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Protein

Superoxide dismutase [Mn], mitochondrial

Gene

SOD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.1 Publication

Catalytic activityi

2 superoxide + 2 H+ = O2 + H2O2.

Cofactori

Mn2+Note: Binds 1 Mn2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi50Manganese1
Metal bindingi98Manganese1
Metal bindingi183Manganese1
Metal bindingi187Manganese1

GO - Molecular functioni

  • manganese ion binding Source: UniProtKB
  • superoxide dismutase activity Source: UniProtKB

GO - Biological processi

  • age-dependent response to reactive oxygen species Source: UniProtKB
  • negative regulation of cell proliferation Source: BHF-UCL
  • negative regulation of neuron apoptotic process Source: BHF-UCL
  • negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  • oxygen homeostasis Source: BHF-UCL
  • protein homotetramerization Source: UniProtKB
  • regulation of blood pressure Source: BHF-UCL
  • regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • release of cytochrome c from mitochondria Source: BHF-UCL
  • removal of superoxide radicals Source: BHF-UCL
  • response to reactive oxygen species Source: Reactome
  • response to superoxide Source: BHF-UCL
  • superoxide metabolic process Source: UniProtKB
  • vasodilation by acetylcholine involved in regulation of systemic arterial blood pressure Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS03515-MONOMER.
ZFISH:HS03515-MONOMER.
BRENDAi1.15.1.1. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.
SIGNORiP04179.

Names & Taxonomyi

Protein namesi
Recommended name:
Superoxide dismutase [Mn], mitochondrial (EC:1.15.1.1)
Gene namesi
Name:SOD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:11180. SOD2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: BHF-UCL
  • mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Microvascular complications of diabetes 6 (MVCD6)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionPathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
See also OMIM:612634

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi58Y → A, H, N, V or F: Reduced enzyme activity. 1 Publication1
Mutagenesisi58Y → F: Loss of nitration. Enhanced dityrosine formation on peroxynitrite treatment. 1 Publication1

Organism-specific databases

DisGeNETi6648.
MalaCardsiSOD2.
MIMi612634. phenotype.
OpenTargetsiENSG00000112096.
PharmGKBiPA36017.

Protein family/group databases

Allergomei784. Hom s MnSOD.

Polymorphism and mutation databases

BioMutaiSOD2.
DMDMi134665.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 24Mitochondrion4 PublicationsAdd BLAST24
ChainiPRO_000003286925 – 222Superoxide dismutase [Mn], mitochondrialAdd BLAST198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei58Nitrated tyrosine2 Publications1
Modified residuei68N6-acetyllysine; alternateCombined sources1
Modified residuei68N6-succinyllysine; alternateBy similarity1
Modified residuei75N6-acetyllysine; alternateBy similarity1
Modified residuei75N6-succinyllysine; alternateBy similarity1
Modified residuei114N6-acetyllysineBy similarity1
Modified residuei122N6-acetyllysine; alternateBy similarity1
Modified residuei122N6-succinyllysine; alternateBy similarity1
Modified residuei130N6-acetyllysine; alternateCombined sources1
Modified residuei130N6-succinyllysine; alternateBy similarity1
Modified residuei202N6-acetyllysineBy similarity1

Post-translational modificationi

Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity.2 Publications
Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting (By similarity).By similarity

Keywords - PTMi

Acetylation, Nitration

Proteomic databases

EPDiP04179.
MaxQBiP04179.
PaxDbiP04179.
PeptideAtlasiP04179.
PRIDEiP04179.
TopDownProteomicsiP04179-1. [P04179-1]
P04179-2. [P04179-2]

2D gel databases

DOSAC-COBS-2DPAGEP04179.
OGPiP04179.
SWISS-2DPAGEP04179.
UCD-2DPAGEP04179.

PTM databases

iPTMnetiP04179.
PhosphoSitePlusiP04179.
SwissPalmiP04179.

Expressioni

Inductioni

Expression is regulated by KRIT1.1 Publication

Gene expression databases

BgeeiENSG00000112096.
CleanExiHS_SOD2.
ExpressionAtlasiP04179. baseline and differential.
GenevisibleiP04179. HS.

Organism-specific databases

HPAiCAB002013.
HPA001814.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-716989,EBI-716989

Protein-protein interaction databases

BioGridi112531. 38 interactors.
IntActiP04179. 20 interactors.
MINTiMINT-5002369.
STRINGi9606.ENSP00000356022.

