Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Superoxide dismutase [Cu-Zn]  

UniProtKB / Swiss-Prot ID :  SODC_HUMAN

Gene Name (Synonyms) : 
SOD1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Note=The pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria. 

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

Protein Sequence MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSR...
Predicted Secondary Structure CCEEEEEEECCCCCEEEEEEEEEECCCCCEEEEEEEECCCCCCCEEEEEECCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
5A -> S (in ALS1). VAR_013518
5A -> T (in ALS1). VAR_007130
5A -> V (in ALS1; severe form; reducesstructural stability and enzyme activity;
7C -> F (in ALS1). VAR_008717
8V -> E (in ALS1). VAR_007132
9L -> Q (in ALS1). VAR_013519
9L -> V (in ALS1). VAR_013520
13G -> R (in ALS1). VAR_013521
15V -> G (in ALS1). VAR_013522
15V -> M (in ALS1). VAR_007133
17G -> S (in ALS1; sporadic young onset). VAR_007134
21F -> C (in ALS1). VAR_045876
22E -> G (in ALS1). VAR_013523
22E -> K (in ALS1). VAR_007135
23Q -> L (in ALS1). VAR_045877
38G -> R (in ALS1; mild form; ubiquitinatedby RNF19A. Ubiquitinated by MARCH5;
39L -> R (in ALS1). VAR_013524
39L -> V (in ALS1). VAR_007137
42G -> D (in ALS1). VAR_007139
42G -> S (in ALS1). VAR_007138
44H -> R (in ALS1; reduces structuralstability and enzyme activity; increases
46F -> C (in ALS1; slow progression). VAR_013525
47H -> R (in ALS1; "benign" form; 80% ofwild-type activity; ubiquitinated by
49H -> Q (in ALS1). VAR_007142
49H -> R (in ALS1). VAR_045878
50E -> K (in ALS1). VAR_013526
55T -> R (in ALS1; reduces tendency to formfibrillar aggregates).
66N -> S (in ALS1). VAR_013527
68L -> P (in ALS1). VAR_065560
68L -> R (in ALS1). VAR_013528
73G -> S (in ALS1). VAR_008718
77D -> Y (in ALS1). VAR_013529
81H -> A (in ALS1; sporadic form;interferes with zinc binding; requires 2
85L -> F (in ALS1). VAR_013530
85L -> V (in ALS1). VAR_007143
86G -> R (in ALS1; ubiquitinated by RNF19A;interferes with zinc-binding.
87N -> S (in ALS1; dbSNP:rs11556620). VAR_013531
88V -> A (in ALS1). VAR_045880
90A -> T (in ALS1). VAR_045881
90A -> V (in ALS1). VAR_013532
91D -> A (in ALS1; does not seem to belinked with a decrease in activity).
91D -> V (in ALS1). VAR_013533
94G -> A (in ALS1; increases tendency toform fibrillar aggregates; ubiquitinated
94G -> C (in ALS1). VAR_007147
94G -> D (in ALS1). VAR_007148
94G -> R (in ALS1; 30% of wild-typeactivity).
94G -> V (in ALS1). VAR_008719
96A -> G (in ALS1). VAR_065194
98V -> M (in ALS1; increases tendency toform fibrillar aggregates).
101E -> G (in ALS1). VAR_007150
101E -> K (in ALS1). VAR_013534
102D -> G (in ALS1). VAR_007151
102D -> N (in ALS1). VAR_007152
105I -> F (in ALS1). VAR_008720
106S -> L (in ALS1). VAR_013535
107L -> V (in ALS1). VAR_007153
109G -> V (in ALS1). VAR_013536
113I -> M (in ALS1). VAR_013537
113I -> T (in ALS1). VAR_007154
114I -> T (in ALS1; destabilizes dimericprotein structure and increases tendency
115G -> A (in ALS1). VAR_013538
116R -> G (in ALS1). VAR_007156
119V -> L (in ALS1). VAR_045883
119V -> VFLQ (in ALS1). VAR_008721
125D -> G (in ALS1). VAR_045884
125D -> V (in ALS1). VAR_008722
