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P62937

- PPIA_HUMAN

UniProt

P62937 - PPIA_HUMAN

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Protein

Peptidyl-prolyl cis-trans isomerase A

Gene
PPIA, CYPA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.

GO - Molecular functioni

  1. peptide binding Source: UniProtKB-KW
  2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. unfolded protein binding Source: UniProtKB
  6. virion binding Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. entry into host cell Source: Reactome
  3. establishment of integrated proviral latency Source: Reactome
  4. leukocyte migration Source: Reactome
  5. lipid particle organization Source: UniProtKB
  6. platelet activation Source: Reactome
  7. platelet degranulation Source: Reactome
  8. positive regulation of protein secretion Source: UniProtKB
  9. positive regulation of viral genome replication Source: UniProtKB
  10. protein folding Source: UniProtKB
  11. protein peptidyl-prolyl isomerization Source: UniProtKB
  12. regulation of viral genome replication Source: UniProtKB
  13. RNA-dependent DNA replication Source: Reactome
  14. uncoating of virus Source: Reactome
  15. viral life cycle Source: Reactome
  16. viral process Source: Reactome
  17. viral release from host cell Source: UniProtKB
  18. virion assembly Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

Cyclosporin

Enzyme and pathway databases

ReactomeiREACT_12560. Basigin interactions.
REACT_6266. Early Phase of HIV Life Cycle.
REACT_6359. Budding and maturation of HIV virion.
REACT_6818. Assembly Of The HIV Virion.
REACT_6903. Binding and entry of HIV virion.
REACT_6918. Integration of provirus.
REACT_6965. Uncoating of the HIV Virion.
REACT_9037. Plus-strand DNA synthesis.
REACT_9055. Minus-strand DNA synthesis.
REACT_9406. APOBEC3G mediated resistance to HIV-1 infection.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase A (EC:5.2.1.8)
Short name:
PPIase A
Alternative name(s):
Cyclophilin A
Cyclosporin A-binding protein
Rotamase A
Cleaved into the following chain:
Gene namesi
Name:PPIA
Synonyms:CYPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:9253. PPIA.

Subcellular locationi

Cytoplasm. Secreted
Note: Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, and mediates ERK1/2 activation.1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProt
  4. extracellular vesicular exosome Source: UniProt
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi121 – 1211W → A: 200-fold decrease of sensitivity to CsA. 1 Publication
Mutagenesisi121 – 1211W → F: 75-fold decrease of sensitivity to CsA. 1 Publication

Organism-specific databases

PharmGKBiPA33574.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 165165Peptidyl-prolyl cis-trans isomerase APRO_0000423240Add
BLAST
Initiator methioninei1 – 11Removed; alternate4 Publications
Chaini2 – 165164Peptidyl-prolyl cis-trans isomerase A, N-terminally processedPRO_0000064115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei2 – 21N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed2 Publications
Modified residuei28 – 281N6-acetyllysine; alternate1 Publication
Cross-linki28 – 28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei44 – 441N6-acetyllysine1 Publication
Modified residuei76 – 761N6-acetyllysine1 Publication
Modified residuei82 – 821N6-acetyllysine1 Publication
Modified residuei93 – 931Phosphothreonine1 Publication
Glycosylationi108 – 1081N-linked (GlcNAc...) Reviewed prediction
Modified residuei125 – 1251N6-acetyllysine2 Publications
Modified residuei131 – 1311N6-acetyllysine1 Publication
Modified residuei133 – 1331N6-acetyllysine By similarity

Post-translational modificationi

Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization and stabilizes cis rather than trans forms of the HIV-1 capsid. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition.2 Publications

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP62937.
PaxDbiP62937.
PeptideAtlasiP62937.
PRIDEiP62937.

2D gel databases

DOSAC-COBS-2DPAGEP62937.
OGPiP62937.
REPRODUCTION-2DPAGEIPI00419585.
P62937.
SWISS-2DPAGEP62937.
UCD-2DPAGEP62937.

PTM databases

PhosphoSiteiP62937.

