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: Q13162 USC-OGP 2-DE database:  Q13162 Q13162 General information about the entry View entry in simple text format Entry name PRDX4_HUMAN Primary accession number Q13162 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-4; EC=1.11.1.15; AltName: Full=Antioxidant enzyme AOE372; Short=AOE37-2; AltName: Full=Peroxiredoxin IV; Short=Prx-IV; AltName: Full=Thioredoxin peroxidase AO372; AltName: Full=Thioredoxin-dependent peroxide reductase A0372; Flags: Precursor;. Gene name Name=PRDX4 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_4-7 {PLATELET 4-7} Homo sapiens (Human)   map experimental info   PLATELET_4-7 MAP LOCATIONS: SPOT OGP-0512: pI=5.34; Mw=26520 PLATELET_5-6 {PLATELET 5-6} Homo sapiens (Human)   map experimental info   PLATELET_5-6 MAP LOCATIONS: SPOT OGP-0794: pI=5.51; Mw=29781 UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10} Homo sapiens (Human)   map experimental info   UVEAL_MELANOMA_3-10 MAP LOCATIONS: SPOT OGP-1279: pI=5.65; Mw=26938 Cross-references UniProtKB/Swiss-Prot Q13162; PRDX4_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 PRDX4_HUMAN Primary accession number Q13162 Secondary accession number(s) Q6FHT3 Sequence was last modified on  November 1, 1996 (version 1) Annotations were last modified on  March 15, 2017 (version 171) Name and origin of the protein Description RecName: Full=Peroxiredoxin-4; EC=1.11.1.15; AltName: Full=Antioxidant enzyme AOE372; Short=AOE37-2; AltName: Full=Peroxiredoxin IV; Short=Prx-IV; AltName: Full=Thioredoxin peroxidase AO372; AltName: Full=Thioredoxin-dependent peroxide reductase A0372; Flags: Precursor; Gene name Name=PRDX4 Encoded on Name=PRDX4 Keywords 3D-structure; Antioxidant; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase; Redox-active center; Reference proteome; Secreted; Signal. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL U25182; AAB95175.1; -; mRNA EMBL CR541668; CAG46469.1; -; mRNA EMBL CR541705; CAG46506.1; -; mRNA EMBL BC003609; AAH03609.1; -; mRNA EMBL BC007107; AAH07107.1; -; mRNA EMBL BC016770; AAH16770.1; -; mRNA CCDS CCDS14206.1; -; . PIR G01790; G01790; . RefSeq NP_006397.1; NM_006406.1; . UniGene Hs.83383; -; . PDB 2PN8; X-ray; 1.80 A; A/B/C/D/E/F/G/H/I/J=84-271 PDB 3TJB; X-ray; 2.38 A; A/B/C/D/E=38-271 PDB 3TJF; X-ray; 2.04 A; A/B/C/D/E=38-271 PDB 3TJG; X-ray; 2.24 A; A/B/C/D/E=38-271 PDB 3TJJ; X-ray; 1.91 A; A/B/C/D/E=38-271 PDB 3TJK; X-ray; 2.09 A; A/B/C/D/E=38-271 PDB 3TKP; X-ray; 2.49 A; A/B/C/D/E=38-271 PDB 3TKQ; X-ray; 2.22 A; A/B/C/D/E=38-271 PDB 3TKR; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=38-271 PDB 3TKS; X-ray; 2.40 A; A/B/C/D/E=38-271 PDB 4RQX; X-ray; 2.26 A; A/B/C/D/E=79-271 PDB 5HQP; X-ray; 2.60 A; A/B=38-271 PDBsum 2PN8; -; . PDBsum 3TJB; -; . PDBsum 3TJF; -; . PDBsum 3TJG; -; . PDBsum 3TJJ; -; . PDBsum 3TJK; -; . PDBsum 3TKP; -; . PDBsum 3TKQ; -; . PDBsum 3TKR; -; . PDBsum 3TKS; -; . PDBsum 4RQX; -; . PDBsum 