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Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Cellular thyroid hormone-binding protein) (Prolyl 4-hydroxylase subunit beta) (p55)

 PDIA1_HUMAN             Reviewed;         508 AA.
P07237; B2RDQ2; P30037; P32079; Q15205; Q6LDE5;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 3.
28-MAR-2018, entry version 232.
RecName: Full=Protein disulfide-isomerase;
Short=PDI;
EC=5.3.4.1;
AltName: Full=Cellular thyroid hormone-binding protein;
AltName: Full=Prolyl 4-hydroxylase subunit beta;
AltName: Full=p55;
Flags: Precursor;
Name=P4HB; Synonyms=ERBA2L, PDI, PDIA1, PO4DB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3034602;
Pihlajaniemi T., Helaakoski T., Tasanen K., Myllylae R.,
Huhtala M.-L., Koivu J., Kivirikko K.I.;
"Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase.
This subunit and protein disulphide isomerase are products of the same
gene.";
EMBO J. 6:643-649(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3611107;
Cheng S.-Y., Gong Q.-H., Parkison C., Robinson E.A., Appella E.,
Merlino G.T., Pastan I.;
"The nucleotide sequence of a human cellular thyroid hormone binding
protein present in endoplasmic reticulum.";
J. Biol. Chem. 262:11221-11227(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Blood;
PubMed=2846539;
Tasanen K., Parkkonen T., Chow L.T., Kivirikko K.I., Pihlajaniemi T.;
"Characterization of the human gene for a polypeptide that acts both
as the beta subunit of prolyl 4-hydroxylase and as protein disulfide
isomerase.";
J. Biol. Chem. 263:16218-16224(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Synovium;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon, Lung, and Skin;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
PubMed=1597478;
Tasanen K., Oikarinen J., Kivirikko K.I., Pihlajaniemi T.;
"Promoter of the gene for the multifunctional protein disulfide
isomerase polypeptide. Functional significance of the six CCAAT boxes
and other promoter elements.";
J. Biol. Chem. 267:11513-11519(1992).
[8]
PROTEIN SEQUENCE OF 18-41.
TISSUE=Colon carcinoma;
PubMed=9150948; DOI=10.1002/elps.1150180344;
Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.;
"A two-dimensional gel database of human colon carcinoma proteins.";
Electrophoresis 18:605-613(1997).
[9]
PROTEIN SEQUENCE OF 18-30.
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).
[10]
PROTEIN SEQUENCE OF 18-29.
TISSUE=Liver;
Frutiger S., Hughes G.J.;
Submitted (FEB-1996) to UniProtKB.
[11]
PROTEIN SEQUENCE OF 18-26.
PubMed=2079031; DOI=10.1002/elps.1150111019;
Ward L.D., Hong J., Whitehead R.H., Simpson R.J.;
"Development of a database of amino acid sequences for human colon
carcinoma proteins separated by two-dimensional polyacrylamide gel
electrophoresis.";
Electrophoresis 11:883-891(1990).
[12]
PRELIMINARY PROTEIN SEQUENCE OF 19-28.
TISSUE=Liver;
PubMed=1286669; DOI=10.1002/elps.11501301201;
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F.,
Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R.,
Appel R.D., Hughes G.J.;
"Human liver protein map: a reference database established by
microsequencing and gel comparison.";
Electrophoresis 13:992-1001(1992).
[13]
PROTEIN SEQUENCE OF 19-28.
PubMed=9399589; DOI=10.1093/oxfordjournals.jbchem.a021830;
Urade R., Oda T., Ito H., Moriyama T., Utsumi S., Kito M.;
"Functions of characteristic Cys-Gly-His-Cys (CGHC) and Gln-Glu-Asp-
Leu (QEDL) motifs of microsomal ER-60 protease.";
J. Biochem. 122:834-842(1997).
[14]
PROTEIN SEQUENCE OF 201-207; 223-230; 286-308 AND 402-409, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 293-508.
