Protein : Qrob_P0047150.2 Q. robur
Protein Identifier  ? Qrob_P0047150.2 Organism . Name  Quercus robur
Score  100.0 Score Type  egn
Protein Description  (M=1) PTHR12326 - PLECKSTRIN HOMOLOGY DOMAIN CONTAINING PROTEIN Gene Prediction Quality  validated
Protein length 

Sequence

Length: 1142  
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0 Synonyms

1 GO Terms

Identifier Name Description
GO:0035091 phosphatidylinositol binding Interacting selectively and non-covalently with any inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives.

30 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|cit:102625347 1 1141 + 1141 Gaps:133 100.00 1138 57.73 0.0 uncharacterized LOC102625347
blastp_kegg lcl|pper:PRUPE_ppa000502mg 1 1141 + 1141 Gaps:139 100.00 1126 59.41 0.0 hypothetical protein
blastp_kegg lcl|pmum:103338357 1 1141 + 1141 Gaps:113 100.00 1126 58.70 0.0 uncharacterized LOC103338357
blastp_kegg lcl|cic:CICLE_v10018588mg 1 1141 + 1141 Gaps:133 100.00 1142 57.27 0.0 hypothetical protein
blastp_kegg lcl|vvi:100853506 58 1141 + 1084 Gaps:70 97.55 1144 56.27 0.0 uncharacterized LOC100853506
blastp_kegg lcl|fve:101296672 56 1141 + 1086 Gaps:80 97.69 1126 58.18 0.0 uncharacterized protein LOC101296672
blastp_kegg lcl|mdm:103455206 1 1141 + 1141 Gaps:104 100.00 1137 55.32 0.0 uncharacterized LOC103455206
blastp_kegg lcl|mdm:103431153 1 1141 + 1141 Gaps:104 100.00 1137 55.32 0.0 uncharacterized LOC103431153
blastp_kegg lcl|pxb:103953004 30 1141 + 1112 Gaps:86 99.29 1126 57.16 0.0 uncharacterized LOC103953004
blastp_kegg lcl|pop:POPTR_0012s08420g 57 1141 + 1085 Gaps:73 97.55 1060 58.41 0.0 POPTRDRAFT_773032 phox domain-containing family protein
blastp_pdb 1xte_A 690 771 + 82 Gaps:10 48.05 154 37.84 5e-06 mol:protein length:154 Serine/threonine-protein kinase Sgk3
blastp_pdb 1xtn_B 690 771 + 82 Gaps:10 61.67 120 37.84 9e-06 mol:protein length:120 Serine/threonine-protein kinase Sgk3
blastp_pdb 1xtn_A 690 771 + 82 Gaps:10 61.67 120 37.84 9e-06 mol:protein length:120 Serine/threonine-protein kinase Sgk3
blastp_uniprot_sprot sp|Q08AW4|PKHM3_XENLA 825 1082 + 258 Gaps:29 31.42 748 30.64 3e-30 Pleckstrin homology domain-containing family M member 3 OS Xenopus laevis GN plekhm3 PE 2 SV 1
blastp_uniprot_sprot sp|Q8BM47|PKHM3_MOUSE 836 1074 + 239 Gaps:23 29.17 761 30.63 7e-30 Pleckstrin homology domain-containing family M member 3 OS Mus musculus GN Plekhm3 PE 1 SV 1
blastp_uniprot_sprot sp|Q6ZWE6|PKHM3_HUMAN 836 1074 + 239 Gaps:23 29.17 761 30.18 1e-29 Pleckstrin homology domain-containing family M member 3 OS Homo sapiens GN PLEKHM3 PE 2 SV 2
blastp_uniprot_sprot sp|A7E316|K226L_BOVIN 827 1085 + 259 Gaps:22 36.35 663 32.37 6e-28 Uncharacterized protein KIAA0226-like OS Bos taurus GN KIAA0226L PE 2 SV 1
blastp_uniprot_sprot sp|Q92622|RUBIC_HUMAN 827 1074 + 248 Gaps:21 23.77 972 32.90 1e-27 Run domain Beclin-1 interacting and cysteine-rich containing protein OS Homo sapiens GN KIAA0226 PE 1 SV 4
blastp_uniprot_sprot sp|Q6DJB3|DEFI8_XENTR 875 1087 + 213 Gaps:12 47.18 443 34.45 9e-27 Differentially expressed in FDCP 8 homolog OS Xenopus tropicalis GN def8 PE 2 SV 1
blastp_uniprot_sprot sp|Q80U62|RUBIC_MOUSE 827 1074 + 248 Gaps:21 24.16 956 32.47 1e-26 Run domain Beclin-1 interacting and cysteine-rich containing protein OS Mus musculus GN Kiaa0226 PE 1 SV 2
blastp_uniprot_sprot sp|Q7T0P6|DFI8B_XENLA 875 1087 + 213 Gaps:12 47.18 443 34.45 2e-26 Differentially expressed in FDCP 8 homolog B OS Xenopus laevis GN def8-b PE 2 SV 1
blastp_uniprot_sprot sp|Q9H714|K226L_HUMAN 827 1085 + 259 Gaps:22 36.40 662 31.54 2e-26 Uncharacterized protein KIAA0226-like OS Homo sapiens GN KIAA0226L PE 1 SV 3
blastp_uniprot_sprot sp|Q9VTT9|DEFI8_DROME 841 1084 + 244 Gaps:26 46.34 492 34.65 3e-26 Differentially expressed in FDCP 8 homolog OS Drosophila melanogaster GN CG11534 PE 1 SV 1
rpsblast_cdd gnl|CDD|206072 875 1080 + 206 Gaps:11 98.51 202 42.21 8e-75 pfam13901 DUF4206 Domain of unknown function (DUF4206). This is a family of cysteine-rich proteins. Many members also carry a pleckstrin-homology domain pfam00169.
rpsblast_cdd gnl|CDD|132768 680 780 + 101 Gaps:11 88.68 106 35.11 1e-13 cd06093 PX_domain The Phox Homology domain a phosphoinositide binding module. The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling vesicular trafficking protein sorting lipid modification cell polarity and division activation of T and B cells and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases other PIs such as PI4P or PI(3 4)P2 among others are the preferred substrates. In addition to protein-lipid interaction the PX domain may also be involved in protein-protein interaction as in the cases of p40phox p47phox and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs which play important roles in endosomal sorting.
rpsblast_cdd gnl|CDD|201443 680 790 + 111 Gaps:13 95.41 109 28.85 5e-12 pfam00787 PX PX domain. PX domains bind to phosphoinositides.
rpsblast_cdd gnl|CDD|132780 690 759 + 70 Gaps:10 56.88 109 41.94 6e-09 cd06870 PX_CISK The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK) also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3) plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins Bad and FKHRL1. CISK/SGK3 also regulates many transporters ion channels and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain CISK contains a PX domain which binds highly phosphorylated PIs directs membrane localization and regulates the enzyme's activity.
rpsblast_cdd gnl|CDD|132781 689 778 + 90 Gaps:14 68.33 120 36.59 1e-07 cd06871 PX_MONaKA The phosphoinositide binding Phox Homology domain of Modulator of Na K-ATPase. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling vesicular trafficking protein sorting and lipid modification among others. MONaKA (Modulator of Na K-ATPase) binds the plasma membrane ion transporter Na K-ATPase and modulates its enzymatic and ion pump activities. It modulates brain Na K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.
rpsblast_cdd gnl|CDD|132785 689 787 + 99 Gaps:16 76.72 116 34.83 2e-07 cd06875 PX_IRAS The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected. The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling vesicular trafficking protein sorting and lipid modification among others. Imidazoline Receptor Antisera-Selected (IRAS) also called nischarin contains an N-terminal PX domain leucine rich repeats and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in PI-binding specificity and affinity and the presence of other protein-protein interaction domains which help determine subcellular localization and specific function in the endocytic pathway.
rpsblast_kog gnl|CDD|37040 825 1080 + 256 Gaps:23 41.55 580 37.34 8e-55 KOG1829 KOG1829 KOG1829 Uncharacterized conserved protein contains C1 PH and RUN domains [Signal transduction mechanisms].

6 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
SUPERFAMILY 686 791 106 SSF64268 none none IPR001683
Pfam 686 788 103 PF00787 none PX domain IPR001683
Pfam 875 1080 206 PF13901 none Domain of unknown function (DUF4206) IPR025258
PANTHER 825 1075 251 PTHR12326 none none none
ProSiteProfiles 673 793 121 PS50195 none PX domain profile. IPR001683
Gene3D 667 791 125 G3DSA:3.30.1520.10 none none IPR001683

0 Localization

17 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Champenoux_2015_nPriLBD_3P Qrob_Chr10 10 v_15000_157 v_15000_310 15,68 15,9 15,91 lod 2.4 5.5
Bourran2_2014_nSecLBD_3P Qrob_Chr08 8 s_1BN2OD_551 s_1B5AYF_599 17,17 0 43,51 lod 1,9229 4,4
Bourran2_2014_nLBD*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,25 0 35,55 lod 2,5951 6
Bourran2_2014_nP*_3P Qrob_Chr08 8 v_5216_549 v_11837_70 12,19 0 31,97 lod 2,8472 6
Bourran2_2002_QTL11_peak_Bud_burst_A4 Qrob_Chr06 6 s_1C41PA_791 s_1AM1AV_1141 19,17 0 34,57 lod 2,3 2,9
Bourran2_2014_aSeqBC_3P Qrob_Chr06 6 v_506_189 v_686_77 30,72 13,58 43,48 lod 2,2746 6,3
Bourran2_2014_aSeqBC*_A4 Qrob_Chr06 6 s_2F5MK3_712 v_444_355 27,13 14,86 39,46 lod 3,7847 9,8
Bourran2_2014_nEpis*_3P Qrob_Chr08 8 s_1DA4QW_688 s_1DNI7D_820 17,96 0 37,75 lod 2,9745 7,5
Bourran2_2014_nEpis*_A4 Qrob_Chr07 7 v_12400_446 s_1BPEBU_1211 6,93 0 15,13 lod 4,7411 11
Bourran2_2014_nFork*_3P Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 34,28 7,43 41,48 lod 2,4044 5,5
Bourran2_2014_nLBD_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 37,41 9,8 50,1 lod 1,9524 4,1
Bourran2_2014_nPriBD_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 34,51 3,36 51,86 lod 1,6747 3,9
Bourran2_2014_nPriLBD*_3P Qrob_Chr11 11 v_12066_307 s_1B15GJ_447 3,37 0,57 16,17 lod 3,4299 6,9
Bourran2_2014_nSecLBD_A4 Qrob_Chr07 7 v_8327_222 s_1A4WGY_363 16,04 0 44,69 lod 2,6373 6,5
Bourran2_2014_vEpiBC_A4 Qrob_Chr06 6 v_12930_125 s_1AMZEI_909 37,55 14,41 50,01 lod 1,7882 4,8
Champenoux_2015_nEpis_3P Qrob_Chr11 11 s_1DG9PM_867 s_1BZ083_1312 26,53 25,47 27,72 lod 4.4 8.9
Champenoux_2015_nP_3P Qrob_Chr06 6 s_1A386O_228 s_1AYZFS_603 27,03 26,47 27,34 lod 2.8 7.2

0 Targeting