    IPR001424. SOD_Cu_Zn_dom.
    [Graphical view ]
    Pfami PF00080. Sod_Cu. 1 hit.
    [Graphical view ]
    PRINTSi PR00068. CUZNDISMTASE.
    SUPFAMi SSF49329. SSF49329. 1 hit.
    PROSITEi PS00087. SOD_CU_ZN_1. 1 hit.
    PS00332. SOD_CU_ZN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA and deduced amino acid sequence of murine Cu-Zn superoxide dismutase."
      Bewley G.C.
      Nucleic Acids Res. 16:2728-2728(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: SWR/J.
      Tissue: Liver.
    2. "Isolation and analysis of the mouse genomic sequence encoding Cu(2+)-Zn2+ superoxide dismutase."
      Benedetto M.T., Anzai Y., Gordon J.W.
      Gene 99:191-195(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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: Ovary, Urinary bladder and Uterus.
    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].
      Strain: C57BL/6J.
      Tissue: Liver, Mammary gland and Retina.
    5. "Purification of an inhibitor of erythroid progenitor cell cycling and antagonist to interleukin 3 from mouse marrow cell supernatants and its identification as cytosolic superoxide dismutase."
      Pluthero F.G., Shreeve M., Eskinazi D., van der Gaag H., Huang K.S., Hulmes J.D., Blum M., Axelrad A.A.
      J. Cell Biol. 111:1217-1223(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 4-23.
    6. Lubec G., Klug S., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 11-24 AND 104-116, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    7. "Knockout of SOD1 promotes conversion of selenocysteine to dehydroalanine in murine hepatic GPX1 protein."
      Wang S.K., Weaver J.D., Zhang S., Lei X.G.
      Free Radic. Biol. Med. 51:197-204(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
      Tissue: Liver.
    8. "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 ALA-2 AND LYS-123, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-10; LYS-92; LYS-123 AND LYS-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    9. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-154 IN COMPLEX WITH ZINC.

    Entry informationi

    Entry nameiSODC_MOUSE
    AccessioniPrimary (citable) accession number: P08228
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 165 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3