Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Programmed cell death protein 6 (Apoptosis-linked gene 2 protein homolog) (ALG-2)

 PDCD6_HUMAN             Reviewed;         191 AA.
O75340; B2RD16; E7ESR3; Q2YDC2; Q5TZS0;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
27-SEP-2017, entry version 169.
RecName: Full=Programmed cell death protein 6;
AltName: Full=Apoptosis-linked gene 2 protein homolog {ECO:0000250|UniProtKB:P12815};
Short=ALG-2 {ECO:0000250|UniProtKB:P12815};
Name=PDCD6; Synonyms=ALG2 {ECO:0000250|UniProtKB:P12815};
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).
Ganjei J.K., D'Adamio L.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Urcelay E., Ibarreta D., Parrilla R., Ayuso M.S.;
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
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).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Colon, Ovary, and Placenta;
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).
[8]
INTERACTION WITH PEF1.
PubMed=11278427; DOI=10.1074/jbc.M008649200;
Kitaura Y., Matsumoto S., Satoh H., Hitomi K., Maki M.;
"Peflin and ALG-2, members of the penta-EF-hand protein family, form a
heterodimer that dissociates in a Ca2+-dependent manner.";
J. Biol. Chem. 276:14053-14058(2001).
[9]
INTERACTION WITH PEF1.
PubMed=11883899; DOI=10.1006/abbi.2001.2736;
Kitaura Y., Satoh H., Takahashi H., Shibata H., Maki M.;
"Both ALG-2 and peflin, penta-EF-hand (PEF) proteins, are stabilized
by dimerization through their fifth EF-hand regions.";
Arch. Biochem. Biophys. 399:12-18(2002).
[10]
INTERACTION WITH ANXA11.
PubMed=11883939; DOI=10.1006/bbrc.2002.6600;
Satoh H., Shibata H., Nakano Y., Kitaura Y., Maki M.;
"ALG-2 interacts with the amino-terminal domain of annexin XI in a
Ca(2+)-dependent manner.";
Biochem. Biophys. Res. Commun. 291:1166-1172(2002).
[11]
FUNCTION, AND INTERACTION WITH DAPK1.
PubMed=16132846; DOI=10.1007/s10529-005-7869-x;
Lee J.H., Rho S.B., Chun T.;
"Programmed cell death 6 (PDCD6) protein interacts with death-
associated protein kinase 1 (DAPk1): additive effect on apoptosis via
caspase-3 dependent pathway.";
Biotechnol. Lett. 27:1011-1015(2005).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH RBM22.
PubMed=17045351; DOI=10.1016/j.bbamcr.2006.09.003;
Montaville P., Dai Y., Cheung C.Y., Giller K., Becker S., Michalak M.,
Webb S.E., Miller A.L., Krebs J.;
"Nuclear translocation of the calcium-binding protein ALG-2 induced by
the RNA-binding protein RBM22.";
Biochim. Biophys. Acta 1763:1335-1343(2006).
[13]
INTERACTION WITH SEC31A AND PDCD6IP, MUTAGENESIS OF GLU-47 AND
GLU-114, AND SUBCELLULAR LOCATION.
PubMed=16957052; DOI=10.1091/mbc.E06-05-0444;
Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.;
"The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum
exit sites by Sec31A and stabilizes the localization of Sec31A.";
Mol. Biol. Cell 17:4876-4887(2006).
[14]
INTERACTION WITH WITH SHISA5.
PubMed=17889823; DOI=10.1016/j.abb.2007.07.028;
Draeby I., Woods Y.L., la Cour J.M., Mollerup J., Bourdon J.C.,
Berchtold M.W.;
"The calcium binding protein ALG-2 binds and stabilizes Scotin, a p53-
inducible gene product localized at the endoplasmic reticulum
membrane.";
Arch. Biochem. Biophys. 467:87-94(2007).
[15]
INTERACTION WITH PLSCR3; PLSCR4; PDCD6IP; ANXA7; ANXA11; SEC31A AND
TSG101, AND MUTAGENESIS OF GLU-47; TRP-57; PHE-60; TYR-91; TRP-95;
GLU-114 AND TYR-180.
PubMed=18256029; DOI=10.1074/jbc.M800717200;
Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
Maki M.;
"Identification of Alix-type and non-Alix-type ALG-2-binding sites in
human phospholipid scramblase 3: differential binding to an
alternatively spliced isoform and amino acid-substituted mutants.";
J. Biol. Chem. 283:9623-9632(2008).
[16]
FUNCTION.
