USC-OGP 2-DE database Two-dimensional polyacrylamide gel electrophoresis database

USC-OGP 2-DE database  Search by                Maps             Select Remote Interfaces [All Interfaces] SWISS-2DPAGE World-2DPAGE Portal World-2DPAGE Repository Exclude local DBs has only effect if a remote interface is selected

Searching in 'USC-OGP 2-DE database' for entry matching: P00441 USC-OGP 2-DE database:  P00441 P00441 General information about the entry View entry in simple text format Entry name SODC_HUMAN Primary accession number P00441 integrated into USC-OGP 2-DE database on  January 17, 2017 (release 1) 2D Annotations were last modified on January 17, 2017 (version 1) General Annotations were last modified on  April 5, 2017 (version 2) Name and origin of the protein Description RecName: Full=Superoxide dismutase [Cu-Zn]; EC=1.15.1.1; AltName: Full=Superoxide dismutase 1; Short=hSod1;. Gene name Name=SOD1 Annotated species Homo sapiens (Human) [TaxID: 9606] Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. References [1]   2D GEL CHARACTERIZATION Author 1., Author 2. Submitted (Mar-2011) to Current 2D PAGE maps for identified proteins How to interpret a protein PLATELET_4-7 {PLATELET 4-7} Homo sapiens (Human)   map experimental info   PLATELET_4-7 MAP LOCATIONS: SPOT OGP-0574: pI=5.55; Mw=18514 PLATELET_5-6 {PLATELET 5-6} Homo sapiens (Human)   map experimental info   PLATELET_5-6 MAP LOCATIONS: SPOT OGP-0843: pI=5.58; Mw=18282 UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10} Homo sapiens (Human)   map experimental info   UVEAL_MELANOMA_3-10 MAP LOCATIONS: SPOT OGP-1321: pI=5.74; Mw=19265 Cross-references UniProtKB/Swiss-Prot P00441; SODC_HUMAN. 2D PAGE maps for identified proteins How to interpret a protein map You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw. Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly. Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed. External data extracted from UniProtKB/Swiss-Prot Extracted from UniProtKB/Swiss-Prot, release: 0.0 Entry name SODC_HUMAN Primary accession number P00441 Secondary accession number(s) A6NHJ0 D3DSE4 Q16669 Q16711 Q16838 Q16839 Q16840 Q6NR85 Sequence was last modified on  January 23, 2007 (version 2) Annotations were last modified on  March 15, 2017 (version 221) Name and origin of the protein Description RecName: Full=Superoxide dismutase [Cu-Zn]; EC=1.15.1.1; AltName: Full=Superoxide dismutase 1; Short=hSod1; Gene name Name=SOD1 Encoded on Name=SOD1 Keywords 3D-structure; Acetylation; Amyotrophic lateral sclerosis; Antioxidant; Complete proteome; Copper; Cytoplasm; Direct protein sequencing; Disease mutation; Disulfide bond; Lipoprotein; Metal-binding; Mitochondrion; Neurodegeneration; Nucleus; Oxidoreductase; Palmitate; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL L44139; AAB05662.1; -; Genomic_DNA EMBL L44135; AAB05662.1; JOINED; Genomic_DNA EMBL L44136; AAB05662.1; JOINED; Genomic_DNA EMBL L44137; AAB05662.1; JOINED; Genomic_DNA