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

USC-OGP 2-DE database  Search by                Maps             Select Remote Interfaces [All Interfaces] SWISS-2DPAGE World-2DPAGE Portal World-2DPAGE Repository Exclude local DBs has only effect if a remote interface is selected

Searching in 'USC-OGP 2-DE database' for entry matching: P62937 USC-OGP 2-DE database:  P62937 P62937 General information about the entry View entry in simple text format Entry name PPIA_HUMAN Primary accession number P62937 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=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; EC=5.2.1.8; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-binding protein; AltName: Full=Rotamase A; Contains: RecName: Full=Peptidyl-prolyl cis-trans isomerase A, N-terminally processed;. Gene name Name=PPIA Synonyms=CYPA 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 UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10} Homo sapiens (Human)   map experimental info   UVEAL_MELANOMA_3-10 MAP LOCATIONS: SPOT OGP-1332: pI=6.89; Mw=16684 SPOT OGP-1334: pI=7.49; Mw=16158 SPOT OGP-1340: pI=6.67; Mw=15436 Cross-references UniProtKB/Swiss-Prot P62937; PPIA_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 PPIA_HUMAN Primary accession number P62937 Secondary accession number(s) A8K220 P05092 Q3KQW3 Q567Q0 Q6IBU5 Q96IX3 Q9BRU4 Q9BTY9 Q9UC61 Sequence was last modified on  January 23, 2007 (version 2) Annotations were last modified on  March 15, 2017 (version 153) Name and origin of the protein Description RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; EC=5.2.1.8; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-binding protein; AltName: Full=Rotamase A; Contains: RecName: Full=Peptidyl-prolyl cis-trans isomerase A, N-terminally processed; Gene name Name=PPIA Synonyms=CYPA Encoded on Name=PPIA; Synonyms=CYPA Keywords 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Glycoprotein; Host-virus interaction; Isomerase; Isopeptide bond; Phosphoprotein; Reference proteome; Rotamase; 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 Y00052; CAA68264.1; -; mRNA EMBL X52851; CAA37039.1; -; Genomic_DNA EMBL AK290085; BAF82774.1; -; mRNA EMBL AK293003; BAF85692.1; -; mRNA EMBL CR456707; CAG32988.1; -; mRNA EMBL AB451307; BAG70121.1; -; mRNA EMBL AB451438; BAG70252.1; -; mRNA EMBL AY739283; AAU13906.1; -; Genomic_DNA EMBL AC004854; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL AC013436; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL BC000689; AAH00689.1; -; mRNA EMBL BC003026; AAH03026.2; -; mRNA EMBL BC005320; AAH05320.1; -; mRNA EMBL BC005982; AAH05982.1; -; mRNA EMBL BC007104; AAH07104.1; -; mRNA EMBL BC013915; AAH13915.1; -; mRNA