PAR6A_HUMAN
ID PAR6A_HUMAN Reviewed; 346 AA.
AC Q9NPB6; O14911; Q9NPJ7;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Partitioning defective 6 homolog alpha;
DE Short=PAR-6;
DE Short=PAR-6 alpha;
DE Short=PAR-6A;
DE AltName: Full=PAR6C;
DE AltName: Full=Tax interaction protein 40;
DE Short=TIP-40;
GN Name=PARD6A; Synonyms=PAR6A;
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 1), CHARACTERIZATION, AND INTERACTION
RP WITH PARD3; CDC42 AND RAC1.
RC TISSUE=B-cell;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP CDC42; RAC1 AND PRKCZ.
RC TISSUE=Cervix carcinoma;
RX PubMed=10873802; DOI=10.1016/s0960-9822(00)00535-2;
RA Qiu R.-G., Abo A., Martin G.S.;
RT "A human homolog of the Caenorhabditis elegans polarity determinant Par-6
RT links Rac and Cdc42 to PKC-zeta signaling and cell transformation.";
RL Curr. Biol. 10:697-707(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH RHOQ.
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT OF A COMPLEX CONTAINING
RP PARD3 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH RAC1; CDC42;
RP PRKCI AND PRKCZ.
RC TISSUE=Neuroblastoma;
RX PubMed=11260256; DOI=10.1046/j.1365-2443.2001.00404.x;
RA Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.;
RT "Human homologues of the Caenorhabditis elegans cell polarity protein PAR6
RT as an adaptor that links the small GTPases Rac and Cdc42 to atypical
RT protein kinase C.";
RL Genes Cells 6:107-119(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 115-345, AND INTERACTION WITH HTLV-1 TAX.
RC TISSUE=Lymphocyte;
RX PubMed=9482110; DOI=10.1038/sj.onc.1201567;
RA Rousset R., Fabre S., Desbois C., Bantignies F., Jalinot P.;
RT "The C-terminus of the HTLV-1 Tax oncoprotein mediates interaction with the
RT PDZ domain of cellular proteins.";
RL Oncogene 16:643-654(1998).
RN [8]
RP INTERACTION WITH PALS1.
RX PubMed=12545177; DOI=10.1038/ncb923;
RA Hurd T.W., Gao L., Roh M.H., Macara I.G., Margolis B.;
RT "Direct interaction of two polarity complexes implicated in epithelial
RT tight junction assembly.";
RL Nat. Cell Biol. 5:137-142(2003).
RN [9]
RP INTERACTION WITH CRB3, AND DOMAIN.
RX PubMed=14718572; DOI=10.1091/mbc.e03-04-0235;
RA Lemmers C., Michel D., Lane-Guermonprez L., Delgrossi M.-H., Medina E.,
RA Arsanto J.-P., Le Bivic A.;
RT "CRB3 binds directly to Par6 and regulates the morphogenesis of the tight
RT junctions in mammalian epithelial cells.";
RL Mol. Biol. Cell 15:1324-1333(2004).
RN [10]
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 [11]
RP INTERACTION WITH TGFBR1, AND PHOSPHORYLATION BY TGF-BETA RECEPTOR.
RX PubMed=15761148; DOI=10.1126/science.1105718;
RA Ozdamar B., Bose R., Barrios-Rodiles M., Wang H.R., Zhang Y., Wrana J.L.;
RT "Regulation of the polarity protein Par6 by TGFbeta receptors controls
RT epithelial cell plasticity.";
RL Science 307:1603-1609(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP IDENTIFICATION BY MASS 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 [14]
RP INTERACTION WITH ECT2 AND PRKCI, AND MUTAGENESIS OF LYS-19.
RX PubMed=19617897; DOI=10.1038/onc.2009.217;
RA Justilien V., Fields A.P.;
RT "Ect2 links the PKCiota-Par6alpha complex to Rac1 activation and cellular
RT transformation.";
RL Oncogene 28:3597-3607(2009).
RN [15]
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 [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DCTN1 AND PCM1.
RX PubMed=20719959; DOI=10.1091/mbc.e10-05-0430;
RA Kodani A., Tonthat V., Wu B., Suetterlin C.;
RT "Par6 alpha interacts with the dynactin subunit p150 Glued and is a
RT critical regulator of centrosomal protein recruitment.";
RL Mol. Biol. Cell 21:3376-3385(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-345, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [18]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 14-95 IN COMPLEX WITH PRKCI, AND
RP MUTAGENESIS OF LYS-19; ARG-28 AND ARG-89.
RX PubMed=15590654; DOI=10.1074/jbc.m409823200;
RA Hirano Y., Yoshinaga S., Takeya R., Suzuki N.N., Horiuchi M., Kohjima M.,
RA Sumimoto H., Inagaki F.;
RT "Structure of a cell polarity regulator, a complex between atypical PKC and
RT Par6 PB1 domains.";
RL J. Biol. Chem. 280:9653-9661(2005).
CC -!- FUNCTION: Adapter protein involved in asymmetrical cell division and
CC cell polarization processes. Probably involved in the formation of
CC epithelial tight junctions. Association with PARD3 may prevent the
CC interaction of PARD3 with F11R/JAM1, thereby preventing tight junction
CC assembly. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to
CC atypical protein kinase C proteins (PubMed:10873802). Regulates
CC centrosome organization and function. Essential for the centrosomal
CC recruitment of key proteins that control centrosomal microtubule
CC organization (PubMed:20719959). {ECO:0000269|PubMed:10873802,
CC ECO:0000269|PubMed:20719959}.
CC -!- SUBUNIT: Interacts with MAP2K5 (By similarity). Interacts with PARD3.
CC Interacts with GTP-bound forms of CDC42, RHOQ/TC10 and RAC1. Interacts
CC with the N-terminal part of PRKCI and PRKCZ. Part of a complex with
CC PARD3, CDC42 or RAC1 and PRKCI or PRKCZ. Part of a complex with LLGL1
CC and PRKCI (By similarity). Interacts with human T-cell leukemia virus
CC type I TAX protein. Interacts with PALS1 and CRB3. Interacts with
CC TGFBR1; involved in TGF-beta induced epithelial to mesenchymal
CC transition. Interacts with ECT2 ('Thr-359' phosphorylated form) and
CC PRKCI. Interacts with DCTN1 and PCM1 (PubMed:20719959).
CC {ECO:0000250|UniProtKB:Q9Z101, ECO:0000269|PubMed:10873802,
CC ECO:0000269|PubMed:10934474, ECO:0000269|PubMed:10954424,
CC ECO:0000269|PubMed:11257119, ECO:0000269|PubMed:11260256,
CC ECO:0000269|PubMed:12545177, ECO:0000269|PubMed:14718572,
CC ECO:0000269|PubMed:15254234, ECO:0000269|PubMed:15590654,
CC ECO:0000269|PubMed:15761148, ECO:0000269|PubMed:19617897,
CC ECO:0000269|PubMed:20719959, ECO:0000269|PubMed:9482110}.
CC -!- INTERACTION:
CC Q9NPB6; P60953: CDC42; NbExp=7; IntAct=EBI-81876, EBI-81752;
CC Q9NPB6; P33151: CDH5; NbExp=4; IntAct=EBI-81876, EBI-2903122;
CC Q9NPB6; Q8TEW0: PARD3; NbExp=9; IntAct=EBI-81876, EBI-81968;
CC Q9NPB6; Q8ND90: PNMA1; NbExp=2; IntAct=EBI-81876, EBI-302345;
CC Q9NPB6; P41743: PRKCI; NbExp=17; IntAct=EBI-81876, EBI-286199;
CC Q9NPB6; Q05513: PRKCZ; NbExp=8; IntAct=EBI-81876, EBI-295351;
CC Q9NPB6; P63000: RAC1; NbExp=2; IntAct=EBI-81876, EBI-413628;
CC Q9NPB6; Q04917: YWHAH; NbExp=2; IntAct=EBI-81876, EBI-306940;
CC Q9NPB6-2; P62993: GRB2; NbExp=3; IntAct=EBI-10693102, EBI-401755;
CC Q9NPB6-2; Q92569: PIK3R3; NbExp=3; IntAct=EBI-10693102, EBI-79893;
CC Q9NPB6-2; P41743: PRKCI; NbExp=3; IntAct=EBI-10693102, EBI-286199;
CC Q9NPB6-2; Q16825: PTPN21; NbExp=3; IntAct=EBI-10693102, EBI-2860264;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Cell projection,
CC ruffle. Cell junction, tight junction. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriolar satellite
CC {ECO:0000269|PubMed:20719959}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:20719959}.