EMBL L44139; AAB05661.1; -; Genomic_DNA EMBL L44135; AAB05661.1; JOINED; Genomic_DNA EMBL L44136; AAB05661.1; JOINED; Genomic_DNA EMBL L44137; AAB05661.1; JOINED; Genomic_DNA EMBL X02317; CAA26182.1; -; mRNA EMBL X01780; CAA25915.1; -; Genomic_DNA EMBL X01781; CAA25916.1; -; Genomic_DNA EMBL X01782; CAA25917.1; ALT_SEQ; Genomic_DNA EMBL X01783; CAA25918.1; -; Genomic_DNA EMBL X01784; CAA25919.1; ALT_SEQ; Genomic_DNA EMBL AY049787; AAL15444.1; -; mRNA EMBL AY450286; AAR21563.1; -; mRNA EMBL EF151142; ABL96616.1; -; mRNA EMBL AK312116; BAG35052.1; -; mRNA EMBL CR450355; CAG29351.1; -; mRNA EMBL CR541742; CAG46542.1; -; mRNA EMBL BT006676; AAP35322.1; -; mRNA EMBL AY835629; AAV80422.1; -; Genomic_DNA EMBL AP000253; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL CH471079; EAX09889.1; -; Genomic_DNA EMBL CH471079; EAX09890.1; -; Genomic_DNA EMBL BC001034; AAH01034.1; -; mRNA EMBL L46374; AAB59626.1; -; Genomic_DNA EMBL L46375; AAB59627.1; -; Genomic_DNA EMBL L44746; AAC41773.1; ALT_SEQ; Genomic_DNA EMBL X95228; CAA64520.1; -; Genomic_DNA CCDS CCDS33536.1; -; . PIR A22703; DSHUCZ; . RefSeq NP_000445.1; NM_000454.4; . UniGene Hs.443914; -; . PDB 1AZV; X-ray; 1.90 A; A/B=2-154 PDB 1BA9; NMR; -; A=2-154 PDB 1DSW; NMR; -; A=2-154 PDB 1FUN; X-ray; 2.85 A; A/B/C/D/E/F/G/H/I/J=2-154 PDB 1HL4; X-ray; 1.82 A; A/B/C/D=2-154 PDB 1HL5; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/S=2-154 PDB 1KMG; NMR; -; A=2-154 PDB 1L3N; NMR; -; A/B=2-154 PDB 1MFM; X-ray; 1.02 A; A=2-154 PDB 1N18; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J=1-154 PDB 1N19; X-ray; 1.86 A; A/B=1-154 PDB 1OEZ; X-ray; 2.15 A; W/X/Y/Z=2-154 PDB 1OZT; X-ray; 2.50 A; G/H/I/J/K/L/M/N=2-154 PDB 1OZU; X-ray; 1.30 A; A/B=2-154 PDB 1P1V; X-ray; 1.40 A; A/B/C=2-154 PDB 1PTZ; X-ray; 1.80 A; A/B=2-154 PDB 1PU0; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J=2-154 PDB 1RK7; NMR; -; A=2-154 PDB 1SOS; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=2-154 PDB 1SPD; X-ray; 2.40 A; A/B=2-154 PDB 1UXL; X-ray; 1.60 A; A/B/C/D/E/F/G/H/I/J=2-154 PDB 1UXM; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=2-154 PDB 2AF2; NMR; -; A/B=2-154 PDB 2C9S; X-ray; 1.24 A; A/F=2-154 PDB 2C9U; X-ray; 1.24 A; A/F=2-154 PDB 2C9V; X-ray; 1.07 A; A/F=2-154 PDB 2GBT; X-ray; 1.70 A; A/B/C/D=2-154 PDB 2GBU; X-ray; 2.00 A; A/B/C/D=2-154 PDB 2GBV; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J=2-154 PDB 2LU5; NMR; -; A=2-154 PDB 2MP3; NMR; -; A=2-126 PDB 2NAM; NMR; -; A=2-154 PDB 2NNX; X-ray; 2.30 A; A/B/C/D=2-154 PDB 2R27; X-ray; 2.00 A; A/B=1-154 PDB 2V0A; X-ray; 1.15 A; A/F=2-154 PDB 2VR6; X-ray; 1.30 A; A/F=2-154 PDB 2VR7; X-ray; 1.58 A; A/F=2-154 PDB 2VR8; X-ray; 1.36 A; A/F=2-154 PDB 2WKO; X-ray; 1.97 A; A/F=2-154 PDB 2WYT; X-ray; 1.00 A; A/F=2-154 PDB 2WYZ; X-ray; 1.70 A; A/F=2-154 PDB 2WZ0; X-ray; 1.72 A; A/F=2-154 PDB 2WZ5; X-ray; 1.50 A; A/F=2-154 PDB 2WZ6; X-ray; 1.55 A; A/F=2-154 PDB 2XJK; X-ray; 1.45 A; A=2-154 PDB 2XJL; X-ray; 1.55 