Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thioredoxin

Gene

TXN

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

Functioni

Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.
ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei26 – 261Deprotonates C-terminal active site Cys
Active sitei32 – 321Nucleophile
Sitei33 – 331Contributes to redox potential value
Sitei34 – 341Contributes to redox potential value
Active sitei35 – 351Nucleophile

GO - Molecular functioni

GO - Biological processi

  • activation of protein kinase B activity Source: ParkinsonsUK-UCL
  • cell-cell signaling Source: ProtInc
  • cell proliferation Source: ProtInc
  • cell redox homeostasis Source: GO_Central
  • glycerol ether metabolic process Source: InterPro
  • movement of cell or subcellular component Source: ProtInc
  • negative regulation of hydrogen peroxide-induced cell death Source: ParkinsonsUK-UCL
  • negative regulation of protein export from nucleus Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • nucleobase-containing small molecule interconversion Source: Reactome
  • oxidation-reduction process Source: UniProtKB
  • positive regulation of DNA binding Source: UniProtKB
  • positive regulation of peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
  • positive regulation of protein kinase B signaling Source: ParkinsonsUK-UCL
  • protein folding Source: GO_Central
  • protein repair Source: Reactome
  • regulation of protein import into nucleus, translocation Source: UniProtKB
  • response to radiation Source: UniProtKB
  • response to reactive oxygen species Source: Reactome
  • signal transduction Source: ProtInc
  • sulfate assimilation Source: GO_Central
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Electron transport, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

ReactomeiR-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-5676934. Protein repair.
R-HSA-844456. The NLRP3 inflammasome.
SignaLinkiP10599.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin
Short name:
Trx
Alternative name(s):
ATL-derived factor
Short name:
ADF
Surface-associated sulphydryl protein
Short name:
SASP
Gene namesi
Name:TXN
Synonyms:TRDX, TRX, TRX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:12435. TXN.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321C → S: Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-35. 1 Publication
Mutagenesisi35 – 351C → S: Loses its reducing activity, interaction with APEX1 and transcription activation; when associated with S-32. 1 Publication
Mutagenesisi60 – 601D → N: Loss of pH-dependence of dimerization.
Mutagenesisi62 – 621C → S: Retains its reducing activity. Retains interaction with APEX1 and transcription activation; when associated with S-69 and S-73. 1 Publication
Mutagenesisi69 – 691C → S: No effect on reducing activity, interaction with APEX1 and on S-nitrosylation of C-73. Retains interaction with APEX1 and transcription activation; when associated with S-62 and S-73. 2 Publications
Mutagenesisi70 – 701E → A: Strongly reduced interaction with CASP3; when associated with A-72. 1 Publication
Mutagenesisi72 – 721K → A: Strongly reduced interaction with CASP3; when associated with A-70. 1 Publication
Mutagenesisi73 – 731C → D: Strongly reduced S-nitrosylation of CASP3. 3 Publications
Mutagenesisi73 – 731C → S: Loss of nitrosylation, and loss of S-nitrosylating activity towards CASP3. Retains interaction with APEX1 and transcription activation; when associated with S-62 and S-69. 3 Publications
Mutagenesisi73 – 731C → S: Retains its reducing activity. 3 Publications

Organism-specific databases

PharmGKBiPA37091.

Protein family/group databases

Allergomei3543. Hom s Trx.

Chemistry

ChEMBLiCHEMBL2010624.

Polymorphism and mutation databases

BioMutaiTXN.
DMDMi135773.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 105104ThioredoxinPRO_0000120005Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N6-acetyllysineCombined sources
Modified residuei8 – 81N6-succinyllysineBy similarity
Disulfide bondi32 ↔ 35Redox-activePROSITE-ProRule annotation2 Publications
Modified residuei39 – 391N6-acetyllysineCombined sources
Modified residuei62 – 621S-nitrosocysteine1 Publication
Modified residuei69 – 691S-nitrosocysteine1 Publication
Modified residuei73 – 731S-nitrosocysteine; alternate2 Publications
Disulfide bondi73 – 73Interchain; alternate1 Publication
Modified residuei94 – 941N6-acetyllysine; alternateBy similarity
Modified residuei94 – 941N6-succinyllysine; alternateBy similarity

Post-translational modificationi

In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins.4 Publications
In case of infection, ubiquitinated by S.typhimurium protein slrP, leading to its degradation.1 Publication

Keywords - PTMi

Acetylation, Disulfide bond, S-nitrosylation, Ubl conjugation

Proteomic databases

EPDiP10599.
MaxQBiP10599.
PaxDbiP10599.
PeptideAtlasiP10599.
PRIDEiP10599.
TopDownProteomicsiP10599-1. [P10599-1]
P10599-2. [P10599-2]

2D gel databases

DOSAC-COBS-2DPAGEP10599.
REPRODUCTION-2DPAGEIPI00216298.
SWISS-2DPAGEP10599.

PTM databases

iPTMnetiP10599.
PhosphoSiteiP10599.
SwissPalmiP10599.

Expressioni

Inductioni

Up-regulated by ionizing radiation.1 Publication

Gene expression databases

BgeeiENSG00000136810.
CleanExiHS_TXN.
ExpressionAtlasiP10599. baseline and differential.
GenevisibleiP10599. HS.

Organism-specific databases

HPAiCAB008678.
HPA047478.
HPA055752.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. In case of infection, interacts with S.typhimurium protein slrP. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-binding activity in a redox-dependent manner.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COPS5Q929058EBI-594644,EBI-594661
EGFRP005334EBI-594644,EBI-297353
MAP3K5Q996832EBI-594644,EBI-476263
MYD88Q998364EBI-594644,EBI-447677
PTPN1P180312EBI-594644,EBI-968788
slrPD0ZRB27EBI-594644,EBI-10762386From a different organism.

Protein-protein interaction databases

BioGridi113146. 111 interactions.
DIPiDIP-6129N.
IntActiP10599. 39 interactions.
MINTiMINT-1522967.
STRINGi9606.ENSP00000363641.

Chemistry

BindingDBiP10599.

Structurei

Secondary structure

1
105
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi8 – 1710Combined sources
Turni18 – 203Combined sources
Beta strandi23 – 286Combined sources
Beta strandi30 – 323Combined sources
Helixi33 – 4816Combined sources
Turni49 – 513Combined sources
Beta strandi52 – 587Combined sources
Turni59 – 624Combined sources
Helixi63 – 697Combined sources
Beta strandi73 – 819Combined sources
Beta strandi84 – 918Combined sources
Helixi94 – 10411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIUX-ray2.00A1-105[»]
1AUCX-ray2.10A1-105[»]
1CQGNMR-A1-105[»]
1CQHNMR-A1-105[»]
1ERTX-ray1.70A1-105[»]
1ERUX-ray2.10A1-105[»]
1ERVX-ray1.65A1-105[»]
1ERWX-ray1.80A1-105[»]
1M7TNMR-A1-66[»]
1MDINMR-A1-105[»]
1MDJNMR-A1-105[»]
1MDKNMR-A1-105[»]
1TRSNMR-A1-105[»]
1TRUNMR-A1-105[»]
1TRVNMR-A1-105[»]
1TRWNMR-A1-105[»]
1W1Cmodel-C1-105[»]
1W1Emodel-C1-105[»]
2HSHX-ray1.35A1-105[»]
2HXKX-ray1.65A/B/C1-105[»]
2IFQX-ray1.20A/B/C1-105[»]
2IIYX-ray1.70A1-105[»]
3E3EX-ray2.01A/B1-105[»]
3KD0X-ray1.70A1-105[»]
3M9JX-ray1.10A/B1-105[»]
3M9KX-ray1.50A/B1-105[»]
3QFAX-ray2.20C/D2-105[»]
3QFBX-ray2.60C/D2-105[»]
3TRXNMR-A1-105[»]
4LL1X-ray2.00B/D1-105[»]
4LL4X-ray2.70B/D1-105[»]
4OO4X-ray0.97A/B1-105[»]
4OO5X-ray1.54A1-105[»]
4POKX-ray2.52A/B/C/D1-105[»]
4POLX-ray2.80A/B/C/D1-105[»]
4POMX-ray1.85A/B/C/D1-105[»]
4PUFX-ray3.30C/D1-105[»]
4TRXNMR-A1-105[»]
5DQYX-ray1.40A1-105[»]
ProteinModelPortaliP10599.
SMRiP10599. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10599.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 105104ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
GeneTreeiENSGT00530000063008.
HOGENOMiHOG000292977.
HOVERGENiHBG009243.
InParanoidiP10599.
KOiK03671.
OMAiAISTHCA.
OrthoDBiEOG091G01FG.
PhylomeDBiP10599.
TreeFamiTF318932.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P10599-1) [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
MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS
60 70 80 90 100
NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT

INELV
Length:105
Mass (Da):11,737
Last modified:January 23, 2007 - v3
Checksum:i256F4E3C8A187693
GO
Isoform 2 (identifier: P10599-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     44-63: Missing.

Show »
Length:85
Mass (Da):9,452
Checksum:i3CC6254BD6A1D66F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391K → N in AAA74596 (PubMed:3170595).Curated
Sequence conflicti39 – 391K → N in AAF86466 (Ref. 4) Curated
Sequence conflicti74 – 741M → T in AAA74596 (PubMed:3170595).Curated
Sequence conflicti74 – 741M → T in AAF86466 (Ref. 4) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei44 – 6320Missing in isoform 2. 1 PublicationVSP_045607Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04026 mRNA. Translation: AAA74596.1.
X77584 mRNA. Translation: CAA54687.1.
X54539, X54540, X54541 Genomic DNA. Translation: CAA38410.1.
AF276919 mRNA. Translation: AAF86466.1.
AY004872 mRNA. Translation: AAF87085.1.
AF313911 mRNA. Translation: AAG34699.1.
AK289508 mRNA. Translation: BAF82197.1.
CR407665 mRNA. Translation: CAG28593.1.
AF548001 Genomic DNA. Translation: AAN33187.1.
AL158158 Genomic DNA. Translation: CAI14066.1.
AL158158 Genomic DNA. Translation: CAI14067.1.
CH471105 Genomic DNA. Translation: EAW59059.1.
CH471105 Genomic DNA. Translation: EAW59060.1.
BC003377 mRNA. Translation: AAH03377.1.
BC054866 mRNA. Translation: AAH54866.1.
AF065241 mRNA. Translation: AAC17430.1.
CCDSiCCDS35103.1. [P10599-1]
CCDS59139.1. [P10599-2]
PIRiJH0568.
RefSeqiNP_001231867.1. NM_001244938.1. [P10599-2]
NP_003320.2. NM_003329.3. [P10599-1]
UniGeneiHs.435136.