PubMed=3342239; DOI=10.1016/0167-4781(88)90080-2;
Morris J.I., Varandani P.T.;
"Characterization of a cDNA for human glutathione-insulin
transhydrogenase (protein-disulfide isomerase/oxidoreductase).";
Biochim. Biophys. Acta 949:169-180(1988).
[16]
PROTEIN SEQUENCE OF 317-325; 350-369 AND 401-419.
PubMed=1699755; DOI=10.1002/elps.1150110703;
Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M.,
Gesser B., Celis J.E., Vandekerckhove J.;
"Two-dimensional gel electrophoresis, protein electroblotting and
microsequencing: a direct link between proteins and genes.";
Electrophoresis 11:528-536(1990).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10636893; DOI=10.1074/jbc.275.3.1920;
Mezghrani A., Courageot J., Mani J.-C., Pugniere M., Bastiani P.,
Miquelis R.;
"Protein-disulfide isomerase (PDI) in FRTL5 cells. pH-dependent
thyroglobulin/PDI interactions determine a novel PDI function in the
post-endoplasmic reticulum of thyrocytes.";
J. Biol. Chem. 275:1920-1929(2000).
[18]
INTERACTION WITH ERO1B.
PubMed=11707400; DOI=10.1093/emboj/20.22.6288;
Mezghrani A., Fassio A., Benham A., Simmen T., Braakman I., Sitia R.;
"Manipulation of oxidative protein folding and PDI redox state in
mammalian cells.";
EMBO J. 20:6288-6296(2001).
[19]
REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS, AND
SUBCELLULAR LOCATION.
PubMed=11181151; DOI=10.1086/318823;
Fenouillet E., Barbouche R., Courageot J., Miquelis R.;
"The catalytic activity of protein disulfide isomerase is involved in
human immunodeficiency virus envelope-mediated membrane fusion after
CD4 cell binding.";
J. Infect. Dis. 183:744-752(2001).
[20]
FUNCTION.
PubMed=12485997; DOI=10.1093/emboj/cdf685;
Lumb R.A., Bulleid N.J.;
"Is protein disulfide isomerase a redox-dependent molecular
chaperone?";
EMBO J. 21:6763-6770(2002).
[21]
INTERACTION WITH UBQLN1.
PubMed=12095988; DOI=10.1074/jbc.M203412200;
Ko H.S., Uehara T., Nomura Y.;
"Role of ubiquilin associated with protein-disulfide isomerase in the
endoplasmic reticulum in stress-induced apoptotic cell death.";
J. Biol. Chem. 277:35386-35392(2002).
[22]
REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
PubMed=12218051; DOI=10.1074/jbc.M204547200;
Gallina A., Hanley T.M., Mandel R., Trahey M., Broder C.C.,
Viglianti G.A., Ryser H.J.;
"Inhibitors of protein-disulfide isomerase prevent cleavage of
disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1
entry.";
J. Biol. Chem. 277:50579-50588(2002).
[23]
REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
PubMed=12218052; DOI=10.1074/jbc.M205467200;
Barbouche R., Miquelis R., Jones I.M., Fenouillet E.;
"Protein-disulfide isomerase-mediated reduction of two disulfide bonds
of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is
required for fusion.";
J. Biol. Chem. 278:3131-3136(2003).
[24]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=12643545; DOI=10.1021/pr025562r;
Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K.,
Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J.,
Hearing V.J., Hunt D.F., Appella E.;
"Proteomic analysis of early melanosomes: identification of novel
melanosomal proteins.";
J. Proteome Res. 2:69-79(2003).
[25]
REVIEW.
PubMed=15158710; DOI=10.1016/j.bbapap.2004.02.017;
Wilkinson B., Gilbert H.F.;
"Protein disulfide isomerase.";
Biochim. Biophys. Acta 1699:35-44(2004).
