Protein : Qrob_P0583940.2 Q. robur
Protein Identifier  ? Qrob_P0583940.2 Organism . Name  Quercus robur
Score  99.0 Score Type  egn
Protein Description  (M=1) PTHR10555:SF122 - SORTING NEXIN 1 (PTHR10555:SF122) Gene Prediction Quality  validated
Protein length 

Sequence

Length: 756  
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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.

19 Blast

Analysis Hit Start End Strand Length Note Hit Coverage Hit Length Hit Pident E Val Hit Description
blastp_kegg lcl|pmum:103319712 1 737 + 737 Gaps:56 98.58 703 76.19 0.0 dynactin subunit 1
blastp_kegg lcl|pper:PRUPE_ppa002294mg 1 735 + 735 Gaps:56 100.00 691 75.83 0.0 hypothetical protein
blastp_kegg lcl|pxb:103946715 1 739 + 739 Gaps:56 99.00 700 74.75 0.0 cingulin-like protein 1
blastp_kegg lcl|cic:CICLE_v10007589mg 2 729 + 728 Gaps:46 96.69 724 74.71 0.0 hypothetical protein
blastp_kegg lcl|pxb:103937927 1 739 + 739 Gaps:56 99.00 700 74.75 0.0 cingulin-like protein 1
blastp_kegg lcl|cit:102628153 2 729 + 728 Gaps:46 96.69 724 74.43 0.0 kinesin-like protein KIF20B-like
blastp_kegg lcl|mdm:103456215 1 739 + 739 Gaps:56 99.00 700 74.46 0.0 dynactin subunit 1-like
blastp_kegg lcl|tcc:TCM_036978 1 745 + 745 Gaps:45 99.44 714 71.41 0.0 Phox domain-containing protein isoform 1
blastp_kegg lcl|pop:POPTR_0018s01880g 1 745 + 745 Gaps:51 99.02 713 73.80 0.0 POPTRDRAFT_578225 phox domain-containing family protein
blastp_kegg lcl|fve:101307855 2 737 + 736 Gaps:51 98.44 706 73.24 0.0 uncharacterized protein LOC101307855
rpsblast_cdd gnl|CDD|132789 71 194 + 124 Gaps:14 100.00 138 68.84 2e-55 cd06879 PX_UP1_plant The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins. The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins 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. In addition to protein-lipid interaction the PX domain may also be involved in protein-protein interaction.
rpsblast_cdd gnl|CDD|132768 73 193 + 121 Gaps:16 99.06 106 39.05 6e-15 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 90 192 + 103 Gaps:1 93.58 109 32.35 9e-15 pfam00787 PX PX domain. PX domains bind to phosphoinositides.
rpsblast_cdd gnl|CDD|197645 92 192 + 101 Gaps:7 97.14 105 33.33 2e-12 smart00312 PX PhoX homologous domain present in p47phox and p40phox. Eukaryotic domain of unknown function present in phox proteins PLD isoforms a PI3K isoform.
rpsblast_cdd gnl|CDD|132795 124 191 + 68 Gaps:1 64.42 104 44.78 2e-08 cd06885 PX_SNX17_31 The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31. The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17) SNX31 and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1 ezrin radixin and moesin) domain and a unique C-terminal region. 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. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. 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. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR VLDLR ApoER2 and others regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.
rpsblast_cdd gnl|CDD|31389 430 619 + 190 Gaps:10 16.51 1163 24.48 4e-08 COG1196 Smc Chromosome segregation ATPases [Cell division and chromosome partitioning].
rpsblast_cdd gnl|CDD|162739 469 728 + 260 Gaps:20 22.73 1179 23.88 6e-08 TIGR02168 SMC_prok_B chromosome segregation protein SMC common bacterial type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria archaea and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle.
rpsblast_kog gnl|CDD|35383 426 727 + 302 Gaps:40 18.65 1930 26.94 3e-07 KOG0161 KOG0161 KOG0161 Myosin class II heavy chain [Cytoskeleton].
rpsblast_kog gnl|CDD|36198 436 717 + 282 Gaps:30 28.37 980 19.42 7e-07 KOG0980 KOG0980 KOG0980 Actin-binding protein SLA2/Huntingtin-interacting protein Hip1 [Cytoskeleton].