EMBL BC073992; AAH73992.1; -; mRNA EMBL BC093076; AAH93076.1; -; mRNA EMBL BC106030; AAI06031.1; -; mRNA EMBL BC137057; AAI37058.1; -; mRNA EMBL BC137058; AAI37059.1; -; mRNA CCDS CCDS5494.1; -. [P62937-1]; . CCDS CCDS75592.1; -. [P62937-2]; . PIR A94496; CSHUA; . RefSeq NP_001287910.1; NM_001300981.1. [P62937-2]; . RefSeq NP_066953.1; NM_021130.4. [P62937-1]; . UniGene Hs.356331; -; . PDB 1AK4; X-ray; 2.36 A; A/B=1-165 PDB 1AWQ; X-ray; 1.58 A; A=2-165 PDB 1AWR; X-ray; 1.58 A; A/B/C/D/E/F=2-165 PDB 1AWS; X-ray; 2.55 A; A=2-165 PDB 1AWT; X-ray; 2.55 A; A/B/C/D/E/F=2-165 PDB 1AWU; X-ray; 2.34 A; A=2-165 PDB 1AWV; X-ray; 2.34 A; A/B/C/D/E/F=2-165 PDB 1BCK; X-ray; 1.80 A; A=1-165 PDB 1CWA; X-ray; 2.10 A; A=1-165 PDB 1CWB; X-ray; 2.20 A; A=1-165 PDB 1CWC; X-ray; 1.86 A; A=1-165 PDB 1CWF; X-ray; 1.86 A; A=1-165 PDB 1CWH; X-ray; 1.86 A; A=1-165 PDB 1CWI; X-ray; 1.90 A; A=1-165 PDB 1CWJ; X-ray; 1.80 A; A=1-165 PDB 1CWK; X-ray; 1.80 A; A=1-165 PDB 1CWL; X-ray; 1.80 A; A=1-165 PDB 1CWM; X-ray; 2.00 A; A=1-165 PDB 1CWO; X-ray; 1.86 A; A=1-165 PDB 1FGL; X-ray; 1.80 A; A=1-165 PDB 1M63; X-ray; 2.80 A; C/G=1-165 PDB 1M9C; X-ray; 2.00 A; A/B=1-165 PDB 1M9D; X-ray; 1.90 A; A/B=1-165 PDB 1M9E; X-ray; 1.72 A; A/B=1-164 PDB 1M9F; X-ray; 1.73 A; A/B=1-165 PDB 1M9X; X-ray; 1.70 A; A/B/E/F=1-165 PDB 1M9Y; X-ray; 1.90 A; A/B/E/F=1-165 PDB 1MF8; X-ray; 3.10 A; C=1-165 PDB 1MIK; X-ray; 1.76 A; A=1-165 PDB 1NMK; X-ray; 2.10 A; A/B=1-165 PDB 1OCA; NMR; -; A=1-165 PDB 1RMH; X-ray; 2.40 A; A/B=2-165 PDB 1VBS; X-ray; 2.00 A; A=1-165 PDB 1VBT; X-ray; 2.30 A; A/B=1-165 PDB 1W8L; X-ray; 1.80 A; A=2-165 PDB 1W8M; X-ray; 1.65 A; A=2-165 PDB 1W8V; X-ray; 1.70 A; A=2-165 PDB 1YND; X-ray; 1.60 A; A/B=1-165 PDB 1ZKF; X-ray; 2.55 A; A/B=1-165 PDB 2ALF; X-ray; 1.90 A; A=2-165 PDB 2CPL; X-ray; 1.63 A; A=1-165 PDB 2CYH; X-ray; 1.64 A; A=2-165 PDB 2MS4; NMR; -; A=1-165 PDB 2MZU; NMR; -; A=1-165 PDB 2N0T; NMR; -; A=1-165 PDB 2RMA; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=1-165 PDB 2RMB; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=1-165 PDB 2X25; X-ray; 1.20 A; B=2-165 PDB 2X2A; X-ray; 1.40 A; A/B=1-165 PDB 2X2C; X-ray; 2.41 A; K/M/O/Q/S=1-165 PDB 2X2D; X-ray; 1.95 A; B/C=1-165 PDB 2XGY; X-ray; 1.80 A; B=1-165 PDB 3CYH; X-ray; 1.90 A; A=2-165 PDB 3CYS; NMR; -; A=1-165 PDB 3K0M; X-ray; 1.25 A; A=1-165 PDB 3K0N; X-ray; 1.39 A; A=1-165 PDB 3K0O; X-ray; 1.55 A; A=1-165 PDB 3K0P; X-ray; 1.65 A; A=1-165 PDB 3K0Q; X-ray; 2.32 A; A=1-165 PDB 3K0R; X-ray; 2.42 A; A=1-165 PDB 3ODI; X-ray; 2.20 A; A/C/E/G/I/K/M/O/Q/S=1-165 PDB 3ODL; X-ray; 2.31 A; A/C/E/G/I/K/M/O/Q/S=1-165 PDB 3RDD; X-ray; 2.14 A; A=1-165 PDB 4CYH; X-ray; 2.10 A; A=2-165 PDB 4IPZ; X-ray; 1.67 A; A=1-165 PDB 4N1M; X-ray; 1.15 