[26]
REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
PubMed=14592831; DOI=10.1182/blood-2003-05-1390;
Markovic I., Stantchev T.S., Fields K.H., Tiffany L.J., Tomic M.,
Weiss C.D., Broder C.C., Strebel K., Clouse K.A.;
"Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1
envelope-mediated T-cell fusion during viral entry.";
Blood 103:1586-1594(2004).
[27]
REDUCTION OF HIV-1 SURFACE PROTEIN GP120 DISULFIDE BONDS.
PubMed=15644496; DOI=10.1124/mol.104.008276;
Barbouche R., Lortat-Jacob H., Jones I.M., Fenouillet E.;
"Glycosaminoglycans and protein disulfide isomerase-mediated reduction
of HIV Env.";
Mol. Pharmacol. 67:1111-1118(2005).
[28]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[29]
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).
[30]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION AS RECEPTOR FOR LGALS9,
AND SUBCELLULAR LOCATION.
PubMed=21670307; DOI=10.1073/pnas.1017954108;
Bi S., Hong P.W., Lee B., Baum L.G.;
"Galectin-9 binding to cell surface protein disulfide isomerase
regulates the redox environment to enhance T-cell migration and HIV
entry.";
Proc. Natl. Acad. Sci. U.S.A. 108:10650-10655(2011).
[31]
INTERACTION WITH MTTP, AND SUBCELLULAR LOCATION.
PubMed=23475612; DOI=10.1194/jlr.M031658;
Khatun I., Walsh M.T., Hussain M.M.;
"Loss of both phospholipid and triglyceride transfer activities of
microsomal triglyceride transfer protein in abetalipoproteinemia.";
J. Lipid Res. 54:1541-1549(2013).
[32]
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).
[33]
PHOSPHORYLATION AT SER-357.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[34]
INVOLVEMENT IN CLCRP1, VARIANT CLCRP1 CYS-393, AND CHARACTERIZATION OF
VARIANT CLCRP1 CYS-393.
PubMed=25683117; DOI=10.1016/j.ajhg.2014.12.027;
Rauch F., Fahiminiya S., Majewski J., Carrot-Zhang J., Boudko S.,
Glorieux F., Mort J.S., Baechinger H.P., Moffatt P.;
"Cole-Carpenter syndrome is caused by a heterozygous missense mutation
in P4HB.";
Am. J. Hum. Genet. 96:425-431(2015).
[35]
INTERACTION WITH MTTP.
PubMed=26224785; DOI=10.1161/CIRCGENETICS.115.001106;
Walsh M.T., Iqbal J., Josekutty J., Soh J., Di Leo E., Oezaydin E.,
Guenduez M., Tarugi P., Hussain M.M.;
"A novel abetalipoproteinemia missense mutation highlights the
importance of N-Terminal beta-barrel in microsomal triglyceride
transfer protein function.";
Circ. Cardiovasc. Genet. 8:677-687(2015).
[36]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-17, 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).
[37]
STRUCTURE BY NMR OF 18-137.
PubMed=8580850; DOI=10.1002/pro.5560041216;
Kemmink J., Darby N.J., Dijkstra K., Scheek R.M., Creighton T.E.;
"Nuclear magnetic resonance characterization of the N-terminal
thioredoxin-like domain of protein disulfide isomerase.";
Protein Sci. 4:2587-2593(1995).
[38]
STRUCTURE BY NMR OF 18-137, AND DISULFIDE BOND.
PubMed=8672469; DOI=10.1021/bi960335m;
Kemmink J., Darby N.J., Dijkstra K., Nilges M., Creighton T.E.;
"Structure determination of the N-terminal thioredoxin-like domain of
protein disulfide isomerase using multidimensional heteronuclear
13C/15N NMR spectroscopy.";
Biochemistry 35:7684-7691(1996).
[39]
STRUCTURE BY NMR OF 136-245.
