Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

PPIA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • peptide binding Source: UniProtKB-KW
  • peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB
  • virion binding Source: UniProtKB

GO - Biological processi

  • entry into host cell Source: Reactome
  • establishment of integrated proviral latency Source: Reactome
  • fusion of virus membrane with host plasma membrane Source: Reactome
  • leukocyte migration Source: Reactome
  • lipid particle organization Source: UniProtKB
  • positive regulation of protein secretion Source: UniProtKB
  • positive regulation of viral genome replication Source: UniProtKB
  • protein folding Source: UniProtKB
  • protein peptidyl-prolyl isomerization Source: UniProtKB
  • regulation of viral genome replication Source: UniProtKB
  • RNA-dependent DNA biosynthetic process Source: Reactome
  • uncoating of virus Source: Reactome
  • viral life cycle Source: Reactome
  • viral release from host cell Source: UniProtKB
  • 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

BioCyciZFISH:HS07363-MONOMER.
BRENDAi5.2.1.8. 2681.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-162585. Uncoating of the HIV Virion.
R-HSA-162588. Budding and maturation of HIV virion.
R-HSA-162592. Integration of provirus.
R-HSA-162594. Early Phase of HIV Life Cycle.
R-HSA-164516. Minus-strand DNA synthesis.
R-HSA-164525. Plus-strand DNA synthesis.
R-HSA-173107. Binding and entry of HIV virion.
R-HSA-175474. Assembly Of The HIV Virion.
R-HSA-180689. APOBEC3G mediated resistance to HIV-1 infection.
R-HSA-210991. Basigin interactions.
R-HSA-6798695. Neutrophil degranulation.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9253. PPIA.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Secreted 1 Publication

  • 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.

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi121W → A: 200-fold decrease of sensitivity to CsA. 1 Publication1
Mutagenesisi121W → F: 75-fold decrease of sensitivity to CsA. 1 Publication1

Organism-specific databases

DisGeNETi5478.
OpenTargetsiENSG00000196262.
PharmGKBiPA33574.

Chemistry databases

ChEMBLiCHEMBL1949.
DrugBankiDB00091. Cyclosporine.
DB00172. L-Proline.
GuidetoPHARMACOLOGYi2751.

Polymorphism and mutation databases

BioMutaiPPIA.
DMDMi51702775.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004232401 – 165Peptidyl-prolyl cis-trans isomerase AAdd BLAST165
Initiator methionineiRemoved; alternateCombined sources4 Publications
ChainiPRO_00000641152 – 165Peptidyl-prolyl cis-trans isomerase A, N-terminally processedAdd BLAST164

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processedCombined sources1 Publication1
Modified residuei28N6-acetyllysine; alternateCombined sources1
Cross-linki28Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei44N6-acetyllysineCombined sources1
Modified residuei76N6-acetyllysineCombined sources1
Modified residuei77PhosphoserineCombined sources1
Modified residuei82N6-acetyllysineCombined sources1
Modified residuei93PhosphothreonineCombined sources1
Glycosylationi108N-linked (GlcNAc...)Sequence analysis1
Modified residuei125N6-acetyllysineCombined sources1 Publication1
Modified residuei131N6-acetyllysineCombined sources1
Modified residuei133N6-acetyllysineBy similarity1

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

EPDiP62937.
PaxDbiP62937.
PeptideAtlasiP62937.
PRIDEiP62937.
TopDownProteomicsiP62937-1. [P62937-1]

2D gel databases

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

PTM databases

iPTMnetiP62937.
PhosphoSitePlusiP62937.
SwissPalmiP62937.

Expressioni

Gene expression databases

BgeeiENSG00000196262.
CleanExiHS_PPIA.
ExpressionAtlasiP62937. baseline and differential.
GenevisibleiP62937. HS.

Organism-specific databases

HPAiCAB004655.
HPA058345.

Interactioni

Subunit structurei

Interacts with HIV-1 Capsid protein.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB82EBI-437708,EBI-6927873From a different organism.
gagQ724977EBI-437708,EBI-1036263From a different organism.
LNX1Q8TBB13EBI-437708,EBI-739832
PTPRNQ168493EBI-437708,EBI-728153
SUPT5HO002672EBI-437708,EBI-710464

GO - Molecular functioni

  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111474. 106 interactors.
DIPiDIP-6080N.
IntActiP62937. 65 interactors.
MINTiMINT-4999116.
STRINGi9606.ENSP00000419425.