Expressioni

Gene expression databases

ArrayExpressiP62937.
BgeeiP62937.
CleanExiHS_PPIA.
GenevestigatoriP62937.

Organism-specific databases

HPAiCAB004655.

Interactioni

Subunit structurei

Interacts with HIV-1 Capsid protein.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB82EBI-437708,EBI-6927873From a different organism.
gagQ724976EBI-437708,EBI-1036263From a different organism.
PTPRNQ168493EBI-437708,EBI-728153
SUPT5HO002672EBI-437708,EBI-710464

Protein-protein interaction databases

BioGridi111474. 62 interactions.
DIPiDIP-6080N.
IntActiP62937. 38 interactions.
MINTiMINT-4999116.
STRINGi9606.ENSP00000419425.

Structurei

Secondary structure

1
165
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128
Beta strandi15 – 2410
Turni26 – 283
Helixi30 – 4112
Turni42 – 443
Beta strandi52 – 576
Turni58 – 603
Beta strandi61 – 644
Turni67 – 693
Beta strandi70 – 734
Beta strandi78 – 814
Beta strandi97 – 1004
Beta strandi102 – 1043
Beta strandi108 – 1103
Beta strandi112 – 1176
Helixi120 – 1223
Turni123 – 1253
Beta strandi128 – 1347
Helixi136 – 1438
Helixi148 – 1503
Turni153 – 1553
Beta strandi156 – 1649

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AK4X-ray2.36A/B1-165[»]
1AWQX-ray1.58A2-165[»]
1AWRX-ray1.58A/B/C/D/E/F2-165[»]
1AWSX-ray2.55A2-165[»]
1AWTX-ray2.55A/B/C/D/E/F2-165[»]
1AWUX-ray2.34A2-165[»]
1AWVX-ray2.34A/B/C/D/E/F2-165[»]
1BCKX-ray1.80A1-165[»]
1CWAX-ray2.10A1-165[»]
1CWBX-ray2.20A1-165[»]
1CWCX-ray1.86A1-165[»]
1CWFX-ray1.86A1-165[»]
1CWHX-ray1.86A1-165[»]
1CWIX-ray1.90A1-165[»]
1CWJX-ray1.80A1-165[»]
1CWKX-ray1.80A1-165[»]
1CWLX-ray1.80A1-165[»]
1CWMX-ray2.00A1-165[»]
1CWOX-ray1.86A1-165[»]
1FGLX-ray1.80A1-165[»]
1M63X-ray2.80C/G1-165[»]
1M9CX-ray2.00A/B1-165[»]
1M9DX-ray1.90A/B1-165[»]
1M9EX-ray1.72A/B1-164[»]
1M9FX-ray1.73A/B1-165[»]
1M9XX-ray1.70A/B/E/F1-165[»]
1M9YX-ray1.90A/B/E/F1-165[»]
1MF8X-ray3.10C1-165[»]
1MIKX-ray1.76A1-165[»]
1NMKX-ray2.10A/B1-165[»]
1OCANMR-A1-165[»]
1RMHX-ray2.40A/B2-165[»]
1VBSX-ray2.00A1-165[»]
1VBTX-ray2.30A/B1-165[»]
1W8LX-ray1.80A2-165[»]
1W8MX-ray1.65A2-165[»]
1W8VX-ray1.70A2-165[»]
1YNDX-ray1.60A/B1-165[»]
1ZKFX-ray2.55A/B1-165[»]
2ALFX-ray1.90A2-165[»]
2CPLX-ray1.63A1-165[»]
2CYHX-ray1.64A2-165[»]
2RMAX-ray2.10A/C/E/G/I/K/M/O/Q/S1-165[»]
2RMBX-ray2.10A/C/E/G/I/K/M/O/Q/S1-165[»]
2X25X-ray1.20B2-165[»]
2X2AX-ray1.40A/B1-165[»]
2X2CX-ray2.41K/M/O/Q/S1-165[»]
2X2DX-ray1.95B/C1-165[»]
2XGYX-ray1.80B1-165[»]
3CYHX-ray1.90A2-165[»]
3CYSNMR-A1-165[»]
3K0MX-ray1.25A1-165[»]
3K0NX-ray1.39A1-165[»]
3K0OX-ray1.55A1-165[»]
3K0PX-ray1.65A1-165[»]
3K0QX-ray2.32A1-165[»]
3K0RX-ray2.42A1-165[»]
3ODIX-ray2.20A/C/E/G/I/K/M/O/Q/S1-165[»]
3ODLX-ray2.31A/C/E/G/I/K/M/O/Q/S1-165[»]
3RDDX-ray2.14A1-165[»]
4CYHX-ray2.10A2-165[»]
4IPZX-ray1.67A1-165[»]
5CYHX-ray2.10A2-165[»]
ProteinModelPortaliP62937.
SMRiP62937. Positions 2-165.