126D -> H (in ALS1). VAR_007157
127L -> S (in ALS1). VAR_013539
134Missing (in ALS). VAR_008723
135S -> N (in ALS1; reduced metal binding;increases tendency to form fibrillar
140N -> K (in ALS1). VAR_007159
145L -> F (in ALS1). VAR_007160
145L -> S (in ALS1). VAR_008724
146A -> T (in ALS1). VAR_008725
147C -> R (in ALS1). VAR_013540
148G -> R (in ALS1). VAR_045885
149V -> G (in ALS1). VAR_007161
149V -> I (in ALS1). VAR_007162
150I -> T (in ALS1). VAR_007163
152I -> T (in ALS1; seems to affectformation of homodimer).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATKAV
---CCEEEE
20.15UniProtKB
Link
3Phosphothreonine--MATKAVC
--CCEEEEE
20.45Phosphositeplus
Link
4N-linked (Glc) (glycation)-MATKAVCV
-CCEEEEEE
29.32HPRD
Link
7S-nitrosocysteineTKAVCVLKG
EEEEEEECC
3.38dbSNO
Link
10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VCVLKGDGP
EEEECCCCC
34.26Phosphositeplus
Link
10N-linked (Glc) (glycation)VCVLKGDGP
EEEECCCCC
34.26HPRD
Link
31Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NGPVKVWGS
CCCEEEEEE
35.09Phosphositeplus
Link
31N-linked (Glc) (glycation)NGPVKVWGS
CCCEEEEEE
35.09HPRD
Link
331-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain).PVKVWGSIK
CEEEEEEEE
6.79UniProtKB
Link
37N-linked (Glc) (glycation)WGSIKGLTE
EEEEECCCC
49.95HPRD
Link
59PhosphothreonineTAGCTSAGP
CCCCCCCCC
22.24Phosphositeplus
Link
60PhosphoserineAGCTSAGPH
CCCCCCCCC
34.99Phosphositeplus
Link
76Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)HGGPKDEER
CCCCCCCCC
79.59Phosphositeplus
Link
99PhosphoserineVADVSIEDS
EEEEEEEEC
22.32HPRD
Link
99PhosphoserineVADVSIEDS
EEEEEEEEC
22.32Phosphositeplus
Link
99PhosphoserineVADVSIEDS
EEEEEEEEC
22.32SysPTM
Link
99Phosphoserine.VADVSIEDS
EEEEEEEEC
22.32UniProtKB
Link
103PhosphoserineSIEDSVISL
EEEECCEEE
14.46HPRD
Link
103PhosphoserineSIEDSVISL
EEEECCEEE
14.46Phosphositeplus
Link
123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VVHEKADDL
EEECCCCCC
42.09Phosphositeplus
Link
123N-linked (Glc) (glycation)VVHEKADDL
EEECCCCCC
42.09HPRD
Link
123N6-acetyllysineVVHEKADDL
EEECCCCCC
42.09HPRD
Link
123N6-acetyllysineVVHEKADDL
EEECCCCCC
42.09Phosphositeplus
Link
123N6-acetyllysine.VVHEKADDL
EEECCCCCC
42.09UniProtKB
Link
129N-linked (Glc) (glycation)DDLGKGGNE
CCCCCCCCC
71.58HPRD
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CCS_HUMANphysical interactionMINT-45807MINT9726962
HS90A_HUMANphysical interactionMINT-14911MINT11457725
PP2BA_HUMANin vitroHPRD:00937HPRD11513882
SODC_HUMANin vitroHPRD:00937HPRD1463506
12754496
CATA_HUMANENSP00000270142STRING
EAA2_HUMANENSP00000270142STRING
CCS_HUMANENSP00000270142STRING
NFH_HUMANENSP00000270142STRING
PP2BA_HUMANENSP00000270142STRING
SODM_HUMANENSP00000270142STRING
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Disease Reference
Kegg disease
OMIM disease
105400Amyotrophic lateral sclerosis 1 (ALS1)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND MASS SPECTROMETRY.
"Atomic structures of wild-type and thermostable mutant recombinanthuman Cu,Zn superoxide dismutase.";
Parge H.E., Hallewell R.A., Tainer J.A.;
Proc. Natl. Acad. Sci. U.S.A. 89:6109-6113(1992).
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures