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: P30405 USC-OGP 2-DE database:  P30405 P30405 General information about the entry View entry in simple text format Entry name PPIF_HUMAN Primary accession number P30405 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 F, mitochondrial; Short=PPIase F; EC=5.2.1.8; AltName: Full=Cyclophilin D; Short=CyP-D; Short=CypD; AltName: Full=Cyclophilin F; AltName: Full=Mitochondrial cyclophilin; Short=CyP-M; AltName: Full=Rotamase F; Flags: Precursor;. Gene name Name=PPIF Synonyms=CYP3 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-1063: pI=8.52; Mw=18003 SPOT OGP-1064: pI=8.75; Mw=17899 Cross-references UniProtKB/Swiss-Prot P30405; PPIF_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 PPIF_HUMAN Primary accession number P30405 Secondary accession number(s) Q2YDB7 Q5W131 Sequence was last modified on  April 1, 1993 (version 1) Annotations were last modified on  March 15, 2017 (version 165) Name and origin of the protein Description RecName: Full=Peptidyl-prolyl cis-trans isomerase F, mitochondrial; Short=PPIase F; EC=5.2.1.8; AltName: Full=Cyclophilin D; Short=CyP-D; Short=CypD; AltName: Full=Cyclophilin F; AltName: Full=Mitochondrial cyclophilin; Short=CyP-M; AltName: Full=Rotamase F; Flags: Precursor; Gene name Name=PPIF Synonyms=CYP3 Encoded on Name=PPIF; Synonyms=CYP3 Keywords 3D-structure; Acetylation; Alternative splicing; Apoptosis; Complete proteome; Isomerase; Mitochondrion; Necrosis; Reference proteome; Rotamase; S-nitrosylation; 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 M80254; AAA58434.1; -; mRNA EMBL AK296669; BAG59266.1; -; mRNA EMBL AL133481; CAH72725.1; -; Genomic_DNA EMBL AL391665; CAH72725.1; JOINED; Genomic_DNA EMBL AL391665; CAI40994.1; -; Genomic_DNA EMBL AL133481; CAI40994.1; JOINED; Genomic_DNA EMBL CH471083; EAW54645.1; -; Genomic_DNA EMBL BC005020; AAH05020.1; -; mRNA EMBL BC110299; AAI10300.1; -; mRNA CCDS CCDS7358.1; -. [P30405-1]; . PIR A41581; A41581; . RefSeq NP_005720.1; NM_005729.3. [P30405-1]; . UniGene Hs.381072; -; . PDB 2BIT; X-ray; 1.71 A; X=43-207 PDB 2BIU; X-ray; 1.71 A; X=43-207 PDB 2Z6W; X-ray; 0.96 A; A/B=44-207 PDB 3QYU; X-ray; 1.54 A; A=44-207 PDB 3R49; X-ray; 1.77 A; A=43-207 PDB 3R4G; X-ray; 1.05 A; A=43-207 PDB 3R54; X-ray; 1.35 A; A=43-207 PDB 3R56; X-ray; 1.40 A; A=43-207 PDB 3R57; X-ray; 1.71 A; A=43-207 PDB 3R59; X-ray; 1.10 A; A=43-207 PDB 3RCF; X-ray; 1.15 A; A=43-207 PDB 3RCG; X-ray; 0.97 A; A=43-207 PDB 3RCI; X-ray; 1.44 A; X=43-207 PDB 3RCK; X-ray; 1.26 A; X=43-207 PDB 3RCL; X-ray; 1.70 A; A=43-207 PDB 3RD9; X-ray; 1.40 A; X=43-207 PDB 3RDA; X-ray; 1.07 A; X=43-207 PDB 3RDB; X-ray; 1.55 A; A=43-207 PDB 3RDC; X-ray; 1.94 A; A=43-207 PDB 4J58; X-ray; 1.28 A; A=44-207 PDB 4J59; X-ray; 1.92 A; A=44-207 PDB 4J5A; X-ray; 1.58 A; X=44-207 PDB 4J5B; X-ray; 2.01 A; A=44-207 PDB 4J5C; X-ray; 1.03 A; X=44-207 PDB 4J5D; X-ray; 1.32 A; X=44-207 PDB 4J5E; X-ray; 0.99 A; X=44-207 PDB 4O8H; X-ray; 0.85 A; A=43-207 PDB 4O8I; X-ray; 1.45 A; A=43-207 PDB 4XNC; X-ray; 2.23 A; A=44-207 PDB 4ZSC; X-ray; 1.50 A; A=44-207 PDB 4ZSD; X-ray; 1.45 A; A=44-207 PDB 5A0E; X-ray; 1.25 A; A/B=43-207 PDB 5CBT; X-ray; 1.45 A; A=44-207 PDB 5CBU; X-ray; 1.40 A; A=44-207 PDB 5CBV; X-ray; 1.80 A; A=44-207 PDB 5CBW; X-ray; 1.80 A; A=44-207 PDB 5CCN; X-ray; 1.80 A; A=44-207 PDB 5CCQ; X-ray; 1.80 A; A=44-207 PDB 5CCR; X-ray; 1.90 A; A=44-207 PDB 5CCS; X-ray; 2.10 A; X=44-207 PDBsum 2BIT; -; . PDBsum 2BIU; -; . PDBsum 2Z6W; -; . PDBsum 3QYU; -; . PDBsum 3R49; -; . PDBsum 3R4G; -; . PDBsum 3R54; -; . PDBsum 3R56; -; . PDBsum 3R57; -; . PDBsum 3R59; -; . PDBsum 3RCF; -; . PDBsum 3RCG; -; . PDBsum 3RCI; -; . PDBsum 3RCK; -; . PDBsum 3RCL; -; . PDBsum 3RD9; -; . PDBsum 3RDA; -; . PDBsum 3RDB; -; . PDBsum 3RDC; -; . PDBsum 4J58; -; . PDBsum 4J59; -; . PDBsum 4J5A; -; . PDBsum 4J5B; -; . PDBsum 4J5C; -; . PDBsum 4J5D; -; . PDBsum 4J5E; -; . PDBsum 4O8H; -; . PDBsum 4O8I; -; . PDBsum 4XNC; -; . PDBsum 4ZSC; -; . PDBsum 4ZSD; -; . PDBsum 5A0E; -; . PDBsum 5CBT; -; . PDBsum 5CBU; -; . PDBsum 5CBV; -; . PDBsum 5CBW; -; . PDBsum 5CCN; -; . PDBsum 5CCQ; -; . PDBsum 5CCR; -; . PDBsum 5CCS; -; . ProteinModelPortal P30405; -; . SMR P30405; -; . BioGrid 115411; 35; . IntAct P30405; 14; . MINT MINT-3011711; -; . STRING 9606.ENSP00000225174; -; . BindingDB P30405; -; . ChEMBL CHEMBL3325306; -; . DrugBank DB02078; 1-Methoxy-2-[2-(2-Methoxy-Ethoxy]-Ethane; . DrugBank DB08168; 7-AMINO-4-METHYL-CHROMEN-2-ONE; . DrugBank DB00091; Cyclosporine; . DrugBank DB00172; L-Proline; . iPTMnet P30405; -; . PhosphoSitePlus P30405; -; . SwissPalm P30405; -; . BioMuta PPIF; -; . DMDM 231968; -; . OGP P30405; -; . UCD-2DPAGE P30405; -; . EPD P30405; -; . MaxQB P30405; -; . PaxDb P30405; -; . PeptideAtlas P30405; -; . PRIDE P30405; -; . TopDownProteomics P30405-1; -. [P30405-1]; . DNASU 10105; -; . Ensembl ENST00000225174; ENSP00000225174; ENSG00000108179. [P30405-1]; . GeneID 10105; -; . KEGG hsa:10105; -; . UCSC uc001kai.4; human. [P30405-1]; . CTD 10105; -; . DisGeNET 10105; -; . GeneCards PPIF; -; . HGNC HGNC:9259; PPIF; . HPA HPA077416; -; . MIM 604486; gene; . neXtProt NX_P30405; -; . OpenTargets ENSG00000108179; -; . PharmGKB PA33584; -; . eggNOG KOG0865; Eukaryota; . eggNOG COG0652; LUCA; . GeneTree ENSGT00760000119119; -; . HOGENOM HOG000065981; -; . HOVERGEN HBG001065; -; . InParanoid P30405; -; . KO K09565; -; . OMA VIPAFMC; -; . OrthoDB EOG091G0BGL; -; . PhylomeDB P30405; -; . TreeFam TF312801; -; . BRENDA 5.2.1.8; 2681; . ChiTaRS PPIF; human; . EvolutionaryTrace P30405; -; . GeneWiki PPIF; -; . GenomeRNAi 10105; -; . PRO PR:P30405; -; . Proteomes UP000005640; Chromosome 10; . Bgee ENSG00000108179; -; . CleanEx HS_PPIF; -; . ExpressionAtlas P30405; baseline and differential; . Genevisible P30405; HS; . GO GO:0016020; C:membrane; TAS:ProtInc; . GO GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl; . GO GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell; . GO GO:0005739; C:mitochondrion; IDA:HPA; . GO GO:0016018; F:cyclosporin A binding; IEA:Ensembl; . GO GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW; . GO GO:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl; . GO GO:0071243; P:cellular response to arsenic-containing substance; ISS:UniProtKB; . GO GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB; . GO GO:0070301; P:cellular response to hydrogen peroxide; IMP:UniProtKB; . GO GO:0070266; P:necroptotic process; IEA:Ensembl; . GO GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB; . GO GO:0032780; P:negative regulation of ATPase activity; ISS:UniProtKB; . GO GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB; . GO GO:0090324; P:negative regulation of oxidative phosphorylation; ISS:UniProtKB; . GO GO:2000276; P:negative regulation of oxidative phosphorylation uncoupler activity; ISS:UniProtKB; . GO GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:UniProtKB; . GO GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISS:UniProtKB; . GO GO:0006457; P:protein folding; IEA:InterPro; . GO GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:UniProtKB; . GO GO:1902445; P:regulation of mitochondrial membrane permeability involved in programmed necrotic cell death; IMP:UniProtKB; . GO GO:0010939; P:regulation of necrotic cell death; IEA:Ensembl; . GO GO:0010849; P:regulation of proton-transporting ATPase activity; rotational mechanism; ISS:UniProtKB GO GO:0002931; P:response to ischemia; ISS:UniProtKB; . 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; . PRINTS PR00153; CSAPPISMRASE; . SUPFAM SSF50891; SSF50891; 1; . PROSITE PS00170; CSA_PPIASE_1; 1; . PROSITE PS50072; CSA_PPIASE_2; 1; .

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