PubMed=10383197; DOI=10.1023/A:1008341820489;
Kemmink J., Dijkstra K., Mariani M., Scheek R.M., Penka E., Nilges M.,
Darby N.J.;
"The structure in solution of the B domain of protein disulfide
isomerase.";
J. Biomol. NMR 13:357-368(1999).
[40]
STRUCTURE BY NMR OF 368-477.
RIKEN structural genomics initiative (RSGI);
"The solution structure of the second thioredoxin-like domain of human
protein disulfide-isomerase.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: This multifunctional protein catalyzes the formation,
breakage and rearrangement of disulfide bonds. At the cell
surface, seems to act as a reductase that cleaves disulfide bonds
of proteins attached to the cell. May therefore cause structural
modifications of exofacial proteins. Inside the cell, seems to
form/rearrange disulfide bonds of nascent proteins. At high
concentrations, functions as a chaperone that inhibits aggregation
of misfolded proteins. At low concentrations, facilitates
aggregation (anti-chaperone activity). May be involved with other
chaperones in the structural modification of the TG precursor in
hormone biogenesis. Also acts a structural subunit of various
enzymes such as prolyl 4-hydroxylase and microsomal
triacylglycerol transfer protein MTTP. Receptor for LGALS9; the
interaction retains P4HB at the cell surface of Th2 T helper
cells, increasing disulfide reductase activity at the plasma
membrane, altering the plasma membrane redox state and enhancing
cell migration (PubMed:21670307). {ECO:0000269|PubMed:10636893,
ECO:0000269|PubMed:12485997, ECO:0000269|PubMed:21670307}.
-!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
proteins.
-!- SUBUNIT: Heterodimer; heterodimerizes with the protein microsomal
triglyceride transfer MTTP (PubMed:23475612, PubMed:26224785).
Homodimer. Monomers and homotetramers may also occur. Also
constitutes the structural subunit of prolyl 4-hydroxylase and of
the microsomal triacylglycerol transfer protein MTTP in mammalian
cells. Stabilizes both enzymes and retain them in the ER without
contributing to the catalytic activity (By similarity). Binds
UBQLN1 (PubMed:12095988). Interacts with ERO1B (PubMed:11707400).
Binds to CD4, and upon HIV-1 binding to the cell membrane, is part
of a P4HB/PDI-CD4-CXCR4-gp120 complex. {ECO:0000250,
ECO:0000269|PubMed:11707400, ECO:0000269|PubMed:12095988,
ECO:0000269|PubMed:23475612, ECO:0000269|PubMed:26224785}.
-!- INTERACTION:
Q96HE7:ERO1A; NbExp=3; IntAct=EBI-395883, EBI-2564539;
P60520:GABARAPL2; NbExp=2; IntAct=EBI-395883, EBI-720116;
Q8TCT9:HM13; NbExp=3; IntAct=EBI-395883, EBI-347472;
Q13162:PRDX4; NbExp=2; IntAct=EBI-395883, EBI-2211957;
Q03518:TAP1; NbExp=4; IntAct=EBI-395883, EBI-747259;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:23475612}. Endoplasmic reticulum lumen
{ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:23475612}.
Melanosome {ECO:0000269|PubMed:12643545,
ECO:0000269|PubMed:17081065}. Cell membrane
{ECO:0000269|PubMed:21670307}; Peripheral membrane protein
{ECO:0000305}. Note=Highly abundant. In some cell types, seems to
be also secreted or associated with the plasma membrane, where it
undergoes constant shedding and replacement from intracellular
sources (Probable). Localizes near CD4-enriched regions on
lymphoid cell surfaces (PubMed:11181151). Identified by mass
spectrometry in melanosome fractions from stage I to stage IV
(PubMed:10636893). Colocalizes with MTTP in the endoplasmic
reticulum (PubMed:23475612). {ECO:0000269|PubMed:10636893,
ECO:0000269|PubMed:11181151, ECO:0000269|PubMed:23475612,
ECO:0000305}.
