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

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Searching in 'USC-OGP 2-DE database' for entry matching: P30044 USC-OGP 2-DE database:  P30044 P30044 General information about the entry View entry in simple text format Entry name PRDX5_HUMAN Primary accession number P30044 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=Peroxiredoxin-5, mitochondrial; EC=1.11.1.15; AltName: Full=Alu corepressor 1; AltName: Full=Antioxidant enzyme B166; Short=AOEB166; AltName: Full=Liver tissue 2D-page spot 71B; AltName: Full=PLP; AltName: Full=Peroxiredoxin V; Short=Prx-V; AltName: Full=Peroxisomal antioxidant enzyme; AltName: Full=TPx type VI; AltName: Full=Thioredoxin peroxidase PMP20; AltName: Full=Thioredoxin reductase; Flags: Precursor;. Gene name Name=PRDX5 Synonyms=ACR1 ORFNames=SBBI10 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_6-11 {PLATELET 6-11} Homo sapiens (Human)   map experimental info   PLATELET_6-11 MAP LOCATIONS: SPOT OGP-1074: pI=6.92; Mw=16885 Cross-references UniProtKB/Swiss-Prot P30044; PRDX5_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 PRDX5_HUMAN Primary accession number P30044 Secondary accession number(s) A6NC19 A6NG06 B7ZLJ4 B7ZVW3 Q14CK0 Q6IAF2 Q9UBU5 Q9UJU4 Q9UKX4 Sequence was last modified on  January 11, 2011 (version 4) Annotations were last modified on  March 15, 2017 (version 184) Name and origin of the protein Description RecName: Full=Peroxiredoxin-5, mitochondrial; EC=1.11.1.15; AltName: Full=Alu corepressor 1; AltName: Full=Antioxidant enzyme B166; Short=AOEB166; AltName: Full=Liver tissue 2D-page spot 71B; AltName: Full=PLP; AltName: Full=Peroxiredoxin V; Short=Prx-V; AltName: Full=Peroxisomal antioxidant enzyme; AltName: Full=TPx type VI; AltName: Full=Thioredoxin peroxidase PMP20; AltName: Full=Thioredoxin reductase; Flags: Precursor; Gene name Name=PRDX5 Synonyms=ACR1 ORFNames=SBBI10 Encoded on Name=PRDX5; Synonyms=ACR1; ORFNames=SBBI10 Keywords 3D-structure; Acetylation; Alternative initiation; Alternative splicing; Antioxidant; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Mitochondrion; Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein; Polymorphism; Redox-active center; Reference proteome; Transit peptide. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL AF231705; AAF78899.1; -; mRNA EMBL AF124993; AAF27531.1; -; mRNA EMBL AF110731; AAF03750.1; -; mRNA EMBL AF197952; AAF04856.1; -; mRNA EMBL AJ249483; CAB62210.1; -; mRNA EMBL AF242525; AAF99605.1; -; mRNA EMBL AF112212; AAF17200.1; ALT_FRAME; mRNA EMBL CR457203; CAG33484.1; -; mRNA EMBL DQ247769; ABB05181.1; -; Genomic_DNA EMBL AP001453; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL AP003774; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL BC110983; AAI10984.1; -; mRNA EMBL BC113723; AAI13724.1; -; mRNA EMBL BC113725; AAI13726.1; -; mRNA EMBL BC143849; AAI43850.1; -; mRNA EMBL BC171733; AAI71733.1; -; mRNA CCDS CCDS8069.1; -. [P30044-1]; . CCDS CCDS8070.1; -. [P30044-3]; . CCDS CCDS8071.1; -. [P30044-4]; . RefSeq NP_036226.1; NM_012094.4; . RefSeq NP_857634.1; NM_181651.2; . RefSeq NP_857635.1; NM_181652.2; . UniGene Hs.502823; -; . PDB 1H4O; X-ray; 1.95 A; A/B/C/D/E/F/G/H=54-214 PDB 1HD2; X-ray; 1.50 A; A=54-214 PDB 1OC3; X-ray; 2.00 A; A/B/C=54-214 PDB 1URM; X-ray; 1.70 A; A=54-214 PDB 2VL2; X-ray; 1.92 A; A/B/C=54-214 PDB 2VL3; X-ray; 1.83 A; A/B/C=54-214 PDB 2VL9; X-ray; 2.70 A; A/B/C/D=54-214 PDB 3MNG; X-ray; 1.45 A; A=54-214 PDB 4K7I; X-ray; 2.25 A; A/B/C=54-214 PDB 4K7N; X-ray; 2.30 A; A/B/C=54-214 PDB 4K7O; X-ray; 1.98 A; A/B/C=54-214 PDB 4MMM; X-ray; 1.47 A; A/C/E/G=54-214 PDBsum 1H4O; -; . PDBsum 1HD2; -; . PDBsum 1OC3; -; . PDBsum 1URM; -; . PDBsum 2VL2; -; . PDBsum 2VL3; -; . PDBsum 2VL9; -; . PDBsum 3MNG; -; . PDBsum 4K7I; -; . PDBsum 4K7N; -; . PDBsum 4K7O; -; . PDBsum 4MMM; -; . ProteinModelPortal P30044; -; . SMR P30044; -; . BioGrid 117352; 76; . IntAct P30044; 28; . MINT MINT-5002532; -; . STRING 9606.ENSP00000265462; -; . ChEMBL CHEMBL3627586; -; . DrugBank DB00995; Auranofin; . DrugBank DB03793; Benzoic Acid; . DrugBank DB03608; Diminazene; . PeroxiBase 4448; HsPrxV; . iPTMnet P30044; -; . PhosphoSitePlus P30044; -; . SwissPalm P30044; -; . BioMuta PRDX5; -; . DMDM 317373539; -; . OGP P30044; -; . REPRODUCTION-2DPAGE IPI00759663; -; . SWISS-2DPAGE P30044; -; . UCD-2DPAGE P30044; -; . EPD P30044; -; . MaxQB P30044; -; . PaxDb P30044; -; . PeptideAtlas P30044; -; . PRIDE P30044; -; . TopDownProteomics P30044-1; -. [P30044-1]; . TopDownProteomics P30044-2; -. [P30044-2]; . DNASU 25824; -; . Ensembl ENST00000265462; ENSP00000265462; ENSG00000126432. [P30044-1]; . Ensembl ENST00000347941; ENSP00000335363; ENSG00000126432. [P30044-4]; . Ensembl ENST00000352435; ENSP00000335334; ENSG00000126432. [P30044-3]; . GeneID 25824; -; . KEGG hsa:25824; -; . UCSC uc001nzu.4; human. [P30044-1]; . CTD 25824; -; . DisGeNET 25824; -; . GeneCards PRDX5; -; . HGNC HGNC:9355; PRDX5; . HPA CAB008661; -; . HPA HPA037915; -; . HPA HPA037916; -; . MIM 606583; gene; . neXtProt NX_P30044; -; . OpenTargets ENSG00000126432; -; . PharmGKB PA33726; -; . eggNOG KOG0541; Eukaryota; . eggNOG COG0678; LUCA; . GeneTree ENSGT00390000018173; -; . HOGENOM HOG000255884; -; . HOVERGEN HBG053675; -; . InParanoid P30044; -; . KO K11187; -; . OMA CKFLGRV; -; . OrthoDB EOG091G0OSA; -; . PhylomeDB P30044; -; . TreeFam TF105182; -; . BRENDA 1.11.1.15; 2681; . Reactome R-HSA-3299685; Detoxification of Reactive Oxygen Species; . Reactome R-HSA-5628897; TP53 Regulates Metabolic Genes; . ChiTaRS PRDX5; human; . EvolutionaryTrace P30044; -; . GeneWiki PRDX5; -; . GenomeRNAi 25824; -; . PRO PR:P30044; -; . Proteomes UP000005640; Chromosome 11; . Bgee ENSG00000126432; -; . CleanEx HS_PRDX5; -; . Genevisible P30044; HS; . GO GO:0005737; C:cytoplasm; IDA:UniProtKB; . GO GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB; . GO GO:0005829; C:cytosol; IDA:UniProtKB; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005615; C:extracellular space; IDA:UniProtKB; . GO GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB; . GO GO:0005759; C:mitochondrial matrix; TAS:Reactome; . GO GO:0005739; C:mitochondrion; IDA:UniProtKB; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB; . GO GO:0005782; C:peroxisomal matrix; IDA:UniProtKB; . GO GO:0005777; C:peroxisome; IDA:UniProtKB; . GO GO:0016209; F:antioxidant activity; IDA:UniProtKB; . GO GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IMP:UniProtKB; . GO GO:0004601; F:peroxidase activity; IDA:UniProtKB; . GO GO:0051920; F:peroxiredoxin activity; IDA:UniProtKB; . GO GO:0072541; F:peroxynitrite reductase activity; IDA:UniProtKB; . GO GO:0046983; F:protein dimerization activity; IDA:UniProtKB; . GO GO:0005102; F:receptor binding; IPI:UniProtKB; . GO GO:0001016; F:RNA polymerase III regulatory region DNA binding; IDA:UniProtKB; . GO GO:0008379; F:thioredoxin peroxidase activity; EXP:Reactome; . GO GO:0045454; P:cell redox homeostasis; IEA:InterPro; . GO GO:0034614; P:cellular response to reactive oxygen species; IMP:UniProtKB; . GO GO:0042744; P:hydrogen peroxide catabolic process; IDA:UniProtKB; . GO GO:0006954; P:inflammatory response; TAS:UniProtKB; . GO GO:0070995; P:NADPH oxidation; IDA:UniProtKB; . GO GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB; . GO GO:0051354; P:negative regulation of oxidoreductase activity; IDA:UniProtKB; . GO GO:0016480; P:negative regulation of transcription from RNA polymerase III promoter; IDA:UniProtKB; . GO GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:UniProtKB; . GO GO:2001057; P:reactive nitrogen species metabolic process; IDA:UniProtKB; . GO GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; IDA:UniProtKB; . GO GO:0006979; P:response to oxidative stress; IDA:UniProtKB; . GO GO:0000302; P:response to reactive oxygen species; TAS:Reactome; . Gene3D 3.40.30.10; -; 1; . InterPro IPR013740; Redoxin; . InterPro IPR012336; Thioredoxin-like_fold; . InterPro IPR013766; Thioredoxin_domain; . Pfam PF08534; Redoxin; 1; . SUPFAM SSF52833; SSF52833; 1; . PROSITE PS51352; THIOREDOXIN_2; 1; .

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