PARD3_HUMAN
ID PARD3_HUMAN Reviewed; 1356 AA.
AC Q8TEW0; F5H5T0; Q5T2U1; Q5VUA2; Q5VUA3; Q5VWV0; Q5VWV1; Q5VWV3; Q5VWV4;
AC Q5VWV5; Q6IQ47; Q8TCZ9; Q8TEW1; Q8TEW2; Q8TEW3; Q96K28; Q96RM6; Q96RM7;
AC Q9BY57; Q9BY58; Q9HC48; Q9NWL4; Q9NYE6;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Partitioning defective 3 homolog;
DE Short=PAR-3;
DE Short=PARD-3;
DE AltName: Full=Atypical PKC isotype-specific-interacting protein;
DE Short=ASIP;
DE AltName: Full=CTCL tumor antigen se2-5;
DE AltName: Full=PAR3-alpha;
GN Name=PARD3 {ECO:0000312|HGNC:HGNC:16051}; Synonyms=PAR3, PAR3A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND INTERACTION WITH
RP PARD6B.
RC TISSUE=Kidney;
RX PubMed=10934474; DOI=10.1038/35019573;
RA Joberty G., Petersen C., Gao L., Macara I.G.;
RT "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to
RT Cdc42.";
RL Nat. Cell Biol. 2:531-539(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 7; 8 AND 9).
RX PubMed=11642408; DOI=10.1038/sj.cr.7290090;
RA Fang C.M., Xu Y.H.;
RT "Down-regulated expression of atypical PKC-binding domain deleted asip
RT isoforms in human hepatocellular carcinomas.";
RL Cell Res. 11:223-229(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX PubMed=12459187; DOI=10.1016/s0006-291x(02)02698-0;
RA Kohjima M., Noda Y., Takeya R., Saito N., Takeuchi K., Sumimoto H.;
RT "PAR3beta, a novel homologue of the cell polarity protein PAR3, localizes
RT to tight junctions.";
RL Biochem. Biophys. Res. Commun. 299:641-646(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), INTERACTION WITH
RP PARD6B AND PRKCZ, AND TISSUE SPECIFICITY.
RX PubMed=12234671; DOI=10.1016/s0378-1119(02)00681-9;
RA Gao L., Macara I.G., Joberty G.;
RT "Multiple splice variants of Par3 and of a novel related gene, Par3L,
RT produce proteins with different binding properties.";
RL Gene 294:99-107(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 860-1356 (ISOFORM 1).
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 955-1356 (ISOFORM 6), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-1356 (ISOFORM 10).
RC TISSUE=Hepatoma, and Ovarian carcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 313-992.
RC TISSUE=Testis;
RX PubMed=11149944; DOI=10.1073/pnas.98.2.629;
RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.;
RT "Serological detection of cutaneous T-cell lymphoma-associated antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
RN [10]
RP FUNCTION, AND INTERACTION WITH PARD6A.
RX PubMed=10954424; DOI=10.1242/jcs.113.18.3267;
RA Johansson A.-S., Driessens M., Aspenstroem P.;
RT "The mammalian homologue of the Caenorhabditis elegans polarity protein
RT PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1.";
RL J. Cell Sci. 113:3267-3275(2000).
RN [11]
RP SUBUNIT OF A COMPLEX CONTAINING PARD6B AND PRKCI.
RC TISSUE=Kidney;
RX PubMed=11257119; DOI=10.1083/jcb.152.6.1183;
RA Suzuki A., Yamanaka T., Hirose T., Manabe N., Mizuno K., Shimizu M.,
RA Akimoto K., Izumi Y., Ohnishi T., Ohno S.;
RT "Atypical protein kinase C is involved in the evolutionarily conserved par
RT protein complex and plays a critical role in establishing epithelia-
RT specific junctional structures.";
RL J. Cell Biol. 152:1183-1196(2001).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [13]
RP INTERACTION WITH ECT2.
RX PubMed=15254234; DOI=10.1128/mcb.24.15.6665-6675.2004;
RA Liu X.F., Ishida H., Raziuddin R., Miki T.;
RT "Nucleotide exchange factor ECT2 interacts with the polarity protein
RT complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta
RT activity.";
RL Mol. Cell. Biol. 24:6665-6675(2004).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A COMPLEX WITH
RP ARHGAP17; AMOT; PALS1 AND PATJ.