-!- DISEASE: Cole-Carpenter syndrome 1 (CLCRP1) [MIM:112240]: A form
of Cole-Carpenter syndrome, a disorder characterized by features
of osteogenesis imperfecta such as bone deformities and severe
bone fragility with frequent fractures, in association with
craniosynostosis, ocular proptosis, hydrocephalus, growth failure
and distinctive facial features. Craniofacial findings include
marked frontal bossing, midface hypoplasia, and micrognathia.
Despite the craniosynostosis and hydrocephalus, intellectual
development is normal. CLCRP1 inheritance is autosomal dominant.
{ECO:0000269|PubMed:25683117}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Reduces and may activate fusogenic properties of
HIV-1 gp120 surface protein, thereby enabling HIV-1 entry into the
cell.
-!- SIMILARITY: Belongs to the protein disulfide isomerase family.
{ECO:0000305}.
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EMBL; X05130; CAA28775.1; -; mRNA.
EMBL; J02783; AAA61169.1; -; mRNA.
EMBL; M22806; AAC13652.1; -; Genomic_DNA.
EMBL; M22803; AAC13652.1; JOINED; Genomic_DNA.
EMBL; M22804; AAC13652.1; JOINED; Genomic_DNA.
EMBL; M22805; AAC13652.1; JOINED; Genomic_DNA.
EMBL; AK315631; BAG37999.1; -; mRNA.
EMBL; CH471099; EAW89690.1; -; Genomic_DNA.
EMBL; BC010859; AAH10859.1; -; mRNA.
EMBL; BC029617; AAH29617.1; -; mRNA.
EMBL; BC071892; AAH71892.1; -; mRNA.
EMBL; S37207; AAB22262.2; -; Genomic_DNA.
EMBL; X07077; CAA30112.1; -; mRNA.
CCDS; CCDS11787.1; -.
PIR; A31913; ISHUSS.
RefSeq; NP_000909.2; NM_000918.3.
UniGene; Hs.464336; -.
PDB; 1BJX; NMR; -; A=136-245.
PDB; 1MEK; NMR; -; A=18-137.
PDB; 1X5C; NMR; -; A=368-475.
PDB; 2BJX; NMR; -; A=136-245.
PDB; 2K18; NMR; -; A=135-357.
PDB; 3BJ5; X-ray; 2.20 A; A=230-368.
PDB; 3UEM; X-ray; 2.29 A; A=137-479.
PDB; 4EKZ; X-ray; 2.51 A; A=18-479.
PDB; 4EL1; X-ray; 2.88 A; A/B=18-479.
PDB; 4JU5; X-ray; 2.28 A; A/B=135-367.
PDBsum; 1BJX; -.
PDBsum; 1MEK; -.
PDBsum; 1X5C; -.
PDBsum; 2BJX; -.
PDBsum; 2K18; -.
PDBsum; 3BJ5; -.
PDBsum; 3UEM; -.
PDBsum; 4EKZ; -.
PDBsum; 4EL1; -.
PDBsum; 4JU5; -.
ProteinModelPortal; P07237; -.
SMR; P07237; -.
BioGrid; 111073; 142.
CORUM; P07237; -.
DIP; DIP-32979N; -.
IntAct; P07237; 83.
MINT; P07237; -.
STRING; 9606.ENSP00000327801; -.
BindingDB; P07237; -.
ChEMBL; CHEMBL5422; -.
DrugBank; DB03615; Ribostamycin.
iPTMnet; P07237; -.
PhosphoSitePlus; P07237; -.
SwissPalm; P07237; -.
BioMuta; P4HB; -.
DMDM; 2507460; -.
DOSAC-COBS-2DPAGE; P07237; -.
OGP; P07237; -.
REPRODUCTION-2DPAGE; IPI00010796; -.
REPRODUCTION-2DPAGE; P07237; -.
SWISS-2DPAGE; P07237; -.
EPD; P07237; -.
MaxQB; P07237; -.
PaxDb; P07237; -.
PeptideAtlas; P07237; -.
PRIDE; P07237; -.
