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Partitioning defective 3 homolog (PAR-3) (PARD-3) (Atypical PKC isotype-specific-interacting protein) (ASIP) (CTCL tumor antigen se2-5) (PAR3-alpha)

 PARD3_HUMAN             Reviewed;        1356 AA.
Q8TEW0; F5H5T0; Q5T2U1; Q5VUA2; Q5VUA3; Q5VWV0; Q5VWV1; Q5VWV3;
Q5VWV4; Q5VWV5; Q6IQ47; Q8TCZ9; Q8TEW1; Q8TEW2; Q8TEW3; Q96K28;
Q96RM6; Q96RM7; Q9BY57; Q9BY58; Q9HC48; Q9NWL4; Q9NYE6;
16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
16-MAY-2003, sequence version 2.
25-OCT-2017, entry version 166.
RecName: Full=Partitioning defective 3 homolog;
Short=PAR-3;
Short=PARD-3;
AltName: Full=Atypical PKC isotype-specific-interacting protein;
Short=ASIP;
AltName: Full=CTCL tumor antigen se2-5;
AltName: Full=PAR3-alpha;
Name=PARD3 {ECO:0000312|HGNC:HGNC:16051}; Synonyms=PAR3, PAR3A;
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 3), AND INTERACTION WITH PARD6B.
TISSUE=Kidney;
PubMed=10934474; DOI=10.1038/35019573;
Joberty G., Petersen C., Gao L., Macara I.G.;
"The cell-polarity protein Par6 links Par3 and atypical protein kinase
C to Cdc42.";
Nat. Cell Biol. 2:531-539(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 7; 8 AND 9).
PubMed=11642408; DOI=10.1038/sj.cr.7290090;
Fang C.M., Xu Y.H.;
"Down-regulated expression of atypical PKC-binding domain deleted asip
isoforms in human hepatocellular carcinomas.";
Cell Res. 11:223-229(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
PubMed=12459187; DOI=10.1016/S0006-291X(02)02698-0;
Kohjima M., Noda Y., Takeya R., Saito N., Takeuchi K., Sumimoto H.;
"PAR3beta, a novel homologue of the cell polarity protein PAR3,
localizes to tight junctions.";
Biochem. Biophys. Res. Commun. 299:641-646(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), INTERACTION
WITH PARD6B AND PRKCZ, AND TISSUE SPECIFICITY.
PubMed=12234671; DOI=10.1016/S0378-1119(02)00681-9;
Gao L., Macara I.G., Joberty G.;
"Multiple splice variants of Par3 and of a novel related gene, Par3L,
produce proteins with different binding properties.";
Gene 294:99-107(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 860-1356 (ISOFORM 1).
TISSUE=Lung, 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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 955-1356 (ISOFORM 6), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-1356 (ISOFORM 10).
TISSUE=Hepatoma, and Ovarian carcinoma;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 313-992.
TISSUE=Testis;
PubMed=11149944; DOI=10.1073/pnas.98.2.629;
Eichmueller S., Usener D., Dummer R., Stein A., Thiel D.,
Schadendorf D.;
"Serological detection of cutaneous T-cell lymphoma-associated
antigens.";
Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
[10]
INTERACTION WITH PARD6A.
PubMed=10954424;
Johansson A.-S., Driessens M., Aspenstroem P.;
"The mammalian homologue of the Caenorhabditis elegans polarity
protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and
Rac1.";
J. Cell Sci. 113:3267-3275(2000).
[11]
SUBUNIT OF A COMPLEX CONTAINING PARD6B AND PRKCI.
TISSUE=Kidney;
PubMed=11257119; DOI=10.1083/jcb.152.6.1183;
Suzuki A., Yamanaka T., Hirose T., Manabe N., Mizuno K., Shimizu M.,
Akimoto K., Izumi Y., Ohnishi T., Ohno S.;
"Atypical protein kinase C is involved in the evolutionarily conserved
par protein complex and plays a critical role in establishing
epithelia-specific junctional structures.";
J. Cell Biol. 152:1183-1196(2001).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[13]
INTERACTION WITH ECT2.
PubMed=15254234; DOI=10.1128/MCB.24.15.6665-6675.2004;
Liu X.F., Ishida H., Raziuddin R., Miki T.;
"Nucleotide exchange factor ECT2 interacts with the polarity protein
complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta
activity.";
Mol. Cell. Biol. 24:6665-6675(2004).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A COMPLEX
WITH ARHGAP17; AMOT; MPP5 AND PATJ.
PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
Starostine A., Metalnikov P., Pawson T.;
"A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
proteins in epithelial cells.";
Cell 125:535-548(2006).
