UniProt Accession

 SODC_HUMAN; P00441; A6NHJ0; D3DSE4; Q16669; Q16711; Q16838; Q16839; Q16840; Q6NR85 

Genbank Protein ID

 L44139; L44135; L44136; L44137; L44139; L44135; L44136; L44137; X02317; X01780; X01781; X01782; X01783; X01784; AY049787; AY450286; EF151142; AK312116; CR450355; CR541742; BT006676; AY835629; AP000253; CH471079; CH471079; BC001034; L46374; L46375; L44746; X95228 

Genbank Nucleotide ID

 AAB05662.1; AAB05662.1; AAB05662.1; AAB05662.1; AAB05661.1; AAB05661.1; AAB05661.1; AAB05661.1; CAA26182.1; CAA25915.1; CAA25916.1; CAA25917.1; CAA25918.1; CAA25919.1; AAL15444.1; AAR21563.1; ABL96616.1; BAG35052.1; CAG29351.1; CAG46542.1; AAP35322.1; AAV80422.1; EAX09889.1; EAX09890.1; AAH01034.1; AAB59626.1; AAB59627.1; AAC41773.1; CAA64520.1 

Protein Name

 Superoxide dismutase [Cu-Zn] 

Protein Synonyms/Alias

 Superoxide dismutase 1; hSod1 

Gene Name

 SOD1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
4	****MATKAVCVLKG	glycation	[1]
4	****MATKAVCVLKG	ubiquitination	[2]
10	TKAVCVLKGDGPVQG	acetylation	[3]
10	TKAVCVLKGDGPVQG	glycation	[1]
10	TKAVCVLKGDGPVQG	ubiquitination	[4, 5]
24	GIINFEQKESNGPVK	acetylation	[3]
24	GIINFEQKESNGPVK	ubiquitination	[2]
31	KESNGPVKVWGSIKG	glycation	[1]
31	KESNGPVKVWGSIKG	ubiquitination	[2, 4, 5]
37	VKVWGSIKGLTEGLH	glycation	[1]
76	SRKHGGPKDEERHVG	sumoylation	[6]
123	RTLVVHEKADDLGKG	acetylation	[7, 8]
123	RTLVVHEKADDLGKG	glycation	[1]
123	RTLVVHEKADDLGKG	ubiquitination	[4, 5]
129	EKADDLGKGGNEEST	glycation	[1]
137	GGNEESTKTGNAGSR	ubiquitination	[9]

Reference

 [1] Glycation and inactivation of human Cu-Zn-superoxide dismutase. Identification of the in vitro glycated sites.
 Arai K, Maguchi S, Fujii S, Ishibashi H, Oikawa K, Taniguchi N.
 J Biol Chem. 1987 Dec 15;262(35):16969-72. [PMID: 3680284]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] SUMO-1 modification increases human SOD1 stability and aggregation.
 Fei E, Jia N, Yan M, Ying Z, Sun Q, Wang H, Zhang T, Ma X, Ding H, Yao X, Shi Y, Wang G.
 Biochem Biophys Res Commun. 2006 Aug 25;347(2):406-12. [PMID: 16828461]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [9] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 

Functional Description

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

Sequence Annotation

 METAL 47 47 Copper; catalytic.
 METAL 49 49 Copper; catalytic.
 METAL 64 64 Copper; catalytic.
 METAL 64 64 Zinc; via pros nitrogen.
 METAL 72 72 Zinc; via pros nitrogen.
 METAL 81 81 Zinc; via pros nitrogen.
 METAL 84 84 Zinc; structural.
 METAL 121 121 Copper; catalytic.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 71 71 N6-acetyllysine (By similarity).
 MOD_RES 99 99 Phosphoserine.
 MOD_RES 123 123 N6-acetyllysine.
 DISULFID 58 147
 CROSSLNK 33 33 1-(tryptophan-3-yl)-tryptophan (Trp-Trp)  

Keyword

 3D-structure; Acetylation; Amyotrophic lateral sclerosis; Antioxidant; Complete proteome; Copper; Cytoplasm; Direct protein sequencing; Disease mutation; Disulfide bond; Metal-binding; Neurodegeneration; Oxidoreductase; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 154 AA 