A; A=1-165 PDB 4N1N; X-ray; 1.50 A; A=1-165 PDB 4N1O; X-ray; 1.75 A; A=1-165 PDB 4N1P; X-ray; 1.90 A; A=1-165 PDB 4N1Q; X-ray; 1.65 A; A=1-165 PDB 4N1R; X-ray; 1.80 A; A=1-165 PDB 4N1S; X-ray; 1.47 A; A=1-165 PDB 4YUG; X-ray; 1.48 A; A=1-165 PDB 4YUH; X-ray; 1.34 A; A=1-165 PDB 4YUI; X-ray; 1.38 A; A=1-165 PDB 4YUJ; X-ray; 1.42 A; A=1-165 PDB 4YUK; X-ray; 1.48 A; A=1-165 PDB 4YUL; X-ray; 1.42 A; A=1-165 PDB 4YUM; X-ray; 1.50 A; A=1-165 PDB 4YUN; X-ray; 1.58 A; A=1-165 PDB 4YUO; X-ray; 1.20 A; A=1-165 PDB 4YUP; X-ray; 1.75 A; A=1-165 PDB 5CYH; X-ray; 2.10 A; A=2-165 PDB 5F66; X-ray; 1.15 A; A=1-165 PDB 5FJB; EM; 9.00 A; C=2-165 PDB 5KUL; X-ray; 1.70 A; A=2-165 PDB 5KUN; X-ray; 1.70 A; A=2-165 PDB 5KUO; X-ray; 1.70 A; A=2-165 PDB 5KUQ; X-ray; 1.70 A; A=2-165 PDB 5KUR; X-ray; 1.70 A; A=2-165 PDB 5KUS; X-ray; 1.70 A; A=2-165 PDB 5KUU; X-ray; 1.70 A; A=2-165 PDB 5KUV; X-ray; 1.70 A; A=2-165 PDB 5KUW; X-ray; 1.70 A; A=2-165 PDB 5KUZ; X-ray; 1.70 A; A=2-165 PDB 5KV0; X-ray; 1.70 A; A=2-165 PDB 5KV1; X-ray; 1.70 A; A=2-165 PDB 5KV2; X-ray; 1.70 A; A=2-165 PDB 5KV3; X-ray; 1.70 A; A=2-165 PDB 5KV4; X-ray; 1.70 A; A=2-165 PDB 5KV5; X-ray; 1.70 A; A=2-165 PDB 5KV6; X-ray; 1.70 A; A=2-165 PDB 5KV7; X-ray; 1.70 A; A=2-165 PDB 5T9U; X-ray; 2.30 A; A/B/C/D=1-164 PDB 5T9W; X-ray; 2.00 A; A=2-165 PDB 5T9Z; X-ray; 1.40 A; A=2-164 PDB 5TA2; X-ray; 1.48 A; A=2-164 PDB 5TA4; X-ray; 1.50 A; A=2-165 PDBsum 1AK4; -; . PDBsum 1AWQ; -; . PDBsum 1AWR; -; . PDBsum 1AWS; -; . PDBsum 1AWT; -; . PDBsum 1AWU; -; . PDBsum 1AWV; -; . PDBsum 1BCK; -; . PDBsum 1CWA; -; . PDBsum 1CWB; -; . PDBsum 1CWC; -; . PDBsum 1CWF; -; . PDBsum 1CWH; -; . PDBsum 1CWI; -; . PDBsum 1CWJ; -; . PDBsum 1CWK; -; . PDBsum 1CWL; -; . PDBsum 1CWM; -; . PDBsum 1CWO; -; . PDBsum 1FGL; -; . PDBsum 1M63; -; . PDBsum 1M9C; -; . PDBsum 1M9D; -; . PDBsum 1M9E; -; . PDBsum 1M9F; -; . PDBsum 1M9X; -; . PDBsum 1M9Y; -; . PDBsum 1MF8; -; . PDBsum 1MIK; -; . PDBsum 1NMK; -; . PDBsum 1OCA; -; . PDBsum 1RMH; -; . PDBsum 1VBS; -; . PDBsum 1VBT; -; . PDBsum 1W8L; -; . PDBsum 1W8M; -; . PDBsum 1W8V; -; . PDBsum 1YND; -; . PDBsum 1ZKF; -; . PDBsum 2ALF; -; . PDBsum 2CPL; -; . PDBsum 2CYH; -; . PDBsum 2MS4; -; . PDBsum 2MZU; -; . PDBsum 2N0T; -; . PDBsum 2RMA; -; . PDBsum 2RMB; -; . PDBsum 2X25; -; . PDBsum 2X2A; -; . PDBsum 2X2C; -; . PDBsum 2X2D; -; . PDBsum 2XGY; -; . PDBsum 3CYH; -; . PDBsum 3CYS; -; . PDBsum 3K0M; -; . PDBsum 3K0N; -; . PDBsum 3K0O; -; . PDBsum 3K0P; -; . PDBsum 3K0Q; -; . PDBsum 3K0R; -; . PDBsum 3ODI; -; . PDBsum 3ODL; -; . PDBsum 3RDD; -; . PDBsum 4CYH; -; . PDBsum 4IPZ; -; . PDBsum 4N1M; -; . PDBsum 4N1N; -; . PDBsum 4N1O; -; . PDBsum 4N1P; -; . PDBsum 4N1Q; -; . PDBsum 4N1R; -; . PDBsum 4N1S; -; . PDBsum 4YUG; -; . PDBsum 