PubMed=19520058; DOI=10.1016/j.bbrc.2009.06.015;
Okumura M., Ichioka F., Kobayashi R., Suzuki H., Yoshida H.,
Shibata H., Maki M.;
"Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor
that bridges Alix and TSG101.";
Biochem. Biophys. Res. Commun. 386:237-241(2009).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MCOLN1.
PubMed=19864416; DOI=10.1074/jbc.M109.047241;
Vergarajauregui S., Martina J.A., Puertollano R.;
"Identification of the penta-EF-hand protein ALG-2 as a Ca2+-dependent
interactor of mucolipin-1.";
J. Biol. Chem. 284:36357-36366(2009).
[18]
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).
[19]
SUBCELLULAR LOCATION.
PubMed=21122810; DOI=10.1016/j.bbamcr.2010.11.010;
Janowicz A., Michalak M., Krebs J.;
"Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7.";
Biochim. Biophys. Acta 1813:1045-1049(2011).
[20]
FUNCTION, AND INTERACTION WITH KDR.
PubMed=21893193; DOI=10.1016/j.cellsig.2011.08.013;
Rho S.B., Song Y.J., Lim M.C., Lee S.H., Kim B.R., Park S.Y.;
"Programmed cell death 6 (PDCD6) inhibits angiogenesis through
PI3K/mTOR/p70S6K pathway by interacting of VEGFR-2.";
Cell. Signal. 24:131-139(2012).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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).
[22]
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).
[23]
FUNCTION, INTERACTION WITH PEF1, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF GLU-47 AND PHE-60.
PubMed=27716508; DOI=10.1016/j.cell.2016.09.026;
McGourty C.A., Akopian D., Walsh C., Gorur A., Werner A., Schekman R.,
Bautista D., Rape M.;
"Regulation of the CUL3 ubiquitin ligase by a calcium-dependent co-
adaptor.";
Cell 167:525-538(2016).
[24]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TFG.
PubMed=27813252; DOI=10.1111/febs.13949;
Kanadome T., Shibata H., Kuwata K., Takahara T., Maki M.;
"The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit
site localization and polymerization of Trk-fused gene (TFG)
protein.";
FEBS J. 284:56-76(2017).
[25]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 24-191 IN COMPLEX WITH
CALCIUM AND ZINC.
PubMed=18997320; DOI=10.1107/S1744309108030297;
Suzuki H., Kawasaki M., Kakiuchi T., Shibata H., Wakatsuki S.,
Maki M.;
"Crystallization and X-ray diffraction analysis of N-terminally
truncated human ALG-2.";
Acta Crystallogr. F 64:974-977(2008).
[26]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 24-191 IN COMPLEXES WITH
CALCIUM; ZINC AND PDCD6IP, SUBUNIT, AND INTERACTION WITH PDCD6IP.
PubMed=18940611; DOI=10.1016/j.str.2008.07.012;
Suzuki H., Kawasaki M., Inuzuka T., Okumura M., Kakiuchi T.,
Shibata H., Wakatsuki S., Maki M.;
"Structural basis for Ca2+ -dependent formation of ALG-2/Alix peptide
complex: Ca2+/EF3-driven arginine switch mechanism.";
Structure 16:1562-1573(2008).
[27]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-191 IN COMPLEX WITH
CALCIUM, INTERACTION WITH PDCD6IP; TSG101; ANXA7 AND ANXA11,
CALCIUM-BINDING, DOMAIN, AND MUTAGENESIS OF PHE-122.
PubMed=20691033; DOI=10.1186/1472-6807-10-25;
Inuzuka T., Suzuki H., Kawasaki M., Shibata H., Wakatsuki S., Maki M.;
"Molecular basis for defect in Alix-binding by alternatively spliced
isoform of ALG-2 (ALG-2DeltaGF122) and structural roles of F122 in
target recognition.";
BMC Struct. Biol. 10:25-25(2010).
[28]
X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 20-191 IN COMPLEX WITH ZINC
AND SEC31A, INTERACTION WITH SEC31A AND PDCD6IP, CALCIUM-BINDING,
DOMAIN, AND MUTAGENESIS OF LEU-52; SER-53; TRP-57; PHE-85; TRP-89;
ILE-92 AND PHE-148.
PubMed=25667979; DOI=10.3390/ijms16023677;
Takahashi T., Kojima K., Zhang W., Sasaki K., Ito M., Suzuki H.,
Kawasaki M., Wakatsuki S., Takahara T., Shibata H., Maki M.;
"Structural analysis of the complex between penta-EF-hand ALG-2
protein and Sec31A peptide reveals a novel target recognition
mechanism of ALG-2.";
Int. J. Mol. Sci. 16:3677-3699(2015).