Protein Sequence

Gene Ontology

 GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0032839; C:dendrite cytoplasm; IDA:UniProtKB.
 GO:0031012; C:extracellular matrix; IDA:UniProtKB.
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0005759; C:mitochondrial matrix; NAS:UniProtKB.
 GO:0043025; C:neuronal cell body; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005777; C:peroxisome; IDA:UniProtKB.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0005507; F:copper ion binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; NAS:UniProtKB.
 GO:0030346; F:protein phosphatase 2B binding; IDA:UniProtKB.
 GO:0048365; F:Rac GTPase binding; IDA:UniProtKB.
 GO:0004784; F:superoxide dismutase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0000187; P:activation of MAPK activity; ISS:UniProtKB.
 GO:0008089; P:anterograde axon cargo transport; ISS:BHF-UCL.
 GO:0006309; P:apoptotic DNA fragmentation; ISS:UniProtKB.
 GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
 GO:0007569; P:cell aging; IMP:UniProtKB.
 GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
 GO:0006302; P:double-strand break repair; ISS:UniProtKB.
 GO:0007566; P:embryo implantation; ISS:UniProtKB.
 GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
 GO:0060047; P:heart contraction; IDA:UniProtKB.
 GO:0050665; P:hydrogen peroxide biosynthetic process; IDA:UniProtKB.
 GO:0007626; P:locomotory behavior; ISS:UniProtKB.
 GO:0046716; P:muscle cell homeostasis; ISS:UniProtKB.
 GO:0002262; P:myeloid cell homeostasis; ISS:UniProtKB.
 GO:0045541; P:negative regulation of cholesterol biosynthetic process; IDA:UniProtKB.
 GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
 GO:0060052; P:neurofilament cytoskeleton organization; ISS:UniProtKB.
 GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
 GO:0032287; P:peripheral nervous system myelin maintenance; ISS:UniProtKB.
 GO:0001890; P:placenta development; NAS:UniProtKB.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0043065; P:positive regulation of apoptotic process; IC:UniProtKB.
 GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
 GO:0032930; P:positive regulation of superoxide anion generation; IDA:UniProtKB.
 GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
 GO:0051881; P:regulation of mitochondrial membrane potential; IMP:UniProtKB.
 GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
 GO:0046620; P:regulation of organ growth; NAS:UniProtKB.
 GO:0032314; P:regulation of Rac GTPase activity; IDA:UniProtKB.
 GO:0033081; P:regulation of T cell differentiation in thymus; NAS:UniProtKB.
 GO:0060087; P:relaxation of vascular smooth muscle; ISS:UniProtKB.
 GO:0019430; P:removal of superoxide radicals; ISS:UniProtKB.
 GO:0001975; P:response to amphetamine; IEA:Compara.
 GO:0048678; P:response to axon injury; ISS:UniProtKB.
 GO:0046688; P:response to copper ion; IEA:Compara.
 GO:0042493; P:response to drug; ISS:UniProtKB.
 GO:0045471; P:response to ethanol; ISS:UniProtKB.
 GO:0009408; P:response to heat; ISS:UniProtKB.
 GO:0042542; P:response to hydrogen peroxide; ISS:UniProtKB.
 GO:0031667; P:response to nutrient levels; IEA:Compara.
 GO:0001895; P:retina homeostasis; ISS:UniProtKB.
 GO:0008090; P:retrograde axon cargo transport; ISS:BHF-UCL.
 GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
 GO:0007283; P:spermatogenesis; ISS:UniProtKB.
 GO:0042554; P:superoxide anion generation; IEA:Compara.
 GO:0048538; P:thymus development; NAS:UniProtKB. 

Interpro

 IPR024134; SOD_Cu/Zn_/chaperones.
 IPR018152; SOD_Cu/Zn_BS.
 IPR001424; SOD_Cu_Zn_dom. 

Pfam

 PF00080; Sod_Cu 

SMART

  

PROSITE

 PS00087; SOD_CU_ZN_1
 PS00332; SOD_CU_ZN_2 

PRINTS

 PR00068; CUZNDISMTASE.