[15]
INTERACTION WITH FBF1.
PubMed=18838552; DOI=10.1083/jcb.200803133;
Sugimoto M., Inoko A., Shiromizu T., Nakayama M., Zou P., Yonemura S.,
Hayashi Y., Izawa I., Sasoh M., Uji Y., Kaibuchi K., Kiyono T.,
Inagaki M.;
"The keratin-binding protein Albatross regulates polarization of
epithelial cells.";
J. Cell Biol. 183:19-28(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND SER-695, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-692; SER-695;
SER-728; SER-809; SER-852 AND SER-873, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
INTERACTION WITH AURKA AND AURKB, FUNCTION, MUTAGENESIS OF SER-962,
AND PHOSPHORYLATION AT SER-962.
PubMed=19812038; DOI=10.1074/jbc.M109.055897;
Khazaei M.R., Puschel A.W.;
"Phosphorylation of the par polarity complex protein Par3 at serine
962 is mediated by aurora A and regulates its function in neuronal
polarity.";
J. Biol. Chem. 284:33571-33579(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-728 AND
SER-852, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=20332120; DOI=10.1242/jcs.059329;
Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G.,
Chapon F., Dejana E.;
"CCM1 regulates vascular-lumen organization by inducing endothelial
polarity.";
J. Cell Sci. 123:1073-1080(2010).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-728; SER-852
AND SER-873, 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).
[22]
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).
[23]
ACETYLATION, DEACETYLATION BY SIRT2, AND INTERACTION WITH SIRT2.
PubMed=21949390; DOI=10.1073/pnas.1104969108;
Beirowski B., Gustin J., Armour S.M., Yamamoto H., Viader A.,
North B.J., Michan S., Baloh R.H., Golden J.P., Schmidt R.E.,
Sinclair D.A., Auwerx J., Milbrandt J.;
"Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through
polarity protein Par-3/atypical protein kinase C (aPKC) signaling.";
Proc. Natl. Acad. Sci. U.S.A. 108:E952-961(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-852 AND
SER-873, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[25]
INTERACTION WITH TIAM1.
PubMed=23832200; DOI=10.1107/S1744309113014206;
Joshi M., Gakhar L., Fuentes E.J.;
"High-resolution structure of the Tiam1 PHn-CC-Ex domain.";
Acta Crystallogr. F 69:744-752(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-383; SER-692;
SER-695; SER-715; SER-728; SER-827; SER-837; SER-852; SER-873;
SER-962; SER-971; SER-973 AND SER-1046, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; THR-91; SER-383 AND
TYR-489, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792 (ISOFORM
5), AND 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).
[28]
INTERACTION WITH SAPCD2.
PubMed=26766442; DOI=10.1016/j.devcel.2015.12.016;
Chiu C.W., Monat C., Robitaille M., Lacomme M., Daulat A.M.,
Macleod G., McNeill H., Cayouette M., Angers S.;
"SAPCD2 controls spindle orientation and asymmetric divisions by
negatively regulating the Galphai-LGN-NuMA ternary complex.";
Dev. Cell 36:50-62(2016).
[29]
STRUCTURE BY NMR OF 451-549.
PubMed=20073081; DOI=10.1002/pro.335;
Jensen D.R., Woytovich C., Li M., Duvnjak P., Cassidy M.S.,
Frederick R.O., Bergeman L.F., Peterson F.C., Volkman B.F.;
"Rapid, robotic, small-scale protein production for NMR screening and
structure determination.";
Protein Sci. 19:570-578(2010).
-!- FUNCTION: Adapter protein involved in asymmetrical cell division
and cell polarization processes. Seems to play a central role in
the formation of epithelial tight junctions. Targets the
phosphatase PTEN to cell junctions. Involved in Schwann cell
peripheral myelination (By similarity). Association with PARD6B
may prevent the interaction of PARD3 with F11R/JAM1, thereby
preventing tight junction assembly. The PARD6-PARD3 complex links
GTP-bound Rho small GTPases to atypical protein kinase C proteins.
Required for establishment of neuronal polarity and normal axon
formation in cultured hippocampal neurons. {ECO:0000250,
ECO:0000269|PubMed:19812038}.
-!- SUBUNIT: Interacts (via PDZ 1 domain) with F11R/JAM1, PARD6A and
PARD6B. Isoform 2, but not at least isoform 3 interacts with
PRKCZ. Interacts with PRCKI and CDH5. Interacts (via PDZ 3 domain)
with PTEN (via C-terminus) (By similarity). Part of a complex with
PARD6A or PARD6B, PRKCI or PRKCZ and CDC42 or RAC1. Component of a
complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, PATJ
and PARD3/PAR3. Interacts with LIMK2, AURKA and AURKB. Component
of the Par polarity complex, composed of at least phosphorylated
PRKCZ, PARD3 and TIAM1. Directly interacts with TIAM1 and TIAM2.