RX PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
RA Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
RA Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
RA Starostine A., Metalnikov P., Pawson T.;
RT "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
RT proteins in epithelial cells.";
RL Cell 125:535-548(2006).
RN [15]
RP INTERACTION WITH FBF1.
RX PubMed=18838552; DOI=10.1083/jcb.200803133;
RA Sugimoto M., Inoko A., Shiromizu T., Nakayama M., Zou P., Yonemura S.,
RA Hayashi Y., Izawa I., Sasoh M., Uji Y., Kaibuchi K., Kiyono T., Inagaki M.;
RT "The keratin-binding protein Albatross regulates polarization of epithelial
RT cells.";
RL J. Cell Biol. 183:19-28(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND SER-695, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-692; SER-695;
RP SER-728; SER-809; SER-852 AND SER-873, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP INTERACTION WITH AURKA AND AURKB, FUNCTION, MUTAGENESIS OF SER-962, AND
RP PHOSPHORYLATION AT SER-962.
RX PubMed=19812038; DOI=10.1074/jbc.m109.055897;
RA Khazaei M.R., Puschel A.W.;
RT "Phosphorylation of the par polarity complex protein Par3 at serine 962 is
RT mediated by aurora A and regulates its function in neuronal polarity.";
RL J. Biol. Chem. 284:33571-33579(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-728 AND SER-852, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=20332120; DOI=10.1242/jcs.059329;
RA Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G.,
RA Chapon F., Dejana E.;
RT "CCM1 regulates vascular-lumen organization by inducing endothelial
RT polarity.";
RL J. Cell Sci. 123:1073-1080(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-728; SER-852 AND
RP SER-873, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP ACETYLATION, DEACETYLATION BY SIRT2, AND INTERACTION WITH SIRT2.
RX PubMed=21949390; DOI=10.1073/pnas.1104969108;
RA Beirowski B., Gustin J., Armour S.M., Yamamoto H., Viader A., North B.J.,
RA Michan S., Baloh R.H., Golden J.P., Schmidt R.E., Sinclair D.A., Auwerx J.,
RA Milbrandt J.;
RT "Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through
RT polarity protein Par-3/atypical protein kinase C (aPKC) signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:E952-961(2011).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-852 AND SER-873, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
RP INTERACTION WITH TIAM1.
RX PubMed=23832200; DOI=10.1107/s1744309113014206;
RA Joshi M., Gakhar L., Fuentes E.J.;
RT "High-resolution structure of the Tiam1 PHn-CC-Ex domain.";
RL Acta Crystallogr. F 69:744-752(2013).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-383; SER-692;
RP SER-695; SER-715; SER-728; SER-827; SER-837; SER-852; SER-873; SER-962;
RP SER-971; SER-973 AND SER-1046, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; THR-91; SER-383 AND
RP TYR-489, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792 (ISOFORM 5), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [28]
RP INTERACTION WITH SAPCD2.
RX PubMed=26766442; DOI=10.1016/j.devcel.2015.12.016;
RA Chiu C.W., Monat C., Robitaille M., Lacomme M., Daulat A.M., Macleod G.,
RA McNeill H., Cayouette M., Angers S.;
RT "SAPCD2 controls spindle orientation and asymmetric divisions by negatively
RT regulating the Galphai-LGN-NuMA ternary complex.";
RL Dev. Cell 36:50-62(2016).
RN [29]
RP FUNCTION, INTERACTION WITH PRKCA, SUBCELLULAR LOCATION, INVOLVEMENT IN NTD,
RP VARIANTS NTD HIS-349; GLY-783 AND GLN-913, AND CHARACTERIZATION OF VARIANTS
RP NTD GLY-783 AND GLN-913.