4YUH; -; . PDBsum 4YUI; -; . PDBsum 4YUJ; -; . PDBsum 4YUK; -; . PDBsum 4YUL; -; . PDBsum 4YUM; -; . PDBsum 4YUN; -; . PDBsum 4YUO; -; . PDBsum 4YUP; -; . PDBsum 5CYH; -; . PDBsum 5F66; -; . PDBsum 5FJB; -; . PDBsum 5KUL; -; . PDBsum 5KUN; -; . PDBsum 5KUO; -; . PDBsum 5KUQ; -; . PDBsum 5KUR; -; . PDBsum 5KUS; -; . PDBsum 5KUU; -; . PDBsum 5KUV; -; . PDBsum 5KUW; -; . PDBsum 5KUZ; -; . PDBsum 5KV0; -; . PDBsum 5KV1; -; . PDBsum 5KV2; -; . PDBsum 5KV3; -; . PDBsum 5KV4; -; . PDBsum 5KV5; -; . PDBsum 5KV6; -; . PDBsum 5KV7; -; . PDBsum 5T9U; -; . PDBsum 5T9W; -; . PDBsum 5T9Z; -; . PDBsum 5TA2; -; . PDBsum 5TA4; -; . ProteinModelPortal P62937; -; . SMR P62937; -; . BioGrid 111474; 109; . DIP DIP-6080N; -; . IntAct P62937; 65; . MINT MINT-4999116; -; . STRING 9606.ENSP00000419425; -; . BindingDB P62937; -; . ChEMBL CHEMBL1949; -; . DrugBank DB01742; (3r)-1-Acetyl-3-Methylpiperidine; . DrugBank DB00091; Cyclosporine; . DrugBank DB02419; Ethyl Oxo(Piperidin-1-Yl)Acetate; . DrugBank DB00172; L-Proline; . GuidetoPHARMACOLOGY 2751; -; . iPTMnet P62937; -; . PhosphoSitePlus P62937; -; . SwissPalm P62937; -; . BioMuta PPIA; -; . DMDM 51702775; -; . DOSAC-COBS-2DPAGE P62937; -; . OGP P62937; -; . REPRODUCTION-2DPAGE IPI00419585; -; . REPRODUCTION-2DPAGE P62937; -; . SWISS-2DPAGE P62937; -; . UCD-2DPAGE P62937; -; . EPD P62937; -; . PaxDb P62937; -; . PeptideAtlas P62937; -; . PRIDE P62937; -; . TopDownProteomics P62937-1; -. [P62937-1]; . DNASU 5478; -; . Ensembl ENST00000355968; ENSP00000430817; ENSG00000196262. [P62937-2]; . Ensembl ENST00000468812; ENSP00000419425; ENSG00000196262. [P62937-1]; . Ensembl ENST00000489459; ENSP00000427976; ENSG00000196262. [P62937-2]; . Ensembl ENST00000620047; ENSP00000479961; ENSG00000196262. [P62937-2]; . GeneID 5478; -; . KEGG hsa:5478; -; . UCSC uc064djo.1; human. [P62937-1]; . CTD 5478; -; . DisGeNET 5478; -; . GeneCards PPIA; -; . HGNC HGNC:9253; PPIA; . HPA CAB004655; -; . HPA HPA058345; -; . MIM 123840; gene; . neXtProt NX_P62937; -; . OpenTargets ENSG00000196262; -; . PharmGKB PA33574; -; . eggNOG KOG0865; Eukaryota; . eggNOG COG0652; LUCA; . GeneTree ENSGT00760000119119; -; . HOGENOM HOG000065981; -; . HOVERGEN HBG001065; -; . InParanoid P62937; -; . KO K03767; -; . OMA MRSAFFQ; -; . OrthoDB EOG091G0BGL; -; . PhylomeDB P62937; -; . TreeFam TF316719; -; . BRENDA 5.2.1.8; 2681; . Reactome R-HSA-114608; Platelet degranulation; . Reactome R-HSA-162585; Uncoating of the HIV Virion; . Reactome R-HSA-162588; Budding and maturation of HIV virion; . Reactome R-HSA-162592; Integration of provirus; . Reactome R-HSA-162594; Early Phase of HIV Life Cycle; . Reactome R-HSA-164516; Minus-strand DNA synthesis; . Reactome R-HSA-164525; Plus-strand