Interacts with ECT2, FBF1 and SIRT2. Interacts (via coiled-coil
domain) with FRMD4A (By similarity). Found in a complex with
PARD3, CYTH1 and FRMD4A (By similarity). Interacts with SAPCD2
(PubMed:26766442). {ECO:0000250|UniProtKB:Q99NH2,
ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:10954424,
ECO:0000269|PubMed:11257119, ECO:0000269|PubMed:12234671,
ECO:0000269|PubMed:15254234, ECO:0000269|PubMed:16678097,
ECO:0000269|PubMed:18838552, ECO:0000269|PubMed:19812038,
ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:21949390,
ECO:0000269|PubMed:23832200, ECO:0000269|PubMed:26766442}.
-!- INTERACTION:
P33151:CDH5; NbExp=5; IntAct=EBI-81968, EBI-2903122;
P35222:CTNNB1; NbExp=2; IntAct=EBI-81968, EBI-491549;
Q9Y624:F11R; NbExp=2; IntAct=EBI-81968, EBI-742600;
Q9NPB6:PARD6A; NbExp=9; IntAct=EBI-81968, EBI-81876;
Q9BYG5:PARD6B; NbExp=5; IntAct=EBI-81968, EBI-295391;
Q9JK83:Pard6b (xeno); NbExp=3; IntAct=EBI-81968, EBI-81861;
Q9BYG4:PARD6G; NbExp=3; IntAct=EBI-81968, EBI-295417;
Q8ND90:PNMA1; NbExp=4; IntAct=EBI-81968, EBI-302345;
P41743:PRKCI; NbExp=3; IntAct=EBI-81968, EBI-286199;
Q62074:Prkci (xeno); NbExp=7; IntAct=EBI-81968, EBI-82016;
Q6ZPF3:Tiam2 (xeno); NbExp=6; IntAct=EBI-9118204, EBI-7565978;
P04637:TP53; NbExp=3; IntAct=EBI-81968, EBI-366083;
Q04917:YWHAH; NbExp=6; IntAct=EBI-81968, EBI-306940;
P63104:YWHAZ; NbExp=4; IntAct=EBI-81968, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endomembrane system
{ECO:0000269|PubMed:20332120}. Cell junction
{ECO:0000269|PubMed:20332120}. Cell junction, tight junction
{ECO:0000269|PubMed:20332120}. Cell junction, adherens junction
{ECO:0000250|UniProtKB:Q99NH2}. Cell membrane
{ECO:0000269|PubMed:20332120}. Cytoplasm, cell cortex
{ECO:0000250}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:20332120}. Note=Localized along the cell-cell
contact region. Colocalizes with PARD6A and PRKCI at epithelial
tight junctions. Colocalizes with the cortical actin that overlays
the meiotic spindle during metaphase I and metaphase II.
Colocalized with SIRT2 in internode region of myelin sheat (By
similarity). Presence of KRIT1, CDH5 and RAP1B is required for its
localization to the cell junction. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=11;
Name=1; Synonyms=A;
IsoId=Q8TEW0-1; Sequence=Displayed;
Name=2; Synonyms=B, La;
IsoId=Q8TEW0-2; Sequence=VSP_007464;
Name=3; Synonyms=C;
IsoId=Q8TEW0-3; Sequence=VSP_007462, VSP_007463, VSP_007464,
VSP_007465;
Name=4; Synonyms=D;
IsoId=Q8TEW0-4; Sequence=VSP_007469;
Name=5; Synonyms=E;
IsoId=Q8TEW0-5; Sequence=VSP_007462, VSP_007463, VSP_007464,
VSP_007466, VSP_007468, VSP_007469;
Note=Contains a phosphoserine at position 792.
{ECO:0000244|PubMed:24275569};
Name=6; Synonyms=F;
IsoId=Q8TEW0-6; Sequence=VSP_007463, VSP_007464, VSP_007465;
Name=7; Synonyms=Lb;
IsoId=Q8TEW0-7; Sequence=VSP_007463, VSP_007464, VSP_007465,
VSP_007469;
Name=8; Synonyms=Sa;
IsoId=Q8TEW0-8; Sequence=VSP_007464, VSP_007470, VSP_007471;
Name=9; Synonyms=Sb;
IsoId=Q8TEW0-9; Sequence=VSP_007463, VSP_007464, VSP_007465,
VSP_007470, VSP_007471;
Name=10;
IsoId=Q8TEW0-10; Sequence=VSP_007464, VSP_007465, VSP_007467,
VSP_007470, VSP_007471;
Note=No experimental confirmation available.;
Name=11;
IsoId=Q8TEW0-11; Sequence=VSP_007463, VSP_007464;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:12234671}.