TopDownProteomics; P07237; -.
DNASU; 5034; -.
Ensembl; ENST00000331483; ENSP00000327801; ENSG00000185624.
GeneID; 5034; -.
KEGG; hsa:5034; -.
UCSC; uc002kbn.2; human.
CTD; 5034; -.
DisGeNET; 5034; -.
EuPathDB; HostDB:ENSG00000185624.14; -.
GeneCards; P4HB; -.
HGNC; HGNC:8548; P4HB.
HPA; CAB012463; -.
HPA; HPA018884; -.
MalaCards; P4HB; -.
MIM; 112240; phenotype.
MIM; 176790; gene.
neXtProt; NX_P07237; -.
OpenTargets; ENSG00000185624; -.
PharmGKB; PA32876; -.
eggNOG; KOG0190; Eukaryota.
eggNOG; COG0526; LUCA.
GeneTree; ENSGT00860000133691; -.
HOGENOM; HOG000162459; -.
HOVERGEN; HBG005920; -.
InParanoid; P07237; -.
KO; K09580; -.
OMA; QYGVRGY; -.
OrthoDB; EOG091G08WM; -.
PhylomeDB; P07237; -.
TreeFam; TF106381; -.
BioCyc; MetaCyc:HS06845-MONOMER; -.
BRENDA; 5.3.4.1; 2681.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-8866423; VLDL assembly.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-8963888; Chylomicron assembly.
Reactome; R-HSA-9020591; Interleukin-12 signaling.
Reactome; R-HSA-9020933; Interleukin-23 signaling.
ChiTaRS; P4HB; human.
EvolutionaryTrace; P07237; -.
GeneWiki; P4HB; -.
GenomeRNAi; 5034; -.
PMAP-CutDB; P07237; -.
PRO; PR:P07237; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000185624; -.
CleanEx; HS_P4HB; -.
ExpressionAtlas; P07237; baseline and differential.
Genevisible; P07237; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016222; C:procollagen-proline 4-dioxygenase complex; IDA:MGI.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0015037; F:peptide disulfide oxidoreductase activity; IDA:UniProtKB.
GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; TAS:ProtInc.
GO; GO:0003756; F:protein disulfide isomerase activity; IDA:CACAO.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
GO; GO:0034378; P:chylomicron assembly; TAS:Reactome.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0038155; P:interleukin-23-mediated signaling pathway; TAS:Reactome.
GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IDA:MGI.
GO; GO:0046598; P:positive regulation of viral entry into host cell; IMP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0006457; P:protein folding; IBA:GO_Central.
GO; GO:1902175; P:regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IMP:BHF-UCL.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:BHF-UCL.
GO; GO:0034379; P:very-low-density lipoprotein particle assembly; TAS:Reactome.
InterPro; IPR005788; Disulphide_isomerase.
InterPro; IPR005792; Prot_disulphide_isomerase.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR017937; Thioredoxin_CS.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF00085; Thioredoxin; 2.
SUPFAM; SSF52833; SSF52833; 4.
TIGRFAMs; TIGR01130; ER_PDI_fam; 1.
TIGRFAMs; TIGR01126; pdi_dom; 2.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00194; THIOREDOXIN_1; 2.
PROSITE; PS51352; THIOREDOXIN_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Cell membrane; Chaperone;
Complete proteome; Craniosynostosis; Direct protein sequencing;
Disease mutation; Disulfide bond; Endoplasmic reticulum; Isomerase;
Membrane; Osteogenesis imperfecta; Phosphoprotein;
Redox-active center; Reference proteome; Repeat; Signal.
SIGNAL 1 17 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:2079031,
ECO:0000269|PubMed:9150948,
ECO:0000269|Ref.10}.
CHAIN 18 508 Protein disulfide-isomerase.
/FTId=PRO_0000034195.
DOMAIN 18 134 Thioredoxin 1. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
DOMAIN 349 475 Thioredoxin 2. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
MOTIF 505 508 Prevents secretion from ER.