Genome annotation databases

EnsembliENST00000374515; ENSP00000363639; ENSG00000136810. [P10599-2]
ENST00000374517; ENSP00000363641; ENSG00000136810. [P10599-1]
GeneIDi7295.
KEGGihsa:7295.
UCSCiuc004bep.3. human. [P10599-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04026 mRNA. Translation: AAA74596.1.
X77584 mRNA. Translation: CAA54687.1.
X54539, X54540, X54541 Genomic DNA. Translation: CAA38410.1.
AF276919 mRNA. Translation: AAF86466.1.
AY004872 mRNA. Translation: AAF87085.1.
AF313911 mRNA. Translation: AAG34699.1.
AK289508 mRNA. Translation: BAF82197.1.
CR407665 mRNA. Translation: CAG28593.1.
AF548001 Genomic DNA. Translation: AAN33187.1.
AL158158 Genomic DNA. Translation: CAI14066.1.
AL158158 Genomic DNA. Translation: CAI14067.1.
CH471105 Genomic DNA. Translation: EAW59059.1.
CH471105 Genomic DNA. Translation: EAW59060.1.
BC003377 mRNA. Translation: AAH03377.1.
BC054866 mRNA. Translation: AAH54866.1.
AF065241 mRNA. Translation: AAC17430.1.
CCDSiCCDS35103.1. [P10599-1]
CCDS59139.1. [P10599-2]
PIRiJH0568.
RefSeqiNP_001231867.1. NM_001244938.1. [P10599-2]
NP_003320.2. NM_003329.3. [P10599-1]
UniGeneiHs.435136.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIUX-ray2.00A1-105[»]
1AUCX-ray2.10A1-105[»]
1CQGNMR-A1-105[»]
1CQHNMR-A1-105[»]
1ERTX-ray1.70A1-105[»]
1ERUX-ray2.10A1-105[»]
1ERVX-ray1.65A1-105[»]
1ERWX-ray1.80A1-105[»]
1M7TNMR-A1-66[»]
1MDINMR-A1-105[»]
1MDJNMR-A1-105[»]
1MDKNMR-A1-105[»]
1TRSNMR-A1-105[»]
1TRUNMR-A1-105[»]
1TRVNMR-A1-105[»]
1TRWNMR-A1-105[»]
1W1Cmodel-C1-105[»]
1W1Emodel-C1-105[»]
2HSHX-ray1.35A1-105[»]
2HXKX-ray1.65A/B/C1-105[»]
2IFQX-ray1.20A/B/C1-105[»]
2IIYX-ray1.70A1-105[»]
3E3EX-ray2.01A/B1-105[»]
3KD0X-ray1.70A1-105[»]
3M9JX-ray1.10A/B1-105[»]
3M9KX-ray1.50A/B1-105[»]
3QFAX-ray2.20C/D2-105[»]
3QFBX-ray2.60C/D2-105[»]
3TRXNMR-A1-105[»]
4LL1X-ray2.00B/D1-105[»]
4LL4X-ray2.70B/D1-105[»]
4OO4X-ray0.97A/B1-105[»]
4OO5X-ray1.54A1-105[»]
4POKX-ray2.52A/B/C/D1-105[»]
4POLX-ray2.80A/B/C/D1-105[»]
4POMX-ray1.85A/B/C/D1-105[»]
4PUFX-ray3.30C/D1-105[»]
4TRXNMR-A1-105[»]
5DQYX-ray1.40A1-105[»]
ProteinModelPortaliP10599.
SMRiP10599. Positions 1-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113146. 111 interactions.
DIPiDIP-6129N.
IntActiP10599. 39 interactions.
MINTiMINT-1522967.
STRINGi9606.ENSP00000363641.

Chemistry

BindingDBiP10599.
ChEMBLiCHEMBL2010624.

Protein family/group databases

Allergomei3543. Hom s Trx.

PTM databases

iPTMnetiP10599.
PhosphoSiteiP10599.
SwissPalmiP10599.

Polymorphism and mutation databases

BioMutaiTXN.
DMDMi135773.

2D gel databases

DOSAC-COBS-2DPAGEP10599.
REPRODUCTION-2DPAGEIPI00216298.
SWISS-2DPAGEP10599.

Proteomic databases

EPDiP10599.
MaxQBiP10599.
PaxDbiP10599.
PeptideAtlasiP10599.
PRIDEiP10599.
TopDownProteomicsiP10599-1. [P10599-1]
P10599-2. [P10599-2]

Protocols and materials databases

DNASUi7295.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374515; ENSP00000363639; ENSG00000136810. [P10599-2]
ENST00000374517; ENSP00000363641; ENSG00000136810. [P10599-1]
GeneIDi7295.
KEGGihsa:7295.
UCSCiuc004bep.3. human. [P10599-1]

Organism-specific databases

CTDi7295.
GeneCardsiTXN.
HGNCiHGNC:12435. TXN.
HPAiCAB008678.
HPA047478.
HPA055752.
MIMi187700. gene.
neXtProtiNX_P10599.
PharmGKBiPA37091.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
GeneTreeiENSGT00530000063008.
HOGENOMiHOG000292977.
HOVERGENiHBG009243.
InParanoidiP10599.
KOiK03671.
OMAiAISTHCA.
OrthoDBiEOG091G01FG.
PhylomeDBiP10599.
TreeFamiTF318932.

Enzyme and pathway databases

ReactomeiR-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-5676934. Protein repair.
R-HSA-844456. The NLRP3 inflammasome.
SignaLinkiP10599.

Miscellaneous databases

ChiTaRSiTXN. human.
EvolutionaryTraceiP10599.
GeneWikiiThioredoxin.
GenomeRNAii7295.
PROiP10599.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136810.
CleanExiHS_TXN.
ExpressionAtlasiP10599. baseline and differential.
GenevisibleiP10599. HS.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHIO_HUMAN
AccessioniPrimary (citable) accession number: P10599
Secondary accession number(s): B1ALW1
, O60744, Q53X69, Q96KI3, Q9UDG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 199 of the entry and version 3 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.