-!- DOMAIN: Contains a conserved N-terminal oligomerization domain
(NTD) that is involved in oligomerization and is essential for
proper subapical membrane localization. {ECO:0000250}.
-!- DOMAIN: The second PDZ domain mediates interaction with membranes
containing phosphoinositol lipids. {ECO:0000250}.
-!- PTM: Acetylated. Deacetylated by SIRT2, thereby inhibiting Schwann
cell peripheral myelination. {ECO:0000269|PubMed:21949390}.
-!- PTM: Phosphorylation at Ser-827 by PRKCZ and PRKCI occurs at the
most apical tip of epithelial cell-cell contacts during the
initial phase of tight junction formation and may promote
dissociation of the complex with PARD6. EGF-induced Tyr-1127
phosphorylation mediates dissociation from LIMK2 (By similarity).
Phosphorylation by AURKA at Ser-962 is required for the normal
establishment of neuronal polarity. {ECO:0000250,
ECO:0000269|PubMed:19812038}.
-!- MISCELLANEOUS: Antibodies against PARD3 are present in sera from
patients with cutaneous T-cell lymphomas.
-!- SIMILARITY: Belongs to the PAR3 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG33676.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA91366.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB55330.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AF252293; AAF71530.1; -; mRNA.
EMBL; AF196185; AAK27891.1; -; mRNA.
EMBL; AF196186; AAK27892.1; -; mRNA.
EMBL; AF332592; AAK69192.1; -; mRNA.
EMBL; AF332593; AAK69193.1; -; mRNA.
EMBL; AB073671; BAC54037.1; -; mRNA.
EMBL; AF467002; AAL76042.1; -; mRNA.
EMBL; AF467003; AAL76043.1; -; mRNA.
EMBL; AF467004; AAL76044.1; -; mRNA.
EMBL; AF467005; AAL76045.1; -; mRNA.
EMBL; AF467006; AAL76046.1; -; mRNA.
EMBL; AL360233; CAH71161.1; -; Genomic_DNA.
EMBL; AL138768; CAH71161.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAH71161.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAH71161.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAH71161.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAH71161.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAH71162.1; -; Genomic_DNA.
EMBL; AL138768; CAH71162.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAH71162.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAH71162.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAH71162.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAH71162.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAH71163.1; -; Genomic_DNA.
EMBL; AL138768; CAH71163.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAH71163.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAH71163.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAH71163.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAH71163.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAH71165.1; -; Genomic_DNA.
EMBL; AL138768; CAH71165.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAH71165.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAH71165.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAH71165.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAH71165.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAH71166.1; -; Genomic_DNA.
EMBL; AL138768; CAH71166.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAH71166.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAH71166.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAH71166.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAH71166.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAH71167.1; -; Genomic_DNA.
EMBL; AL138768; CAH71167.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAH71167.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAH71167.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAH71167.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAH73524.1; -; Genomic_DNA.
EMBL; AL138768; CAH73524.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAH73524.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAH73524.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAH73524.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAH73524.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAH73525.1; -; Genomic_DNA.
EMBL; AL138768; CAH73525.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAH73525.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAH73525.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAH73525.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAH73525.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAH73526.1; -; Genomic_DNA.
EMBL; AL138768; CAH73526.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAH73526.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAH73526.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAH73526.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAH73526.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAH73528.1; -; Genomic_DNA.
EMBL; AL138768; CAH73528.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAH73528.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAH73528.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAH73528.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAH73528.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAH73529.1; -; Genomic_DNA.
EMBL; AL138768; CAH73529.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAH73529.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAH73529.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAH73529.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAH73529.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI15036.1; -; Genomic_DNA.
EMBL; AL138768; CAI15036.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI15036.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI15036.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI15036.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI15036.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI15037.1; -; Genomic_DNA.
EMBL; AL138768; CAI15037.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI15037.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI15037.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI15037.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI15037.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI15038.1; -; Genomic_DNA.
EMBL; AL138768; CAI15038.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI15038.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI15038.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI15038.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI15038.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI15039.1; -; Genomic_DNA.
EMBL; AL138768; CAI15039.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI15039.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI15039.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI15039.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI15039.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI15040.1; -; Genomic_DNA.