ACT_SITE 53 53 Nucleophile.
ACT_SITE 56 56 Nucleophile.
ACT_SITE 397 397 Nucleophile. {ECO:0000250}.
ACT_SITE 400 400 Nucleophile. {ECO:0000250}.
SITE 54 54 Contributes to redox potential value.
SITE 55 55 Contributes to redox potential value.
SITE 120 120 Lowers pKa of C-terminal Cys of first
active site.
SITE 398 398 Contributes to redox potential value.
{ECO:0000250}.
SITE 399 399 Contributes to redox potential value.
{ECO:0000250}.
SITE 461 461 Lowers pKa of C-terminal Cys of second
active site. {ECO:0000250}.
MOD_RES 200 200 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09103}.
MOD_RES 222 222 N6-succinyllysine.
{ECO:0000250|UniProtKB:P09103}.
MOD_RES 271 271 N6-succinyllysine.
{ECO:0000250|UniProtKB:P09103}.
MOD_RES 357 357 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
DISULFID 53 56 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691,
ECO:0000269|PubMed:8672469}.
DISULFID 397 400 Redox-active. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
VARIANT 393 393 Y -> C (in CLCRP1; impairs ability to act
as a disulfide isomerase enzyme;
dbSNP:rs786204843).
{ECO:0000269|PubMed:25683117}.
/FTId=VAR_073440.
CONFLICT 10 11 AV -> PW (in Ref. 1; CAA28775).
{ECO:0000305}.
CONFLICT 21 21 E -> D (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 24 24 D -> V (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 44 45 LL -> PP (in Ref. 1; CAA28775).
{ECO:0000305}.
CONFLICT 49 49 Y -> H (in Ref. 1; CAA28775).
{ECO:0000305}.
CONFLICT 141 141 P -> R (in Ref. 2; AAA61169).
{ECO:0000305}.
CONFLICT 360 362 LPE -> RAG (in Ref. 2; AAA61169).
{ECO:0000305}.
CONFLICT 372 372 L -> P (in Ref. 2; AAA61169).
{ECO:0000305}.
CONFLICT 439 439 S -> G (in Ref. 1; CAA28775).
{ECO:0000305}.
CONFLICT 444 444 K -> G (in Ref. 1; CAA28775).
{ECO:0000305}.
CONFLICT 460 460 E -> Q (in Ref. 15; CAA30112).
{ECO:0000305}.
CONFLICT 481 481 D -> V (in Ref. 1; CAA28775).
{ECO:0000305}.
STRAND 21 23 {ECO:0000244|PDB:4EKZ}.
STRAND 26 28 {ECO:0000244|PDB:4EKZ}.
TURN 31 33 {ECO:0000244|PDB:4EL1}.
HELIX 34 40 {ECO:0000244|PDB:4EKZ}.
STRAND 42 49 {ECO:0000244|PDB:4EKZ}.
HELIX 54 72 {ECO:0000244|PDB:4EKZ}.
STRAND 78 83 {ECO:0000244|PDB:4EKZ}.
TURN 84 86 {ECO:0000244|PDB:4EKZ}.
HELIX 88 93 {ECO:0000244|PDB:4EKZ}.
STRAND 101 106 {ECO:0000244|PDB:4EKZ}.
STRAND 110 112 {ECO:0000244|PDB:4EL1}.
STRAND 114 116 {ECO:0000244|PDB:4EL1}.
HELIX 122 132 {ECO:0000244|PDB:4EKZ}.
STRAND 137 139 {ECO:0000244|PDB:3UEM}.
HELIX 143 151 {ECO:0000244|PDB:4JU5}.
STRAND 153 160 {ECO:0000244|PDB:4JU5}.
TURN 162 165 {ECO:0000244|PDB:1BJX}.
HELIX 167 178 {ECO:0000244|PDB:4JU5}.
STRAND 180 182 {ECO:0000244|PDB:4JU5}.