RX PubMed=27925688; DOI=10.1002/humu.23153;
RA Chen X., An Y., Gao Y., Guo L., Rui L., Xie H., Sun M., Lam Hung S.,
RA Sheng X., Zou J., Bao Y., Guan H., Niu B., Li Z., Finnell R.H.,
RA Gusella J.F., Wu B.L., Zhang T.;
RT "Rare deleterious PARD3 variants in the aPKC-binding region are implicated
RT in the pathogenesis of human cranial neural tube defects via disrupting
RT apical tight junction formation.";
RL Hum. Mutat. 38:378-389(2017).
RN [30]
RP STRUCTURE BY NMR OF 451-549.
RX PubMed=20073081; DOI=10.1002/pro.335;
RA Jensen D.R., Woytovich C., Li M., Duvnjak P., Cassidy M.S., Frederick R.O.,
RA Bergeman L.F., Peterson F.C., Volkman B.F.;
RT "Rapid, robotic, small-scale protein production for NMR screening and
RT structure determination.";
RL Protein Sci. 19:570-578(2010).
CC -!- FUNCTION: Adapter protein involved in asymmetrical cell division and
CC cell polarization processes (PubMed:27925688, PubMed:10954424). Seems
CC to play a central role in the formation of epithelial tight junctions
CC (PubMed:27925688). Targets the phosphatase PTEN to cell junctions (By
CC similarity). Involved in Schwann cell peripheral myelination (By
CC similarity). Association with PARD6B may prevent the interaction of
CC PARD3 with F11R/JAM1, thereby preventing tight junction assembly (By
CC similarity). The PARD6-PARD3 complex links GTP-bound Rho small GTPases
CC to atypical protein kinase C proteins (PubMed:10934474). Required for
CC establishment of neuronal polarity and normal axon formation in
CC cultured hippocampal neurons (PubMed:19812038, PubMed:27925688).
CC {ECO:0000250|UniProtKB:Q99NH2, ECO:0000250|UniProtKB:Q9Z340,
CC ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:10954424,
CC ECO:0000269|PubMed:19812038, ECO:0000269|PubMed:27925688}.
CC -!- SUBUNIT: Interacts (via PDZ 1 domain) with F11R/JAM1, PARD6A and
CC PARD6B. Interacts with PRCKI and CDH5. Interacts (via PDZ 3 domain)
CC with PTEN (via C-terminus) (By similarity). Part of a complex with
CC PARD6A or PARD6B, PRKCI or PRKCZ and CDC42 or RAC1. Component of a
CC complex whose core is composed of ARHGAP17, AMOT, PALS1, PATJ and
CC PARD3/PAR3. Interacts with LIMK2, AURKA and AURKB. Component of the Par
CC polarity complex, composed of at least phosphorylated PRKCZ, PARD3 and
CC TIAM1. Directly interacts with TIAM1 and TIAM2. Interacts with ECT2,
CC FBF1 and SIRT2. Interacts (via coiled-coil domain) with FRMD4A (By
CC similarity). Found in a complex with PARD3, CYTH1 and FRMD4A (By
CC similarity). Interacts with SAPCD2 (PubMed:26766442). Interacts with
CC PRKCA (PubMed:27925688). {ECO:0000250|UniProtKB:Q99NH2,
CC ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:10954424,
CC ECO:0000269|PubMed:11257119, ECO:0000269|PubMed:12234671,
CC ECO:0000269|PubMed:15254234, ECO:0000269|PubMed:16678097,
CC ECO:0000269|PubMed:18838552, ECO:0000269|PubMed:19812038,
CC ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:21949390,
CC ECO:0000269|PubMed:23832200, ECO:0000269|PubMed:26766442,
CC ECO:0000269|PubMed:27925688}.
CC -!- SUBUNIT: [Isoform 8]: Interacts with PRKCZ.
CC {ECO:0000250|UniProtKB:Q99NH2}.