Miscellaneous databases

EvolutionaryTraceiP62937.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 163157PPIase cyclophilin-typeAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0652.
HOVERGENiHBG001065.
InParanoidiP62937.
KOiK03767.
OMAiHVERMVT.
PhylomeDBiP62937.
TreeFamiTF316719.

Family and domain databases

Gene3Di2.40.100.10. 1 hit.
InterProiIPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view]
PfamiPF00160. Pro_isomerase. 1 hit.
[Graphical view]
PIRSFiPIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSiPR00153. CSAPPISMRASE.
SUPFAMiSSF50891. SSF50891. 1 hit.
PROSITEiPS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62937-1 [UniParc]FASTAAdd to Basket

« Hide

MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG    50
SCFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM 100
ANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG 150
KTSKKITIAD CGQLE 165
Length:165
Mass (Da):18,012
Last modified:January 23, 2007 - v2
Checksum:i9B2E637A555E4434
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891I → T in AAH05982. 1 Publication
Sequence conflicti106 – 1061N → I in AAH07104. 1 Publication
Sequence conflicti165 – 1651E → D in CAG32988. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00052 mRNA. Translation: CAA68264.1.
X52851 Genomic DNA. Translation: CAA37039.1.
AK290085 mRNA. Translation: BAF82774.1.
CR456707 mRNA. Translation: CAG32988.1.
AB451307 mRNA. Translation: BAG70121.1.
AB451438 mRNA. Translation: BAG70252.1.
AY739283 Genomic DNA. Translation: AAU13906.1.
BC000689 mRNA. Translation: AAH00689.1.
BC003026 mRNA. Translation: AAH03026.2.
BC005320 mRNA. Translation: AAH05320.1.
BC005982 mRNA. Translation: AAH05982.1.
BC007104 mRNA. Translation: AAH07104.1.
BC013915 mRNA. Translation: AAH13915.1.
BC073992 mRNA. Translation: AAH73992.1.
BC106030 mRNA. Translation: AAI06031.1.
BC137057 mRNA. Translation: AAI37058.1.
BC137058 mRNA. Translation: AAI37059.1.
CCDSiCCDS5494.1.
PIRiA94496. CSHUA.
RefSeqiNP_066953.1. NM_021130.3.
UniGeneiHs.356331.

Genome annotation databases

EnsembliENST00000468812; ENSP00000419425; ENSG00000196262.
GeneIDi5478.
KEGGihsa:5478.
UCSCiuc003tlw.3. human.

Polymorphism databases

DMDMi51702775.