Structurei

Secondary structure

1222
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni35 – 41Combined sources7
Helixi44 – 52Combined sources9
Helixi54 – 74Combined sources21
Helixi78 – 83Combined sources6
Helixi85 – 103Combined sources19
Helixi115 – 125Combined sources11
Helixi128 – 140Combined sources13
Beta strandi144 – 153Combined sources10
Turni154 – 157Combined sources4
Beta strandi158 – 165Combined sources8
Helixi170 – 174Combined sources5
Beta strandi177 – 183Combined sources7
Helixi186 – 188Combined sources3
Helixi190 – 193Combined sources4
Helixi197 – 204Combined sources8
Helixi205 – 207Combined sources3
Helixi210 – 219Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AP5X-ray2.20A/B25-222[»]
1AP6X-ray1.90A/B25-222[»]
1EM1X-ray2.13A/B25-222[»]
1JA8X-ray2.12A/B25-222[»]
1LUVX-ray1.85A/B25-222[»]
1LUWX-ray2.30A/B25-222[»]
1MSDX-ray3.20A/B25-222[»]
1N0JX-ray2.20A/B25-222[»]
1N0NX-ray1.82A/B25-222[»]
1PL4X-ray1.47A/B/C/D25-222[»]
1PM9X-ray1.70A/B25-222[»]
1QNMX-ray2.30A/B25-222[»]
1SZXX-ray1.95A/B25-222[»]
1VARX-ray2.50A/B25-222[»]
1XDCX-ray1.85A/B25-222[»]
1XILX-ray1.53A/B25-222[»]
1ZSPX-ray1.90A/B25-222[»]
1ZTEX-ray1.85A/B/C/D25-222[»]
1ZUQX-ray2.00A/B25-222[»]
2ADPX-ray2.40A25-222[»]
2ADQX-ray2.40B25-222[»]
2GDSX-ray2.30A/B/C/D25-222[»]
2P4KX-ray1.48A/B/C/D25-222[»]
2QKAX-ray2.20A/C25-220[»]
2QKCX-ray2.30A/C25-220[»]
3C3SX-ray2.50A/B25-222[»]
3C3TX-ray2.20A/B25-222[»]
ProteinModelPortaliP04179.
SMRiP04179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04179.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
HOVERGENiHBG004451.
InParanoidiP04179.
KOiK04564.
PhylomeDBiP04179.
TreeFamiTF105132.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P04179-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLSRAVCGTS RQLAPALGYL GSRQKHSLPD LPYDYGALEP HINAQIMQLH
60 70 80 90 100
HSKHHAAYVN NLNVTEEKYQ EALAKGDVTA QIALQPALKF NGGGHINHSI
110 120 130 140 150
FWTNLSPNGG GEPKGELLEA IKRDFGSFDK FKEKLTAASV GVQGSGWGWL
160 170 180 190 200
GFNKERGHLQ IAACPNQDPL QGTTGLIPLL GIDVWEHAYY LQYKNVRPDY
210 220
LKAIWNVINW ENVTERYMAC KK
Length:222
Mass (Da):24,722
Last modified:April 1, 1990 - v2
Checksum:i648435C080E6E47B
GO
Isoform 2 (identifier: P04179-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     75-113: Missing.

Note: No experimental confirmation available.
Show »
Length:183
Mass (Da):20,696
Checksum:i1C427B935D71B90F
GO
Isoform 3 (identifier: P04179-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     115-174: Missing.

Note: No experimental confirmation available.
Show »
Length:162
Mass (Da):18,234
Checksum:i4256776626017959
GO
Isoform 4 (identifier: P04179-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: Missing.

Note: No experimental confirmation available.
Show »
Length:176
Mass (Da):19,730
Checksum:i5AB24FB15A80A1AF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14A → P (PubMed:3399391).Curated1
Sequence conflicti65T → N in CAA42066 (PubMed:1699607).Curated1
Sequence conflicti65T → N in CAA33228 (PubMed:1699607).Curated1
Sequence conflicti66E → Q (PubMed:1988135).Curated1
Sequence conflicti112E → Q (PubMed:1988135).Curated1
Sequence conflicti123R → L in CAA30687 (PubMed:3399391).Curated1
Sequence conflicti133E → Q (PubMed:1988135).Curated1
Sequence conflicti148 – 149Missing (PubMed:1988135).Curated2
Sequence conflicti155E → Q in CAA68533 (PubMed:3684581).Curated1
Sequence conflicti155E → Q (PubMed:1988135).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01936310S → I.1 PublicationCorresponds to variant rs5746096dbSNPEnsembl.1
Natural variantiVAR_01618316A → V Very frequent polymorphism; associated with susceptibility to diabetic nephropathy in Japanese patients with type 2 diabetes. 8 PublicationsCorresponds to variant rs4880dbSNPEnsembl.1
Natural variantiVAR_01936466E → V.1 PublicationCorresponds to variant rs5746097dbSNPEnsembl.1
Natural variantiVAR_02589876G → R.Corresponds to variant rs4987023dbSNPEnsembl.1
Natural variantiVAR_00716582I → T.1 PublicationCorresponds to variant rs1141718dbSNPEnsembl.1
Natural variantiVAR_019365156R → W.1 PublicationCorresponds to variant rs5746129dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0537611 – 46Missing in isoform 4. 1 PublicationAdd BLAST46
Alternative sequenceiVSP_04255875 – 113Missing in isoform 2. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_053762115 – 174Missing in isoform 3. 1 PublicationAdd BLAST60