A; A=2-154 PDB 2ZKW; X-ray; 1.90 A; A/B=1-154 PDB 2ZKX; X-ray; 2.72 A; A/B/C/D=1-154 PDB 2ZKY; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J=1-154 PDB 3CQP; X-ray; 1.95 A; A/B/C/D=2-154 PDB 3CQQ; X-ray; 1.90 A; A/B=2-154 PDB 3ECU; X-ray; 1.90 A; A/B/C/D=2-154 PDB 3ECV; X-ray; 1.90 A; A/B/C/D=2-154 PDB 3ECW; X-ray; 2.15 A; A/B/C/D=2-154 PDB 3GQF; X-ray; 2.20 A; A/B/C/D/E/F=2-154 PDB 3GTV; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=2-81 PDB 3GZO; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=2-154 PDB 3GZP; X-ray; 3.10 A; A/B/C/D=2-154 PDB 3GZQ; X-ray; 1.40 A; A/B=2-154 PDB 3H2P; X-ray; 1.55 A; A/B=2-154 PDB 3H2Q; X-ray; 1.85 A; A/B/C/D=2-154 PDB 3HFF; X-ray; 2.20 A; A=2-154 PDB 3K91; X-ray; 1.75 A; A/B=2-154 PDB 3KH3; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L=2-154 PDB 3KH4; X-ray; 3.50 A; A/B/C/D/E/F=2-154 PDB 3LTV; X-ray; 2.45 A; A/B/C/D/E/F=82-154 PDB 3QQD; X-ray; 1.65 A; A/B=2-154 PDB 3RE0; X-ray; 2.28 A; A/B/C/D=2-154 PDB 3T5W; X-ray; 1.80 A; A/B/D/E/F/G/H/I/J/K/L/M=2-154 PDB 4A7G; X-ray; 1.24 A; A/F=2-154 PDB 4A7Q; X-ray; 1.22 A; A/F=2-154 PDB 4A7S; X-ray; 1.06 A; A/F=2-154 PDB 4A7T; X-ray; 1.45 A; A/F=2-154 PDB 4A7U; X-ray; 0.98 A; A/F=2-154 PDB 4A7V; X-ray; 1.00 A; A/F=2-154 PDB 4B3E; X-ray; 2.15 A; A/B/C/D/E/F/G/H/I/J=1-154 PDB 4BCY; X-ray; 1.27 A; A=2-154 PDB 4BCZ; X-ray; 1.93 A; A/B=2-49 A/B=83-124 A/B=141-154; PDB; 4BD4; X-ray 2.78 A A/B/C/D/E/F/G/H/I=2-49; A/B/C/D/E/F/G/H/I=83-124; A/B/C/D/E/F/G/H/I=141-154; PDB 4FF9 X-ray; 2.50 A; A/B=2-154; PDB 4MCM X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=2-154; PDB 4MCN X-ray; 2.60 A; A/B=2-154; PDB 4NIN X-ray; 1.40 A; A=102-108; PDB 4NIO X-ray; 1.30 A; A=148-154; PDB 4NIP X-ray; 1.90 A; A=148-154; PDB 4OH2 X-ray; 2.38 A; A/B/C/D/E/F/G/H/I/J=2-154; PDB 4SOD Model; -; A=1-154; PDB 4XCR X-ray; 3.60 A; A/B=2-154; PDB 5DLI X-ray; 2.10 A; A/B/C/D/E/F/G/H=29-39; PDB 5J07 X-ray; 2.00 A; A/B=14-49; A/B=84-124 A/B=141-154 PDB; 5J0C; X-ray; 1.60 A A/B=29-49 A/B=84-124; PDB; 5J0F; X-ray 1.25 A A/B=83-124; PDB; 5J0G; X-ray 2.50 A A/B=2-124; PDB; 5K02; X-ray 1.99 A A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=2-154; PDBsum; 1AZV; - PDBsum 1BA9; -; . PDBsum 1DSW; -; . PDBsum 1FUN; -; . PDBsum 1HL4; -; . PDBsum 1HL5; -; . PDBsum 1KMG; -; . PDBsum 1L3N; -; . PDBsum 1MFM; -; . PDBsum 1N18; -; . PDBsum 1N19; -; . PDBsum 1OEZ; -; . PDBsum 1OZT; -; . PDBsum 1OZU; -; . PDBsum 1P1V; -; . PDBsum 1PTZ; -; . PDBsum 1PU0; -; . PDBsum 1RK7; -; . PDBsum 1SOS; -; . PDBsum 1SPD; -; . PDBsum 1UXL; -; . PDBsum 1UXM; -; . PDBsum 2AF2; -; . PDBsum 2C9S; -; . PDBsum 2C9U; -; . PDBsum 2C9V; -; . PDBsum 2GBT; -; . PDBsum 2GBU; -; . PDBsum 2GBV; -; . PDBsum 2LU5; -; . PDBsum 2MP3; -; . PDBsum 2NAM; -; . PDBsum 2NNX; -; . PDBsum 2R27; -; . PDBsum 2V0A; -; . PDBsum 2VR6; -; . PDBsum 2VR7; -; . PDBsum 2VR8; -; . PDBsum 2WKO; -; . PDBsum 2WYT; -; . PDBsum 2WYZ; -; . PDBsum 2WZ0; -; . PDBsum 2WZ5; -; . PDBsum 2WZ6; -; . PDBsum 2XJK; -; . PDBsum 2XJL; -; . PDBsum 2ZKW; -; . PDBsum 2ZKX; -; . PDBsum 2ZKY; -; . PDBsum 3CQP; -; . PDBsum 3CQQ; -; . PDBsum 3ECU; -; . PDBsum 3ECV; -; . PDBsum 3ECW; -; . PDBsum 3GQF; -; . PDBsum 3GTV; -; . PDBsum 3GZO; -; . PDBsum 3GZP; -; . PDBsum 3GZQ; -; . PDBsum 3H2P; -; . PDBsum 3H2Q; -; . PDBsum 3HFF; -; . PDBsum 3K91; -; . PDBsum 3KH3; -; . PDBsum 3KH4; -; . PDBsum 3LTV; -; . PDBsum 3QQD; -; . PDBsum 3RE0; -; . PDBsum 3T5W; -; . PDBsum 4A7G; -; . PDBsum 4A7Q; -; . PDBsum 4A7S; -; . PDBsum 4A7T; -; . PDBsum 4A7U; -; . PDBsum 4A7V; -; . PDBsum 4B3E; -; . PDBsum 4BCY; -; . PDBsum 4BCZ; -; . PDBsum 4BD4; -; . PDBsum 4FF9; -; . PDBsum 4MCM; -; . PDBsum 4MCN; -; . PDBsum 4NIN; -; . PDBsum 4NIO; -; . PDBsum 4NIP; -; . PDBsum 4OH2; -; . PDBsum 4SOD; -; . PDBsum 4XCR; -; . PDBsum 5DLI; -; . PDBsum 5J07; -; . PDBsum 5J0C; -; . PDBsum 5J0F; -; . PDBsum 5J0G; -; . PDBsum 5K02; -; . DisProt DP00652; -; . ProteinModelPortal P00441; -; . SMR P00441; -; . BioGrid 112530; 162; . DIP DIP-44941N; -; . IntAct P00441; 29; . MINT MINT-204523; -; . STRING 9606.ENSP00000270142; -; . BindingDB P00441; -; . ChEMBL CHEMBL2354; -; . DrugBank DB05025; Arimoclomol; . DrugBank DB00958; Carboplatin; . DrugBank DB00515; Cisplatin; . DrugBank DB00526; Oxaliplatin; . DrugBank DB03382; S-Oxy Cysteine; . DrugBank DB00163; Vitamin E; . iPTMnet P00441; -; . PhosphoSitePlus P00441; -; . SwissPalm P00441; -; . BioMuta SOD1; -; . DOSAC-COBS-2DPAGE P00441; -; . OGP P00441; -; . REPRODUCTION-2DPAGE IPI00783680; -; . SWISS-2DPAGE P00441; -; . UCD-2DPAGE P00441; -; . EPD P00441; -; . PaxDb P00441; -; . PeptideAtlas P00441; -; . PRIDE P00441; -; . TopDownProteomics P00441; -; . DNASU 6647; -; . Ensembl ENST00000270142; ENSP00000270142; ENSG00000142168; . GeneID 6647; -; . KEGG hsa:6647; -; . CTD 6647; -; . DisGeNET 6647; -; . GeneCards SOD1; -; . GeneReviews SOD1; -; . HGNC HGNC:11179; SOD1; . HPA CAB008670; -; . HPA HPA001401; -; . MalaCards SOD1; -; . MIM 105400; phenotype; . MIM 147450; gene; . neXtProt NX_P00441; -; . OpenTargets ENSG00000142168; -; . Orphanet 803; Amyotrophic lateral sclerosis; . PharmGKB PA334; -; . eggNOG KOG0441; Eukaryota; . eggNOG COG2032; LUCA; . GeneTree ENSGT00530000063226; -; . HOVERGEN HBG000062; -; . InParanoid P00441; -; . KO K04565; -; . OMA VCVLKGT; -; . OrthoDB EOG091G0OG2; -; . PhylomeDB P00441; -; . TreeFam TF105131; -; . BioCyc MetaCyc:HS06899-MONOMER; -; . BRENDA 1.15.1.1; 2681; . Reactome R-HSA-114608; Platelet degranulation; . Reactome R-HSA-3299685; Detoxification of Reactive Oxygen Species; . ChiTaRS SOD1; human; . EvolutionaryTrace P00441; -; . GeneWiki SOD1; -; . GenomeRNAi 6647; -; . PRO PR:P00441; -; . Proteomes UP000005640; Chromosome 21; . Bgee ENSG00000142168; -; . CleanEx HS_SOD1; -; . ExpressionAtlas P00441; baseline and differential; . Genevisible P00441; HS; . GO GO:1904115; C:axon cytoplasm; IEA:GOC; . GO GO:0005737; C:cytoplasm; IDA:UniProtKB; . GO GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB; . GO