[29]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 24-191 IN COMPLEX WITH
HEBP2, FUNCTION, INTERACTION WITH HEBP2, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF TRP-57.
PubMed=27784779; DOI=10.1074/jbc.M116.752444;
Ma J., Zhang X., Feng Y., Zhang H., Wang X., Zheng Y., Qiao W.,
Liu X.;
"Structural and functional study of apoptosis-linked gene-2.Heme-
binding protein 2 interactions in HIV-1 production.";
J. Biol. Chem. 291:26670-26685(2016).
[30]
VARIANT [LARGE SCALE ANALYSIS] CYS-123.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Calcium sensor that plays a key role in processes such
as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal
biogenesis or membrane repair. Acts as an adapter that bridges
unrelated proteins or stabilizes weak protein-protein complexes in
response to calcium: calcium-binding triggers exposure of apolar
surface, promoting interaction with different sets of proteins
thanks to 3 different hydrophobic pockets, leading to
translocation to membranes (PubMed:20691033, PubMed:25667979).
Involved in ER-Golgi transport by promoting the association
between PDCD6IP and TSG101, thereby bridging together the ESCRT-
III and ESCRT-I complexes (PubMed:19520058). Together with PEF1,
acts as calcium-dependent adapter for the BCR(KLHL12) complex, a
complex involved in ER-Golgi transport by regulating the size of
COPII coats (PubMed:27716508). In response to cytosolic calcium
increase, the heterodimer formed with PEF1 interacts with, and
bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or
SEC31B), promoting monoubiquitination of SEC31 and subsequent
collagen export, which is required for neural crest specification
(PubMed:27716508). Involved in the regulation of the distribution
and function of MCOLN1 in the endosomal pathway (PubMed:19864416).
Promotes localization and polymerization of TFG at endoplasmic
reticulum exit site (PubMed:27813252). Required for T-cell
receptor-, Fas-, and glucocorticoid-induced apoptosis (By
similarity). May mediate Ca(2+)-regulated signals along the death
pathway: interaction with DAPK1 can accelerate apoptotic cell
death by increasing caspase-3 activity (PubMed:16132846). Its role
in apoptosis may however be indirect, as suggested by knockout
experiments (By similarity). May inhibit KDR/VEGFR2-dependent
angiogenesis; the function involves inhibition of VEGF-induced
phosphorylation of the Akt signaling pathway (PubMed:21893193). In
case of infection by HIV-1 virus, indirectly inhibits HIV-1
production by affecting viral Gag expression and distribution
(PubMed:27784779). {ECO:0000250|UniProtKB:P12815,
ECO:0000269|PubMed:16132846, ECO:0000269|PubMed:19520058,
ECO:0000269|PubMed:19864416, ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:21893193, ECO:0000269|PubMed:25667979,
ECO:0000269|PubMed:27716508, ECO:0000269|PubMed:27784779,
ECO:0000269|PubMed:27813252}.
-!- FUNCTION: Isoform 2: Has a lower Ca(2+) affinity than isoform 1
(By similarity). {ECO:0000250|UniProtKB:P12815}.
-!- SUBUNIT: Homodimer and heterodimer; heterodimerizes (via the EF-
hand 5) with PEF1 (PubMed:11278427, PubMed:11883899,
PubMed:27784779). Isoform 1 and isoform 2 self-associate; probably
forming homodimers. Interacts with CPNE4 (via VWFA domain) (By
similarity). Interacts with PDCD6IP; the interaction is calcium-
dependent (PubMed:16957052, PubMed:18256029, PubMed:18940611,
PubMed:20691033, PubMed:25667979). Interacts with RBM22
(PubMed:17045351). Interacts with PLSCR4 (PubMed:18256029).
Interacts with ANXA7 and TSG101 (PubMed:18256029,
PubMed:20691033). Interacts with DAPK1 (PubMed:16132846).
Interacts with SEC31A; the interaction is calcium-dependent and
promotes monoubiquitination of SEC31A (PubMed:16957052,
PubMed:18256029, PubMed:27716508, PubMed:25667979). Interacts with
ANXA11 (via N-terminus); the interaction is calcium-dependent
(PubMed:11883939, PubMed:18256029, PubMed:18940611). Interacts
with PLSCR3 (via N-terminus); the interaction is calcium-dependent
(PubMed:18256029). Interacts with MCOLN1; the interaction is
calcium-dependent (PubMed:19864416). Interacts with KDR; the
interaction is calcium-dependent (PubMed:21893193). Interacts with
HEBP2; the interaction is calcium-dependent (PubMed:27784779).