5HQP; -; . ProteinModelPortal Q13162; -; . SMR Q13162; -; . BioGrid 115800; 55; . IntAct Q13162; 49; . MINT MINT-3027265; -; . STRING 9606.ENSP00000368646; -; . PeroxiBase 4530; Hs2CysPrx04; . iPTMnet Q13162; -; . PhosphoSitePlus Q13162; -; . SwissPalm Q13162; -; . BioMuta PRDX4; -; . DMDM 3024727; -; . OGP Q13162; -; . REPRODUCTION-2DPAGE IPI00011937; -; . UCD-2DPAGE Q13162; -; . EPD Q13162; -; . PaxDb Q13162; -; . PeptideAtlas Q13162; -; . PRIDE Q13162; -; . TopDownProteomics Q13162; -; . DNASU 10549; -; . Ensembl ENST00000379341; ENSP00000368646; ENSG00000123131; . GeneID 10549; -; . KEGG hsa:10549; -; . CTD 10549; -; . DisGeNET 10549; -; . GeneCards PRDX4; -; . HGNC HGNC:17169; PRDX4; . HPA CAB008659; -; . HPA CAB027389; -; . HPA CAB047362; -; . MIM 300927; gene; . neXtProt NX_Q13162; -; . OpenTargets ENSG00000123131; -; . PharmGKB PA33725; -; . eggNOG KOG0852; Eukaryota; . eggNOG COG0450; LUCA; . GeneTree ENSGT00390000004653; -; . HOGENOM HOG000022343; -; . HOVERGEN HBG000286; -; . InParanoid Q13162; -; . KO K03386; -; . OMA YAGGHVY; -; . OrthoDB EOG091G0IE5; -; . PhylomeDB Q13162; -; . TreeFam TF105181; -; . BRENDA 1.11.1.15; 2681; . Reactome R-HSA-6798695; Neutrophil degranulation; . ChiTaRS PRDX4; human; . EvolutionaryTrace Q13162; -; . GeneWiki PRDX4; -; . GenomeRNAi 10549; -; . PRO PR:Q13162; -; . Proteomes UP000005640; Chromosome X; . Bgee ENSG00000123131; -; . CleanEx HS_PRDX4; -; . ExpressionAtlas Q13162; baseline and differential; . Genevisible Q13162; HS; . GO GO:0005829; C:cytosol; IEA:Ensembl; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:0005615; C:extracellular space; IEA:Ensembl; . GO GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome; . GO GO:0005739; C:mitochondrion; IEA:Ensembl; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0034774; C:secretory granule lumen; TAS:Reactome; . GO GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl; . GO GO:0008379; F:thioredoxin peroxidase activity; TAS:ProtInc; . GO GO:0019471; P:4-hydroxyproline metabolic process; IEA:Ensembl; . GO GO:0045454; P:cell redox homeostasis; IEA:Ensembl; . GO GO:0030198; P:extracellular matrix organization; IEA:Ensembl; . GO GO:0007252; P:I-kappaB phosphorylation; TAS:ProtInc; . GO GO:0008584; P:male gonad development; IEA:Ensembl; . GO GO:2000255; P:negative regulation of male germ cell proliferation; IEA:Ensembl; . GO GO:0043312; P:neutrophil degranulation; TAS:Reactome; . GO GO:0022417; P:protein maturation by protein folding; IEA:Ensembl; . GO GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl; . GO GO:0007283; P:spermatogenesis; IEA:Ensembl; . Gene3D 3.40.30.10; -; 1; . InterPro IPR000866; AhpC/TSA; . InterPro IPR019479; Peroxiredoxin_C; . InterPro IPR012336; Thioredoxin-like_fold; . InterPro IPR013766; Thioredoxin_domain; . Pfam PF10417; 1-cysPrx_C; 1; . Pfam PF00578; AhpC-TSA; 1; . SUPFAM SSF52833; SSF52833; 1; . PROSITE PS51352; THIOREDOXIN_2; 1; .

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