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Protein

Superoxide dismutase [Cu-Zn]

Gene

Sod1

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

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

Protein has several cofactor binding sites:
  • Cu cationBy similarityNote: Binds 1 copper ion per subunit.By similarity
  • Zn2+By similarityNote: 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. identical protein binding Source: MGI
  4. protein phosphatase 2B binding Source: UniProtKB
  5. Rac GTPase binding Source: MGI
  6. superoxide dismutase activity Source: MGI
  7. 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: MGI
  6. cellular iron ion homeostasis Source: MGI
  7. cellular response to ATP Source: Ensembl
  8. cellular response to cadmium ion Source: Ensembl
  9. cellular response to potassium ion Source: Ensembl
  10. embryo implantation Source: MGI
  11. glutathione metabolic process Source: MGI
  12. heart contraction Source: MGI
  13. hydrogen peroxide biosynthetic process Source: MGI
  14. locomotory behavior Source: MGI
  15. muscle cell cellular homeostasis Source: MGI
  16. myeloid cell homeostasis Source: MGI
  17. negative regulation of apoptotic process Source: MGI
  18. negative regulation of cholesterol biosynthetic process Source: UniProtKB
  19. negative regulation of neuron apoptotic process Source: MGI
  20. neurofilament cytoskeleton organization Source: MGI
  21. ovarian follicle development Source: MGI
  22. peripheral nervous system myelin maintenance Source: MGI
  23. positive regulation of catalytic activity Source: UniProtKB
  24. positive regulation of cytokine production Source: UniProtKB
  25. positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: MGI
  26. positive regulation of superoxide anion generation Source: MGI
  27. reactive oxygen species metabolic process Source: UniProtKB
  28. regulation of blood pressure Source: MGI
  29. regulation of mitochondrial membrane potential Source: UniProtKB
  30. regulation of multicellular organism growth Source: MGI
  31. regulation of protein kinase activity Source: UniProtKB
  32. regulation of Rac GTPase activity Source: MGI
  33. relaxation of vascular smooth muscle Source: MGI
  34. removal of superoxide radicals Source: MGI
  35. response to amphetamine Source: Ensembl
  36. response to antibiotic Source: Ensembl
  37. response to antipsychotic drug Source: Ensembl
  38. response to axon injury Source: MGI
  39. response to carbon monoxide Source: Ensembl
  40. response to copper ion Source: Ensembl
  41. response to drug Source: MGI
  42. response to ethanol Source: MGI
  43. response to heat Source: MGI
  44. response to hydrogen peroxide Source: MGI
  45. response to nutrient levels Source: Ensembl
  46. response to organic substance Source: UniProtKB
  47. response to oxidative stress Source: MGI
  48. response to reactive oxygen species Source: MGI
  49. response to superoxide Source: MGI
  50. retina homeostasis Source: MGI
  51. retrograde axon cargo transport Source: BHF-UCL
  52. sensory perception of sound Source: MGI
  53. spermatogenesis Source: MGI
  54. superoxide anion generation Source: MGI
  55. superoxide metabolic process Source: MGI
  56. transmission of nerve impulse Source: MGI
Complete GO annotation...

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. dense core granule Source: Ensembl
  6. extracellular matrix Source: UniProtKB
  7. extracellular space Source: UniProtKB
  8. extracellular vesicular exosome Source: MGI
  9. mitochondrial intermembrane space Source: Ensembl
  10. mitochondrion Source: UniProtKB
  11. myelin sheath Source: UniProtKB
  12. neuronal cell body Source: UniProtKB
  13. nucleoplasm Source: MGI
  14. nucleus Source: UniProtKB
  15. peroxisome Source: MGI
  16. plasma membrane Source: Ensembl
  17. protein complex Source: UniProtKB
Complete GO annotation...

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 – 11Removed1 Publication
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 – 108Combined sources
Beta strandi12 – 143Combined sources
Beta strandi16 – 2510Combined sources
Beta strandi30 – 389Combined sources
Beta strandi41 – 5010Combined sources
Turni55 – 584Combined sources
Helixi59 – 613Combined sources
Beta strandi84 – 907Combined sources
Beta strandi96 – 10914Combined sources
Beta strandi116 – 1238Combined sources
Beta strandi130 – 1323Combined sources
Helixi133 – 1386Combined sources
Beta strandi143 – 1497Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ
60 70 80 90 100
YGDNTQGCTS AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI
110 120 130 140 150
EDRVISLSGE HSIIGRTMVV HEKQDDLGKG GNEESTKTGN AGSRLACGVI

GIAQ
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP08228.

2D gel databases

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

Proteomic databases

MaxQBiP08228.
PaxDbiP08228.
PRIDEiP08228.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6647.
MGIiMGI:98351. Sod1.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiSod1. mouse.
EvolutionaryTraceiP08228.
NextBioi299081.
PROiP08228.
SOURCEiSearch...

Gene expression databases

BgeeiP08228.
CleanExiMM_SOD1.
GenevestigatoriP08228.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 170 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.