Interacts with TFG (PubMed:27813252). Isoform 1: Interacts with
SHISA5, leading to stabilize it (PubMed:17889823). Isoform 2: Does
not interact with SHISA5 (PubMed:17889823). Isoform 2: Does not
interact with PDCD6IP, TSG101, ANXA7 and ANXA11 (PubMed:18256029,
PubMed:20691033). {ECO:0000250|UniProtKB:P12815,
ECO:0000269|PubMed:11278427, ECO:0000269|PubMed:11883899,
ECO:0000269|PubMed:11883939, ECO:0000269|PubMed:16132846,
ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:17045351,
ECO:0000269|PubMed:17889823, ECO:0000269|PubMed:18256029,
ECO:0000269|PubMed:18940611, ECO:0000269|PubMed:19864416,
ECO:0000269|PubMed:20691033, ECO:0000269|PubMed:21893193,
ECO:0000269|PubMed:25667979, ECO:0000269|PubMed:27716508,
ECO:0000269|PubMed:27784779, ECO:0000269|PubMed:27813252}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-352915, EBI-352915;
P50995:ANXA11; NbExp=4; IntAct=EBI-352915, EBI-715243;
Q5T0G8:ANXA11; NbExp=3; IntAct=EBI-352915, EBI-10245225;
P53355:DAPK1; NbExp=3; IntAct=EBI-352915, EBI-358616;
Q9Y5Z4:HEBP2; NbExp=6; IntAct=EBI-352915, EBI-741593;
P35968:KDR; NbExp=4; IntAct=EBI-352915, EBI-1005487;
Q8WUM4:PDCD6IP; NbExp=5; IntAct=EBI-352915, EBI-310624;
Q9UBV8:PEF1; NbExp=11; IntAct=EBI-352915, EBI-724639;
Q9NRY6:PLSCR3; NbExp=9; IntAct=EBI-352915, EBI-750734;
Q9H3S7:PTPN23; NbExp=3; IntAct=EBI-352915, EBI-724478;
O94979:SEC31A; NbExp=6; IntAct=EBI-352915, EBI-1767898;
A5D8V6:VPS37C; NbExp=5; IntAct=EBI-352915, EBI-2559305;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:27813252};
Peripheral membrane protein {ECO:0000269|PubMed:16957052}.
Cytoplasmic vesicle, COPII-coated vesicle membrane
{ECO:0000269|PubMed:27716508}. Cytoplasm
{ECO:0000269|PubMed:27716508, ECO:0000269|PubMed:27784779}.
Nucleus {ECO:0000269|PubMed:17045351, ECO:0000269|PubMed:21122810,
ECO:0000269|PubMed:27784779}. Endosome
{ECO:0000269|PubMed:19864416}. Note=Interaction with RBM22 induces
relocalization from the cytoplasm to the nucleus
(PubMed:17045351). Translocated from the cytoplasm to the nucleus
after heat shock cell treatment. Accumulates in cytoplasmic
vesicle-like organelles after heat shock treatment, which may
represent stress granules (PubMed:21122810). In response to
calcium increase, relocates from cytolasm to COPII vesicle coat
(PubMed:27716508). Localizes to endoplasmic reticulum exit site
(ERES) (PubMed:27813252). {ECO:0000269|PubMed:17045351,
ECO:0000269|PubMed:21122810, ECO:0000269|PubMed:27716508,
ECO:0000269|PubMed:27813252}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O75340-1; Sequence=Displayed;
Name=2; Synonyms=ALG-2(delta)GF122;
IsoId=O75340-2; Sequence=VSP_045113;
Name=3;
IsoId=O75340-3; Sequence=VSP_045542;
Note=No experimental confirmation available.;
-!- DOMAIN: Interacts with different set of proteins thanks to 3
different hydrophobic pockets (PubMed:20691033, PubMed:25667979).
Hydrophobic pockets 1 and 2, which mediate interaction with
PDCD6IP, are largely formed by residues from EF-hand 3 (EF3) to 5
(EF5), as well as by Tyr-180 (EF5) of a dimerizing molecule
(Pocket 1) and from EF-hand (EF2) to 4 (EF4) (Pocket 2)
(PubMed:20691033). Hydrophobic pocket 3, which mediates
interaction with SEC31A, is mainly formed by residues from EF-hand
1 (EF1) to 3 (EF3) (PubMed:25667979).