GO:0005829; C:cytosol; IDA:UniProtKB; . GO GO:0032839; C:dendrite cytoplasm; IDA:UniProtKB; . GO GO:0031045; C:dense core granule; IEA:Ensembl; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0031012; C:extracellular matrix; IDA:UniProtKB; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:0005615; C:extracellular space; IDA:UniProtKB; . GO GO:0005764; C:lysosome; IEA:Ensembl; . GO GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome; . GO GO:0005759; C:mitochondrial matrix; NAS:UniProtKB; . GO GO:0005739; C:mitochondrion; IDA:UniProtKB; . GO GO:0043209; C:myelin sheath; IEA:Ensembl; . GO GO:0043025; C:neuronal cell body; IDA:UniProtKB; . GO GO:0005654; C:nucleoplasm; IDA:HPA; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0005777; C:peroxisome; IDA:UniProtKB; . GO GO:0043234; C:protein complex; IDA:UniProtKB; . GO GO:0051087; F:chaperone binding; IPI:UniProtKB; . GO GO:0005507; F:copper ion binding; IDA:UniProtKB; . GO GO:0042802; F:identical protein binding; IPI:IntAct; . GO GO:0042803; F:protein homodimerization activity; NAS:UniProtKB; . GO GO:0030346; F:protein phosphatase 2B binding; IDA:UniProtKB; . GO GO:0048365; F:Rac GTPase binding; IDA:UniProtKB; . GO GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB; . GO GO:0008270; F:zinc ion binding; IDA:UniProtKB; . GO GO:0000187; P:activation of MAPK activity; ISS:UniProtKB; . GO GO:0008089; P:anterograde axonal transport; ISS:BHF-UCL; . GO GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB; . GO GO:0007569; P:cell aging; IMP:UniProtKB; . GO GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB; . GO GO:0071318; P:cellular response to ATP; IEA:Ensembl; . GO GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl; . GO GO:0035865; P:cellular response to potassium ion; IEA:Ensembl; . GO GO:0007566; P:embryo implantation; ISS:UniProtKB; . GO GO:0006749; P:glutathione metabolic process; ISS:UniProtKB; . GO GO:0060047; P:heart contraction; IDA:UniProtKB; . GO GO:0050665; P:hydrogen peroxide biosynthetic process; IDA:UniProtKB; . GO GO:0007626; P:locomotory behavior; ISS:UniProtKB; . GO GO:0046716; P:muscle cell cellular homeostasis; ISS:UniProtKB; . GO GO:0002262; P:myeloid cell homeostasis; ISS:UniProtKB; . GO GO:0045541; P:negative regulation of cholesterol biosynthetic process; IDA:UniProtKB; . GO GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB; . GO GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB; . GO GO:0001541; P:ovarian follicle development; ISS:UniProtKB; . GO GO:0032287; P:peripheral nervous system myelin maintenance; ISS:UniProtKB; . GO GO:0001890; P:placenta development; NAS:UniProtKB; . GO GO:0002576; P:platelet degranulation; TAS:Reactome; . GO GO:0043065; P:positive regulation of apoptotic process; IC:UniProtKB; . GO GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB; . GO GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB; . GO GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL; . GO