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: P23284 USC-OGP 2-DE database:  P23284 P23284 General information about the entry View entry in simple text format Entry name PPIB_HUMAN Primary accession number P23284 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 B; Short=PPIase B; EC=5.2.1.8; AltName: Full=CYP-S1; AltName: Full=Cyclophilin B; AltName: Full=Rotamase B; AltName: Full=S-cyclophilin; Short=SCYLP; Flags: Precursor;. Gene name Name=PPIB Synonyms=CYPB 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-0954: pI=6.43; Mw=40454 SPOT OGP-1065: pI=8.67; Mw=17794 SPOT OGP-1067: pI=8.81; Mw=17639 Cross-references UniProtKB/Swiss-Prot P23284; PPIB_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 PPIB_HUMAN Primary accession number P23284 Secondary accession number(s) A8K534 Q6IBH5 Q9BVK5 Sequence was last modified on  November 25, 2008 (version 2) Annotations were last modified on  March 15, 2017 (version 183) Name and origin of the protein Description RecName: Full=Peptidyl-prolyl cis-trans isomerase B; Short=PPIase B; EC=5.2.1.8; AltName: Full=CYP-S1; AltName: Full=Cyclophilin B; AltName: Full=Rotamase B; AltName: Full=S-cyclophilin; Short=SCYLP; Flags: Precursor; Gene name Name=PPIB Synonyms=CYPB Encoded on Name=PPIB; Synonyms=CYPB Keywords 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Disease mutation; Dwarfism; Endoplasmic reticulum; Glycoprotein; Isomerase; Osteogenesis imperfecta; Polymorphism; Reference proteome; Rotamase; 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 M63573; AAA36601.1; -; mRNA EMBL AK291149; BAF83838.1; -; mRNA EMBL CR456829; CAG33110.1; -; mRNA EMBL AY962310; AAX44050.1; -; Genomic_DNA EMBL AC100840; -; NOT_ANNOTATED_CDS; Genomic_DNA EMBL CH471082; EAW77669.1; -; Genomic_DNA EMBL BC001125; AAH01125.1; -; mRNA EMBL BC008848; AAH08848.1; -; mRNA EMBL BC020800; AAH20800.1; -; mRNA EMBL BC032138; AAH32138.1; -; mRNA EMBL M60857; AAA52150.1; ALT_INIT; mRNA EMBL M60457; AAA35733.1; -; mRNA CCDS CCDS10191.1; -; . PIR A39118; CSHUB; . RefSeq NP_000933.1; NM_000942.4; . UniGene Hs.434937; -; . PDB 1CYN; X-ray; 1.85 A; A=39-216 PDB 3ICH; X-ray; 1.20 A; A=34-216 PDB 3ICI; X-ray; 1.70 A; A/B=34-216 PDBsum 1CYN; -; . PDBsum 3ICH; -; . PDBsum 3ICI; -; . ProteinModelPortal P23284; -; . SMR P23284; -; . BioGrid 111475; 92; . IntAct P23284; 32; . MINT MINT-1142578; -; . STRING 9606.ENSP00000300026; -; . BindingDB P23284; -; . ChEMBL CHEMBL2075; -; . DrugBank DB00172; L-Proline; . iPTMnet P23284; -; . PhosphoSitePlus P23284; -; . SwissPalm P23284; -; . BioMuta PPIB; -; . DMDM 215273869; -; . OGP P23284; -; . REPRODUCTION-2DPAGE IPI00646304; -; . SWISS-2DPAGE P23284; -; . EPD P23284; -; . MaxQB P23284; -; . PaxDb P23284; -; . PeptideAtlas P23284; -; . PRIDE P23284; -; . TopDownProteomics P23284; -; . DNASU 5479; -; . Ensembl ENST00000300026; ENSP00000300026; ENSG00000166794; . GeneID 5479; -; . KEGG hsa:5479; -; . UCSC uc002and.4; human; . CTD 5479; -; . DisGeNET 5479; -; . GeneCards PPIB; -; . HGNC HGNC:9255; PPIB; . HPA CAB011487; -; . HPA HPA012720; -; . MalaCards PPIB; -; . MIM 123841; gene; . MIM 259440; phenotype; . neXtProt NX_P23284; -; . OpenTargets ENSG00000166794; -; . Orphanet 216804; Osteogenesis imperfecta type 2; . Orphanet 216812; Osteogenesis imperfecta type 3; . Orphanet 216820; Osteogenesis imperfecta type 4; . PharmGKB PA33580; -; . eggNOG KOG0880; Eukaryota; . eggNOG ENOG410Z0G4; LUCA; . GeneTree ENSGT00760000119072; -; . HOGENOM HOG000065981; -; . HOVERGEN HBG001065; -; . InParanoid P23284; -; . KO K03768; -; . OMA SPAYANE; -; . OrthoDB EOG091G0BGL; -; . PhylomeDB P23284; -; . TreeFam TF354259; -; . BRENDA 5.2.1.8; 2681; . Reactome R-HSA-1650814; Collagen biosynthesis and modifying enzymes; . ChiTaRS PPIB; human; . EvolutionaryTrace P23284; -; . GeneWiki PPIB; -; . GenomeRNAi 5479; -; . PRO PR:P23284; -; . Proteomes UP000005640; Chromosome 15; . Bgee ENSG00000166794; -; . CleanEx HS_PPIB; -; . Genevisible P23284; HS; . GO GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB; . GO GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl; . GO GO:0005788; C:endoplasmic reticulum lumen; NAS:UniProtKB; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005925; C:focal adhesion; IDA:UniProtKB; . GO GO:0032991; C:macromolecular complex; ISS:UniProtKB; . GO GO:0042470; C:melanosome; IEA:UniProtKB-SubCell; . GO GO:0016020; C:membrane; IDA:UniProtKB; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase; . GO GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl; . GO GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB; . GO GO:0032403; F:protein complex binding; ISS:UniProtKB; . GO GO:0003723; F:RNA binding; IDA:UniProtKB; . GO GO:0070063; F:RNA polymerase binding; IPI:AgBase; . GO GO:0051082; F:unfolded protein binding; TAS:ProtInc; . GO GO:0060348; P:bone development; IMP:UniProtKB; . GO GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB; . GO GO:0044829; P:positive regulation by host of viral genome replication; IMP:AgBase; . GO GO:0044794; P:positive regulation by host of viral process; IMP:AgBase; . GO GO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB; . GO GO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB; . GO GO:0050821; P:protein stabilization; IMP: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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