{ECO:0000269|PubMed:20691033, ECO:0000269|PubMed:25667979}.
-!- DOMAIN: EF-hand 1 (EF1) and 3 (EF3) are the high-affinity calcium-
binding sites, while EF-hand 5 (EF5) binds calcium with low-
affinity (PubMed:18940611, PubMed:20691033). A one-residue
insertion in the EF5-binding loop prevents the glutamyl residue at
the C-terminal end of the loop from serving as the canonical
bidentate calcium ligand (PubMed:18940611, PubMed:20691033). EF5
acts as a high-affinity magnesium-binding domain instead (By
similarity). Magnesium, may affect dimerization (By similarity).
EF5 may bind either calcium or magnesium depending on the context
(By similarity). {ECO:0000250|UniProtKB:P12815,
ECO:0000269|PubMed:18940611, ECO:0000269|PubMed:20691033}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PDCD6ID43402ch5p15.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF035606; AAC27697.1; -; mRNA.
EMBL; U58773; AAF14336.1; -; mRNA.
EMBL; AK315370; BAG37763.1; -; mRNA.
EMBL; BT020072; AAV38875.1; -; mRNA.
EMBL; AC010442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC021087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC118458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471235; EAW50991.1; -; Genomic_DNA.
EMBL; BC012384; AAH12384.1; -; mRNA.
EMBL; BC106706; AAI06707.1; -; mRNA.
EMBL; BC110291; AAI10292.1; -; mRNA.
EMBL; CB991882; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS3854.1; -. [O75340-1]
CCDS; CCDS58940.1; -. [O75340-2]
CCDS; CCDS58941.1; -. [O75340-3]
RefSeq; NP_001254485.1; NM_001267556.1. [O75340-2]
RefSeq; NP_001254486.1; NM_001267557.1.
RefSeq; NP_001254487.1; NM_001267558.1.
RefSeq; NP_001254488.1; NM_001267559.1. [O75340-3]
RefSeq; NP_037364.1; NM_013232.3. [O75340-1]
UniGene; Hs.50823; -.
PDB; 2ZN8; X-ray; 2.70 A; A=2-191.
PDB; 2ZN9; X-ray; 2.40 A; A/B=20-191.
PDB; 2ZND; X-ray; 1.70 A; A=20-191.
PDB; 2ZNE; X-ray; 2.20 A; A/B=24-191.
PDB; 2ZRS; X-ray; 3.10 A; A/B/C/D/E/F/G/H=24-191.
PDB; 2ZRT; X-ray; 3.30 A; A/B/C/D/E/F/G/H=24-191.
PDB; 3AAJ; X-ray; 2.40 A; A/B=24-191.
PDB; 3AAK; X-ray; 2.70 A; A=20-191.
PDB; 3WXA; X-ray; 2.36 A; A/B=20-191.
PDB; 5GQQ; X-ray; 2.20 A; C/D=24-191.
PDBsum; 2ZN8; -.
PDBsum; 2ZN9; -.
PDBsum; 2ZND; -.
PDBsum; 2ZNE; -.
PDBsum; 2ZRS; -.
PDBsum; 2ZRT; -.
PDBsum; 3AAJ; -.
PDBsum; 3AAK; -.
PDBsum; 3WXA; -.
PDBsum; 5GQQ; -.
ProteinModelPortal; O75340; -.
SMR; O75340; -.
BioGrid; 115333; 104.
CORUM; O75340; -.
DIP; DIP-33217N; -.
ELM; O75340; -.
IntAct; O75340; 63.
MINT; MINT-5000341; -.
STRING; 9606.ENSP00000264933; -.
TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
iPTMnet; O75340; -.
PhosphoSitePlus; O75340; -.
BioMuta; PDCD6; -.
EPD; O75340; -.
MaxQB; O75340; -.
PaxDb; O75340; -.
PeptideAtlas; O75340; -.
PRIDE; O75340; -.
TopDownProteomics; O75340-1; -. [O75340-1]
DNASU; 10016; -.
Ensembl; ENST00000264933; ENSP00000264933; ENSG00000249915. [O75340-1]
Ensembl; ENST00000505221; ENSP00000422085; ENSG00000249915. [O75340-3]
Ensembl; ENST00000507528; ENSP00000423815; ENSG00000249915. [O75340-2]
GeneID; 10016; -.
KEGG; hsa:10016; -.
UCSC; uc003jat.1; human. [O75340-1]
CTD; 10016; -.
DisGeNET; 10016; -.
EuPathDB; HostDB:ENSG00000249915.7; -.
