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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: PPIA_HUMAN




USC-OGP 2-DE database:  PPIA_HUMAN


PPIA_HUMAN


General information about the entry
View entry in simple text format
Entry namePPIA_HUMAN
Primary accession numberP62937
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 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 nameName=PPIA
Synonyms=CYPA
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

UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10}
Homo sapiens (Human)
UVEAL_MELANOMA_3-10
  map experimental info
 
UVEAL_MELANOMA_3-10

MAP LOCATIONS:
pI=6.89; Mw=16684
pI=7.49; Mw=16158
pI=6.67; Mw=15436

Cross-references
UniProtKB/Swiss-ProtP62937; 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 namePPIA_HUMAN
Primary accession numberP62937
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
DescriptionRecName: 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 nameName=PPIA
Synonyms=CYPA
Encoded onName=PPIA; Synonyms=CYPA
Keywords3D-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
EMBLY00052; CAA68264.1; -; mRNA
EMBLX52851; CAA37039.1; -; Genomic_DNA
EMBLAK290085; BAF82774.1; -; mRNA
EMBLAK293003; BAF85692.1; -; mRNA
EMBLCR456707; CAG32988.1; -; mRNA
EMBLAB451307; BAG70121.1; -; mRNA
EMBLAB451438; BAG70252.1; -; mRNA
EMBLAY739283; AAU13906.1; -; Genomic_DNA
EMBLAC004854; -; NOT_ANNOTATED_CDS; Genomic_DNA
EMBLAC013436; -; NOT_ANNOTATED_CDS; Genomic_DNA
EMBLBC000689; AAH00689.1; -; mRNA
EMBLBC003026; AAH03026.2; -; mRNA
EMBLBC005320; AAH05320.1; -; mRNA
EMBLBC005982; AAH05982.1; -; mRNA
EMBLBC007104; AAH07104.1; -; mRNA
EMBLBC013915; AAH13915.1; -; mRNA
EMBLBC073992; AAH73992.1; -; mRNA
EMBLBC093076; AAH93076.1; -; mRNA
EMBLBC106030; AAI06031.1; -; mRNA
EMBLBC137057; AAI37058.1; -; mRNA
EMBLBC137058; AAI37059.1; -; mRNA
CCDSCCDS5494.1; -. [P62937-1]; .
CCDSCCDS75592.1; -. [P62937-2]; .
PIRA94496; CSHUA; .
RefSeqNP_001287910.1; NM_001300981.1. [P62937-2]; .
RefSeqNP_066953.1; NM_021130.4. [P62937-1]; .
UniGeneHs.356331; -; .
PDB1AK4; X-ray; 2.36 A; A/B=1-165
PDB1AWQ; X-ray; 1.58 A; A=2-165
PDB1AWR; X-ray; 1.58 A; A/B/C/D/E/F=2-165
PDB1AWS; X-ray; 2.55 A; A=2-165
PDB1AWT; X-ray; 2.55 A; A/B/C/D/E/F=2-165
PDB1AWU; X-ray; 2.34 A; A=2-165
PDB1AWV; X-ray; 2.34 A; A/B/C/D/E/F=2-165
PDB1BCK; X-ray; 1.80 A; A=1-165
PDB1CWA; X-ray; 2.10 A; A=1-165
PDB1CWB; X-ray; 2.20 A; A=1-165
PDB1CWC; X-ray; 1.86 A; A=1-165
PDB1CWF; X-ray; 1.86 A; A=1-165
PDB1CWH; X-ray; 1.86 A; A=1-165
PDB1CWI; X-ray; 1.90 A; A=1-165
PDB1CWJ; X-ray; 1.80 A; A=1-165
PDB1CWK; X-ray; 1.80 A; A=1-165
PDB1CWL; X-ray; 1.80 A; A=1-165
PDB1CWM; X-ray; 2.00 A; A=1-165
PDB1CWO; X-ray; 1.86 A; A=1-165
PDB1FGL; X-ray; 1.80 A; A=1-165
PDB1M63; X-ray; 2.80 A; C/G=1-165
PDB1M9C; X-ray; 2.00 A; A/B=1-165
PDB1M9D; X-ray; 1.90 A; A/B=1-165
PDB1M9E; X-ray; 1.72 A; A/B=1-164
PDB1M9F; X-ray; 1.73 A; A/B=1-165
PDB1M9X; X-ray; 1.70 A; A/B/E/F=1-165
PDB1M9Y; X-ray; 1.90 A; A/B/E/F=1-165
PDB1MF8; X-ray; 3.10 A; C=1-165
PDB1MIK; X-ray; 1.76 A; A=1-165
PDB1NMK; X-ray; 2.10 A; A/B=1-165
PDB1OCA; NMR; -; A=1-165
PDB1RMH; X-ray; 2.40 A; A/B=2-165
PDB1VBS; X-ray; 2.00 A; A=1-165
PDB1VBT; X-ray; 2.30 A; A/B=1-165
PDB1W8L; X-ray; 1.80 A; A=2-165
PDB1W8M; X-ray; 1.65 A; A=2-165
PDB1W8V; X-ray; 1.70 A; A=2-165
PDB1YND; X-ray; 1.60 A; A/B=1-165
PDB1ZKF; X-ray; 2.55 A; A/B=1-165
PDB2ALF; X-ray; 1.90 A; A=2-165
PDB2CPL; X-ray; 1.63 A; A=1-165
PDB2CYH; X-ray; 1.64 A; A=2-165
PDB2MS4; NMR; -; A=1-165
PDB2MZU; NMR; -; A=1-165
PDB2N0T; NMR; -; A=1-165
PDB2RMA; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=1-165
PDB2RMB; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=1-165
PDB2X25; X-ray; 1.20 A; B=2-165
PDB2X2A; X-ray; 1.40 A; A/B=1-165
PDB2X2C; X-ray; 2.41 A; K/M/O/Q/S=1-165
PDB2X2D; X-ray; 1.95 A; B/C=1-165
PDB2XGY; X-ray; 1.80 A; B=1-165
PDB3CYH; X-ray; 1.90 A; A=2-165
PDB3CYS; NMR; -; A=1-165
PDB3K0M; X-ray; 1.25 A; A=1-165
PDB3K0N; X-ray; 1.39 A; A=1-165
PDB3K0O; X-ray; 1.55 A; A=1-165
PDB3K0P; X-ray; 1.65 A; A=1-165
PDB3K0Q; X-ray; 2.32 A; A=1-165
PDB3K0R; X-ray; 2.42 A; A=1-165
PDB3ODI; X-ray; 2.20 A; A/C/E/G/I/K/M/O/Q/S=1-165
PDB3ODL; X-ray; 2.31 A; A/C/E/G/I/K/M/O/Q/S=1-165
PDB3RDD; X-ray; 2.14 A; A=1-165
PDB4CYH; X-ray; 2.10 A; A=2-165
PDB4IPZ; X-ray; 1.67 A; A=1-165
PDB4N1M; X-ray; 1.15 A; A=1-165
PDB4N1N; X-ray; 1.50 A; A=1-165
PDB4N1O; X-ray; 1.75 A; A=1-165
PDB4N1P; X-ray; 1.90 A; A=1-165
PDB4N1Q; X-ray; 1.65 A; A=1-165
PDB4N1R; X-ray; 1.80 A; A=1-165
PDB4N1S; X-ray; 1.47 A; A=1-165
PDB4YUG; X-ray; 1.48 A; A=1-165
PDB4YUH; X-ray; 1.34 A; A=1-165
PDB4YUI; X-ray; 1.38 A; A=1-165
PDB4YUJ; X-ray; 1.42 A; A=1-165
PDB4YUK; X-ray; 1.48 A; A=1-165
PDB4YUL; X-ray; 1.42 A; A=1-165
PDB4YUM; X-ray; 1.50 A; A=1-165
PDB4YUN; X-ray; 1.58 A; A=1-165
PDB4YUO; X-ray; 1.20 A; A=1-165
PDB4YUP; X-ray; 1.75 A; A=1-165
PDB5CYH; X-ray; 2.10 A; A=2-165
PDB5F66; X-ray; 1.15 A; A=1-165
PDB5FJB; EM; 9.00 A; C=2-165
PDB5KUL; X-ray; 1.70 A; A=2-165
PDB5KUN; X-ray; 1.70 A; A=2-165
PDB5KUO; X-ray; 1.70 A; A=2-165
PDB5KUQ; X-ray; 1.70 A; A=2-165
PDB5KUR; X-ray; 1.70 A; A=2-165
PDB5KUS; X-ray; 1.70 A; A=2-165
PDB5KUU; X-ray; 1.70 A; A=2-165
PDB5KUV; X-ray; 1.70 A; A=2-165
PDB5KUW; X-ray; 1.70 A; A=2-165
PDB5KUZ; X-ray; 1.70 A; A=2-165
PDB5KV0; X-ray; 1.70 A; A=2-165
PDB5KV1; X-ray; 1.70 A; A=2-165
PDB5KV2; X-ray; 1.70 A; A=2-165
PDB5KV3; X-ray; 1.70 A; A=2-165
PDB5KV4; X-ray; 1.70 A; A=2-165
PDB5KV5; X-ray; 1.70 A; A=2-165
PDB5KV6; X-ray; 1.70 A; A=2-165
PDB5KV7; X-ray; 1.70 A; A=2-165
PDB5T9U; X-ray; 2.30 A; A/B/C/D=1-164
PDB5T9W; X-ray; 2.00 A; A=2-165
PDB5T9Z; X-ray; 1.40 A; A=2-164
PDB5TA2; X-ray; 1.48 A; A=2-164
PDB5TA4; X-ray; 1.50 A; A=2-165
PDBsum1AK4; -; .
PDBsum1AWQ; -; .
PDBsum1AWR; -; .
PDBsum1AWS; -; .
PDBsum1AWT; -; .
PDBsum1AWU; -; .
PDBsum1AWV; -; .
PDBsum1BCK; -; .
PDBsum1CWA; -; .
PDBsum1CWB; -; .
PDBsum1CWC; -; .
PDBsum1CWF; -; .
PDBsum1CWH; -; .
PDBsum1CWI; -; .
PDBsum1CWJ; -; .
PDBsum1CWK; -; .
PDBsum1CWL; -; .
PDBsum1CWM; -; .
PDBsum1CWO; -; .
PDBsum1FGL; -; .
PDBsum1M63; -; .
PDBsum1M9C; -; .
PDBsum1M9D; -; .
PDBsum1M9E; -; .
PDBsum1M9F; -; .
PDBsum1M9X; -; .
PDBsum1M9Y; -; .
PDBsum1MF8; -; .
PDBsum1MIK; -; .
PDBsum1NMK; -; .
PDBsum1OCA; -; .
PDBsum1RMH; -; .
PDBsum1VBS; -; .
PDBsum1VBT; -; .
PDBsum1W8L; -; .
PDBsum1W8M; -; .
PDBsum1W8V; -; .
PDBsum1YND; -; .
PDBsum1ZKF; -; .
PDBsum2ALF; -; .
PDBsum2CPL; -; .
PDBsum2CYH; -; .
PDBsum2MS4; -; .
PDBsum2MZU; -; .
PDBsum2N0T; -; .
PDBsum2RMA; -; .
PDBsum2RMB; -; .
PDBsum2X25; -; .
PDBsum2X2A; -; .
PDBsum2X2C; -; .
PDBsum2X2D; -; .
PDBsum2XGY; -; .
PDBsum3CYH; -; .
PDBsum3CYS; -; .
PDBsum3K0M; -; .
PDBsum3K0N; -; .
PDBsum3K0O; -; .
PDBsum3K0P; -; .
PDBsum3K0Q; -; .
PDBsum3K0R; -; .
PDBsum3ODI; -; .
PDBsum3ODL; -; .
PDBsum3RDD; -; .
PDBsum4CYH; -; .
PDBsum4IPZ; -; .
PDBsum4N1M; -; .
PDBsum4N1N; -; .
PDBsum4N1O; -; .
PDBsum4N1P; -; .
PDBsum4N1Q; -; .
PDBsum4N1R; -; .
PDBsum4N1S; -; .
PDBsum4YUG; -; .
PDBsum4YUH; -; .
PDBsum4YUI; -; .
PDBsum4YUJ; -; .
PDBsum4YUK; -; .
PDBsum4YUL; -; .
PDBsum4YUM; -; .
PDBsum4YUN; -; .
PDBsum4YUO; -; .
PDBsum4YUP; -; .
PDBsum5CYH; -; .
PDBsum5F66; -; .
PDBsum5FJB; -; .
PDBsum5KUL; -; .
PDBsum5KUN; -; .
PDBsum5KUO; -; .
PDBsum5KUQ; -; .
PDBsum5KUR; -; .
PDBsum5KUS; -; .
PDBsum5KUU; -; .
PDBsum5KUV; -; .
PDBsum5KUW; -; .
PDBsum5KUZ; -; .
PDBsum5KV0; -; .
PDBsum5KV1; -; .
PDBsum5KV2; -; .
PDBsum5KV3; -; .
PDBsum5KV4; -; .
PDBsum5KV5; -; .
PDBsum5KV6; -; .
PDBsum5KV7; -; .
PDBsum5T9U; -; .
PDBsum5T9W; -; .
PDBsum5T9Z; -; .
PDBsum5TA2; -; .
PDBsum5TA4; -; .
ProteinModelPortalP62937; -; .
SMRP62937; -; .
BioGrid111474; 109; .
DIPDIP-6080N; -; .
IntActP62937; 65; .
MINTMINT-4999116; -; .
STRING9606.ENSP00000419425; -; .
BindingDBP62937; -; .
ChEMBLCHEMBL1949; -; .
DrugBankDB01742; (3r)-1-Acetyl-3-Methylpiperidine; .
DrugBankDB00091; Cyclosporine; .
DrugBankDB02419; Ethyl Oxo(Piperidin-1-Yl)Acetate; .
DrugBankDB00172; L-Proline; .
GuidetoPHARMACOLOGY2751; -; .
iPTMnetP62937; -; .
PhosphoSitePlusP62937; -; .
SwissPalmP62937; -; .
BioMutaPPIA; -; .
DMDM51702775; -; .
DOSAC-COBS-2DPAGEP62937; -; .
OGPP62937; -; .
REPRODUCTION-2DPAGEIPI00419585; -; .
REPRODUCTION-2DPAGEP62937; -; .
SWISS-2DPAGEP62937; -; .
UCD-2DPAGEP62937; -; .
EPDP62937; -; .
PaxDbP62937; -; .
PeptideAtlasP62937; -; .
PRIDEP62937; -; .
TopDownProteomicsP62937-1; -. [P62937-1]; .
DNASU5478; -; .
EnsemblENST00000355968; ENSP00000430817; ENSG00000196262. [P62937-2]; .
EnsemblENST00000468812; ENSP00000419425; ENSG00000196262. [P62937-1]; .
EnsemblENST00000489459; ENSP00000427976; ENSG00000196262. [P62937-2]; .
EnsemblENST00000620047; ENSP00000479961; ENSG00000196262. [P62937-2]; .
GeneID5478; -; .
KEGGhsa:5478; -; .
UCSCuc064djo.1; human. [P62937-1]; .
CTD5478; -; .
DisGeNET5478; -; .
GeneCardsPPIA; -; .
HGNCHGNC:9253; PPIA; .
HPACAB004655; -; .
HPAHPA058345; -; .
MIM123840; gene; .
neXtProtNX_P62937; -; .
OpenTargetsENSG00000196262; -; .
PharmGKBPA33574; -; .
eggNOGKOG0865; Eukaryota; .
eggNOGCOG0652; LUCA; .
GeneTreeENSGT00760000119119; -; .
HOGENOMHOG000065981; -; .
HOVERGENHBG001065; -; .
InParanoidP62937; -; .
KOK03767; -; .
OMAMRSAFFQ; -; .
OrthoDBEOG091G0BGL; -; .
PhylomeDBP62937; -; .
TreeFamTF316719; -; .
BRENDA5.2.1.8; 2681; .
ReactomeR-HSA-114608; Platelet degranulation; .
ReactomeR-HSA-162585; Uncoating of the HIV Virion; .
ReactomeR-HSA-162588; Budding and maturation of HIV virion; .
ReactomeR-HSA-162592; Integration of provirus; .
ReactomeR-HSA-162594; Early Phase of HIV Life Cycle; .
ReactomeR-HSA-164516; Minus-strand DNA synthesis; .
ReactomeR-HSA-164525; Plus-strand DNA synthesis; .
ReactomeR-HSA-173107; Binding and entry of HIV virion; .
ReactomeR-HSA-175474; Assembly Of The HIV Virion; .
ReactomeR-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection; .
ReactomeR-HSA-210991; Basigin interactions; .
ReactomeR-HSA-6798695; Neutrophil degranulation; .
ChiTaRSPPIA; human; .
EvolutionaryTraceP62937; -; .
GeneWikiPeptidylprolyl_isomerase_A; -; .
GenomeRNAi5478; -; .
PROPR:P62937; -; .
ProteomesUP000005640; Chromosome 7; .
BgeeENSG00000196262; -; .
CleanExHS_PPIA; -; .
ExpressionAtlasP62937; baseline and differential; .
GenevisibleP62937; HS; .
GOGO:0005829; C:cytosol; IDA:UniProtKB; .
GOGO:0070062; C:extracellular exosome; IDA:UniProtKB; .
GOGO:0005576; C:extracellular region; TAS:Reactome; .
GOGO:0005615; C:extracellular space; IDA:UniProtKB; .
GOGO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome; .
GOGO:0005925; C:focal adhesion; IDA:UniProtKB; .
GOGO:0016020; C:membrane; IDA:UniProtKB; .
GOGO:0005634; C:nucleus; IDA:UniProtKB; .
GOGO:0034774; C:secretory granule lumen; TAS:Reactome; .
GOGO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB; .
GOGO:0003723; F:RNA binding; IDA:UniProtKB; .
GOGO:0051082; F:unfolded protein binding; TAS:UniProtKB; .
GOGO:0046790; F:virion binding; NAS:UniProtKB; .
GOGO:0030260; P:entry into host cell; TAS:Reactome; .
GOGO:0075713; P:establishment of integrated proviral latency; TAS:Reactome; .
GOGO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome; .
GOGO:0050900; P:leukocyte migration; TAS:Reactome; .
GOGO:0034389; P:lipid particle organization; IMP:UniProtKB; .
GOGO:0043312; P:neutrophil degranulation; TAS:Reactome; .
GOGO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB; .
GOGO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB; .
GOGO:0006457; P:protein folding; TAS:UniProtKB; .
GOGO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB; .
GOGO:0045069; P:regulation of viral genome replication; IMP:UniProtKB; .
GOGO:0006278; P:RNA-dependent DNA biosynthetic process; TAS:Reactome; .
GOGO:0019061; P:uncoating of virus; TAS:Reactome; .
GOGO:0019058; P:viral life cycle; TAS:Reactome; .
GOGO:0019076; P:viral release from host cell; TAS:UniProtKB; .
GOGO:0019068; P:virion assembly; TAS:Reactome; .
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; .
PIRSFPIRSF001467; Peptidylpro_ismrse; 1; .
PRINTSPR00153; CSAPPISMRASE; .
SUPFAMSSF50891; SSF50891; 1; .
PROSITEPS00170; CSA_PPIASE_1; 1; .
PROSITEPS50072; CSA_PPIASE_2; 1; .



USC-OGP 2-DE database image


Gateways to other related servers


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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