EMBL; AL138768; CAI15040.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI15040.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI15040.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI15040.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI15040.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI15041.1; -; Genomic_DNA.
EMBL; AL138768; CAI15041.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI15041.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI15041.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI15041.1; JOINED; Genomic_DNA.
EMBL; AL138768; CAI16985.1; -; Genomic_DNA.
EMBL; AL160409; CAI16985.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI16985.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI16985.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI16985.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI16985.1; JOINED; Genomic_DNA.
EMBL; AL138768; CAI16986.1; -; Genomic_DNA.
EMBL; AL160409; CAI16986.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI16986.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI16986.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI16986.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI16986.1; JOINED; Genomic_DNA.
EMBL; AL138768; CAI16987.1; -; Genomic_DNA.
EMBL; AL160409; CAI16987.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI16987.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI16987.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI16987.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI16987.1; JOINED; Genomic_DNA.
EMBL; AL138768; CAI16988.1; -; Genomic_DNA.
EMBL; AL160409; CAI16988.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI16988.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI16988.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI16988.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI16988.1; JOINED; Genomic_DNA.
EMBL; AL138768; CAI16989.1; -; Genomic_DNA.
EMBL; AL160409; CAI16989.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI16989.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI16989.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI16989.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI16989.1; JOINED; Genomic_DNA.
EMBL; AL138768; CAI16991.1; -; Genomic_DNA.
EMBL; AL360233; CAI16991.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI16991.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI16991.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI16991.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17304.1; -; Genomic_DNA.
EMBL; AL138768; CAI17304.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI17304.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17304.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17304.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17304.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17305.1; -; Genomic_DNA.
EMBL; AL138768; CAI17305.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI17305.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17305.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17305.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17305.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17306.1; -; Genomic_DNA.
EMBL; AL138768; CAI17306.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI17306.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17306.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17306.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17306.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17308.1; -; Genomic_DNA.
EMBL; AL138768; CAI17308.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI17308.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17308.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17308.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17308.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17309.1; -; Genomic_DNA.
EMBL; AL138768; CAI17309.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI17309.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17309.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17309.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17309.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17310.1; -; Genomic_DNA.
EMBL; AL138768; CAI17310.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17310.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17310.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17310.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17327.1; -; Genomic_DNA.
EMBL; AL138768; CAI17327.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI17327.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17327.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17327.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17327.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17328.1; -; Genomic_DNA.
EMBL; AL138768; CAI17328.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI17328.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17328.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17328.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17328.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17329.1; -; Genomic_DNA.
EMBL; AL138768; CAI17329.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI17329.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17329.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17329.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17329.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17331.1; -; Genomic_DNA.
EMBL; AL138768; CAI17331.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI17331.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17331.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17331.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17331.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17332.1; -; Genomic_DNA.
EMBL; AL138768; CAI17332.1; JOINED; Genomic_DNA.
EMBL; AL160409; CAI17332.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17332.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17332.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17332.1; JOINED; Genomic_DNA.
EMBL; AL392123; CAI17333.1; -; Genomic_DNA.
EMBL; AL138768; CAI17333.1; JOINED; Genomic_DNA.
EMBL; AL360233; CAI17333.1; JOINED; Genomic_DNA.
EMBL; AL390766; CAI17333.1; JOINED; Genomic_DNA.
EMBL; AL450337; CAI17333.1; JOINED; Genomic_DNA.
EMBL; CH471072; EAW85932.1; -; Genomic_DNA.
EMBL; CH471072; EAW85934.1; -; Genomic_DNA.
EMBL; BC011711; AAH11711.2; -; mRNA.
EMBL; BC071566; AAH71566.1; -; mRNA.
EMBL; AK000761; BAA91366.1; ALT_INIT; mRNA.
EMBL; AK027735; BAB55330.1; ALT_INIT; mRNA.
EMBL; AF177228; AAG33676.1; ALT_SEQ; mRNA.
