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: 1433S_HUMAN USC-OGP 2-DE database:  1433S_HUMAN 1433S_HUMAN General information about the entry View entry in simple text format Entry name 1433S_HUMAN Primary accession number P31947 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=14-3-3 protein sigma; AltName: Full=Epithelial cell marker protein 1; AltName: Full=Stratifin;. Gene name Name=SFN Synonyms=HME1 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_4-5 {PLATELET 4-5} Homo sapiens (Human)   map experimental info   PLATELET_4-5 MAP LOCATIONS: SPOT OGP-0173: pI=4.70; Mw=27414 Cross-references UniProtKB/Swiss-Prot P31947; 1433S_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 1433S_HUMAN Primary accession number P31947 Secondary accession number(s) Q6FH30 Q6FH51 Q96DH0 Sequence was last modified on  July 1, 1993 (version 1) Annotations were last modified on  March 15, 2017 (version 182) Name and origin of the protein Description RecName: Full=14-3-3 protein sigma; AltName: Full=Epithelial cell marker protein 1; AltName: Full=Stratifin; Gene name Name=SFN Synonyms=HME1 Encoded on Name=SFN; Synonyms=HME1 Keywords 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Secreted; Ubl conjugation. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL M93010; AAA59546.1; -; mRNA EMBL X57348; CAA40623.1; -; mRNA EMBL AF029081; AAC52029.1; -; Genomic_DNA EMBL AF029082; AAC52030.1; -; mRNA EMBL CR541905; CAG46703.1; -; mRNA EMBL CR541926; CAG46724.1; -; mRNA EMBL AL034380; CAB92118.1; -; Genomic_DNA EMBL BC000329; AAH00329.1; -; mRNA EMBL BC000995; AAH00995.1; -; mRNA EMBL BC001550; AAH01550.1; -; mRNA EMBL BC002995; AAH02995.1; -; mRNA EMBL BC023552; AAH23552.1; -; mRNA CCDS CCDS288.1; -. [P31947-1]; . PIR S34753; S34753; . PIR S38956; S38956; . RefSeq NP_006133.1; NM_006142.3. [P31947-1]; . UniGene Hs.523718; -; . PDB 1YWT; X-ray; 2.40 A; A/B=1-248 PDB 1YZ5; X-ray; 2.80 A; A/B=1-248 PDB 3IQJ; X-ray; 1.15 A; A=1-231 PDB 3IQU; X-ray; 1.05 A; A=1-231 PDB 3IQV; X-ray; 1.20 A; A=1-231 PDB 3LW1; X-ray; 1.28 A; A=1-248 PDB 3MHR; X-ray; 1.15 A; A=1-231 PDB 3O8I; X-ray; 2.00 A; A=1-231 PDB 3P1N; X-ray; 1.40 A; A=1-231 PDB 3P1O; X-ray; 1.90 A; A=1-231 PDB 3P1P; X-ray; 1.95 A; A=1-231 PDB 3P1Q; X-ray; 1.70 A; A=1-231 PDB 3P1R; X-ray; 1.70 A; A=1-231 PDB 3P1S; X-ray; 1.65 A; A=1-231 PDB 3SMK; X-ray; 2.10 A; A=1-231 PDB 3SML; X-ray; 1.90 A; A=1-231 PDB 3SMM; X-ray; 2.00 A; A=1-231 PDB 3SMN; X-ray; 2.00 A; A=1-231 PDB 3SMO; X-ray; 1.80 A; A=1-231 PDB 3SP5; X-ray; 1.80 A; A=1-231 PDB 3SPR; X-ray; 1.99 A; A=1-231 PDB 3T0L; X-ray; 1.60 A; A=1-231 PDB 3T0M; X-ray; 1.62 A; A=1-231 PDB 3U9X; X-ray; 1.80 A; A=1-231 PDB 3UX0; X-ray; 1.75 A; A=1-231 PDB 4DAT; X-ray; 1.40 A; A=1-231 PDB 4DAU; X-ray; 2.00 A; A=1-231 PDB 4DHM; X-ray; 1.70 A; A=1-231 PDB 4DHN; X-ray; 1.80 A; A=1-231 PDB 