14 Domain Motifs

Analysis Begin End Length Domain Identifier Cross Ref Description Inter Pro
PANTHER 539 734 196 PTHR10555:SF122 none none none
Coils 506 527 22 Coil none none none
PANTHER 1 28 28 PTHR10555 none none none
Pfam 102 193 92 PF00787 none PX domain IPR001683
SMART 85 194 110 SM00312 none PhoX homologous domain, present in p47phox and p40phox. IPR001683
ProSiteProfiles 81 198 118 PS50195 none PX domain profile. IPR001683
SUPERFAMILY 64 194 131 SSF64268 none none IPR001683
Gene3D 103 194 92 G3DSA:3.30.1520.10 none none IPR001683
Coils 541 608 68 Coil none none none
Coils 463 491 29 Coil none none none
PANTHER 54 229 176 PTHR10555 none none none
PANTHER 539 734 196 PTHR10555 none none none
PANTHER 54 229 176 PTHR10555:SF122 none none none
PANTHER 1 28 28 PTHR10555:SF122 none none none

0 Localization

19 Qtllist

Qtl Name Chromosome Name Linkage Group Prox Marker Dist Marker Position QTL Pos One Pos Two Test Type Test Value R 2
Bourran1_2003_QTL2_peak_Bud_burst_A4 Qrob_Chr02 2 s_1B0H8U_259 s_1CB1VL_554 17 0 87 lod 3,3 8,7
Bourran2_2004_QTL9_peak_Bud_burst_3P Qrob_Chr02 2 s_1C34E9_788 v_12238_322 50 25 75 lod 4,4 10,1
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL2_d13Cf Qrob_Chr02 2 s_1AQA4Z_1644 s_1AK5QX_947 53.67 14,01 79,68 lod 5.6594 0.03
Bourran1_2004_QTL2_peak_Bud_burst_3P Qrob_Chr02 2 s_1AW12F_382 s_1A77MR_223 42 6 64 lod 3,6 9,6
Bourran2_2002_QTL7_peak_Bud_burst_3P Qrob_Chr02 2 s_1ANG6_1446 v_11270_161 40 29 52 lod 8,1 16
Bourran2_2002_QTL9_peak_Bud_burst_A4 Qrob_Chr02 2 s_1BFNDA_375 s_1A3VA1_2139 32,5 17 62 lod 3,1 4,2
Bourran2_2003_QTL8_peak_Bud_burst_3P Qrob_Chr02 2 s_1ANG6_1446 v_11270_161 40 0 72 lod 4,4 9,9
Bourran2_2014_nP_A4 Qrob_Chr11 11 s_1B58GB_1413 s_1A5BYY_1671 11,15 0 42,38 lod 1,8913 4,5
Bourran2_2015_nP_A4 Qrob_Chr02 2 s_1A0FUE_1868 s_1A1UAI_500 20,64 20,47 21,36 lod 5.8 10.9
Bourran2_2015_nPriLBD_A4 Qrob_Chr02 2 s_1CP5DI_1183 s_1A63ZX_1277 24,87 24,63 26,18 lod 3.8 7
NancyGreenhouseCO2_2001_ambient_elevated_leaf_cellulose_QTL6_d13Cf Qrob_Chr02 2 s_1AEP21_172 v_6048_204 46.33 22,5 65,23 lod 4.972 0.03
Bourran2_2015_nEpis_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 34,94 34,88 37,45 lod 3.1 7
Bourran2_2015_nSecLBD_A4 Qrob_Chr09 9 v_15847_485 v_8329_369 35,81 34,88 37,45 lod 4.4 10.4
Bourran1_2003_QTL1_peak_Bud_burst_3P Qrob_Chr02 2 s_1AR8KI_1183 s_1B0QB1_473 22 6 41 lod 4,2 11,5
Bourran1_2004_QTL3_peak_Bud_burst_A4 Qrob_Chr02 2 s_1B0H8U_259 s_1CB1VL_554 17 0 46 lod 2,9 6,4
Bourran2_2015_nEpiBC_A4 Qrob_Chr07 7 s_1DP9TW_798 v_8128_173 22,61 22,14 22,73 lod 3.1 8.5
Champenoux_2015_nEpis_A4 Qrob_Chr02 2 s_1BAGIZ_823 s_1BN4CB_644 23,06 23,06 23,06 lod 4.9 11
Champenoux_2015_nP_A4 Qrob_Chr02 2 s_1BN4CB_644 v_508_128 23,76 23,06 24,51 lod 2.8 6.2
Champenoux_2015_nPriLBD_A4 Qrob_Chr02 2 s_1CP5DI_1183 s_1A63ZX_1277 25,35 24,63 26,18 lod 4.0 8.7

0 Targeting