CC -!- INTERACTION:
CC Q8TEW0; P33151: CDH5; NbExp=5; IntAct=EBI-81968, EBI-2903122;
CC Q8TEW0; Q9Y624: F11R; NbExp=2; IntAct=EBI-81968, EBI-742600;
CC Q8TEW0; Q9NPB6: PARD6A; NbExp=9; IntAct=EBI-81968, EBI-81876;
CC Q8TEW0; Q9BYG5: PARD6B; NbExp=5; IntAct=EBI-81968, EBI-295391;
CC Q8TEW0; Q9BYG4: PARD6G; NbExp=3; IntAct=EBI-81968, EBI-295417;
CC Q8TEW0; Q8ND90: PNMA1; NbExp=4; IntAct=EBI-81968, EBI-302345;
CC Q8TEW0; P41743: PRKCI; NbExp=5; IntAct=EBI-81968, EBI-286199;
CC Q8TEW0; P04637: TP53; NbExp=3; IntAct=EBI-81968, EBI-366083;
CC Q8TEW0; Q04917: YWHAH; NbExp=7; IntAct=EBI-81968, EBI-306940;
CC Q8TEW0; P63104: YWHAZ; NbExp=5; IntAct=EBI-81968, EBI-347088;
CC Q8TEW0; Q9JK83: Pard6b; Xeno; NbExp=3; IntAct=EBI-81968, EBI-81861;
CC Q8TEW0; Q62074: Prkci; Xeno; NbExp=7; IntAct=EBI-81968, EBI-82016;
CC Q8TEW0; Q6ZPF3: Tiam2; Xeno; NbExp=2; IntAct=EBI-81968, EBI-7565978;
CC Q8TEW0-2; Q6ZPF3: Tiam2; Xeno; NbExp=6; IntAct=EBI-9118204, EBI-7565978;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endomembrane system
CC {ECO:0000269|PubMed:20332120}. Cell junction
CC {ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:27925688}. Cell
CC junction, tight junction {ECO:0000269|PubMed:20332120,
CC ECO:0000269|PubMed:27925688}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q99NH2}. Cell membrane
CC {ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:27925688}. Cytoplasm,
CC cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20332120}. Note=Localized along the cell-cell
CC contact region. Colocalizes with PARD6A and PRKCI at epithelial tight
CC junctions. Colocalizes with the cortical actin that overlays the
CC meiotic spindle during metaphase I and metaphase II. Colocalized with
CC SIRT2 in internode region of myelin sheath (By similarity). Presence of
CC KRIT1, CDH5 and RAP1B is required for its localization to the cell
CC junction. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Name=1; Synonyms=A;
CC IsoId=Q8TEW0-1; Sequence=Displayed;
CC Name=2; Synonyms=B, La;
CC IsoId=Q8TEW0-2; Sequence=VSP_007464;
CC Name=3; Synonyms=C;
CC IsoId=Q8TEW0-3; Sequence=VSP_007462, VSP_007463, VSP_007464,
CC VSP_007465;
CC Name=4; Synonyms=D;
CC IsoId=Q8TEW0-4; Sequence=VSP_007469;
CC Name=5; Synonyms=E;
CC IsoId=Q8TEW0-5; Sequence=VSP_007462, VSP_007463, VSP_007464,
CC VSP_007466, VSP_007468, VSP_007469;
CC Name=6; Synonyms=F;
CC IsoId=Q8TEW0-6; Sequence=VSP_007463, VSP_007464, VSP_007465;
CC Name=7; Synonyms=Lb;
CC IsoId=Q8TEW0-7; Sequence=VSP_007463, VSP_007464, VSP_007465,
CC VSP_007469;
CC Name=8; Synonyms=Sa;
CC IsoId=Q8TEW0-8; Sequence=VSP_007464, VSP_007470, VSP_007471;
CC Name=9; Synonyms=Sb;
CC IsoId=Q8TEW0-9; Sequence=VSP_007463, VSP_007464, VSP_007465,
CC VSP_007470, VSP_007471;
CC Name=10;
CC IsoId=Q8TEW0-10; Sequence=VSP_007464, VSP_007465, VSP_007467,
CC VSP_007470, VSP_007471;
CC Name=11;
CC IsoId=Q8TEW0-11; Sequence=VSP_007463, VSP_007464;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12234671}.
CC -!- DOMAIN: Contains a conserved N-terminal oligomerization domain (NTD)
CC that is involved in oligomerization and is essential for proper
CC subapical membrane localization. {ECO:0000250}.
CC -!- DOMAIN: The second PDZ domain mediates interaction with membranes
CC containing phosphoinositol lipids. {ECO:0000250}.