GeneCards; PDCD6; -.
HGNC; HGNC:8765; PDCD6.
HPA; HPA047221; -.
MIM; 601057; gene.
neXtProt; NX_O75340; -.
OpenTargets; ENSG00000249915; -.
PharmGKB; PA33115; -.
eggNOG; KOG0037; Eukaryota.
eggNOG; ENOG410YKQK; LUCA.
GeneTree; ENSGT00620000087734; -.
HOGENOM; HOG000231984; -.
HOVERGEN; HBG004492; -.
InParanoid; O75340; -.
OMA; FLWNIFQ; -.
OrthoDB; EOG091G0ISY; -.
PhylomeDB; O75340; -.
TreeFam; TF314682; -.
ChiTaRS; PDCD6; human.
EvolutionaryTrace; O75340; -.
GeneWiki; PDCD6; -.
GenomeRNAi; 10016; -.
PRO; PR:O75340; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000249915; -.
CleanEx; HS_ALG2; -.
CleanEx; HS_PDCD6; -.
ExpressionAtlas; O75340; baseline and differential.
Genevisible; O75340; HS.
GO; GO:0030127; C:COPII vesicle coat; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:GOC.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0060090; F:binding, bridging; IMP:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
GO; GO:0043495; F:protein anchor; IMP:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc.
GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO; GO:0048208; P:COPII vesicle coating; IMP:UniProtKB.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0032007; P:negative regulation of TOR signaling; IDA:UniProtKB.
GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0014032; P:neural crest cell development; IMP:UniProtKB.
GO; GO:0014029; P:neural crest formation; IMP:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
GO; GO:1902527; P:positive regulation of protein monoubiquitination; IMP:UniProtKB.
GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
GO; GO:0036324; P:vascular endothelial growth factor receptor-2 signaling pathway; IDA:UniProtKB.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13202; EF-hand_5; 1.
Pfam; PF13499; EF-hand_7; 1.
SMART; SM00054; EFh; 5.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Angiogenesis;
Apoptosis; Calcium; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Endoplasmic reticulum; Endosome; Magnesium; Membrane; Metal-binding;
Nucleus; Polymorphism; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 191 Programmed cell death protein 6.
/FTId=PRO_0000073729.
DOMAIN 23 58 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 59 89 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 90 125 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 126 161 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 162 191 EF-hand 5. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 36 47 1. {ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
CA_BIND 73 84 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 103 114 3. {ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
METAL 36 36 Calcium 1. {ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
METAL 38 38 Calcium 1. {ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
METAL 40 40 Calcium 1. {ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
METAL 42 42 Calcium 1; via carbonyl oxygen.
{ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
METAL 47 47 Calcium 1. {ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
METAL 103 103 Calcium 2. {ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
METAL 105 105 Calcium 2. {ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
METAL 107 107 Calcium 2. {ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
METAL 109 109 Calcium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
METAL 114 114 Calcium 2. {ECO:0000269|PubMed:18940611,
ECO:0000269|PubMed:18997320,
ECO:0000269|PubMed:20691033,
ECO:0000269|PubMed:25667979}.
METAL 169 169 Magnesium.
{ECO:0000250|UniProtKB:P12815}.
METAL 171 171 Magnesium.
{ECO:0000250|UniProtKB:P12815}.
METAL 173 173 Magnesium.
{ECO:0000250|UniProtKB:P12815}.
METAL 175 175 Magnesium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P12815}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
VAR_SEQ 70 191 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045542.
VAR_SEQ 121 122 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045113.
VARIANT 123 123 G -> C (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035459.
MUTAGEN 47 47 E->A: Loss of interaction with SEC31A and
PLSCR3, and loss of localization to the
endoplasmic reticulum; when associated
with A-114. {ECO:0000269|PubMed:16957052,
ECO:0000269|PubMed:18256029,
ECO:0000269|PubMed:27716508}.
MUTAGEN 52 52 L->A: Stronly impaired interaction with
SEC31A. Slightly reduced interaction with
PDCD6IP. {ECO:0000269|PubMed:25667979}.
MUTAGEN 53 53 S->G: Slightly reduced interaction with
SEC31A. Does not affect interaction with
PDCD6IP. {ECO:0000269|PubMed:25667979}.
MUTAGEN 57 57 W->A: Does not affect interaction with
SEC31A. Reduces the interaction with
HEBP2, PDCD6IP and ANXA7.
{ECO:0000269|PubMed:18256029,
ECO:0000269|PubMed:25667979,
ECO:0000269|PubMed:27784779}.