CC Note=Colocalizes with GTP-bound CDC42 or RAC1 at membrane ruffles and
CC with PARD3 and PRKCI at epithelial tight junctions. Recruited to the
CC centrosome by a microtubule and dynein-dynactin-dependent mechanism.
CC {ECO:0000269|PubMed:20719959}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NPB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPB6-2; Sequence=VSP_007459;
CC -!- TISSUE SPECIFICITY: Expressed in pancreas, skeletal muscle, brain and
CC heart. Weakly expressed in kidney and placenta.
CC -!- DOMAIN: The pseudo-CRIB domain together with the PDZ domain is required
CC for the interaction with Rho small GTPases. {ECO:0000250}.
CC -!- DOMAIN: The PB1 domain mediates interactions with MAP2K5.
CC {ECO:0000250}.
CC -!- DOMAIN: The PDZ domain mediates the interaction with CRB3.
CC {ECO:0000269|PubMed:14718572}.
CC -!- PTM: Phosphorylated by the TGF-beta receptor. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAR6 family. {ECO:0000305}.
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DR EMBL; AJ277095; CAB85490.1; -; mRNA.
DR EMBL; AF265565; AAF75548.1; -; mRNA.
DR EMBL; AF252292; AAF71529.1; -; mRNA.
DR EMBL; AB043634; BAA96235.1; -; mRNA.
DR EMBL; AB041642; BAB16105.1; -; mRNA.
DR EMBL; BC015626; AAH15626.1; -; mRNA.
DR EMBL; AF028827; AAB84252.1; -; mRNA.
DR CCDS; CCDS10843.1; -. [Q9NPB6-1]
DR CCDS; CCDS45514.1; -. [Q9NPB6-2]
DR RefSeq; NP_001032358.1; NM_001037281.1. [Q9NPB6-2]
DR RefSeq; NP_058644.1; NM_016948.2. [Q9NPB6-1]
DR PDB; 1WMH; X-ray; 1.50 A; B=14-95.
DR PDBsum; 1WMH; -.
DR AlphaFoldDB; Q9NPB6; -.
DR SMR; Q9NPB6; -.
DR BioGRID; 119157; 59.
DR ComplexPortal; CPX-6183; PAR cell polarity complex, PARD6A-PRKCI variant.
DR ComplexPortal; CPX-6197; PAR cell polarity complex, PARD6A-PRKCZ variant.
DR CORUM; Q9NPB6; -.
DR DIP; DIP-31312N; -.
DR IntAct; Q9NPB6; 46.
DR MINT; Q9NPB6; -.
DR STRING; 9606.ENSP00000219255; -.
DR iPTMnet; Q9NPB6; -.
DR PhosphoSitePlus; Q9NPB6; -.
DR BioMuta; PARD6A; -.
DR DMDM; 30913215; -.
DR jPOST; Q9NPB6; -.
DR MassIVE; Q9NPB6; -.
DR MaxQB; Q9NPB6; -.
DR PaxDb; Q9NPB6; -.
DR PeptideAtlas; Q9NPB6; -.
DR PRIDE; Q9NPB6; -.
DR ProteomicsDB; 81959; -. [Q9NPB6-1]
DR ProteomicsDB; 81960; -. [Q9NPB6-2]
DR Antibodypedia; 4052; 294 antibodies from 33 providers.
DR DNASU; 50855; -.
DR Ensembl; ENST00000219255.3; ENSP00000219255.3; ENSG00000102981.10. [Q9NPB6-1]
DR Ensembl; ENST00000458121.7; ENSP00000392388.1; ENSG00000102981.10. [Q9NPB6-2]
DR GeneID; 50855; -.
DR KEGG; hsa:50855; -.
DR MANE-Select; ENST00000458121.7; ENSP00000392388.1; NM_001037281.2; NP_001032358.1. [Q9NPB6-2]
DR UCSC; uc002ets.3; human. [Q9NPB6-1]
DR CTD; 50855; -.
DR DisGeNET; 50855; -.
DR GeneCards; PARD6A; -.
DR HGNC; HGNC:15943; PARD6A.
DR HPA; ENSG00000102981; Tissue enhanced (brain, testis).
DR MIM; 607484; gene.
DR neXtProt; NX_Q9NPB6; -.
DR OpenTargets; ENSG00000102981; -.
DR PharmGKB; PA32937; -.
DR VEuPathDB; HostDB:ENSG00000102981; -.
DR eggNOG; KOG3606; Eukaryota.
DR GeneTree; ENSGT00950000183211; -.
DR HOGENOM; CLU_040653_0_0_1; -.
DR InParanoid; Q9NPB6; -.
DR OMA; SQGSPCW; -.
DR OrthoDB; 825211at2759; -.
DR PhylomeDB; Q9NPB6; -.
DR TreeFam; TF312899; -.
DR PathwayCommons; Q9NPB6; -.
DR Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-HSA-420029; Tight junction interactions.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR SignaLink; Q9NPB6; -.
DR SIGNOR; Q9NPB6; -.
DR BioGRID-ORCS; 50855; 13 hits in 1075 CRISPR screens.
DR ChiTaRS; PARD6A; human.
DR EvolutionaryTrace; Q9NPB6; -.
DR GeneWiki; PARD6A; -.
DR GenomeRNAi; 50855; -.
DR Pharos; Q9NPB6; Tbio.
DR PRO; PR:Q9NPB6; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NPB6; protein.
DR Bgee; ENSG00000102981; Expressed in right hemisphere of cerebellum and 162 other tissues.
DR ExpressionAtlas; Q9NPB6; baseline and differential.
DR Genevisible; Q9NPB6; HS.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0034451; C:centriolar satellite; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0120157; C:PAR polarity complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0070160; C:tight junction; IC:ComplexPortal.
DR GO; GO:0030742; F:GTP-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045217; P:cell-cell junction maintenance; ISS:UniProtKB.
DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IDA:ComplexPortal.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; IMP:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0060341; P:regulation of cellular localization; IBA:GO_Central.
DR GO; GO:0016032; P:viral process; TAS:ProtInc.
DR CDD; cd06403; PB1_Par6; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR034872; PAR-6_a.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR034868; PB1_Par6.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR14102:SF9; PTHR14102:SF9; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW Cell junction; Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Membrane; Phosphoprotein; Reference proteome; Tight junction.
FT CHAIN 1..346
FT /note="Partitioning defective 6 homolog alpha"
FT /id="PRO_0000112513"
FT DOMAIN 15..95
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 133..150
FT /note="Pseudo-CRIB"
FT DOMAIN 157..250
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..116
FT /note="Interaction with PRKCI and PRKCZ"
FT REGION 126..253
FT /note="Interaction with PARD3 and CDC42"
FT /evidence="ECO:0000250"
FT REGION 257..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10873802,
FT ECO:0000303|PubMed:10934474, ECO:0000303|PubMed:11260256,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007459"
FT VARIANT 286
FT /note="V -> I (in dbSNP:rs35356834)"
FT /id="VAR_050454"
FT MUTAGEN 19
FT /note="K->A: Loss of interaction with ECT2 and PRKCI."
FT /evidence="ECO:0000269|PubMed:15590654,
FT ECO:0000269|PubMed:19617897"
FT MUTAGEN 28
FT /note="R->A: Slight decrease of interaction with PRKCI.
FT Loss of interaction with PRKCI; when associated with A-89."
FT /evidence="ECO:0000269|PubMed:15590654"
FT MUTAGEN 89
FT /note="R->A: Slight decrease of interaction with PRKCI.
FT Loss of interaction with PRKCI; when associated with A-28."
FT /evidence="ECO:0000269|PubMed:15590654"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1WMH"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:1WMH"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1WMH"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:1WMH"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1WMH"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1WMH"
FT HELIX 74..80
FT /evidence="ECO:0007829|PDB:1WMH"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1WMH"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1WMH"
SQ SEQUENCE 346 AA; 37388 MW; 9241E0EDC3694AD4 CRC64;
MARPQRTPAR SPDSIVEVKS KFDAEFRRFA LPRASVSGFQ EFSRLLRAVH QIPGLDVLLG
YTDAHGDLLP LTNDDSLHRA LASGPPPLRL LVQKRAEADS SGLAFASNSL QRRKKGLLLR
PVAPLRTRPP LLISLPQDFR QVSSVIDVDL LPETHRRVRL HKHGSDRPLG FYIRDGMSVR
VAPQGLERVP GIFISRLVRG GLAESTGLLA VSDEILEVNG IEVAGKTLDQ VTDMMVANSH
NLIVTVKPAN QRNNVVRGAS GRLTGPPSAG PGPAEPDSDD DSSDLVIENR QPPSSNGLSQ
GPPCWDLHPG CRHPGTRSSL PSLDDQEQAS SGWGSRIRGD GSGFSL