Chemistry databases

BindingDBiP62937.

Structurei

Secondary structure

1165
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 12Combined sources8
Beta strandi15 – 24Combined sources10
Turni26 – 28Combined sources3
Helixi30 – 41Combined sources12
Turni42 – 44Combined sources3
Beta strandi55 – 57Combined sources3
Turni58 – 60Combined sources3
Beta strandi61 – 64Combined sources4
Turni67 – 69Combined sources3
Beta strandi70 – 73Combined sources4
Beta strandi74 – 77Combined sources4
Beta strandi78 – 81Combined sources4
Beta strandi97 – 100Combined sources4
Beta strandi102 – 104Combined sources3
Beta strandi108 – 110Combined sources3
Beta strandi112 – 117Combined sources6
Helixi120 – 122Combined sources3
Turni123 – 125Combined sources3
Beta strandi128 – 134Combined sources7
Helixi136 – 143Combined sources8
Helixi148 – 150Combined sources3
Beta strandi152 – 154Combined sources3
Beta strandi156 – 164Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2MS4NMR-A1-165[»]
2MZUNMR-A1-165[»]
2N0TNMR-A1-165[»]
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[»]
4N1MX-ray1.15A1-165[»]
4N1NX-ray1.50A1-165[»]
4N1OX-ray1.75A1-165[»]
4N1PX-ray1.90A1-165[»]
4N1QX-ray1.65A1-165[»]
4N1RX-ray1.80A1-165[»]
4N1SX-ray1.47A1-165[»]
4YUGX-ray1.48A1-165[»]
4YUHX-ray1.34A1-165[»]
4YUIX-ray1.38A1-165[»]
4YUJX-ray1.42A1-165[»]
4YUKX-ray1.48A1-165[»]
4YULX-ray1.42A1-165[»]
4YUMX-ray1.50A1-165[»]
4YUNX-ray1.58A1-165[»]
4YUOX-ray1.20A1-165[»]
4YUPX-ray1.75A1-165[»]
5CYHX-ray2.10A2-165[»]
5F66X-ray1.15A1-165[»]
5FJBelectron microscopy9.00C2-165[»]
5KULX-ray1.70A2-165[»]
5KUNX-ray1.70A2-165[»]
5KUOX-ray1.70A2-165[»]
5KUQX-ray1.70A2-165[»]
5KURX-ray1.70A2-165[»]
5KUSX-ray1.70A2-165[»]
5KUUX-ray1.70A2-165[»]
5KUVX-ray1.70A2-165[»]
5KUWX-ray1.70A2-165[»]
5KUZX-ray1.70A2-165[»]
5KV0X-ray1.70A2-165[»]
5KV1X-ray1.70A2-165[»]
5KV2X-ray1.70A2-165[»]
5KV3X-ray1.70A2-165[»]
5KV4X-ray1.70A2-165[»]
5KV5X-ray1.70A2-165[»]
5KV6X-ray1.70A2-165[»]
5KV7X-ray1.70A2-165[»]
ProteinModelPortaliP62937.
SMRiP62937.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62937.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 163PPIase cyclophilin-typePROSITE-ProRule annotationAdd BLAST157

Sequence similaritiesi

Contains 1 PPIase cyclophilin-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP62937.
KOiK03767.
OMAiMRSAFFQ.
OrthoDBiEOG091G0BGL.
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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P62937-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG
60 70 80 90 100
SCFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM
110 120 130 140 150
ANAGPNTNGS QFFICTAKTE WLDGKHVVFG KVKEGMNIVE AMERFGSRNG
160
KTSKKITIAD CGQLE
Length:165
Mass (Da):18,012
Last modified:January 23, 2007 - v2
Checksum:i9B2E637A555E4434
GO
Isoform 2 (identifier: P62937-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.