MUTAGEN 60 60 F->A: Abolishes the interaction with
SEC31A, PDCD6IP, ANXA7 and ANXA11.
{ECO:0000269|PubMed:18256029,
ECO:0000269|PubMed:27716508}.
MUTAGEN 85 85 F->A: Stronly impaired interaction with
SEC31A and TFG. Does not affect
interaction with PDCD6IP.
{ECO:0000269|PubMed:25667979,
ECO:0000269|PubMed:27813252}.
MUTAGEN 89 89 W->A: Does not affect interaction with
SEC31A. Does not affect interaction with
PDCD6IP. {ECO:0000269|PubMed:25667979}.
MUTAGEN 91 91 Y->A: Abolishes the interaction with
PDCD6IP, ANXA7 and ANXA11.
{ECO:0000269|PubMed:18256029}.
MUTAGEN 92 92 I->A: Does not affect interaction with
SEC31A. Does not affect interaction with
PDCD6IP. {ECO:0000269|PubMed:25667979}.
MUTAGEN 95 95 W->A: Abolishes the interaction with
PDCD6IP, ANXA7 and ANXA11.
{ECO:0000269|PubMed:18256029}.
MUTAGEN 114 114 E->A: Loss of interaction with SEC31A and
PLSCR3, and loss of localization to the
endoplasmic reticulum; when associated
with A-47. {ECO:0000269|PubMed:16957052,
ECO:0000269|PubMed:18256029}.
MUTAGEN 122 122 F->A: Increases interaction with PDCD6IP
and ANXA7. Impairs interaction with
ANXA11. Augments stauroporine-induced
cell death.
{ECO:0000269|PubMed:20691033}.
MUTAGEN 122 122 F->G: Increases interaction with PDCD6IP.
Impairs interaction with ANXA11.
{ECO:0000269|PubMed:20691033}.
MUTAGEN 122 122 F->S: Increases interaction with PDCD6IP.
Impairs interaction with ANAX7 and
ANXA11. {ECO:0000269|PubMed:20691033}.
MUTAGEN 122 122 F->W: Impairs interaction with ANXA11.
{ECO:0000269|PubMed:20691033}.
MUTAGEN 148 148 F->S: Slightly reduced interaction with
SEC31A. Does not affect interaction with
PDCD6IP. {ECO:0000269|PubMed:25667979}.
MUTAGEN 180 180 Y->A: Abolishes the interaction with
PDCD6IP, TSG101, ANXA7 and ANXA11. Does
not affect interaction with TFG and
SEC31A. {ECO:0000269|PubMed:18256029,
ECO:0000269|PubMed:27813252}.
HELIX 26 35 {ECO:0000244|PDB:2ZND}.
STRAND 36 40 {ECO:0000244|PDB:2ZRT}.
STRAND 41 43 {ECO:0000244|PDB:2ZNE}.
HELIX 45 51 {ECO:0000244|PDB:2ZND}.
STRAND 55 58 {ECO:0000244|PDB:2ZND}.
HELIX 62 72 {ECO:0000244|PDB:2ZND}.
STRAND 74 80 {ECO:0000244|PDB:2ZND}.
HELIX 82 102 {ECO:0000244|PDB:2ZND}.
STRAND 107 110 {ECO:0000244|PDB:2ZND}.
HELIX 112 121 {ECO:0000244|PDB:2ZND}.
HELIX 128 138 {ECO:0000244|PDB:2ZND}.
STRAND 143 147 {ECO:0000244|PDB:2ZND}.
HELIX 148 168 {ECO:0000244|PDB:2ZND}.
STRAND 172 174 {ECO:0000244|PDB:2ZND}.
HELIX 180 188 {ECO:0000244|PDB:2ZND}.
