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USC-OGP 2-DE database

Two-dimensional polyacrylamide gel electrophoresis database


USC-OGP 2-DE database 
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Searching in 'USC-OGP 2-DE database' for entry matching: PPIB_HUMAN




USC-OGP 2-DE database:  PPIB_HUMAN


PPIB_HUMAN


General information about the entry
View entry in simple text format
Entry namePPIB_HUMAN
Primary accession numberP23284
integrated into USC-OGP 2-DE database on January 17, 2017 (release 1)
2D Annotations were last modified onJanuary 17, 2017 (version 1)
General Annotations were last modified on April 5, 2017 (version 2)
Name and origin of the protein
DescriptionRecName: 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 nameName=PPIB
Synonyms=CYPB
Annotated speciesHomo sapiens (Human) [TaxID: 9606]
TaxonomyEukaryota; 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)
PLATELET_6-11
  map experimental info
 
PLATELET_6-11

MAP LOCATIONS:
pI=6.43; Mw=40454
pI=8.67; Mw=17794
pI=8.81; Mw=17639

Cross-references
UniProtKB/Swiss-ProtP23284; 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 namePPIB_HUMAN
Primary accession numberP23284
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
DescriptionRecName: 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 nameName=PPIB
Synonyms=CYPB
Encoded onName=PPIB; Synonyms=CYPB
Keywords3D-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
EMBLM63573; AAA36601.1; -; mRNA
EMBLAK291149; BAF83838.1; -; mRNA
EMBLCR456829; CAG33110.1; -; mRNA
EMBLAY962310; AAX44050.1; -; Genomic_DNA
EMBLAC100840; -; NOT_ANNOTATED_CDS; Genomic_DNA
EMBLCH471082; EAW77669.1; -; Genomic_DNA
EMBLBC001125; AAH01125.1; -; mRNA
EMBLBC008848; AAH08848.1; -; mRNA
EMBLBC020800; AAH20800.1; -; mRNA
EMBLBC032138; AAH32138.1; -; mRNA
EMBLM60857; AAA52150.1; ALT_INIT; mRNA
EMBLM60457; AAA35733.1; -; mRNA
CCDSCCDS10191.1; -; .
PIRA39118; CSHUB; .
RefSeqNP_000933.1; NM_000942.4; .
UniGeneHs.434937; -; .
PDB1CYN; X-ray; 1.85 A; A=39-216
PDB3ICH; X-ray; 1.20 A; A=34-216
PDB3ICI; X-ray; 1.70 A; A/B=34-216
PDBsum1CYN; -; .
PDBsum3ICH; -; .
PDBsum3ICI; -; .
ProteinModelPortalP23284; -; .
SMRP23284; -; .
BioGrid111475; 92; .
IntActP23284; 32; .
MINTMINT-1142578; -; .
STRING9606.ENSP00000300026; -; .
BindingDBP23284; -; .
ChEMBLCHEMBL2075; -; .
DrugBankDB00172; L-Proline; .
iPTMnetP23284; -; .
PhosphoSitePlusP23284; -; .
SwissPalmP23284; -; .
BioMutaPPIB; -; .
DMDM215273869; -; .
OGPP23284; -; .
REPRODUCTION-2DPAGEIPI00646304; -; .
SWISS-2DPAGEP23284; -; .
EPDP23284; -; .
MaxQBP23284; -; .
PaxDbP23284; -; .
PeptideAtlasP23284; -; .
PRIDEP23284; -; .
TopDownProteomicsP23284; -; .
DNASU5479; -; .
EnsemblENST00000300026; ENSP00000300026; ENSG00000166794; .
GeneID5479; -; .
KEGGhsa:5479; -; .
UCSCuc002and.4; human; .
CTD5479; -; .
DisGeNET5479; -; .
GeneCardsPPIB; -; .
HGNCHGNC:9255; PPIB; .
HPACAB011487; -; .
HPAHPA012720; -; .
MalaCardsPPIB; -; .
MIM123841; gene; .
MIM259440; phenotype; .
neXtProtNX_P23284; -; .
OpenTargetsENSG00000166794; -; .
Orphanet216804; Osteogenesis imperfecta type 2; .
Orphanet216812; Osteogenesis imperfecta type 3; .
Orphanet216820; Osteogenesis imperfecta type 4; .
PharmGKBPA33580; -; .
eggNOGKOG0880; Eukaryota; .
eggNOGENOG410Z0G4; LUCA; .
GeneTreeENSGT00760000119072; -; .
HOGENOMHOG000065981; -; .
HOVERGENHBG001065; -; .
InParanoidP23284; -; .
KOK03768; -; .
OMASPAYANE; -; .
OrthoDBEOG091G0BGL; -; .
PhylomeDBP23284; -; .
TreeFamTF354259; -; .
BRENDA5.2.1.8; 2681; .
ReactomeR-HSA-1650814; Collagen biosynthesis and modifying enzymes; .
ChiTaRSPPIB; human; .
EvolutionaryTraceP23284; -; .
GeneWikiPPIB; -; .
GenomeRNAi5479; -; .
PROPR:P23284; -; .
ProteomesUP000005640; Chromosome 15; .
BgeeENSG00000166794; -; .
CleanExHS_PPIB; -; .
GenevisibleP23284; HS; .
GOGO:0005783; C:endoplasmic reticulum; IDA:UniProtKB; .
GOGO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl; .
GOGO:0005788; C:endoplasmic reticulum lumen; NAS:UniProtKB; .
GOGO:0070062; C:extracellular exosome; IDA:UniProtKB; .
GOGO:0005925; C:focal adhesion; IDA:UniProtKB; .
GOGO:0032991; C:macromolecular complex; ISS:UniProtKB; .
GOGO:0042470; C:melanosome; IEA:UniProtKB-SubCell; .
GOGO:0016020; C:membrane; IDA:UniProtKB; .
GOGO:0005634; C:nucleus; IDA:UniProtKB; .
GOGO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase; .
GOGO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl; .
GOGO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; ISS:UniProtKB; .
GOGO:0032403; F:protein complex binding; ISS:UniProtKB; .
GOGO:0003723; F:RNA binding; IDA:UniProtKB; .
GOGO:0070063; F:RNA polymerase binding; IPI:AgBase; .
GOGO:0051082; F:unfolded protein binding; TAS:ProtInc; .
GOGO:0060348; P:bone development; IMP:UniProtKB; .
GOGO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB; .
GOGO:0044829; P:positive regulation by host of viral genome replication; IMP:AgBase; .
GOGO:0044794; P:positive regulation by host of viral process; IMP:AgBase; .
GOGO:0040018; P:positive regulation of multicellular organism growth; IMP:UniProtKB; .
GOGO:0000413; P:protein peptidyl-prolyl isomerization; ISS:UniProtKB; .
GOGO:0050821; P:protein stabilization; IMP:UniProtKB; .
Gene3D2.40.100.10; -; 1; .
InterProIPR029000; Cyclophilin-like_dom; .
InterProIPR024936; Cyclophilin-type_PPIase; .
InterProIPR020892; Cyclophilin-type_PPIase_CS; .
InterProIPR002130; Cyclophilin-type_PPIase_dom; .
PANTHERPTHR11071; PTHR11071; 1; .
PfamPF00160; Pro_isomerase; 1; .
PRINTSPR00153; CSAPPISMRASE; .
SUPFAMSSF50891; SSF50891; 1; .
PROSITEPS00170; CSA_PPIASE_1; 1; .
PROSITEPS50072; CSA_PPIASE_2; 1; .



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Database constructed and maintained by Angel Garcia, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server

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