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P62937

- PPIA_HUMAN

UniProt

P62937 - PPIA_HUMAN

Protein

Peptidyl-prolyl cis-trans isomerase A

Gene

PPIA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    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 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

    1. cytosol Source: UniProtKB
    2. extracellular region Source: Reactome
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB
    6. nucleus Source: UniProtKB

    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...)Sequence Analysis
    Modified residuei125 – 1251N6-acetyllysine2 Publications
    Modified residuei131 – 1311N6-acetyllysine1 Publication
    Modified residuei133 – 1331N6-acetyllysineBy 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.6 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.4 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62937.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini7 – 163157PPIase cyclophilin-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    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]

    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. Align

    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

    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
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti89 – 891I → T in AAH05982. (PubMed:15489334)Curated
    Sequence conflicti106 – 1061N → I in AAH07104. (PubMed:15489334)Curated
    Sequence conflicti165 – 1651E → D in CAG32988. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6060Missing in isoform 2. 2 PublicationsVSP_056050Add
    BLAST

    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.
    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.
    PIRiA94496. CSHUA.
    RefSeqiNP_066953.1. NM_021130.3.
    XP_005249848.1. XM_005249791.1.
    UniGeneiHs.356331.

    Genome annotation databases

    EnsembliENST00000355968; ENSP00000430817; ENSG00000196262.
    ENST00000468812; ENSP00000419425; ENSG00000196262.
    GeneIDi5478.
    KEGGihsa:5478.
    UCSCiuc003tlw.3. human.

    Polymorphism databases

    DMDMi51702775.

    Keywords - Coding sequence diversityi

    Alternative splicing

    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 .
    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 .
    CCDSi CCDS5494.1.
    PIRi A94496. CSHUA.
    RefSeqi NP_066953.1. NM_021130.3.
    XP_005249848.1. XM_005249791.1.
    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 ENST00000355968 ; ENSP00000430817 ; ENSG00000196262 .
    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

    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] (ISOFORM 1).
      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] (ISOFORMS 1 AND 2).
      Tissue: Subthalamic nucleus and Trachea.
    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] (ISOFORM 1).
    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] (ISOFORM 1).
    6. NIEHS SNPs program
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 1 AND 2).
      Tissue: Blood, Bone marrow, Brain, Cervix, Colon, Lung, Skeletal muscle, Skin and Urinary bladder.
    9. "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.
    10. "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.
    11. 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.
    12. 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.
    13. "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.
    14. "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.
    15. "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.
    16. "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].
    17. "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].
    18. "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.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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].
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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.
    23. "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).
    24. "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.
    25. "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).
    26. "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).
    27. "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).
    28. "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).
    29. "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.
    30. "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.
    31. "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.
    32. "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.
    33. "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, Q567Q0, Q6IBU5, Q96IX3, Q9BRU4, Q9BTY9, Q9UC61
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 126 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