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Cyclophilin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00052 mRNA. Translation: CAA68264.1 .
X52851 Genomic DNA. Translation: CAA37039.1 .
AK290085 mRNA. Translation: BAF82774.1 .
CR456707 mRNA. Translation: CAG32988.1 .
AB451307 mRNA. Translation: BAG70121.1 .
AB451438 mRNA. Translation: BAG70252.1 .
AY739283 Genomic DNA. Translation: AAU13906.1 .
BC000689 mRNA. Translation: AAH00689.1 .
BC003026 mRNA. Translation: AAH03026.2 .
BC005320 mRNA. Translation: AAH05320.1 .
BC005982 mRNA. Translation: AAH05982.1 .
BC007104 mRNA. Translation: AAH07104.1 .
BC013915 mRNA. Translation: AAH13915.1 .
BC073992 mRNA. Translation: AAH73992.1 .
BC106030 mRNA. Translation: AAI06031.1 .
BC137057 mRNA. Translation: AAI37058.1 .
BC137058 mRNA. Translation: AAI37059.1 .
CCDSi CCDS5494.1.
PIRi A94496. CSHUA.
RefSeqi NP_066953.1. NM_021130.3.
UniGenei Hs.356331.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AK4 X-ray 2.36 A/B 1-165 [» ]
1AWQ X-ray 1.58 A 2-165 [» ]
1AWR X-ray 1.58 A/B/C/D/E/F 2-165 [» ]
1AWS X-ray 2.55 A 2-165 [» ]
1AWT X-ray 2.55 A/B/C/D/E/F 2-165 [» ]
1AWU X-ray 2.34 A 2-165 [» ]
1AWV X-ray 2.34 A/B/C/D/E/F 2-165 [» ]
1BCK X-ray 1.80 A 1-165 [» ]
1CWA X-ray 2.10 A 1-165 [» ]
1CWB X-ray 2.20 A 1-165 [» ]
1CWC X-ray 1.86 A 1-165 [» ]
1CWF X-ray 1.86 A 1-165 [» ]
1CWH X-ray 1.86 A 1-165 [» ]
1CWI X-ray 1.90 A 1-165 [» ]
1CWJ X-ray 1.80 A 1-165 [» ]
1CWK X-ray 1.80 A 1-165 [» ]
1CWL X-ray 1.80 A 1-165 [» ]
1CWM X-ray 2.00 A 1-165 [» ]
1CWO X-ray 1.86 A 1-165 [» ]
1FGL X-ray 1.80 A 1-165 [» ]
1M63 X-ray 2.80 C/G 1-165 [» ]
1M9C X-ray 2.00 A/B 1-165 [» ]
1M9D X-ray 1.90 A/B 1-165 [» ]
1M9E X-ray 1.72 A/B 1-164 [» ]
1M9F X-ray 1.73 A/B 1-165 [» ]
1M9X X-ray 1.70 A/B/E/F 1-165 [» ]
1M9Y X-ray 1.90 A/B/E/F 1-165 [» ]
1MF8 X-ray 3.10 C 1-165 [» ]
1MIK X-ray 1.76 A 1-165 [» ]
1NMK X-ray 2.10 A/B 1-165 [» ]
1OCA NMR - A 1-165 [» ]
1RMH X-ray 2.40 A/B 2-165 [» ]
1VBS X-ray 2.00 A 1-165 [» ]
1VBT X-ray 2.30 A/B 1-165 [» ]
1W8L X-ray 1.80 A 2-165 [» ]
1W8M X-ray 1.65 A 2-165 [» ]
1W8V X-ray 1.70 A 2-165 [» ]
1YND X-ray 1.60 A/B 1-165 [» ]
1ZKF X-ray 2.55 A/B 1-165 [» ]
2ALF X-ray 1.90 A 2-165 [» ]
2CPL X-ray 1.63 A 1-165 [» ]
2CYH X-ray 1.64 A 2-165 [» ]
2RMA X-ray 2.10 A/C/E/G/I/K/M/O/Q/S 1-165 [» ]
2RMB X-ray 2.10 A/C/E/G/I/K/M/O/Q/S 1-165 [» ]
2X25 X-ray 1.20 B 2-165 [» ]
2X2A X-ray 1.40 A/B 1-165 [» ]
2X2C X-ray 2.41 K/M/O/Q/S 1-165 [» ]
2X2D X-ray 1.95 B/C 1-165 [» ]
2XGY X-ray 1.80 B 1-165 [» ]
3CYH X-ray 1.90 A 2-165 [» ]
3CYS NMR - A 1-165 [» ]
3K0M X-ray 1.25 A 1-165 [» ]
3K0N X-ray 1.39 A 1-165 [» ]
3K0O X-ray 1.55 A 1-165 [» ]
3K0P X-ray 1.65 A 1-165 [» ]
3K0Q X-ray 2.32 A 1-165 [» ]
3K0R X-ray 2.42 A 1-165 [» ]
3ODI X-ray 2.20 A/C/E/G/I/K/M/O/Q/S 1-165 [» ]
3ODL X-ray 2.31 A/C/E/G/I/K/M/O/Q/S 1-165 [» ]
3RDD X-ray 2.14 A 1-165 [» ]
4CYH X-ray 2.10 A 2-165 [» ]
4IPZ X-ray 1.67 A 1-165 [» ]
5CYH X-ray 2.10 A 2-165 [» ]
ProteinModelPortali P62937.
SMRi P62937. Positions 2-165.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111474. 62 interactions.
DIPi DIP-6080N.
IntActi P62937. 38 interactions.
MINTi MINT-4999116.
STRINGi 9606.ENSP00000419425.