GO:0032930; P:positive regulation of superoxide anion generation; IDA:UniProtKB; . GO GO:0072593; P:reactive oxygen species metabolic process; IDA:UniProtKB; . GO GO:0008217; P:regulation of blood pressure; ISS:UniProtKB; . GO GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB; . GO GO:0051881; P:regulation of mitochondrial membrane potential; IMP:UniProtKB; . GO GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB; . GO GO:0046620; P:regulation of organ growth; NAS:UniProtKB; . GO GO:0045859; P:regulation of protein kinase activity; IDA:UniProtKB; . GO GO:0033081; P:regulation of T cell differentiation in thymus; NAS:UniProtKB; . GO GO:0060087; P:relaxation of vascular smooth muscle; ISS:UniProtKB; . GO GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB; . GO GO:0001975; P:response to amphetamine; IEA:Ensembl; . GO GO:0046677; P:response to antibiotic; IEA:Ensembl; . GO GO:0097332; P:response to antipsychotic drug; IEA:Ensembl; . GO GO:0048678; P:response to axon injury; ISS:UniProtKB; . GO GO:0034465; P:response to carbon monoxide; IEA:Ensembl; . GO GO:0046688; P:response to copper ion; IEA:Ensembl; . GO GO:0042493; P:response to drug; ISS:UniProtKB; . GO GO:0045471; P:response to ethanol; ISS:UniProtKB; . GO GO:0009408; P:response to heat; ISS:UniProtKB; . GO GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB; . GO GO:0031667; P:response to nutrient levels; IEA:Ensembl; . GO GO:0010033; P:response to organic substance; IDA:UniProtKB; . GO GO:0000302; P:response to reactive oxygen species; TAS:Reactome; . GO GO:0000303; P:response to superoxide; IDA:UniProtKB; . GO GO:0001895; P:retina homeostasis; ISS:UniProtKB; . GO GO:0008090; P:retrograde axonal transport; ISS:BHF-UCL; . GO GO:0007605; P:sensory perception of sound; ISS:UniProtKB; . GO GO:0007283; P:spermatogenesis; ISS:UniProtKB; . GO GO:0042554; P:superoxide anion generation; IEA:Ensembl; . GO GO:0006801; P:superoxide metabolic process; ISS:UniProtKB; . GO GO:0048538; P:thymus development; NAS:UniProtKB; . GO GO:0019226; P:transmission of nerve impulse; ISS:UniProtKB; . CDD cd00305; Cu-Zn_Superoxide_Dismutase; 1; . Gene3D 2.60.40.200; -; 1; . InterPro IPR018152; SOD_Cu/Zn_BS; . InterPro IPR001424; SOD_Cu_Zn_dom; . Pfam PF00080; Sod_Cu; 1; . PRINTS PR00068; CUZNDISMTASE; . SUPFAM SSF49329; SSF49329; 1; . PROSITE PS00087; SOD_CU_ZN_1; 1; . PROSITE PS00332; SOD_CU_ZN_2; 1; .

Gateways to other related servers

• The World-2DPAGE Constellation - Entry point to the world-wide 2-DPAGE resources.
• World-2DPAGE Repository - A public repository for gel-based proteomics data linked to protein identification published in the literature.
• World-2DPAGE Portal - A dynamic portal to query simultaneously world-wide gel-based proteomics databases.
• SWISS-2DPAGE - The Geneva Two-dimensional polyacrylamide gel electrophoresis database.
• ExPASy - The resources web server of the Swiss Institute of Bioinformatics

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