4DHO; X-ray; 1.70 A; A=1-231 PDB 4DHP; X-ray; 1.75 A; A=1-231 PDB 4DHQ; X-ray; 1.75 A; A=1-231 PDB 4DHR; X-ray; 1.40 A; A=1-231 PDB 4DHS; X-ray; 1.74 A; A=1-231 PDB 4DHT; X-ray; 1.80 A; A=1-231 PDB 4DHU; X-ray; 1.67 A; A=1-231 PDB 4FL5; X-ray; 1.90 A; A/B=1-231 PDB 4FR3; X-ray; 1.90 A; A=1-231 PDB 4HQW; X-ray; 2.35 A; A=1-231 PDB 4HRU; X-ray; 3.15 A; A=1-231 PDB 4IEA; X-ray; 1.70 A; A=1-231 PDB 4JC3; X-ray; 2.05 A; A=1-231 PDB 4JDD; X-ray; 2.10 A; A=1-231 PDB 4QLI; X-ray; 1.45 A; A=1-231 PDB 4Y32; X-ray; 1.70 A; A/B=1-231 PDB 4Y3B; X-ray; 1.80 A; A/B=1-231 PDB 4Y5I; X-ray; 1.40 A; A/B=1-231 PDB 5BTV; X-ray; 1.70 A; A=1-231 PDB 5HF3; X-ray; 1.80 A; A=1-231 PDB 5LTW; X-ray; 4.50 A; A/B/E/F/I/J=1-231 PDB 5LU1; X-ray; 2.40 A; A/B/E/F=1-231 PDB 5LU2; X-ray; 2.50 A; A/B=1-231 PDBsum 1YWT; -; . PDBsum 1YZ5; -; . PDBsum 3IQJ; -; . PDBsum 3IQU; -; . PDBsum 3IQV; -; . PDBsum 3LW1; -; . PDBsum 3MHR; -; . PDBsum 3O8I; -; . PDBsum 3P1N; -; . PDBsum 3P1O; -; . PDBsum 3P1P; -; . PDBsum 3P1Q; -; . PDBsum 3P1R; -; . PDBsum 3P1S; -; . PDBsum 3SMK; -; . PDBsum 3SML; -; . PDBsum 3SMM; -; . PDBsum 3SMN; -; . PDBsum 3SMO; -; . PDBsum 3SP5; -; . PDBsum 3SPR; -; . PDBsum 3T0L; -; . PDBsum 3T0M; -; . PDBsum 3U9X; -; . PDBsum 3UX0; -; . PDBsum 4DAT; -; . PDBsum 4DAU; -; . PDBsum 4DHM; -; . PDBsum 4DHN; -; . PDBsum 4DHO; -; . PDBsum 4DHP; -; . PDBsum 4DHQ; -; . PDBsum 4DHR; -; . PDBsum 4DHS; -; . PDBsum 4DHT; -; . PDBsum 4DHU; -; . PDBsum 4FL5; -; . PDBsum 4FR3; -; . PDBsum 4HQW; -; . PDBsum 4HRU; -; . PDBsum 4IEA; -; . PDBsum 4JC3; -; . PDBsum 4JDD; -; . PDBsum 4QLI; -; . PDBsum 4Y32; -; . PDBsum 4Y3B; -; . PDBsum 4Y5I; -; . PDBsum 5BTV; -; . PDBsum 5HF3; -; . PDBsum 5LTW; -; . PDBsum 5LU1; -; . PDBsum 5LU2; -; . ProteinModelPortal P31947; -; . SMR P31947; -; . BioGrid 109072; 254; . DIP DIP-29861N; -; . IntAct P31947; 167; . MINT MINT-108060; -; . STRING 9606.ENSP00000340989; -; . BindingDB P31947; -; . ChEMBL CHEMBL1909482; -; . iPTMnet P31947; -; . PhosphoSitePlus P31947; -; . SwissPalm P31947; -; . BioMuta SFN; -; . DMDM 398953; -; . OGP P31947; -; . SWISS-2DPAGE P31947; -; . EPD P31947; -; . MaxQB P31947; -; . PaxDb P31947; -; . PeptideAtlas P31947; -; . PRIDE P31947; -; . TopDownProteomics P31947-1; -. [P31947-1]; . TopDownProteomics P31947-2; -. [P31947-2]; . DNASU 2810; -; . Ensembl ENST00000339276; ENSP00000340989; ENSG00000175793. [P31947-1]; . GeneID 2810; -; . KEGG hsa:2810; -; . UCSC uc001bnc.2; human. [P31947-1]; . CTD 2810; -; . DisGeNET 2810; -; . GeneCards SFN; -; . HGNC HGNC:10773; SFN; . HPA CAB006268; -; . HPA CAB040552; -; . HPA HPA011105; -; . MIM 601290; gene; . neXtProt NX_P31947; -; . OpenTargets ENSG00000175793; -; . PharmGKB PA177; -; . eggNOG KOG0841; Eukaryota; . eggNOG COG5040; LUCA; . GeneTree ENSGT00760000119116; -; . HOGENOM HOG000240379; -; . HOVERGEN