CC -!- PTM: Acetylated. Deacetylated by SIRT2, thereby inhibiting Schwann cell
CC peripheral myelination. {ECO:0000269|PubMed:21949390}.
CC -!- PTM: Phosphorylation at Ser-827 by PRKCZ and PRKCI occurs at the most
CC apical tip of epithelial cell-cell contacts during the initial phase of
CC tight junction formation and may promote dissociation of the complex
CC with PARD6. EGF-induced Tyr-1127 phosphorylation mediates dissociation
CC from LIMK2 (By similarity). Phosphorylation by AURKA at Ser-962 is
CC required for the normal establishment of neuronal polarity
CC (PubMed:19812038). {ECO:0000250, ECO:0000269|PubMed:19812038}.
CC -!- DISEASE: Neural tube defects (NTD) [MIM:182940]: Congenital
CC malformations of the central nervous system and adjacent structures
CC related to defective neural tube closure during the first trimester of
CC pregnancy. Failure of neural tube closure can occur at any level of the
CC embryonic axis. Common NTD forms include anencephaly, myelomeningocele
CC and spina bifida, which result from the failure of fusion in the
CC cranial and spinal region of the neural tube. NTDs have a
CC multifactorial etiology encompassing both genetic and environmental
CC components. {ECO:0000269|PubMed:27925688}. Note=Disease susceptibility
CC is associated with variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Antibodies against PARD3 are present in sera from
CC patients with cutaneous T-cell lymphomas.
CC -!- SIMILARITY: Belongs to the PAR3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG33676.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA91366.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55330.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF252293; AAF71530.1; -; mRNA.
DR EMBL; AF196185; AAK27891.1; -; mRNA.
DR EMBL; AF196186; AAK27892.1; -; mRNA.
DR EMBL; AF332592; AAK69192.1; -; mRNA.
DR EMBL; AF332593; AAK69193.1; -; mRNA.
DR EMBL; AB073671; BAC54037.1; -; mRNA.
DR EMBL; AF467002; AAL76042.1; -; mRNA.
DR EMBL; AF467003; AAL76043.1; -; mRNA.
DR EMBL; AF467004; AAL76044.1; -; mRNA.
DR EMBL; AF467005; AAL76045.1; -; mRNA.
DR EMBL; AF467006; AAL76046.1; -; mRNA.
DR EMBL; AL138768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL360233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL392123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW85932.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW85934.1; -; Genomic_DNA.
DR EMBL; BC011711; AAH11711.2; -; mRNA.
DR EMBL; BC071566; AAH71566.1; -; mRNA.
DR EMBL; AK000761; BAA91366.1; ALT_INIT; mRNA.
DR EMBL; AK027735; BAB55330.1; ALT_INIT; mRNA.
DR EMBL; AF177228; AAG33676.1; ALT_SEQ; mRNA.
DR CCDS; CCDS53509.1; -. [Q8TEW0-5]
DR CCDS; CCDS53510.1; -. [Q8TEW0-3]
DR CCDS; CCDS53511.1; -. [Q8TEW0-11]
DR CCDS; CCDS53512.1; -. [Q8TEW0-6]
DR CCDS; CCDS53513.1; -. [Q8TEW0-9]
DR CCDS; CCDS53514.1; -. [Q8TEW0-4]
DR CCDS; CCDS53515.1; -. [Q8TEW0-2]
DR CCDS; CCDS53516.1; -. [Q8TEW0-8]
DR CCDS; CCDS7178.1; -. [Q8TEW0-1]
DR RefSeq; NP_001171714.1; NM_001184785.1. [Q8TEW0-2]
DR RefSeq; NP_001171715.1; NM_001184786.1. [Q8TEW0-11]
DR RefSeq; NP_001171716.1; NM_001184787.1. [Q8TEW0-4]
DR RefSeq; NP_001171717.1; NM_001184788.1. [Q8TEW0-6]
DR RefSeq; NP_001171718.1; NM_001184789.1. [Q8TEW0-7]
DR RefSeq; NP_001171719.1; NM_001184790.1. [Q8TEW0-3]
DR RefSeq; NP_001171720.1; NM_001184791.1. [Q8TEW0-5]
DR RefSeq; NP_001171721.1; NM_001184792.1. [Q8TEW0-8]
DR RefSeq; NP_001171722.1; NM_001184793.1. [Q8TEW0-10]
DR RefSeq; NP_001171723.1; NM_001184794.1. [Q8TEW0-9]
DR RefSeq; NP_062565.2; NM_019619.3. [Q8TEW0-1]
DR PDB; 2KOM; NMR; -; A=451-549.
DR PDBsum; 2KOM; -.
DR AlphaFoldDB; Q8TEW0; -.
DR SMR; Q8TEW0; -.
DR BioGRID; 121134; 264.
DR ComplexPortal; CPX-6183; PAR cell polarity complex, PARD6A-PRKCI variant.
DR ComplexPortal; CPX-6193; PAR cell polarity complex, PARD6B-PRKCI variant.
DR ComplexPortal; CPX-6194; PAR cell polarity complex, PARD6G-PRKCI variant.
DR ComplexPortal; CPX-6195; PAR cell polarity complex, PARD6G-PRKCZ variant.
DR ComplexPortal; CPX-6196; PAR cell polarity complex, PARD6B-PRKCZ variant.
DR ComplexPortal; CPX-6197; PAR cell polarity complex, PARD6A-PRKCZ variant.
DR CORUM; Q8TEW0; -.
DR DIP; DIP-31315N; -.
DR IntAct; Q8TEW0; 67.
DR MINT; Q8TEW0; -.
DR STRING; 9606.ENSP00000363921; -.
DR GlyGen; Q8TEW0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TEW0; -.
DR MetOSite; Q8TEW0; -.
DR PhosphoSitePlus; Q8TEW0; -.
DR BioMuta; PARD3; -.
DR DMDM; 30913162; -.
DR EPD; Q8TEW0; -.
DR jPOST; Q8TEW0; -.
DR MassIVE; Q8TEW0; -.
DR MaxQB; Q8TEW0; -.
DR PaxDb; Q8TEW0; -.
DR PeptideAtlas; Q8TEW0; -.
DR PRIDE; Q8TEW0; -.
DR ProteomicsDB; 26974; -.
DR ProteomicsDB; 74506; -. [Q8TEW0-1]
DR ProteomicsDB; 74507; -. [Q8TEW0-10]
DR ProteomicsDB; 74508; -. [Q8TEW0-2]
DR ProteomicsDB; 74509; -. [Q8TEW0-3]
DR ProteomicsDB; 74510; -. [Q8TEW0-4]
DR ProteomicsDB; 74511; -. [Q8TEW0-5]
DR ProteomicsDB; 74512; -. [Q8TEW0-6]
DR ProteomicsDB; 74513; -. [Q8TEW0-7]
DR ProteomicsDB; 74514; -. [Q8TEW0-8]
DR ProteomicsDB; 74515; -. [Q8TEW0-9]
DR Antibodypedia; 26597; 265 antibodies from 35 providers.
DR DNASU; 56288; -.
DR Ensembl; ENST00000340077.9; ENSP00000341844.5; ENSG00000148498.16. [Q8TEW0-8]
DR Ensembl; ENST00000346874.9; ENSP00000340591.4; ENSG00000148498.16. [Q8TEW0-4]
DR Ensembl; ENST00000350537.9; ENSP00000311986.6; ENSG00000148498.16. [Q8TEW0-6]
DR Ensembl; ENST00000374776.6; ENSP00000363908.1; ENSG00000148498.16. [Q8TEW0-9]
DR Ensembl; ENST00000374788.8; ENSP00000363920.3; ENSG00000148498.16. [Q8TEW0-2]
DR Ensembl; ENST00000374789.8; ENSP00000363921.3; ENSG00000148498.16. [Q8TEW0-1]
DR Ensembl; ENST00000374794.8; ENSP00000363926.3; ENSG00000148498.16. [Q8TEW0-5]
DR Ensembl; ENST00000545260.5; ENSP00000440857.1; ENSG00000148498.16. [Q8TEW0-3]
DR Ensembl; ENST00000545693.5; ENSP00000443147.1; ENSG00000148498.16. [Q8TEW0-11]
DR GeneID; 56288; -.
DR KEGG; hsa:56288; -.
DR MANE-Select; ENST00000374788.8; ENSP00000363920.3; NM_001184785.2; NP_001171714.1. [Q8TEW0-2]
DR UCSC; uc001ixq.3; human. [Q8TEW0-1]
DR CTD; 56288; -.
DR DisGeNET; 56288; -.
DR GeneCards; PARD3; -.
DR HGNC; HGNC:16051; PARD3.
DR HPA; ENSG00000148498; Low tissue specificity.
DR MalaCards; PARD3; -.
DR MIM; 182940; phenotype.
DR MIM; 606745; gene.
DR neXtProt; NX_Q8TEW0; -.
DR OpenTargets; ENSG00000148498; -.
DR PharmGKB; PA32936; -.
DR VEuPathDB; HostDB:ENSG00000148498; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00950000183214; -.
DR HOGENOM; CLU_006629_0_0_1; -.
DR InParanoid; Q8TEW0; -.
DR OMA; EPRGHHA; -.
DR OrthoDB; 908238at2759; -.
DR PhylomeDB; Q8TEW0; -.
DR TreeFam; TF323729; -.
DR PathwayCommons; Q8TEW0; -.
DR Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-HSA-420029; Tight junction interactions.
DR SignaLink; Q8TEW0; -.
DR SIGNOR; Q8TEW0; -.
DR BioGRID-ORCS; 56288; 57 hits in 1098 CRISPR screens.
DR ChiTaRS; PARD3; human.
DR EvolutionaryTrace; Q8TEW0; -.
DR GeneWiki; PARD3; -.
DR GenomeRNAi; 56288; -.
DR Pharos; Q8TEW0; Tbio.
DR PRO; PR:Q8TEW0; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8TEW0; protein.
DR Bgee; ENSG00000148498; Expressed in cervix squamous epithelium and 198 other tissues.
DR ExpressionAtlas; Q8TEW0; baseline and differential.
DR Genevisible; Q8TEW0; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0033269; C:internode region of axon; ISS:UniProtKB.
DR GO; GO:0120157; C:PAR polarity complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0070160; C:tight junction; IC:ComplexPortal.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0008356; P:asymmetric cell division; TAS:ProtInc.
DR GO; GO:0007409; P:axonogenesis; TAS:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030010; P:establishment of cell polarity; IBA:GO_Central.
DR GO; GO:0051660; P:establishment of centrosome localization; IBA:GO_Central.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; ISS:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IDA:ComplexPortal.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISS:UniProtKB.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:0031643; P:positive regulation of myelination; ISS:UniProtKB.
DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR Gene3D; 2.30.42.10; -; 3.
DR InterPro; IPR021922; Par3/HAL_N.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF12053; Par3_HAL_N_term; 1.
DR Pfam; PF00595; PDZ; 2.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50156; SSF50156; 3.
DR PROSITE; PS50106; PDZ; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Cell junction; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Differentiation; Disease variant; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1356
FT /note="Partitioning defective 3 homolog"
FT /id="PRO_0000185069"
FT DOMAIN 271..359
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 461..546
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 590..677
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 81..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..936
FT /note="Interaction with PRKCI and PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:Q9Z340"
FT REGION 865..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1356
FT /note="Interaction with FRMD4A"
FT /evidence="ECO:0000250|UniProtKB:Q99NH2"
FT REGION 1129..1356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1049..1077
FT /evidence="ECO:0000255"
FT COILED 1151..1174
FT /evidence="ECO:0000255"
FT COILED 1201..1224
FT /evidence="ECO:0000255"
FT COILED 1280..1301
FT /evidence="ECO:0000255"
FT COMPBIAS 154..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1025
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99NH2"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 489
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 834
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99NH2"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 851
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99NH2"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 885
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99NH2"
FT MOD_RES 962
FT /note="Phosphoserine; by AURKA"