CCDS; CCDS53509.1; -. [Q8TEW0-5]
CCDS; CCDS53510.1; -. [Q8TEW0-3]
CCDS; CCDS53511.1; -. [Q8TEW0-11]
CCDS; CCDS53512.1; -. [Q8TEW0-6]
CCDS; CCDS53513.1; -. [Q8TEW0-9]
CCDS; CCDS53514.1; -. [Q8TEW0-4]
CCDS; CCDS53515.1; -. [Q8TEW0-2]
CCDS; CCDS53516.1; -. [Q8TEW0-8]
CCDS; CCDS7178.1; -. [Q8TEW0-1]
RefSeq; NP_001171714.1; NM_001184785.1. [Q8TEW0-2]
RefSeq; NP_001171715.1; NM_001184786.1. [Q8TEW0-11]
RefSeq; NP_001171716.1; NM_001184787.1. [Q8TEW0-4]
RefSeq; NP_001171717.1; NM_001184788.1. [Q8TEW0-6]
RefSeq; NP_001171718.1; NM_001184789.1. [Q8TEW0-7]
RefSeq; NP_001171719.1; NM_001184790.1. [Q8TEW0-3]
RefSeq; NP_001171720.1; NM_001184791.1. [Q8TEW0-5]
RefSeq; NP_001171721.1; NM_001184792.1. [Q8TEW0-8]
RefSeq; NP_001171722.1; NM_001184793.1. [Q8TEW0-10]
RefSeq; NP_001171723.1; NM_001184794.1. [Q8TEW0-9]
RefSeq; NP_062565.2; NM_019619.3. [Q8TEW0-1]
UniGene; Hs.131489; -.
PDB; 2KOM; NMR; -; A=451-549.
PDBsum; 2KOM; -.
ProteinModelPortal; Q8TEW0; -.
SMR; Q8TEW0; -.
BioGrid; 121134; 67.
CORUM; Q8TEW0; -.
DIP; DIP-31315N; -.
IntAct; Q8TEW0; 52.
MINT; MINT-7711810; -.
STRING; 9606.ENSP00000363921; -.
iPTMnet; Q8TEW0; -.
PhosphoSitePlus; Q8TEW0; -.
BioMuta; PARD3; -.
DMDM; 30913162; -.
EPD; Q8TEW0; -.
MaxQB; Q8TEW0; -.
PaxDb; Q8TEW0; -.
PeptideAtlas; Q8TEW0; -.
PRIDE; Q8TEW0; -.
Ensembl; ENST00000340077; ENSP00000341844; ENSG00000148498. [Q8TEW0-8]
Ensembl; ENST00000346874; ENSP00000340591; ENSG00000148498. [Q8TEW0-4]
Ensembl; ENST00000350537; ENSP00000311986; ENSG00000148498. [Q8TEW0-6]
Ensembl; ENST00000374776; ENSP00000363908; ENSG00000148498. [Q8TEW0-9]
Ensembl; ENST00000374788; ENSP00000363920; ENSG00000148498. [Q8TEW0-2]
Ensembl; ENST00000374789; ENSP00000363921; ENSG00000148498. [Q8TEW0-1]
Ensembl; ENST00000374794; ENSP00000363926; ENSG00000148498. [Q8TEW0-5]
Ensembl; ENST00000545260; ENSP00000440857; ENSG00000148498. [Q8TEW0-3]
Ensembl; ENST00000545693; ENSP00000443147; ENSG00000148498. [Q8TEW0-11]
GeneID; 56288; -.
KEGG; hsa:56288; -.
UCSC; uc001ixq.3; human. [Q8TEW0-1]
CTD; 56288; -.
DisGeNET; 56288; -.
EuPathDB; HostDB:ENSG00000148498.15; -.
GeneCards; PARD3; -.
HGNC; HGNC:16051; PARD3.
HPA; HPA030443; -.
MIM; 606745; gene.
neXtProt; NX_Q8TEW0; -.
OpenTargets; ENSG00000148498; -.
PharmGKB; PA32936; -.
eggNOG; ENOG410ITAJ; Eukaryota.
eggNOG; ENOG410ZDVK; LUCA.
GeneTree; ENSGT00760000119017; -.
HOGENOM; HOG000232109; -.
HOVERGEN; HBG053508; -.
InParanoid; Q8TEW0; -.
KO; K04237; -.
OMA; FQRDNAR; -.
OrthoDB; EOG091G04AU; -.
PhylomeDB; Q8TEW0; -.
TreeFam; TF323729; -.
Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-HSA-420029; Tight junction interactions.
SignaLink; Q8TEW0; -.
SIGNOR; Q8TEW0; -.
ChiTaRS; PARD3; human.
EvolutionaryTrace; Q8TEW0; -.
GeneWiki; PARD3; -.
GenomeRNAi; 56288; -.
PRO; PR:Q8TEW0; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000148498; -.
ExpressionAtlas; Q8TEW0; baseline and differential.
Genevisible; Q8TEW0; HS.
GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
GO; GO:0033269; C:internode region of axon; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0008356; P:asymmetric cell division; TAS:ProtInc.
GO; GO:0007409; P:axonogenesis; TAS:UniProtKB.
GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0090162; P:establishment of epithelial cell polarity; ISS:UniProtKB.
GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB.