Chemistry

BindingDBi P62937.
ChEMBLi CHEMBL1949.
DrugBanki DB00091. Cyclosporine.
DB00172. L-Proline.
GuidetoPHARMACOLOGYi 2751.

PTM databases

PhosphoSitei P62937.

Polymorphism databases

DMDMi 51702775.

2D gel databases

DOSAC-COBS-2DPAGE P62937.
OGPi P62937.
REPRODUCTION-2DPAGE IPI00419585.
P62937.
SWISS-2DPAGE P62937.
UCD-2DPAGE P62937.

Proteomic databases

MaxQBi P62937.
PaxDbi P62937.
PeptideAtlasi P62937.
PRIDEi P62937.

Protocols and materials databases

DNASUi 5478.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000468812 ; ENSP00000419425 ; ENSG00000196262 .
GeneIDi 5478.
KEGGi hsa:5478.
UCSCi uc003tlw.3. human.

Organism-specific databases

CTDi 5478.
GeneCardsi GC07P044803.
HGNCi HGNC:9253. PPIA.
HPAi CAB004655.
MIMi 123840. gene.
neXtProti NX_P62937.
PharmGKBi PA33574.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0652.
HOVERGENi HBG001065.
InParanoidi P62937.
KOi K03767.
OMAi HVERMVT.
PhylomeDBi P62937.
TreeFami TF316719.

Enzyme and pathway databases

Reactomei REACT_12560. Basigin interactions.
REACT_6266. Early Phase of HIV Life Cycle.
REACT_6359. Budding and maturation of HIV virion.
REACT_6818. Assembly Of The HIV Virion.
REACT_6903. Binding and entry of HIV virion.
REACT_6918. Integration of provirus.
REACT_6965. Uncoating of the HIV Virion.
REACT_9037. Plus-strand DNA synthesis.
REACT_9055. Minus-strand DNA synthesis.
REACT_9406. APOBEC3G mediated resistance to HIV-1 infection.

Miscellaneous databases

ChiTaRSi PPIA. human.
EvolutionaryTracei P62937.
GeneWikii Peptidylprolyl_isomerase_A.
GenomeRNAii 5478.
NextBioi 21206.
PROi P62937.
SOURCEi Search...

Gene expression databases

ArrayExpressi P62937.
Bgeei P62937.
CleanExi HS_PPIA.
Genevestigatori P62937.