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59445 mRNA. Translation: CAA42066.1.
Y00472 mRNA. Translation: CAA68533.1.
Y00985 mRNA. Translation: CAA68791.1.
X07834 mRNA. Translation: CAA30687.1.
M36693 mRNA. Translation: AAA36622.1.
X15132 mRNA. Translation: CAA33228.1.
X14322 mRNA. Translation: CAA32502.1.
S77127 Genomic DNA. Translation: AAD14248.1. Sequence problems.
BT006967 mRNA. Translation: AAP35613.1.
AY267901 Genomic DNA. Translation: AAP03428.1.
AK097395 mRNA. Translation: BAG53464.1.
AK296809 mRNA. Translation: BAG59382.1.
AK304766 mRNA. Translation: BAG65521.1.
AK313082 mRNA. Translation: BAG35908.1.
AL135914 Genomic DNA. Translation: CAI21845.1.
CH471051 Genomic DNA. Translation: EAW47630.1.
CH471051 Genomic DNA. Translation: EAW47631.1.
BC012423 mRNA. Translation: AAH12423.1.
CCDSiCCDS34564.1. [P04179-2]
CCDS5265.1. [P04179-1]
CCDS83141.1. [P04179-4]
CCDS83143.1. [P04179-3]
PIRiS13162. DSHUN.
RefSeqiNP_000627.2. NM_000636.3.
NP_001019636.1. NM_001024465.2.
NP_001019637.1. NM_001024466.2.
NP_001309743.1. NM_001322814.1.
NP_001309744.1. NM_001322815.1.
NP_001309746.1. NM_001322817.1. [P04179-4]
NP_001309748.1. NM_001322819.1. [P04179-4]
NP_001309749.1. NM_001322820.1. [P04179-4]
UniGeneiHs.487046.

Genome annotation databases

EnsembliENST00000546087; ENSP00000442920; ENSG00000112096. [P04179-4]
GeneIDi6648.
KEGGihsa:6648.
UCSCiuc003qsf.6. human. [P04179-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Superoxide dismutase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59445 mRNA. Translation: CAA42066.1.
Y00472 mRNA. Translation: CAA68533.1.
Y00985 mRNA. Translation: CAA68791.1.
X07834 mRNA. Translation: CAA30687.1.
M36693 mRNA. Translation: AAA36622.1.
X15132 mRNA. Translation: CAA33228.1.
X14322 mRNA. Translation: CAA32502.1.
S77127 Genomic DNA. Translation: AAD14248.1. Sequence problems.
BT006967 mRNA. Translation: AAP35613.1.
AY267901 Genomic DNA. Translation: AAP03428.1.
AK097395 mRNA. Translation: BAG53464.1.
AK296809 mRNA. Translation: BAG59382.1.
AK304766 mRNA. Translation: BAG65521.1.
AK313082 mRNA. Translation: BAG35908.1.
AL135914 Genomic DNA. Translation: CAI21845.1.
CH471051 Genomic DNA. Translation: EAW47630.1.
CH471051 Genomic DNA. Translation: EAW47631.1.
BC012423 mRNA. Translation: AAH12423.1.
CCDSiCCDS34564.1. [P04179-2]
CCDS5265.1. [P04179-1]
CCDS83141.1. [P04179-4]
CCDS83143.1. [P04179-3]
PIRiS13162. DSHUN.
RefSeqiNP_000627.2. NM_000636.3.
NP_001019636.1. NM_001024465.2.
NP_001019637.1. NM_001024466.2.
NP_001309743.1. NM_001322814.1.
NP_001309744.1. NM_001322815.1.
NP_001309746.1. NM_001322817.1. [P04179-4]
NP_001309748.1. NM_001322819.1. [P04179-4]
NP_001309749.1. NM_001322820.1. [P04179-4]
UniGeneiHs.487046.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AP5X-ray2.20A/B25-222[»]
1AP6X-ray1.90A/B25-222[»]
1EM1X-ray2.13A/B25-222[»]
1JA8X-ray2.12A/B25-222[»]
1LUVX-ray1.85A/B25-222[»]
1LUWX-ray2.30A/B25-222[»]
1MSDX-ray3.20A/B25-222[»]
1N0JX-ray2.20A/B25-222[»]
1N0NX-ray1.82A/B25-222[»]
1PL4X-ray1.47A/B/C/D25-222[»]
1PM9X-ray1.70A/B25-222[»]
1QNMX-ray2.30A/B25-222[»]
1SZXX-ray1.95A/B25-222[»]
1VARX-ray2.50A/B25-222[»]
1XDCX-ray1.85A/B25-222[»]
1XILX-ray1.53A/B25-222[»]
1ZSPX-ray1.90A/B25-222[»]
1ZTEX-ray1.85A/B/C/D25-222[»]
1ZUQX-ray2.00A/B25-222[»]
2ADPX-ray2.40A25-222[»]
2ADQX-ray2.40B25-222[»]
2GDSX-ray2.30A/B/C/D25-222[»]
2P4KX-ray1.48A/B/C/D25-222[»]
2QKAX-ray2.20A/C25-220[»]
2QKCX-ray2.30A/C25-220[»]
3C3SX-ray2.50A/B25-222[»]
3C3TX-ray2.20A/B25-222[»]
ProteinModelPortaliP04179.
SMRiP04179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112531. 38 interactors.
IntActiP04179. 20 interactors.
MINTiMINT-5002369.
STRINGi9606.ENSP00000356022.