GO; GO:0022011; P:myelination in peripheral nervous system; ISS:UniProtKB.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0031643; P:positive regulation of myelination; ISS:UniProtKB.
GO; GO:0006461; P:protein complex assembly; TAS:ProtInc.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; TAS:UniProtKB.
GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
GO; GO:0060341; P:regulation of cellular localization; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
InterPro; IPR021922; Par3/HAL_N.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
Pfam; PF12053; DUF3534; 1.
Pfam; PF00595; PDZ; 2.
SMART; SM00228; PDZ; 3.
SUPFAM; SSF50156; SSF50156; 3.
PROSITE; PS50106; PDZ; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Cell junction; Cell membrane; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Differentiation;
Lipid-binding; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Tight junction.
CHAIN 1 1356 Partitioning defective 3 homolog.
/FTId=PRO_0000185069.
DOMAIN 271 359 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 461 546 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 590 677 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
REGION 712 936 Interaction with PRKCI and PRKCZ.
{ECO:0000250|UniProtKB:Q9Z340}.
REGION 935 1356 Interaction with FRMD4A.
{ECO:0000250|UniProtKB:Q99NH2}.
COILED 1049 1077 {ECO:0000255}.
COILED 1151 1174 {ECO:0000255}.
COILED 1201 1224 {ECO:0000255}.
COILED 1280 1301 {ECO:0000255}.
COMPBIAS 984 1042 Lys-rich.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 91 91 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000250|UniProtKB:Q99NH2}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 489 489 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 692 692 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 715 715 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 728 728 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 809 809 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 827 827 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 834 834 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99NH2}.
MOD_RES 837 837 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 851 851 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99NH2}.
MOD_RES 852 852 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 873 873 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 885 885 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99NH2}.
MOD_RES 962 962 Phosphoserine; by AURKA.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19812038}.
MOD_RES 971 971 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 973 973 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1046 1046 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1350 1350 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99NH2}.
VAR_SEQ 195 238 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:10934474,
ECO:0000303|PubMed:11642408,
ECO:0000303|PubMed:12234671,
ECO:0000303|PubMed:12459187}.
/FTId=VSP_007462.
VAR_SEQ 557 569 Missing (in isoform 3, isoform 5, isoform
6, isoform 7, isoform 9 and isoform 11).
{ECO:0000303|PubMed:10934474,
ECO:0000303|PubMed:11642408,
ECO:0000303|PubMed:12234671,
ECO:0000303|PubMed:12459187,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007463.
VAR_SEQ 740 742 Missing (in isoform 2, isoform 3, isoform
5, isoform 6, isoform 7, isoform 8,
isoform 9, isoform 10 and isoform 11).
{ECO:0000303|PubMed:10934474,
ECO:0000303|PubMed:11642408,
ECO:0000303|PubMed:12234671,
ECO:0000303|PubMed:12459187,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007464.
VAR_SEQ 827 856 Missing (in isoform 3, isoform 6, isoform
7, isoform 9 and isoform 10).
{ECO:0000303|PubMed:10934474,
ECO:0000303|PubMed:11642408,
ECO:0000303|PubMed:12234671,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_007465.
VAR_SEQ 857 858 IA -> T (in isoform 10).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_007467.
VAR_SEQ 857 857 I -> S (in isoform 5).
{ECO:0000303|PubMed:12234671,
ECO:0000303|PubMed:12459187}.
/FTId=VSP_007466.
VAR_SEQ 858 872 Missing (in isoform 5).
{ECO:0000303|PubMed:12234671,
ECO:0000303|PubMed:12459187}.
/FTId=VSP_007468.
VAR_SEQ 1025 1061 Missing (in isoform 4, isoform 5 and
isoform 7). {ECO:0000303|PubMed:11642408,
ECO:0000303|PubMed:12234671,
ECO:0000303|PubMed:12459187}.
/FTId=VSP_007469.
VAR_SEQ 1025 1034 RFGKHRKDDK -> SLAKLKPEKR (in isoform 8,
isoform 9 and isoform 10).
{ECO:0000303|PubMed:11642408,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_007470.
VAR_SEQ 1035 1356 Missing (in isoform 8, isoform 9 and
isoform 10).
{ECO:0000303|PubMed:11642408,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_007471.
VARIANT 107 107 E -> D (in dbSNP:rs1436731).
/FTId=VAR_015663.
VARIANT 575 575 D -> N (in dbSNP:rs3758459).
/FTId=VAR_050453.
MUTAGEN 962 962 S->A: Abolishes phosphorylation by AURKA.
{ECO:0000269|PubMed:19812038}.
MUTAGEN 1127 1127 Y->F: Delayed epithelial tight junction
assembly.