SEQUENCE 191 AA; 21868 MW; D0B5944CF3C696AD CRC64;
MAAYSYRPGP GAGPGPAAGA ALPDQSFLWN VFQRVDKDRS GVISDTELQQ ALSNGTWTPF
NPVTVRSIIS MFDRENKAGV NFSEFTGVWK YITDWQNVFR TYDRDNSGMI DKNELKQALS
GFGYRLSDQF HDILIRKFDR QGRGQIAFDD FIQGCIVLQR LTDIFRRYDT DQDGWIQVSY
EQYLSMVFSI V


Related products :

Catalog number Product name Quantity
EIAAB36003 Alg4,Apoptosis-linked gene 4 protein,Kiaa0185,Mouse,Mus musculus,Pdcd11,Programmed cell death protein 11,Protein RRP5 homolog
EIAAB30267 ALG2,Apoptosis-linked gene 2 protein,Homo sapiens,Human,PDCD6,Probable calcium-binding protein ALG-2,Programmed cell death protein 6
EIAAB30250 CCM3,Cerebral cavernous malformations 3 protein,Homo sapiens,Human,PDCD10,Programmed cell death protein 10,TF-1 cell apoptosis-related protein 15,TFAR15
EIAAB30251 Mouse,Mus musculus,Pdcd10,Programmed cell death protein 10,TF-1 cell apoptosis-related protein 15,Tfar15
EIAAB30261 Death up-regulated gene protein,Dug,Pdcd4,Programmed cell death protein 4,Rat,Rattus norvegicus
EIAAB30264 Homo sapiens,Human,PDCD5,Programmed cell death protein 5,Protein TFAR19,TF-1 cell apoptosis-related protein 19,TFAR19
EIAAB30263 Mouse,Mus musculus,Pdcd5,Programmed cell death protein 5,Protein TFAR19,TF-1 cell apoptosis-related protein 19,Tfar19
18-003-44154 Apoptosis-inducing factor 1. mitochondrial - EC 1.-.-.-; Programmed cell death protein 8 Polyclonal 0.05 mg Aff Pur
18-661-15091 Programmed cell death protein 8. mitochondrial - EC 1.-.-.-; Apoptosis-inducing factor Polyclonal 0.1 mg
18-661-15085 Programmed cell death protein 8. mitochondrial - EC 1.-.-.-; Apoptosis-inducing factor Polyclonal 0.1 mg
18-661-15098 Programmed cell death protein 8. mitochondrial - EC 1.-.-.-; Apoptosis-inducing factor Polyclonal 0.1 mg
EIAAB36001 Homo sapiens,Human,KIAA0185,NFBP,NF-kappa-B-binding protein,PDCD11,Programmed cell death protein 11,Protein RRP5 homolog
EIAAB36002 Bos taurus,Bovine,PDCD11,Programmed cell death protein 11,Protein RRP5 homolog
E0513m ELISA B7 homolog 1,B7h1,B7-H1,Cd274,Mouse,Mus musculus,PDCD1 ligand 1,Pdcd1l1,Pdcd1lg1,Pdl1,PD-L1,Programmed cell death 1 ligand 1,Programmed death ligand 1 96T
U0513m CLIA B7 homolog 1,B7h1,B7-H1,Cd274,Mouse,Mus musculus,PDCD1 ligand 1,Pdcd1l1,Pdcd1lg1,Pdl1,PD-L1,Programmed cell death 1 ligand 1,Programmed death ligand 1 96T
E0513m ELISA kit B7 homolog 1,B7h1,B7-H1,Cd274,Mouse,Mus musculus,PDCD1 ligand 1,Pdcd1l1,Pdcd1lg1,Pdl1,PD-L1,Programmed cell death 1 ligand 1,Programmed death ligand 1 96T
E0513h ELISA kit B7 homolog 1,B7H1,B7-H1,CD274,Homo sapiens,Human,PDCD1 ligand 1,PDCD1L1,PDCD1LG1,PDL1,PD-L1,Programmed cell death 1 ligand 1,Programmed death ligand 1 96T
E0513h ELISA B7 homolog 1,B7H1,B7-H1,CD274,Homo sapiens,Human,PDCD1 ligand 1,PDCD1L1,PDCD1LG1,PDL1,PD-L1,Programmed cell death 1 ligand 1,Programmed death ligand 1 96T
U0513h CLIA B7 homolog 1,B7H1,B7-H1,CD274,Homo sapiens,Human,PDCD1 ligand 1,PDCD1L1,PDCD1LG1,PDL1,PD-L1,Programmed cell death 1 ligand 1,Programmed death ligand 1 96T
PDCL PDCD6IP Gene programmed cell death 6 interacting protein
PDCD2_RAT ELISA Kit FOR Programmed cell death protein 2; organism: Rat; gene name: Pdcd2 96T
PDC10_RAT ELISA Kit FOR Programmed cell death protein 10; organism: Rat; gene name: Pdcd10 96T
PDCD4_RAT ELISA Kit FOR Programmed cell death protein 4; organism: Rat; gene name: Pdcd4 96T
E0515m ELISA Kit FOR Programmed cell death protein 1; organism: Mouse; gene name: Pdcd1 96T
PDC10_MOUSE ELISA Kit FOR Programmed cell death protein 10; organism: Mouse; gene name: Pdcd10 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur