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Peptidyl-prolyl cis-trans isomerase A (PPIase A) (EC 5.2.1.8) (Cyclophilin A) (Cyclosporin A-binding protein) (Rotamase A) [Cleaved into: Peptidyl-prolyl cis-trans isomerase A, N-terminally processed]

 PPIA_HUMAN              Reviewed;         165 AA.
P62937; A8K220; P05092; Q3KQW3; Q567Q0; Q6IBU5; Q96IX3; Q9BRU4;
Q9BTY9; Q9UC61;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 162.
RecName: 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;
Name=PPIA; Synonyms=CYPA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Leukemic T-cell;
PubMed=3297675;
Haendler B., Hofer-Warbinek R., Hofer E.;
"Complementary DNA for human T-cell cyclophilin.";
EMBO J. 6:947-950(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2197089; DOI=10.1111/j.1432-1033.1990.tb15598.x;
Haendler B., Hofer E.;
"Characterization of the human cyclophilin gene and of related
processed pseudogenes.";
Eur. J. Biochem. 190:477-482(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Subthalamic nucleus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
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.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
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.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Blood, Bone marrow, Brain, Cervix, Colon, Lung,
Skeletal muscle, Skin, and Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 2-30.
PubMed=7657784; DOI=10.1093/oxfordjournals.humrep.a136138;
Meier U., Beier-Hellwig K., Klug J., Linder D., Beier H.M.;
"Identification of cyclophilin A from human decidual and placental
tissue in the first trimester of pregnancy.";
Hum. Reprod. 10:1305-1310(1995).
[10]
PROTEIN SEQUENCE OF 2-19.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[11]
PROTEIN SEQUENCE OF 2-31; 56-69; 77-118; 132-144 AND 155-165, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[12]
PROTEIN SEQUENCE OF 2-28, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT VAL-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Platelet;
Bienvenut W.V., Claeys D.;
Submitted (NOV-2005) to UniProtKB.
[13]
MUTAGENESIS OF TRP-121.
PubMed=2001362; DOI=10.1021/bi00223a003;
Liu J., Chen C.-M., Walsh C.T.;
"Human and Escherichia coli cyclophilins: sensitivity to inhibition by
the immunosuppressant cyclosporin A correlates with a specific
tryptophan residue.";
Biochemistry 30:2306-2310(1991).
[14]
INTERACTION WITH HIV-1 CAPSID PROTEIN.
PubMed=8513493; DOI=10.1016/0092-8674(93)90637-6;
Luban J., Bossolt K.L., Franke E.K., Kalpana G.V., Goff S.P.;
"Human immunodeficiency virus type 1 Gag protein binds to cyclophilins
A and B.";
Cell 73:1067-1078(1993).
[15]
SUBCELLULAR LOCATION.
PubMed=16527992; DOI=10.1161/01.RES.0000216405.85080.a6;
Suzuki J., Jin Z.G., Meoli D.F., Matoba T., Berk B.C.;
"Cyclophilin A is secreted by a vesicular pathway in vascular smooth
muscle cells.";
Circ. Res. 98:811-817(2006).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-28; LYS-44; LYS-76; LYS-82;
LYS-125 AND LYS-131, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
ACETYLATION AT VAL-2, AND CLEAVAGE OF INITIATOR METHIONINE.
PubMed=25489052; DOI=10.1093/hmg/ddu611;
Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K.,
Arnesen T.;
"Biochemical and cellular analysis of Ogden syndrome reveals
downstream Nt-acetylation defects.";
Hum. Mol. Genet. 24:1956-1976(2015).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-28 AND LYS-82, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[27]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), AND STRUCTURE BY NMR.
PubMed=1896075; DOI=10.1038/353276a0;
Kallen J., Spitzfaden C., Zurini M.G.M., Wider G., Widmer H.,
Wuethrich K., Walkinshaw M.D.;
"Structure of human cyclophilin and its binding site for cyclosporin A
determined by X-ray crystallography and NMR spectroscopy.";
Nature 353:276-279(1991).
[28]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=1946361; DOI=10.1073/pnas.88.21.9483;
Ke H., Zydowsky L.D., Liu J., Walsh C.T.;
"Crystal structure of recombinant human T-cell cyclophilin A at 2.5-A
resolution.";
Proc. Natl. Acad. Sci. U.S.A. 88:9483-9487(1991).
[29]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH CYCLOPHILIN.
PubMed=8421501; DOI=10.1038/361091a0;
Pfuegl G., Kallen J., Schirmer T., Jansonius J.N., Zurini M.G.M.,
Walkinshaw M.D.;
"X-ray structure of a decameric cyclophilin-cyclosporin crystal
complex.";
Nature 361:91-94(1993).
[30]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=8263916; DOI=10.1006/jmbi.1993.1664;
Mikol V., Kallen J., Pfluegl G., Walkinshaw M.D.;
"X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal
complex at 2.1-A resolution.";
J. Mol. Biol. 234:1119-1130(1993).
[31]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
PubMed=8652511; DOI=10.1021/bi9602775;
Zhao Y., Ke H.;
"Crystal structure implies that cyclophilin predominantly catalyzes
the trans to cis isomerization.";
Biochemistry 35:7356-7361(1996).
[32]
X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS).
PubMed=9385632; DOI=10.1002/pro.5560061103;
Vajdos F.F., Yoo S., Houseweart M., Sundquist W.I., Hill C.P.;
"Crystal structure of cyclophilin A complexed with a binding site
peptide from the HIV-1 capsid protein.";
Protein Sci. 6:2297-2307(1997).
[33]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=9769216; DOI=10.1006/jmbi.1998.2108;
Kallen J., Mikol V., Taylor P., Walkinshaw M.D.;
"X-ray structures and analysis of 11 cyclosporin derivatives complexed
with cyclophilin A.";
J. Mol. Biol. 283:435-449(1998).
[34]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
PubMed=12218175; DOI=10.1073/pnas.192206699;
Huai Q., Kim H.Y., Liu Y., Zhao Y., Mondragon A., Liu J.O., Ke H.;
"Crystal structure of calcineurin-cyclophilin-cyclosporin shows common
but distinct recognition of immunophilin-drug complexes.";
Proc. Natl. Acad. Sci. U.S.A. 99:12037-12042(2002).
[35]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CALCINEURIN B.
PubMed=12357034; DOI=10.1073/pnas.212504399;
Jin L., Harrison S.C.;
"Crystal structure of human calcineurin complexed with cyclosporin A
and human cyclophilin.";
Proc. Natl. Acad. Sci. U.S.A. 99:13522-13526(2002).
[36]
STRUCTURE BY NMR OF COMPLEX WITH CYCLOPHILIN.
PubMed=8421500; DOI=10.1038/361088a0;
Theriault Y., Logan T.M., Meadows R., Yu L., Olejniczak E.T.,
Holzman T.F., Simmer R.L., Fesik S.W.;
"Solution structure of the cyclosporin A/cyclophilin complex by NMR.";
Nature 361:88-91(1993).
[37]
STRUCTURE BY NMR.
PubMed=9299338; DOI=10.1006/jmbi.1997.1220;
Ottiger M., Zerbe O., Guentert P., Wuethrich K.;
"The NMR solution conformation of unligated human cyclophilin A.";
J. Mol. Biol. 272:64-81(1997).
[38]
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) ALONE AND IN COMPLEX WITH
CYCLOSPORINE AND HIV-1 CAPSID, AND ACETYLATION AT LYS-125.
PubMed=20364129; DOI=10.1038/nchembio.342;
Lammers M., Neumann H., Chin J.W., James L.C.;
"Acetylation regulates cyclophilin A catalysis, immunosuppression and
HIV isomerization.";
Nat. Chem. Biol. 6:331-337(2010).
-!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
the cis-trans isomerization of proline imidic peptide bonds in
oligopeptides.
-!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
(omega=0).
-!- ENZYME REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
its effects via an inhibitory action on PPIase.
-!- SUBUNIT: Interacts with HIV-1 Capsid protein.
{ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034,
ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:8513493}.
-!- INTERACTION:
Q99IB8:- (xeno); NbExp=2; IntAct=EBI-437708, EBI-6927873;
P46108-1:CRK; NbExp=4; IntAct=EBI-437708, EBI-287556;
Q72497:gag (xeno); NbExp=7; IntAct=EBI-437708, EBI-1036263;
Q8TBB1:LNX1; NbExp=3; IntAct=EBI-437708, EBI-739832;
Q16849:PTPRN; NbExp=3; IntAct=EBI-437708, EBI-728153;
O00267:SUPT5H; NbExp=2; IntAct=EBI-437708, EBI-710464;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16527992}.
Secreted {ECO:0000269|PubMed:16527992}. 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P62937-1; Sequence=Displayed;
Name=2;
IsoId=P62937-2; Sequence=VSP_056050;
-!- PTM: 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. {ECO:0000269|PubMed:20364129, ECO:0000269|Ref.12}.
-!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
A subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ppia/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Cyclophilin entry;
URL="https://en.wikipedia.org/wiki/Cyclophilin";
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EMBL; Y00052; CAA68264.1; -; mRNA.
EMBL; X52851; CAA37039.1; -; Genomic_DNA.
EMBL; AK290085; BAF82774.1; -; mRNA.
EMBL; AK293003; BAF85692.1; -; mRNA.
EMBL; CR456707; CAG32988.1; -; mRNA.
EMBL; AB451307; BAG70121.1; -; mRNA.
EMBL; AB451438; BAG70252.1; -; mRNA.
EMBL; AY739283; AAU13906.1; -; Genomic_DNA.
EMBL; AC004854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC013436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000689; AAH00689.1; -; mRNA.
EMBL; BC003026; AAH03026.2; -; mRNA.
EMBL; BC005320; AAH05320.1; -; mRNA.
EMBL; BC005982; AAH05982.1; -; mRNA.
EMBL; BC007104; AAH07104.1; -; mRNA.
EMBL; BC013915; AAH13915.1; -; mRNA.
EMBL; BC073992; AAH73992.1; -; mRNA.
EMBL; BC093076; AAH93076.1; -; mRNA.
EMBL; BC106030; AAI06031.1; -; mRNA.
EMBL; BC137057; AAI37058.1; -; mRNA.
EMBL; BC137058; AAI37059.1; -; mRNA.
CCDS; CCDS5494.1; -. [P62937-1]
CCDS; CCDS75592.1; -. [P62937-2]
PIR; A94496; CSHUA.
RefSeq; NP_001287910.1; NM_001300981.1. [P62937-2]
RefSeq; NP_066953.1; NM_021130.4. [P62937-1]
UniGene; Hs.356331; -.
PDB; 1AK4; X-ray; 2.36 A; A/B=1-165.
PDB; 1AWQ; X-ray; 1.58 A; A=2-165.
PDB; 1AWR; X-ray; 1.58 A; A/B/C/D/E/F=2-165.
PDB; 1AWS; X-ray; 2.55 A; A=2-165.
PDB; 1AWT; X-ray; 2.55 A; A/B/C/D/E/F=2-165.
PDB; 1AWU; X-ray; 2.34 A; A=2-165.
PDB; 1AWV; X-ray; 2.34 A; A/B/C/D/E/F=2-165.
PDB; 1BCK; X-ray; 1.80 A; A=1-165.
PDB; 1CWA; X-ray; 2.10 A; A=1-165.
PDB; 1CWB; X-ray; 2.20 A; A=1-165.
PDB; 1CWC; X-ray; 1.86 A; A=1-165.
PDB; 1CWF; X-ray; 1.86 A; A=1-165.
PDB; 1CWH; X-ray; 1.86 A; A=1-165.
PDB; 1CWI; X-ray; 1.90 A; A=1-165.
PDB; 1CWJ; X-ray; 1.80 A; A=1-165.
PDB; 1CWK; X-ray; 1.80 A; A=1-165.
PDB; 1CWL; X-ray; 1.80 A; A=1-165.
PDB; 1CWM; X-ray; 2.00 A; A=1-165.
PDB; 1CWO; X-ray; 1.86 A; A=1-165.
PDB; 1FGL; X-ray; 1.80 A; A=1-165.
PDB; 1M63; X-ray; 2.80 A; C/G=1-165.
PDB; 1M9C; X-ray; 2.00 A; A/B=1-165.
PDB; 1M9D; X-ray; 1.90 A; A/B=1-165.
PDB; 1M9E; X-ray; 1.72 A; A/B=1-164.
PDB; 1M9F; X-ray; 1.73 A; A/B=1-165.
PDB; 1M9X; X-ray; 1.70 A; A/B/E/F=1-165.
PDB; 1M9Y; X-ray; 1.90 A; A/B/E/F=1-165.
PDB; 1MF8; X-ray; 3.10 A; C=1-165.
PDB; 1MIK; X-ray; 1.76 A; A=1-165.
PDB; 1NMK; X-ray; 2.10 A; A/B=1-165.
PDB; 1OCA; NMR; -; A=1-165.
PDB; 1RMH; X-ray; 2.40 A; A/B=2-165.
PDB; 1VBS; X-ray; 2.00 A; A=1-165.
PDB; 1VBT; X-ray; 2.30 A; A/B=1-165.
PDB; 1W8L; X-ray; 1.80 A; A=2-165.
PDB; 1W8M; X-ray; 1.65 A; A=2-165.
PDB; 1W8V; X-ray; 1.70 A; A=2-165.
PDB; 1YND; X-ray; 1.60 A; A/B=1-165.
PDB; 1ZKF; X-ray; 2.55 A; A/B=1-165.
PDB; 2ALF; X-ray; 1.90 A; A=2-165.
PDB; 2CPL; X-ray; 1.63 A; A=1-165.
PDB; 2CYH; X-ray; 1.64 A; A=2-165.
PDB; 2MS4; NMR; -; A=1-165.
PDB; 2MZU; NMR; -; A=1-165.
PDB; 2N0T; NMR; -; A=1-165.
PDB; 2RMA; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=1-165.
PDB; 2RMB; X-ray; 2.10 A; A/C/E/G/I/K/M/O/Q/S=1-165.
PDB; 2X25; X-ray; 1.20 A; B=2-165.
PDB; 2X2A; X-ray; 1.40 A; A/B=1-165.
PDB; 2X2C; X-ray; 2.41 A; K/M/O/Q/S=1-165.
PDB; 2X2D; X-ray; 1.95 A; B/C=1-165.
PDB; 2XGY; X-ray; 1.80 A; B=1-165.
PDB; 3CYH; X-ray; 1.90 A; A=2-165.
PDB; 3CYS; NMR; -; A=1-165.
PDB; 3K0M; X-ray; 1.25 A; A=1-165.
PDB; 3K0N; X-ray; 1.39 A; A=1-165.
PDB; 3K0O; X-ray; 1.55 A; A=1-165.
PDB; 3K0P; X-ray; 1.65 A; A=1-165.
PDB; 3K0Q; X-ray; 2.32 A; A=1-165.
PDB; 3K0R; X-ray; 2.42 A; A=1-165.
PDB; 3ODI; X-ray; 2.20 A; A/C/E/G/I/K/M/O/Q/S=1-165.
PDB; 3ODL; X-ray; 2.31 A; A/C/E/G/I/K/M/O/Q/S=1-165.
PDB; 3RDD; X-ray; 2.14 A; A=1-165.
PDB; 4CYH; X-ray; 2.10 A; A=2-165.
PDB; 4IPZ; X-ray; 1.67 A; A=1-165.
PDB; 4N1M; X-ray; 1.15 A; A=1-165.
PDB; 4N1N; X-ray; 1.50 A; A=1-165.
PDB; 4N1O; X-ray; 1.75 A; A=1-165.
PDB; 4N1P; X-ray; 1.90 A; A=1-165.
PDB; 4N1Q; X-ray; 1.65 A; A=1-165.
PDB; 4N1R; X-ray; 1.80 A; A=1-165.
PDB; 4N1S; X-ray; 1.47 A; A=1-165.
PDB; 4YUG; X-ray; 1.48 A; A=1-165.
PDB; 4YUH; X-ray; 1.34 A; A=1-165.
PDB; 4YUI; X-ray; 1.38 A; A=1-165.
PDB; 4YUJ; X-ray; 1.42 A; A=1-165.
PDB; 4YUK; X-ray; 1.48 A; A=1-165.
PDB; 4YUL; X-ray; 1.42 A; A=1-165.
PDB; 4YUM; X-ray; 1.50 A; A=1-165.
PDB; 4YUN; X-ray; 1.58 A; A=1-165.
PDB; 4YUO; X-ray; 1.20 A; A=1-165.
PDB; 4YUP; X-ray; 1.75 A; A=1-165.
PDB; 5CYH; X-ray; 2.10 A; A=2-165.
PDB; 5F66; X-ray; 1.15 A; A=1-165.
PDB; 5FJB; EM; 9.00 A; C=2-165.
PDB; 5KUL; X-ray; 1.70 A; A=2-165.
PDB; 5KUN; X-ray; 1.70 A; A=2-165.
PDB; 5KUO; X-ray; 1.70 A; A=2-165.
PDB; 5KUQ; X-ray; 1.70 A; A=2-165.
PDB; 5KUR; X-ray; 1.70 A; A=2-165.
PDB; 5KUS; X-ray; 1.70 A; A=2-165.
PDB; 5KUU; X-ray; 1.70 A; A=2-165.
PDB; 5KUV; X-ray; 1.70 A; A=2-165.
PDB; 5KUW; X-ray; 1.70 A; A=2-165.
PDB; 5KUZ; X-ray; 1.70 A; A=2-165.
PDB; 5KV0; X-ray; 1.70 A; A=2-165.
PDB; 5KV1; X-ray; 1.70 A; A=2-165.
PDB; 5KV2; X-ray; 1.70 A; A=2-165.
PDB; 5KV3; X-ray; 1.70 A; A=2-165.
PDB; 5KV4; X-ray; 1.70 A; A=2-165.
PDB; 5KV5; X-ray; 1.70 A; A=2-165.
PDB; 5KV6; X-ray; 1.70 A; A=2-165.
PDB; 5KV7; X-ray; 1.70 A; A=2-165.
PDB; 5LUD; X-ray; 1.25 A; A=1-165.
PDB; 5NOQ; X-ray; 1.60 A; A=1-165.
PDB; 5NOR; X-ray; 1.80 A; A=1-165.
PDB; 5NOS; X-ray; 1.35 A; A=1-165.
PDB; 5NOT; X-ray; 1.45 A; A=1-165.
PDB; 5NOU; X-ray; 1.30 A; A=1-165.
PDB; 5NOV; X-ray; 2.00 A; A=1-165.
PDB; 5NOW; X-ray; 1.48 A; A=1-165.
PDB; 5NOX; X-ray; 1.49 A; A=1-165.
PDB; 5NOY; X-ray; 1.43 A; A=1-165.
PDB; 5NOZ; X-ray; 1.61 A; A=1-165.
PDB; 5T9U; X-ray; 2.30 A; A/B/C/D=1-164.
PDB; 5T9W; X-ray; 2.00 A; A=2-165.
PDB; 5T9Z; X-ray; 1.40 A; A=2-164.
PDB; 5TA2; X-ray; 1.48 A; A=2-164.
PDB; 5TA4; X-ray; 1.50 A; A=2-165.
PDBsum; 1AK4; -.
PDBsum; 1AWQ; -.
PDBsum; 1AWR; -.
PDBsum; 1AWS; -.
PDBsum; 1AWT; -.
PDBsum; 1AWU; -.
PDBsum; 1AWV; -.
PDBsum; 1BCK; -.
PDBsum; 1CWA; -.
PDBsum; 1CWB; -.
PDBsum; 1CWC; -.
PDBsum; 1CWF; -.
PDBsum; 1CWH; -.
PDBsum; 1CWI; -.
PDBsum; 1CWJ; -.
PDBsum; 1CWK; -.
PDBsum; 1CWL; -.
PDBsum; 1CWM; -.
PDBsum; 1CWO; -.
PDBsum; 1FGL; -.
PDBsum; 1M63; -.
PDBsum; 1M9C; -.
PDBsum; 1M9D; -.
PDBsum; 1M9E; -.
PDBsum; 1M9F; -.
PDBsum; 1M9X; -.
PDBsum; 1M9Y; -.
PDBsum; 1MF8; -.
PDBsum; 1MIK; -.
PDBsum; 1NMK; -.
PDBsum; 1OCA; -.
PDBsum; 1RMH; -.
PDBsum; 1VBS; -.
PDBsum; 1VBT; -.
PDBsum; 1W8L; -.
PDBsum; 1W8M; -.
PDBsum; 1W8V; -.
PDBsum; 1YND; -.
PDBsum; 1ZKF; -.
PDBsum; 2ALF; -.
PDBsum; 2CPL; -.
PDBsum; 2CYH; -.
PDBsum; 2MS4; -.
PDBsum; 2MZU; -.
PDBsum; 2N0T; -.
PDBsum; 2RMA; -.
PDBsum; 2RMB; -.
PDBsum; 2X25; -.
PDBsum; 2X2A; -.
PDBsum; 2X2C; -.
PDBsum; 2X2D; -.
PDBsum; 2XGY; -.
PDBsum; 3CYH; -.
PDBsum; 3CYS; -.
PDBsum; 3K0M; -.
PDBsum; 3K0N; -.
PDBsum; 3K0O; -.
PDBsum; 3K0P; -.
PDBsum; 3K0Q; -.
PDBsum; 3K0R; -.
PDBsum; 3ODI; -.
PDBsum; 3ODL; -.
PDBsum; 3RDD; -.
PDBsum; 4CYH; -.
PDBsum; 4IPZ; -.
PDBsum; 4N1M; -.
PDBsum; 4N1N; -.
PDBsum; 4N1O; -.
PDBsum; 4N1P; -.
PDBsum; 4N1Q; -.
PDBsum; 4N1R; -.
PDBsum; 4N1S; -.
PDBsum; 4YUG; -.
PDBsum; 4YUH; -.
PDBsum; 4YUI; -.
PDBsum; 4YUJ; -.
PDBsum; 4YUK; -.
PDBsum; 4YUL; -.
PDBsum; 4YUM; -.
PDBsum; 4YUN; -.
PDBsum; 4YUO; -.
PDBsum; 4YUP; -.
PDBsum; 5CYH; -.
PDBsum; 5F66; -.
PDBsum; 5FJB; -.
PDBsum; 5KUL; -.
PDBsum; 5KUN; -.
PDBsum; 5KUO; -.
PDBsum; 5KUQ; -.
PDBsum; 5KUR; -.
PDBsum; 5KUS; -.
PDBsum; 5KUU; -.
PDBsum; 5KUV; -.
PDBsum; 5KUW; -.
PDBsum; 5KUZ; -.
PDBsum; 5KV0; -.
PDBsum; 5KV1; -.
PDBsum; 5KV2; -.
PDBsum; 5KV3; -.
PDBsum; 5KV4; -.
PDBsum; 5KV5; -.
PDBsum; 5KV6; -.
PDBsum; 5KV7; -.
PDBsum; 5LUD; -.
PDBsum; 5NOQ; -.
PDBsum; 5NOR; -.
PDBsum; 5NOS; -.
PDBsum; 5NOT; -.
PDBsum; 5NOU; -.
PDBsum; 5NOV; -.
PDBsum; 5NOW; -.
PDBsum; 5NOX; -.
PDBsum; 5NOY; -.
PDBsum; 5NOZ; -.
PDBsum; 5T9U; -.
PDBsum; 5T9W; -.
PDBsum; 5T9Z; -.
PDBsum; 5TA2; -.
PDBsum; 5TA4; -.
ProteinModelPortal; P62937; -.
SMR; P62937; -.
BioGrid; 111474; 120.
CORUM; P62937; -.
DIP; DIP-6080N; -.
IntAct; P62937; 67.
MINT; P62937; -.
STRING; 9606.ENSP00000419425; -.
BindingDB; P62937; -.
ChEMBL; CHEMBL1949; -.
DrugBank; DB01742; (3r)-1-Acetyl-3-Methylpiperidine.
DrugBank; DB00091; Cyclosporine.
DrugBank; DB02419; Ethyl Oxo(Piperidin-1-Yl)Acetate.
DrugBank; DB00172; L-Proline.
GuidetoPHARMACOLOGY; 2751; -.
iPTMnet; P62937; -.
PhosphoSitePlus; P62937; -.
SwissPalm; P62937; -.
BioMuta; PPIA; -.
DMDM; 51702775; -.
DOSAC-COBS-2DPAGE; P62937; -.
OGP; P62937; -.
REPRODUCTION-2DPAGE; IPI00419585; -.
REPRODUCTION-2DPAGE; P62937; -.
SWISS-2DPAGE; P62937; -.
UCD-2DPAGE; P62937; -.
EPD; P62937; -.
PaxDb; P62937; -.
PeptideAtlas; P62937; -.
PRIDE; P62937; -.
TopDownProteomics; P62937-1; -. [P62937-1]
DNASU; 5478; -.
Ensembl; ENST00000355968; ENSP00000430817; ENSG00000196262. [P62937-2]
Ensembl; ENST00000468812; ENSP00000419425; ENSG00000196262. [P62937-1]
Ensembl; ENST00000489459; ENSP00000427976; ENSG00000196262. [P62937-2]
Ensembl; ENST00000620047; ENSP00000479961; ENSG00000196262. [P62937-2]
GeneID; 5478; -.
KEGG; hsa:5478; -.
UCSC; uc064djo.1; human. [P62937-1]
CTD; 5478; -.
DisGeNET; 5478; -.
EuPathDB; HostDB:ENSG00000196262.13; -.
GeneCards; PPIA; -.
HGNC; HGNC:9253; PPIA.
HPA; CAB004655; -.
HPA; HPA058345; -.
MIM; 123840; gene.
neXtProt; NX_P62937; -.
OpenTargets; ENSG00000196262; -.
PharmGKB; PA33574; -.
eggNOG; KOG0865; Eukaryota.
eggNOG; COG0652; LUCA.
GeneTree; ENSGT00760000119119; -.
HOGENOM; HOG000065981; -.
HOVERGEN; HBG001065; -.
InParanoid; P62937; -.
KO; K03767; -.
OMA; FFINFKD; -.
OrthoDB; EOG091G0BGL; -.
PhylomeDB; P62937; -.
TreeFam; TF316719; -.
BRENDA; 5.2.1.8; 2681.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-162585; Uncoating of the HIV Virion.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-162592; Integration of provirus.
Reactome; R-HSA-162594; Early Phase of HIV Life Cycle.
Reactome; R-HSA-164516; Minus-strand DNA synthesis.
Reactome; R-HSA-164525; Plus-strand DNA synthesis.
Reactome; R-HSA-173107; Binding and entry of HIV virion.
Reactome; R-HSA-175474; Assembly Of The HIV Virion.
Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
Reactome; R-HSA-2025928; Calcineurin activates NFAT.
Reactome; R-HSA-210991; Basigin interactions.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
ChiTaRS; PPIA; human.
EvolutionaryTrace; P62937; -.
GeneWiki; Peptidylprolyl_isomerase_A; -.
GenomeRNAi; 5478; -.
PRO; PR:P62937; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000196262; -.
CleanEx; HS_PPIA; -.
ExpressionAtlas; P62937; baseline and differential.
Genevisible; P62937; HS.
GO; GO:0005829; C:cytosol; HDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0016018; F:cyclosporin A binding; IDA:CAFA.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; TAS:UniProtKB.
GO; GO:0046790; F:virion binding; NAS:UniProtKB.
GO; GO:0030260; P:entry into host cell; TAS:Reactome.
GO; GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; TAS:Reactome.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0034389; P:lipid particle organization; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
GO; GO:0045070; P:positive regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0006457; P:protein folding; TAS:UniProtKB.
GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IDA:UniProtKB.
GO; GO:0045069; P:regulation of viral genome replication; IMP:UniProtKB.
GO; GO:0006278; P:RNA-dependent DNA biosynthetic process; TAS:Reactome.
GO; GO:0019061; P:uncoating of virus; TAS:Reactome.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
GO; GO:0019076; P:viral release from host cell; TAS:UniProtKB.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
Gene3D; 2.40.100.10; -; 1.