CONFLICT 190 190 T -> A (in Ref. 8; BAB55330).
{ECO:0000305}.
CONFLICT 233 233 L -> Q (in Ref. 8; BAB55330).
{ECO:0000305}.
CONFLICT 594 594 N -> S (in Ref. 8; BAB55330).
{ECO:0000305}.
CONFLICT 764 764 D -> N (in Ref. 7; AAH71566).
{ECO:0000305}.
CONFLICT 996 1000 GKEKK -> VELHE (in Ref. 8; BAA91366).
{ECO:0000305}.
STRAND 458 465 {ECO:0000244|PDB:2KOM}.
STRAND 473 476 {ECO:0000244|PDB:2KOM}.
STRAND 481 485 {ECO:0000244|PDB:2KOM}.
STRAND 488 493 {ECO:0000244|PDB:2KOM}.
HELIX 498 501 {ECO:0000244|PDB:2KOM}.
STRAND 507 514 {ECO:0000244|PDB:2KOM}.
HELIX 524 533 {ECO:0000244|PDB:2KOM}.
STRAND 539 546 {ECO:0000244|PDB:2KOM}.
SEQUENCE 1356 AA; 151423 MW; A4FD3F4F9AD8B92A CRC64;
MKVTVCFGRT RVVVPCGDGH MKVFSLIQQA VTRYRKAIAK DPNYWIQVHR LEHGDGGILD
LDDILCDVAD DKDRLVAVFD EQDPHHGGDG TSASSTGTQS PEIFGSELGT NNVSAFQPYQ
ATSEIEVTPS VLRANMPLHV RRSSDPALIG LSTSVSDSNF SSEEPSRKNP TRWSTTAGFL
KQNTAGSPKT CDRKKDENYR SLPRDTSNWS NQFQRDNARS SLSASHPMVG KWLEKQEQDE
DGTEEDNSRV EPVGHADTGL EHIPNFSLDD MVKLVEVPND GGPLGIHVVP FSARGGRTLG
LLVKRLEKGG KAEHENLFRE NDCIVRINDG DLRNRRFEQA QHMFRQAMRT PIIWFHVVPA
ANKEQYEQLS QSEKNNYYSS RFSPDSQYID NRSVNSAGLH TVQRAPRLNH PPEQIDSHSR
LPHSAHPSGK PPSAPASAPQ NVFSTTVSSG YNTKKIGKRL NIQLKKGTEG LGFSITSRDV
TIGGSAPIYV KNILPRGAAI QDGRLKAGDR LIEVNGVDLV GKSQEEVVSL LRSTKMEGTV
SLLVFRQEDA FHPRELNAEP SQMQIPKETK AEDEDIVLTP DGTREFLTFE VPLNDSGSAG
LGVSVKGNRS KENHADLGIF VKSIINGGAA SKDGRLRVND QLIAVNGESL LGKTNQDAME
TLRRSMSTEG NKRGMIQLIV ARRISKCNEL KSPGSPPGPE LPIETALDDR ERRISHSLYS
GIEGLDESPS RNAALSRIMG ESGKYQLSPT VNMPQDDTVI IEDDRLPVLP PHLSDQSSSS
SHDDVGFVTA DAGTWAKAAI SDSADCSLSP DVDPVLAFQR EGFGRQSMSE KRTKQFSDAS
QLDFVKTRKS KSMDLGIADE TKLNTVDDQK AGSPSRDVGP SLGLKKSSSL ESLQTAVAEV
TLNGDIPFHR PRPRIIRGRG CNESFRAAID KSYDKPAVDD DDEGMETLEE DTEESSRSGR
ESVSTASDQP SHSLERQMNG NQEKGDKTDR KKDKTGKEKK KDRDKEKDKM KAKKGMLKGL
GDMFRFGKHR KDDKIEKTGK IKIQESFTSE EERIRMKQEQ ERIQAKTREF RERQARERDY
AEIQDFHRTF GCDDELMYGG VSSYEGSMAL NARPQSPREG HMMDALYAQV KKPRNSKPSP
VDSNRSTPSN HDRIQRLRQE FQQAKQDEDV EDRRRTYSFE QPWPNARPAT QSGRHSVSVE
VQMQRQRQEE RESSQQAQRQ YSSLPRQSRK NASSVSQDSW EQNYSPGEGF QSAKENPRYS
SYQGSRNGYL GGHGFNARVM LETQELLRQE QRRKEQQMKK QPPSEGPSNY DSYKKVQDPS
YAPPKGPFRQ DVPPSPSQVA RLNRLQTPEK GRPFYS


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