STRAND 184 187 {ECO:0000244|PDB:4JU5}.
HELIX 190 195 {ECO:0000244|PDB:4JU5}.
STRAND 199 209 {ECO:0000244|PDB:4JU5}.
STRAND 212 215 {ECO:0000244|PDB:4JU5}.
HELIX 222 232 {ECO:0000244|PDB:4JU5}.
STRAND 237 239 {ECO:0000244|PDB:3BJ5}.
TURN 242 244 {ECO:0000244|PDB:3BJ5}.
HELIX 245 249 {ECO:0000244|PDB:3BJ5}.
STRAND 250 252 {ECO:0000244|PDB:3BJ5}.
STRAND 255 260 {ECO:0000244|PDB:3BJ5}.
STRAND 265 267 {ECO:0000244|PDB:3BJ5}.
HELIX 268 280 {ECO:0000244|PDB:3BJ5}.
TURN 281 285 {ECO:0000244|PDB:3BJ5}.
STRAND 287 291 {ECO:0000244|PDB:3BJ5}.
HELIX 296 298 {ECO:0000244|PDB:3BJ5}.
HELIX 299 304 {ECO:0000244|PDB:3BJ5}.
HELIX 309 311 {ECO:0000244|PDB:3BJ5}.
STRAND 313 319 {ECO:0000244|PDB:3BJ5}.
STRAND 321 323 {ECO:0000244|PDB:3BJ5}.
STRAND 325 327 {ECO:0000244|PDB:3BJ5}.
STRAND 330 332 {ECO:0000244|PDB:4EKZ}.
HELIX 336 347 {ECO:0000244|PDB:3BJ5}.
STRAND 353 355 {ECO:0000244|PDB:3BJ5}.
HELIX 362 364 {ECO:0000244|PDB:3BJ5}.
STRAND 367 372 {ECO:0000244|PDB:3UEM}.
TURN 374 376 {ECO:0000244|PDB:3UEM}.
HELIX 377 381 {ECO:0000244|PDB:3UEM}.
STRAND 387 393 {ECO:0000244|PDB:3UEM}.
HELIX 398 413 {ECO:0000244|PDB:3UEM}.
TURN 414 416 {ECO:0000244|PDB:3UEM}.
STRAND 418 426 {ECO:0000244|PDB:3UEM}.
TURN 427 429 {ECO:0000244|PDB:3UEM}.
STRAND 439 446 {ECO:0000244|PDB:3UEM}.
STRAND 448 451 {ECO:0000244|PDB:3UEM}.
HELIX 463 470 {ECO:0000244|PDB:3UEM}.
TURN 471 473 {ECO:0000244|PDB:3UEM}.
SEQUENCE 508 AA; 57116 MW; 906CE6D9900B8FCE CRC64;
MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA PWCGHCKALA
PEYAKAAGKL KAEGSEIRLA KVDATEESDL AQQYGVRGYP TIKFFRNGDT ASPKEYTAGR
EADDIVNWLK KRTGPAATTL PDGAAAESLV ESSEVAVIGF FKDVESDSAK QFLQAAEAID
DIPFGITSNS DVFSKYQLDK DGVVLFKKFD EGRNNFEGEV TKENLLDFIK HNQLPLVIEF
TEQTAPKIFG GEIKTHILLF LPKSVSDYDG KLSNFKTAAE SFKGKILFIF IDSDHTDNQR
ILEFFGLKKE ECPAVRLITL EEEMTKYKPE SEELTAERIT EFCHRFLEGK IKPHLMSQEL
PEDWDKQPVK VLVGKNFEDV AFDEKKNVFV EFYAPWCGHC KQLAPIWDKL GETYKDHENI
VIAKMDSTAN EVEAVKVHSF PTLKFFPASA DRTVIDYNGE RTLDGFKKFL ESGGQDGAGD
DDDLEDLEEA EEPDMEEDDD QKAVKDEL


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