Protein family/group databases

Allergomei784. Hom s MnSOD.

PTM databases

iPTMnetiP04179.
PhosphoSitePlusiP04179.
SwissPalmiP04179.

Polymorphism and mutation databases

BioMutaiSOD2.
DMDMi134665.

2D gel databases

DOSAC-COBS-2DPAGEP04179.
OGPiP04179.
SWISS-2DPAGEP04179.
UCD-2DPAGEP04179.

Proteomic databases

EPDiP04179.
MaxQBiP04179.
PaxDbiP04179.
PeptideAtlasiP04179.
PRIDEiP04179.
TopDownProteomicsiP04179-1. [P04179-1]
P04179-2. [P04179-2]

Protocols and materials databases

DNASUi6648.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000546087; ENSP00000442920; ENSG00000112096. [P04179-4]
GeneIDi6648.
KEGGihsa:6648.
UCSCiuc003qsf.6. human. [P04179-1]

Organism-specific databases

CTDi6648.
DisGeNETi6648.
GeneCardsiSOD2.
HGNCiHGNC:11180. SOD2.
HPAiCAB002013.
HPA001814.
MalaCardsiSOD2.
MIMi147460. gene.
612634. phenotype.
neXtProtiNX_P04179.
OpenTargetsiENSG00000112096.
PharmGKBiPA36017.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0876. Eukaryota.
COG0605. LUCA.
GeneTreeiENSGT00390000011877.
HOGENOMiHOG000013583.
HOVERGENiHBG004451.
InParanoidiP04179.
KOiK04564.
PhylomeDBiP04179.
TreeFamiTF105132.

Enzyme and pathway databases

BioCyciMetaCyc:HS03515-MONOMER.
ZFISH:HS03515-MONOMER.
BRENDAi1.15.1.1. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.
SIGNORiP04179.

Miscellaneous databases

ChiTaRSiSOD2. human.
EvolutionaryTraceiP04179.
GeneWikiiSOD2.
GenomeRNAii6648.
PROiP04179.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000112096.
CleanExiHS_SOD2.
ExpressionAtlasiP04179. baseline and differential.
GenevisibleiP04179. HS.

Family and domain databases

InterProiIPR001189. Mn/Fe_SOD.
IPR019833. Mn/Fe_SOD_BS.
IPR019832. Mn/Fe_SOD_C.
IPR019831. Mn/Fe_SOD_N.
[Graphical view]
PANTHERiPTHR11404. PTHR11404. 1 hit.
PfamiPF02777. Sod_Fe_C. 1 hit.
PF00081. Sod_Fe_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000349. SODismutase. 1 hit.
PRINTSiPR01703. MNSODISMTASE.
SUPFAMiSSF46609. SSF46609. 1 hit.
SSF54719. SSF54719. 1 hit.
PROSITEiPS00088. SOD_MN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSODM_HUMAN
AccessioniPrimary (citable) accession number: P04179
Secondary accession number(s): B2R7R1
, B3KUK2, B4DL20, B4E3K9, E1P5A9, P78434, Q16792, Q5TCM1, Q96EE6, Q9P2Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: April 1, 1990
Last modified: November 2, 2016
This is version 205 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.