FT /evidence="ECO:0000269|PubMed:19812038,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99NH2"
FT VAR_SEQ 195..238
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10934474,
FT ECO:0000303|PubMed:11642408, ECO:0000303|PubMed:12234671,
FT ECO:0000303|PubMed:12459187"
FT /id="VSP_007462"
FT VAR_SEQ 557..569
FT /note="Missing (in isoform 3, isoform 5, isoform 6, isoform
FT 7, isoform 9 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:10934474,
FT ECO:0000303|PubMed:11642408, ECO:0000303|PubMed:12234671,
FT ECO:0000303|PubMed:12459187, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007463"
FT VAR_SEQ 740..742
FT /note="Missing (in isoform 2, isoform 3, isoform 5, isoform
FT 6, isoform 7, isoform 8, isoform 9, isoform 10 and isoform
FT 11)"
FT /evidence="ECO:0000303|PubMed:10934474,
FT ECO:0000303|PubMed:11642408, ECO:0000303|PubMed:12234671,
FT ECO:0000303|PubMed:12459187, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007464"
FT VAR_SEQ 827..856
FT /note="Missing (in isoform 3, isoform 6, isoform 7, isoform
FT 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:10934474,
FT ECO:0000303|PubMed:11642408, ECO:0000303|PubMed:12234671,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_007465"
FT VAR_SEQ 857..858
FT /note="IA -> T (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007467"
FT VAR_SEQ 857
FT /note="I -> S (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12234671,
FT ECO:0000303|PubMed:12459187"
FT /id="VSP_007466"
FT VAR_SEQ 858..872
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12234671,
FT ECO:0000303|PubMed:12459187"
FT /id="VSP_007468"
FT VAR_SEQ 1025..1061
FT /note="Missing (in isoform 4, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:11642408,
FT ECO:0000303|PubMed:12234671, ECO:0000303|PubMed:12459187"
FT /id="VSP_007469"
FT VAR_SEQ 1025..1034
FT /note="RFGKHRKDDK -> SLAKLKPEKR (in isoform 8, isoform 9
FT and isoform 10)"
FT /evidence="ECO:0000303|PubMed:11642408,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_007470"
FT VAR_SEQ 1035..1356
FT /note="Missing (in isoform 8, isoform 9 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:11642408,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_007471"
FT VARIANT 107
FT /note="E -> D (in dbSNP:rs1436731)"
FT /id="VAR_015663"
FT VARIANT 349
FT /note="R -> H (in NTD; unknown pathological significance;
FT dbSNP:rs199923448)"
FT /evidence="ECO:0000269|PubMed:27925688"
FT /id="VAR_079846"
FT VARIANT 575
FT /note="D -> N (in dbSNP:rs3758459)"
FT /id="VAR_050453"
FT VARIANT 783
FT /note="D -> G (in NTD; reduces interaction with PRKCA,
FT disrupts tight junction formation in epithelial cells;
FT dbSNP:rs1114167354)"
FT /evidence="ECO:0000269|PubMed:27925688"
FT /id="VAR_079847"
FT VARIANT 913
FT /note="P -> Q (in NTD; reduces interaction with PRKCA;
FT increases phosphorylation; disrupts tight junction
FT formation in epithelial cells; dbSNP:rs781461462)"
FT /evidence="ECO:0000269|PubMed:27925688"
FT /id="VAR_079848"
FT MUTAGEN 962
FT /note="S->A: Abolishes phosphorylation by AURKA."
FT /evidence="ECO:0000269|PubMed:19812038"
FT MUTAGEN 1127
FT /note="Y->F: Delayed epithelial tight junction assembly."
FT CONFLICT 190
FT /note="T -> A (in Ref. 8; BAB55330)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="L -> Q (in Ref. 8; BAB55330)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="N -> S (in Ref. 8; BAB55330)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="D -> N (in Ref. 7; AAH71566)"
FT /evidence="ECO:0000305"
FT CONFLICT 996..1000
FT /note="GKEKK -> VELHE (in Ref. 8; BAA91366)"
FT /evidence="ECO:0000305"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:2KOM"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:2KOM"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:2KOM"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:2KOM"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:2KOM"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:2KOM"
FT HELIX 524..533
FT /evidence="ECO:0007829|PDB:2KOM"
FT STRAND 539..546
FT /evidence="ECO:0007829|PDB:2KOM"
FT MOD_RES Q8TEW0-5:792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ 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
