PARD3_RAT
ID PARD3_RAT Reviewed; 1337 AA.
AC Q9Z340;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 179.
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=Atypical PKC-specific-binding protein;
DE Short=ASBP;
GN Name=Pard3; Synonyms=Par3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH PRKCI AND
RP PRKCZ.
RC TISSUE=Fibroblast;
RX PubMed=9763423; DOI=10.1083/jcb.143.1.95;
RA Izumi Y., Hirose T., Tamai Y., Hirai S., Nagashima Y., Fujimoto T.,
RA Tabuse Y., Kemphues K.J., Ohno S.;
RT "An atypical PKC directly associates and colocalizes at the epithelial
RT tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans
RT polarity protein PAR-3.";
RL J. Cell Biol. 143:95-106(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION AT SER-827.
RX PubMed=12045219; DOI=10.1242/jcs.115.12.2485;
RA Hirose T., Izumi Y., Nagashima Y., Tamai-Nagai Y., Kurihara H., Sakai T.,
RA Suzuki Y., Yamanaka T., Suzuki A., Mizuno K., Ohno S.;
RT "Involvement of ASIP/PAR-3 in the promotion of epithelial tight junction
RT formation.";
RL J. Cell Sci. 115:2485-2495(2002).
RN [3]
RP FUNCTION IN REGULATION OF PERIPHERAL MYELINATION, ACETYLATION, AND
RP DEACETYLATION BY 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 AND SER-852, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP STRUCTURE BY NMR OF 2-83, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=17476308; DOI=10.1038/sj.emboj.7601702;
RA Feng W., Wu H., Chan L.N., Zhang M.;
RT "The Par-3 NTD adopts a PB1-like structure required for Par-3
RT oligomerization and membrane localization.";
RL EMBO J. 26:2786-2796(2007).
RN [6]
RP STRUCTURE BY NMR OF 454-550, SUBCELLULAR LOCATION, FUNCTION,
RP PHOSPHOINOSITOL LIPID BINDING, DOMAIN, MUTAGENESIS OF LYS-458; LYS-491;
RP ARG-504; LYS-506; ARG-532; LYS-535 AND ARG-546, AND INTERACTION WITH PTEN.
RX PubMed=18082612; DOI=10.1016/j.molcel.2007.10.028;
RA Wu H., Feng W., Chen J., Chan L.N., Huang S., Zhang M.;
RT "PDZ domains of Par-3 as potential phosphoinositide signaling
RT integrators.";
RL Mol. Cell 28:886-898(2007).
RN [7]
RP STRUCTURE BY NMR OF 582-685 IN COMPLEX WITH PTEN, SUBUNIT, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=18550519; DOI=10.1074/jbc.m802482200;
RA Feng W., Wu H., Chan L.N., Zhang M.;
RT "Par-3-mediated junctional localization of the lipid phosphatase PTEN is
RT required for cell polarity establishment.";
RL J. Biol. Chem. 283:23440-23449(2008).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 813-840 IN COMPLEX WITH MOUSE
RP PRKCI, PHOSPHORYLATION AT SER-827, AND MUTAGENESIS OF SER-827 AND SER-829.
RX PubMed=22579248; DOI=10.1016/j.str.2012.02.022;
RA Wang C., Shang Y., Yu J., Zhang M.;
RT "Substrate recognition mechanism of atypical protein kinase Cs revealed by
RT the structure of PKCiota in complex with a substrate peptide from Par-3.";
RL Structure 20:791-801(2012).
CC -!- FUNCTION: Adapter protein involved in asymmetrical cell division and
CC cell polarization processes (PubMed:18550519). Seems to play a central
CC role in the formation of epithelial tight junctions (By similarity).
CC Association with PARD6B may prevent the interaction of PARD3 with
CC F11R/JAM1, thereby preventing tight junction assembly (By similarity).
CC The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical
CC protein kinase C proteins (By similarity). Required for establishment
CC of neuronal polarity and normal axon formation in cultured hippocampal
CC neurons (By similarity). Involved in Schwann cell peripheral
CC myelination (PubMed:21949390). Targets the phosphatase PTEN to cell
CC junctions (PubMed:18082612). {ECO:0000250|UniProtKB:Q8TEW0,
CC ECO:0000250|UniProtKB:Q99NH2, ECO:0000269|PubMed:18082612,
CC ECO:0000269|PubMed:18550519, ECO:0000269|PubMed:21949390}.
CC -!- SUBUNIT: Component of a complex whose core is composed of ARHGAP17,
CC AMOT, PALS1, PATJ and PARD3/PAR3. Interacts (via PDZ 1 domain) with
CC PARD6A, PARD6B and F11R/JAM1. Interacts with AURKA, AURKB and SIRT2 (By
CC similarity). Interacts with PRKCI. Interacts with PRKCZ (Probable).
CC Part of a complex with PARD6A or PARD6B, PRKCI or PRKCZ and CDC42 or
CC RAC1. Interacts with LIMK2 and CDH5. Component of the Par polarity
CC complex, composed of at least phosphorylated PRKCZ, PARD3 and TIAM1.
CC Directly interacts with TIAM1 and TIAM2. Interacts with ECT2 and FBF1
CC (By similarity). Interacts (via PDZ 3 domain) with PTEN (via C-
CC terminus). 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 (By similarity). Interacts with
CC PRKCA (By similarity). {ECO:0000250|UniProtKB:Q8TEW0,
CC ECO:0000250|UniProtKB:Q99NH2, ECO:0000269|PubMed:18082612,
CC ECO:0000269|PubMed:18550519, ECO:0000269|PubMed:22579248,
CC ECO:0000269|PubMed:9763423, ECO:0000305}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with PRKCZ.
CC {ECO:0000250|UniProtKB:Q99NH2}.
CC -!- INTERACTION:
CC Q9Z340; Q9Z340: Pard3; NbExp=6; IntAct=EBI-349441, EBI-349441;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endomembrane system.
CC Cell junction. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q99NH2}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q99NH2}. Cytoplasm, cell cortex {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}.
CC Note=Localized along the cell-cell contact region. Colocalizes with
CC PARD6A and PRKCI at epithelial tight junctions. Colocalizes with the
CC cortical actin that overlays the meiotic spindle during metaphase I and
CC metaphase II. Presence of KRIT1, CDH5 and RAP1B is required for its
CC localization to the cell junction. Colocalized with SIRT2 in internode
CC region of myelin sheat (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=180 kDa;
CC IsoId=Q9Z340-1; Sequence=Displayed;
CC Name=2; Synonyms=150 kDa;
CC IsoId=Q9Z340-2; Sequence=VSP_007475;
CC -!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in lung,
CC glandular stomach, prostate, ovary and uterus. Isoform 1 is also
CC expressed in brain, with a high expression in the cortex, hippocampus
CC and in the striatum. Isoform 2 is predominantly expressed in intestinal
CC epithelial cells, kidney and prostate.
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.
CC -!- DOMAIN: The second PDZ domain mediates interaction with membranes
CC containing phosphoinositol lipids.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PAR3 family. {ECO:0000305}.
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DR EMBL; AB005549; BAA34216.1; -; mRNA.
DR PIR; T13948; T13948.
DR RefSeq; NP_112514.1; NM_031235.1. [Q9Z340-1]
DR PDB; 2K1Z; NMR; -; A=582-685.
DR PDB; 2K20; NMR; -; A=582-685.
DR PDB; 2NS5; NMR; -; A=2-83.
DR PDB; 2OGP; NMR; -; A=454-550.
DR PDB; 3ZEE; EM; 6.10 A; A=2-82.
DR PDB; 4DC2; X-ray; 2.40 A; Z=813-840.
DR PDB; 4I6P; X-ray; 2.90 A; A/B=2-83.
DR PDB; 6JUE; X-ray; 1.55 A; L=582-685.
DR PDBsum; 2K1Z; -.
DR PDBsum; 2K20; -.
DR PDBsum; 2NS5; -.
DR PDBsum; 2OGP; -.
DR PDBsum; 3ZEE; -.
DR PDBsum; 4DC2; -.
DR PDBsum; 4I6P; -.
DR PDBsum; 6JUE; -.
DR AlphaFoldDB; Q9Z340; -.
DR SMR; Q9Z340; -.
DR BioGRID; 249693; 4.
DR CORUM; Q9Z340; -.
DR DIP; DIP-33271N; -.
DR IntAct; Q9Z340; 2.
DR MINT; Q9Z340; -.
DR STRING; 10116.ENSRNOP00000048964; -.
DR iPTMnet; Q9Z340; -.
DR PhosphoSitePlus; Q9Z340; -.
DR PaxDb; Q9Z340; -.
DR PRIDE; Q9Z340; -.
DR Ensembl; ENSRNOT00000042623; ENSRNOP00000048964; ENSRNOG00000032437. [Q9Z340-1]
DR GeneID; 81918; -.
DR KEGG; rno:81918; -.
DR UCSC; RGD:620374; rat. [Q9Z340-1]
DR CTD; 56288; -.
DR RGD; 620374; Pard3.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00950000183214; -.
DR HOGENOM; CLU_006629_0_0_1; -.
DR InParanoid; Q9Z340; -.
DR OMA; EPRGHHA; -.
DR OrthoDB; 908238at2759; -.
DR PhylomeDB; Q9Z340; -.
DR Reactome; R-RNO-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-RNO-420029; Tight junction interactions.
DR EvolutionaryTrace; Q9Z340; -.
DR PRO; PR:Q9Z340; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000032437; Expressed in esophagus and 19 other tissues.
DR ExpressionAtlas; Q9Z340; baseline and differential.
DR Genevisible; Q9Z340; RN.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0043296; C:apical junction complex; ISO:RGD.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0044295; C:axonal growth cone; IDA:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0033269; C:internode region of axon; ISS:UniProtKB.
DR GO; GO:0043219; C:lateral loop; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0120157; C:PAR polarity complex; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0003383; P:apical constriction; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051642; P:centrosome localization; ISO:RGD.
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; IMP:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
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:0002092; P:positive regulation of receptor internalization; ISO:RGD.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0032970; P:regulation of actin filament-based process; ISO:RGD.
DR GO; GO:0060341; P:regulation of cellular localization; IMP:RGD.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISO:RGD.
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; 3.
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; Lipid-binding; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1337
FT /note="Partitioning defective 3 homolog"
FT /id="PRO_0000185071"
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..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..936
FT /note="Interaction with PRKCI and PRKCZ"
FT /evidence="ECO:0000269|PubMed:9763423"
FT REGION 866..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1337
FT /note="Interaction with FRMD4A"
FT /evidence="ECO:0000250|UniProtKB:Q99NH2"
FT REGION 1028..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1050..1082
FT /evidence="ECO:0000255"
FT COILED 1149..1172
FT /evidence="ECO:0000255"
FT COILED 1199..1222
FT /evidence="ECO:0000255"
FT COILED 1278..1299
FT /evidence="ECO:0000255"
FT COMPBIAS 88..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..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..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1015
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
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:22673903"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 489
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12045219,
FT ECO:0000269|PubMed:22579248"
FT MOD_RES 834
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99NH2"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
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:22673903"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
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:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 973
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 1046
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW0"
FT MOD_RES 1331
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99NH2"
FT VAR_SEQ 1034..1337
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12045219"
FT /id="VSP_007475"
FT MUTAGEN 458
FT /note="K->E: Reduces binding to membranes containing
FT phosphoinositol lipids by half. Abolishes binding to
FT membranes containing phosphoinositol lipids; when
FT associated with E-546."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 491
FT /note="K->A: Slightly reduced binding to membranes
FT containing phosphoinositol lipids."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 491
FT /note="K->E: Strongly reduced binding to membranes
FT containing phosphoinositol lipids."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 504
FT /note="R->A: Slightly reduced binding to membranes
FT containing phosphoinositol lipids; when associated with A-
FT 506."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 504
FT /note="R->E: Abolishes binding to membranes containing
FT phosphoinositol lipids; when associated with E-506."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 506
FT /note="K->A: Slightly reduced binding to membranes
FT containing phosphoinositol lipids; when associated with A-
FT 504."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 506
FT /note="K->E: Abolishes binding to membranes containing
FT phosphoinositol lipids; when associated with E-504."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 532
FT /note="R->A: Reduces binding to membranes containing
FT phosphoinositol lipids by half; when associated with A-
FT 535."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 532
FT /note="R->E: Almost abolished binding to membranes
FT containing phosphoinositol lipids; when associated with E-
FT 535."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 535
FT /note="K->A: Reduces binding to membranes containing
FT phosphoinositol lipids by half; when associated with A-
FT 532."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 535
FT /note="K->E: Almost abolished binding to membranes
FT containing phosphoinositol lipids; when associated with E-
FT 532."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 546
FT /note="R->E: Abolishes binding to membranes containing
FT phosphoinositol lipids; when associated with E-458."
FT /evidence="ECO:0000269|PubMed:18082612"
FT MUTAGEN 827
FT /note="S->E: Abolishes binding to PKCI."
FT /evidence="ECO:0000269|PubMed:22579248"
FT MUTAGEN 829
FT /note="S->A: No detectable impact on binding to PKCI."
FT /evidence="ECO:0000269|PubMed:22579248"
FT MUTAGEN 829
FT /note="S->E: Abolishes binding to PKCI."
FT /evidence="ECO:0000269|PubMed:22579248"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4I6P"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:4I6P"
FT HELIX 23..38
FT /evidence="ECO:0007829|PDB:4I6P"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:4I6P"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2NS5"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:4I6P"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:4I6P"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:2OGP"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:2OGP"
FT STRAND 481..484
FT /evidence="ECO:0007829|PDB:2OGP"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:2OGP"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:2OGP"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:2OGP"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:2OGP"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:2OGP"
FT HELIX 524..533
FT /evidence="ECO:0007829|PDB:2OGP"
FT STRAND 539..546
FT /evidence="ECO:0007829|PDB:2OGP"
FT STRAND 585..593
FT /evidence="ECO:0007829|PDB:6JUE"
FT TURN 594..599
FT /evidence="ECO:0007829|PDB:2K1Z"
FT STRAND 603..610
FT /evidence="ECO:0007829|PDB:6JUE"
FT TURN 611..614
FT /evidence="ECO:0007829|PDB:6JUE"
FT STRAND 615..624
FT /evidence="ECO:0007829|PDB:6JUE"
FT HELIX 629..633
FT /evidence="ECO:0007829|PDB:6JUE"
FT STRAND 641..645
FT /evidence="ECO:0007829|PDB:6JUE"
FT STRAND 648..653
FT /evidence="ECO:0007829|PDB:2K1Z"
FT HELIX 655..666
FT /evidence="ECO:0007829|PDB:6JUE"
FT TURN 667..669
FT /evidence="ECO:0007829|PDB:2K20"
FT STRAND 674..682
FT /evidence="ECO:0007829|PDB:6JUE"
SQ SEQUENCE 1337 AA; 149448 MW; EC980C5106B52F9C CRC64;
MKVTVCFGRT RVVVPCGDGR MKVFSLIQQA VTRYRKAVAK DPNYWIQVHR LEHGDGGILD
LDDILCDVAD DKDRLVAVFD EQDPHHGGDG TSASSTGTQS PEIFGSELGT NNVSAFRPYQ
TTSEIEVTPS VLRANMPLHV RRSSDPALTG LSTSVSDNNF SSEEPSRKNP TRWSTTAGFL
KQNTTGSPKT CDRKKDENYR SLPRDPSSWS NQFQRDNARS SLSASHPMVD RWLEKQEQDE
EGTEEDSSRV EPVGHADTGL ENMPNFSLDD MVKLVQVPND GGPLGIHVVP FSARGGRTLG
LLVKRLEKGG KAEQENLFHE NDCIVRINDG DLRNRRFEQA QHMFRQAMRA RVIWFHVVPA
ANKEQYEQLS QREMNNYSPG RFSPDSHCVA NRSVANNAPQ ALPRAPRLSQ PPEQLDAHPR
LPHSAHASTK PPTAPALAPP NVLSTSVGSV YNTKRVGKRL NIQLKKGTEG LGFSITSRDV
TIGGSAPIYV KNILPRGAAI QDGRLKAGDR LIEVNGVDLA GKSQEEVVSL LRSTKMEGTV
SLLVFRQEEA FHPREMNAEP SQMQSPKETK AEDEDIVLTP DGTREFLTFE VPLNDSGSAG
LGVSVKGNRS KENHADLGIF VKSIINGGAA SKDGRLRVND QLIAVNGESL LGKANQEAME
TLRRSMSTEG NKRGMIQLIV ARRISRCNEL RSPGSPAAPE LPIETELDDR ERRISHSLYS
GIEGLDESPT RNAALSRIMG ESGKCQLSPT VNMPHDDTVM IEDDRLPVLP PHLSDQSSSS
SHDDVGFIMT EAGTWAKATI SDSADCSLSP DVDPVLAFQR EGFGRQSMSE KRTKQFSNAS
QLDFVKTRKS KSMDLGIADE TKLNTVDDQR AGSPNRDVGP SLGLKKSSSL ESLQTAVAEV
TLNGNIPFHR PRPRIIRGRG CNESFRAAID KSYDKPMVDD DDEGMETLEE DTEESSRSGR
ESVSTSSDQP SYSLERQMNG DPEKRDKAEK KKDKAGKDKK KDREKEKDKL KAKKGMLKGL
GDMFRFGKHR KDDKMEKMGR IKIQDSFTSE EDRVRMKEEQ ERIQAKTREF RERQARERDY
AEIQDFHRTF GCDDELLYGG MSSYDGCLAL NARPQSPREG HLMDTLYAQV KKPRSSKPGD
SNRSTPSNHD RIQRLRQEFQ QAKQDEDVED RRRTYSFEQS WSSSRPASQS GRHSVSVEVQ
VQRQRQEERE SFQQAQRQYS SLPRQSRKNA SSVSQDSWEQ NYAPGEGFQS AKENPRYSSY
QGSRNGYLGG HGFNARVMLE TQELLRQEQR RKEQQLKKQP PADGVRGPFR QDVPPSPSQV
ARLNRLQTPE KGRPFYS