InterPro; IPR029000; Cyclophilin-like_dom_sf.
InterPro; IPR024936; Cyclophilin-type_PPIase.
InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
PANTHER; PTHR11071; PTHR11071; 1.
Pfam; PF00160; Pro_isomerase; 1.
PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
PRINTS; PR00153; CSAPPISMRASE.
SUPFAM; SSF50891; SSF50891; 1.
PROSITE; PS00170; CSA_PPIASE_1; 1.
PROSITE; PS50072; CSA_PPIASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Glycoprotein;
Host-virus interaction; Isomerase; Isopeptide bond; Phosphoprotein;
Reference proteome; Rotamase; Secreted; Ubl conjugation.
CHAIN 1 165 Peptidyl-prolyl cis-trans isomerase A.
/FTId=PRO_0000423240.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:25489052,
ECO:0000269|PubMed:7657784,
ECO:0000269|Ref.11, ECO:0000269|Ref.12}.
CHAIN 2 165 Peptidyl-prolyl cis-trans isomerase A, N-
terminally processed.
/FTId=PRO_0000064115.
DOMAIN 7 163 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
MOD_RES 2 2 N-acetylvaline; partial; in Peptidyl-
prolyl cis-trans isomerase A, N-
terminally processed.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:25489052,
ECO:0000269|Ref.12}.
MOD_RES 28 28 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 44 44 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 76 76 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 82 82 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 93 93 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 125 125 N6-acetyllysine.
{ECO:0000244|PubMed:19608861,
ECO:0000269|PubMed:20364129}.
MOD_RES 131 131 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 133 133 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17742}.
CARBOHYD 108 108 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 28 28 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 28 28 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
CROSSLNK 82 82 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 60 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_056050.
MUTAGEN 121 121 W->A: 200-fold decrease of sensitivity to
CsA. {ECO:0000269|PubMed:2001362}.
MUTAGEN 121 121 W->F: 75-fold decrease of sensitivity to
CsA. {ECO:0000269|PubMed:2001362}.
CONFLICT 89 89 I -> T (in Ref. 8; AAH05982).
{ECO:0000305}.
CONFLICT 106 106 N -> I (in Ref. 8; AAH07104).
{ECO:0000305}.
CONFLICT 165 165 E -> D (in Ref. 4; CAG32988).
{ECO:0000305}.
STRAND 5 12 {ECO:0000244|PDB:4N1M}.
STRAND 15 24 {ECO:0000244|PDB:4N1M}.
TURN 26 28 {ECO:0000244|PDB:4N1M}.
HELIX 30 41 {ECO:0000244|PDB:4N1M}.
TURN 42 44 {ECO:0000244|PDB:4N1M}.
STRAND 55 57 {ECO:0000244|PDB:4N1M}.
TURN 58 60 {ECO:0000244|PDB:4N1M}.
STRAND 61 64 {ECO:0000244|PDB:4N1M}.
TURN 67 69 {ECO:0000244|PDB:4N1M}.
STRAND 70 73 {ECO:0000244|PDB:4N1M}.
STRAND 74 77 {ECO:0000244|PDB:2MS4}.
STRAND 78 81 {ECO:0000244|PDB:4YUI}.
STRAND 97 100 {ECO:0000244|PDB:4N1M}.
STRAND 102 104 {ECO:0000244|PDB:4IPZ}.
STRAND 108 110 {ECO:0000244|PDB:1FGL}.
STRAND 112 117 {ECO:0000244|PDB:4N1M}.
HELIX 120 122 {ECO:0000244|PDB:4N1M}.
TURN 123 125 {ECO:0000244|PDB:4N1M}.
STRAND 128 134 {ECO:0000244|PDB:4N1M}.
HELIX 136 143 {ECO:0000244|PDB:4N1M}.
HELIX 148 150 {ECO:0000244|PDB:3K0O}.
STRAND 152 154 {ECO:0000244|PDB:2MS4}.
STRAND 156 164 {ECO:0000244|PDB:4N1M}.
SEQUENCE 165 AA; 18012 MW; 9B2E637A555E4434 CRC64;
MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF
MCQGGDFTRH NGTGGKSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE
WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITIAD CGQLE


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