HBG050423; -; . InParanoid P31947; -; . KO K06644; -; . OMA GPEVQEY; -; . OrthoDB EOG091G0VKY; -; . PhylomeDB P31947; -; . TreeFam TF102003; -; . Reactome R-HSA-111447; Activation of BAD and translocation to mitochondria; . Reactome R-HSA-1445148; Translocation of GLUT4 to the plasma membrane; . Reactome R-HSA-5625740; RHO GTPases activate PKNs; . Reactome R-HSA-5628897; TP53 Regulates Metabolic Genes; . Reactome R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest; . Reactome R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex; . SignaLink P31947; -; . SIGNOR P31947; -; . EvolutionaryTrace P31947; -; . GeneWiki Stratifin; -; . GenomeRNAi 2810; -; . PRO PR:P31947; -; . Proteomes UP000005640; Chromosome 1; . Bgee ENSG00000175793; -; . CleanEx HS_SFN; -; . Genevisible P31947; HS; . GO GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome; . GO GO:0005829; C:cytosol; IDA:HPA; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005615; C:extracellular space; TAS:ProtInc; . GO GO:0005739; C:mitochondrion; IEA:GOC; . GO GO:0005634; C:nucleus; IEA:UniProtKB-SubCell; . GO GO:0045296; F:cadherin binding; IDA:BHF-UCL; . GO GO:0042802; F:identical protein binding; IPI:IntAct; . GO GO:0008426; F:protein kinase C inhibitor activity; TAS:ProtInc; . GO GO:0006977; P:DNA damage response; signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome GO GO:0061436; P:establishment of skin barrier; ISS:UniProtKB; . GO GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:HGNC; . GO GO:0031424; P:keratinization; IEA:Ensembl; . GO GO:0003334; P:keratinocyte development; IEA:Ensembl; . GO GO:0061024; P:membrane organization; TAS:Reactome; . GO GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:HGNC; . GO GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl; . GO GO:0006469; P:negative regulation of protein kinase activity; TAS:ProtInc; . GO GO:0030307; P:positive regulation of cell growth; IEA:Ensembl; . GO GO:0045606; P:positive regulation of epidermal cell differentiation; ISS:UniProtKB; . GO GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl; . GO GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome; . GO GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl; . GO GO:0010482; P:regulation of epidermal cell division; ISS:UniProtKB; . GO GO:0001836; P:release of cytochrome c from mitochondria; IDA:HGNC; . GO GO:0007165; P:signal transduction; TAS:ProtInc; . Gene3D 1.20.190.20; -; 1; . InterPro IPR000308; 14-3-3; . InterPro IPR023409; 14-3-3_CS; . InterPro IPR023410; 14-3-3_domain; . PANTHER PTHR18860; PTHR18860; 1; . Pfam PF00244; 14-3-3; 1; . PIRSF PIRSF000868; 14-3-3; 1; . PRINTS PR00305; 1433ZETA; . SMART SM00101; 14_3_3; 1; . SUPFAM SSF48445; SSF48445; 1; . PROSITE PS00796; 1433_1; 1; . PROSITE PS00797; 1433_2; 1; .

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