DNA synthesis; . Reactome R-HSA-173107; Binding and entry of HIV virion; . Reactome R-HSA-175474; Assembly Of The HIV Virion; . Reactome R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection; . Reactome R-HSA-210991; Basigin interactions; . Reactome R-HSA-6798695; Neutrophil degranulation; . ChiTaRS PPIA; human; . EvolutionaryTrace P62937; -; . GeneWiki Peptidylprolyl_isomerase_A; -; . GenomeRNAi 5478; -; . PRO PR:P62937; -; . Proteomes UP000005640; Chromosome 7; . Bgee ENSG00000196262; -; . CleanEx HS_PPIA; -; . ExpressionAtlas P62937; baseline and differential; . Genevisible P62937; HS; . GO GO:0005829; C:cytosol; IDA:UniProtKB; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:0005615; C:extracellular space; IDA:UniProtKB; . GO GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome; . GO GO:0005925; C:focal adhesion; IDA:UniProtKB; . GO GO:0016020; C:membrane; IDA:UniProtKB; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0034774; C:secretory granule lumen; TAS:Reactome; . GO GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB; . GO GO:0003723; F:RNA binding; IDA:UniProtKB; . GO GO:0051082; F:unfolded protein binding; TAS:UniProtKB; . GO GO:0046790; F:virion binding; NAS:UniProtKB; . GO GO:0030260; P:entry into host cell; TAS:Reactome; . GO GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome; . GO GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome; . GO GO:0050900; P:leukocyte migration; TAS:Reactome; . GO GO:0034389; P:lipid particle organization; IMP:UniProtKB; . GO GO:0043312; P:neutrophil degranulation; TAS:Reactome; . GO GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB; . GO GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB; . GO GO:0006457; P:protein folding; TAS:UniProtKB; . GO GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB; . GO GO:0045069; P:regulation of viral genome replication; IMP:UniProtKB; . GO GO:0006278; P:RNA-dependent DNA biosynthetic process; TAS:Reactome; . GO GO:0019061; P:uncoating of virus; TAS:Reactome; . GO GO:0019058; P:viral life cycle; TAS:Reactome; . GO GO:0019076; P:viral release from host cell; TAS:UniProtKB; . GO GO:0019068; P:virion assembly; TAS:Reactome; . Gene3D 2.40.100.10; -; 1; . InterPro IPR029000; Cyclophilin-like_dom; . InterPro IPR024936; Cyclophilin-type_PPIase; . InterPro IPR020892; Cyclophilin-type_PPIase_CS; . InterPro IPR002130; Cyclophilin-type_PPIase_dom; . PANTHER PTHR11071; PTHR11071; 1; . Pfam PF00160; Pro_isomerase; 1; . PIRSF PIRSF001467; Peptidylpro_ismrse; 1; . PRINTS PR00153; CSAPPISMRASE; . SUPFAM SSF50891; SSF50891; 1; . PROSITE PS00170; CSA_PPIASE_1; 1; . PROSITE PS50072; CSA_PPIASE_2; 1; .

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