Family and domain databases

Gene3Di 2.40.100.10. 1 hit.
InterProi IPR029000. Cyclophilin-like_dom.
IPR024936. Cyclophilin-type_PPIase.
IPR020892. Cyclophilin-type_PPIase_CS.
IPR002130. Cyclophilin-type_PPIase_dom.
[Graphical view ]
Pfami PF00160. Pro_isomerase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001467. Peptidylpro_ismrse. 1 hit.
PRINTSi PR00153. CSAPPISMRASE.
SUPFAMi SSF50891. SSF50891. 1 hit.
PROSITEi PS00170. CSA_PPIASE_1. 1 hit.
PS50072. CSA_PPIASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complementary DNA for human T-cell cyclophilin."
    Haendler B., Hofer-Warbinek R., Hofer E.
    EMBO J. 6:947-950(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leukemic T-cell.
  2. "Characterization of the human cyclophilin gene and of related processed pseudogenes."
    Haendler B., Hofer E.
    Eur. J. Biochem. 190:477-482(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Subthalamic nucleus.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. NIEHS SNPs program
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow, Brain, Cervix, Colon, Lung, Skeletal muscle, Skin and Urinary bladder.
  8. "Identification of cyclophilin A from human decidual and placental tissue in the first trimester of pregnancy."
    Meier U., Beier-Hellwig K., Klug J., Linder D., Beier H.M.
    Hum. Reprod. 10:1305-1310(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-30.
  9. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19.
    Tissue: Platelet.
  10. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-31; 56-69; 77-118; 132-144 AND 155-165, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  11. Bienvenut W.V., Claeys D.
    Submitted (NOV-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-28, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  12. "Human and Escherichia coli cyclophilins: sensitivity to inhibition by the immunosuppressant cyclosporin A correlates with a specific tryptophan residue."
    Liu J., Chen C.-M., Walsh C.T.
    Biochemistry 30:2306-2310(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TRP-121.
  13. "Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B."
    Luban J., Bossolt K.L., Franke E.K., Kalpana G.V., Goff S.P.
    Cell 73:1067-1078(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 CAPSID PROTEIN.
  14. "Cyclophilin A is secreted by a vesicular pathway in vascular smooth muscle cells."
    Suzuki J., Jin Z.G., Meoli D.F., Matoba T., Berk B.C.
    Circ. Res. 98:811-817(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-44; LYS-76; LYS-82; LYS-125 AND LYS-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy."
    Kallen J., Spitzfaden C., Zurini M.G.M., Wider G., Widmer H., Wuethrich K., Walkinshaw M.D.
    Nature 353:276-279(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), STRUCTURE BY NMR.
  22. "Crystal structure of recombinant human T-cell cyclophilin A at 2.5-A resolution."
    Ke H., Zydowsky L.D., Liu J., Walsh C.T.
    Proc. Natl. Acad. Sci. U.S.A. 88:9483-9487(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  23. "X-ray structure of a decameric cyclophilin-cyclosporin crystal complex."
    Pfuegl G., Kallen J., Schirmer T., Jansonius J.N., Zurini M.G.M., Walkinshaw M.D.
    Nature 361:91-94(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH CYCLOPHILIN.
  24. "X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1-A resolution."
    Mikol V., Kallen J., Pfluegl G., Walkinshaw M.D.
    J. Mol. Biol. 234:1119-1130(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  25. "Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization."
    Zhao Y., Ke H.
    Biochemistry 35:7356-7361(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  26. "Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein."
    Vajdos F.F., Yoo S., Houseweart M., Sundquist W.I., Hill C.P.
    Protein Sci. 6:2297-2307(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS).
  27. "X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A."
    Kallen J., Mikol V., Taylor P., Walkinshaw M.D.
    J. Mol. Biol. 283:435-449(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  28. "Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes."
    Huai Q., Kim H.Y., Liu Y., Zhao Y., Mondragon A., Liu J.O., Ke H.
    Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
  29. "Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin."
    Jin L., Harrison S.C.
    Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
  30. "Solution structure of the cyclosporin A/cyclophilin complex by NMR."
    Theriault Y., Logan T.M., Meadows R., Yu L., Olejniczak E.T., Holzman T.F., Simmer R.L., Fesik S.W.
    Nature 361:88-91(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF COMPLEX WITH CYCLOPHILIN.
  31. "The NMR solution conformation of unligated human cyclophilin A."
    Ottiger M., Zerbe O., Guentert P., Wuethrich K.
    J. Mol. Biol. 272:64-81(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  32. "Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization."
    Lammers M., Neumann H., Chin J.W., James L.C.
    Nat. Chem. Biol. 6:331-337(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) ALONE AND IN COMPLEX WITH CYCLOSPORINE AND HIV-1 CAPSID, ACETYLATION AT LYS-125.

Entry informationi

Entry nameiPPIA_HUMAN
AccessioniPrimary (citable) accession number: P62937
Secondary accession number(s): A8K220
, P05092, Q3KQW3, Q6IBU5, Q96IX3, Q9BRU4, Q9BTY9, Q9UC61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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