Show »
Length:105
Mass (Da):11,418
Checksum:i4629A635A48F744B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti89I → T in AAH05982 (PubMed:15489334).Curated1
Sequence conflicti106N → I in AAH07104 (PubMed:15489334).Curated1
Sequence conflicti165E → D in CAG32988 (Ref. 4) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0560501 – 60Missing in isoform 2. 2 PublicationsAdd BLAST60

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00052 mRNA. Translation: CAA68264.1.
X52851 Genomic DNA. Translation: CAA37039.1.
AK290085 mRNA. Translation: BAF82774.1.
AK293003 mRNA. Translation: BAF85692.1.
CR456707 mRNA. Translation: CAG32988.1.
AB451307 mRNA. Translation: BAG70121.1.
AB451438 mRNA. Translation: BAG70252.1.
AY739283 Genomic DNA. Translation: AAU13906.1.
AC004854 Genomic DNA. No translation available.
AC013436 Genomic DNA. No translation available.
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.
BC093076 mRNA. Translation: AAH93076.1.
BC106030 mRNA. Translation: AAI06031.1.
BC137057 mRNA. Translation: AAI37058.1.
BC137058 mRNA. Translation: AAI37059.1.
CCDSiCCDS5494.1. [P62937-1]
CCDS75592.1. [P62937-2]
PIRiA94496. CSHUA.
RefSeqiNP_001287910.1. NM_001300981.1. [P62937-2]
NP_066953.1. NM_021130.4. [P62937-1]
UniGeneiHs.356331.

Genome annotation databases

EnsembliENST00000355968; ENSP00000430817; ENSG00000196262. [P62937-2]
ENST00000468812; ENSP00000419425; ENSG00000196262. [P62937-1]
ENST00000489459; ENSP00000427976; ENSG00000196262. [P62937-2]
ENST00000620047; ENSP00000479961; ENSG00000196262. [P62937-2]
GeneIDi5478.
KEGGihsa:5478.
UCSCiuc064djo.1. human. [P62937-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Cyclophilin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00052 mRNA. Translation: CAA68264.1.
X52851 Genomic DNA. Translation: CAA37039.1.
AK290085 mRNA. Translation: BAF82774.1.
AK293003 mRNA. Translation: BAF85692.1.
CR456707 mRNA. Translation: CAG32988.1.
AB451307 mRNA. Translation: BAG70121.1.
AB451438 mRNA. Translation: BAG70252.1.
AY739283 Genomic DNA. Translation: AAU13906.1.
AC004854 Genomic DNA. No translation available.
AC013436 Genomic DNA. No translation available.
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.
BC093076 mRNA. Translation: AAH93076.1.
BC106030 mRNA. Translation: AAI06031.1.
BC137057 mRNA. Translation: AAI37058.1.
BC137058 mRNA. Translation: AAI37059.1.
CCDSiCCDS5494.1. [P62937-1]
CCDS75592.1. [P62937-2]
PIRiA94496. CSHUA.
RefSeqiNP_001287910.1. NM_001300981.1. [P62937-2]
NP_066953.1. NM_021130.4. [P62937-1]
UniGeneiHs.356331.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2MS4NMR-A1-165[»]
2MZUNMR-A1-165[»]
2N0TNMR-A1-165[»]
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[»]
4N1MX-ray1.15A1-165[»]
4N1NX-ray1.50A1-165[»]
4N1OX-ray1.75A1-165[»]
4N1PX-ray1.90A1-165[»]
4N1QX-ray1.65A1-165[»]
4N1RX-ray1.80A1-165[»]
4N1SX-ray1.47A1-165[»]
4YUGX-ray1.48A1-165[»]
4YUHX-ray1.34A1-165[»]
4YUIX-ray1.38A1-165[»]
4YUJX-ray1.42A1-165[»]
4YUKX-ray1.48A1-165[»]
4YULX-ray1.42A1-165[»]
4YUMX-ray1.50A1-165[»]
4YUNX-ray1.58A1-165[»]
4YUOX-ray1.20A1-165[»]
4YUPX-ray1.75A1-165[»]
5CYHX-ray2.10A2-165[»]
5F66X-ray1.15A1-165[»]
5FJBelectron microscopy9.00C2-165[»]
5KULX-ray1.70A2-165[»]
5KUNX-ray1.70A2-165[»]
5KUOX-ray1.70A2-165[»]
5KUQX-ray1.70A2-165[»]
5KURX-ray1.70A2-165[»]
5KUSX-ray1.70A2-165[»]
5KUUX-ray1.70A2-165[»]
5KUVX-ray1.70A2-165[»]
5KUWX-ray1.70A2-165[»]
5KUZX-ray1.70A2-165[»]
5KV0X-ray1.70A2-165[»]
5KV1X-ray1.70A2-165[»]
5KV2X-ray1.70A2-165[»]
5KV3X-ray1.70A2-165[»]
5KV4X-ray1.70A2-165[»]
5KV5X-ray1.70A2-165[»]
5KV6X-ray1.70A2-165[»]
5KV7X-ray1.70A2-165[»]
ProteinModelPortaliP62937.
SMRiP62937.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111474. 106 interactors.
DIPiDIP-6080N.
IntActiP62937. 65 interactors.
MINTiMINT-4999116.
STRINGi9606.ENSP00000419425.

Chemistry databases

BindingDBiP62937.
ChEMBLiCHEMBL1949.
DrugBankiDB00091. Cyclosporine.
DB00172. L-Proline.
GuidetoPHARMACOLOGYi2751.

PTM databases

iPTMnetiP62937.
PhosphoSitePlusiP62937.
SwissPalmiP62937.

Polymorphism and mutation databases

BioMutaiPPIA.
DMDMi51702775.

2D gel databases

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

Proteomic databases

EPDiP62937.
PaxDbiP62937.
PeptideAtlasiP62937.
PRIDEiP62937.
TopDownProteomicsiP62937-1. [P62937-1]

Protocols and materials databases

DNASUi5478.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355968; ENSP00000430817; ENSG00000196262. [P62937-2]
ENST00000468812; ENSP00000419425; ENSG00000196262. [P62937-1]
ENST00000489459; ENSP00000427976; ENSG00000196262. [P62937-2]
ENST00000620047; ENSP00000479961; ENSG00000196262. [P62937-2]
GeneIDi5478.
KEGGihsa:5478.
UCSCiuc064djo.1. human. [P62937-1]

Organism-specific databases

CTDi5478.
DisGeNETi5478.
GeneCardsiPPIA.
HGNCiHGNC:9253. PPIA.
HPAiCAB004655.
HPA058345.
MIMi123840. gene.
neXtProtiNX_P62937.
OpenTargetsiENSG00000196262.
PharmGKBiPA33574.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0865. Eukaryota.
COG0652. LUCA.
GeneTreeiENSGT00760000119119.
HOGENOMiHOG000065981.
HOVERGENiHBG001065.
InParanoidiP62937.
KOiK03767.
OMAiMRSAFFQ.
OrthoDBiEOG091G0BGL.
PhylomeDBiP62937.
TreeFamiTF316719.

Enzyme and pathway databases

BioCyciZFISH:HS07363-MONOMER.
BRENDAi5.2.1.8. 2681.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-162585. Uncoating of the HIV Virion.
R-HSA-162588. Budding and maturation of HIV virion.
R-HSA-162592. Integration of provirus.
R-HSA-162594. Early Phase of HIV Life Cycle.
R-HSA-164516. Minus-strand DNA synthesis.
R-HSA-164525. Plus-strand DNA synthesis.
R-HSA-173107. Binding and entry of HIV virion.
R-HSA-175474. Assembly Of The HIV Virion.
R-HSA-180689. APOBEC3G mediated resistance to HIV-1 infection.
R-HSA-210991. Basigin interactions.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

ChiTaRSiPPIA. human.
EvolutionaryTraceiP62937.
GeneWikiiPeptidylprolyl_isomerase_A.
GenomeRNAii5478.
PROiP62937.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196262.
CleanExiHS_PPIA.
ExpressionAtlasiP62937. baseline and differential.
GenevisibleiP62937. HS.

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]
PANTHERiPTHR11071. PTHR11071. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiPPIA_HUMAN
AccessioniPrimary (citable) accession number: P62937
Secondary accession number(s): A8K220
, P05092, Q3KQW3, Q567Q0, Q6IBU5, Q96IX3, Q9BRU4, Q9BTY9, Q9UC61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 150 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.