SitesBLAST
Comparing 16753 b2663 gamma-aminobutyrate transporter (NCBI) to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
49% identity, 97% coverage: 1:454/466 of query aligns to 1:451/469 of P46349
- G33 (= G35) mutation to D: Lack of activity.
- G42 (= G44) mutation to S: Lack of activity.
- G301 (≠ A304) mutation to V: Lack of activity.
- G338 (≠ S341) mutation to E: Lack of activity.
- F341 (≠ A344) mutation to S: Lack of activity.
- G414 (≠ F416) mutation to R: Lack of activity.
P15993 Aromatic amino acid transport protein AroP; Aromatic amino acid:H(+) symporter AroP; General aromatic amino acid permease; General aromatic transport system from Escherichia coli (strain K12) (see paper)
37% identity, 92% coverage: 1:431/466 of query aligns to 2:430/457 of P15993
- Y103 (≠ W102) Key residue for tryptophan transport; mutation to F: Decreases tryptophan transport to less than 50% of wild-type levels and reduces the ability of tryptophan to inhibit phenylalanine transport from 95 to 62%.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
37% identity, 92% coverage: 4:432/466 of query aligns to 13:439/458 of P24207
- R26 (= R17) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P45) mutation to A: 50% of wild-type phenylalanine transport activity.; mutation to G: No change in phenylalanine transport activity.; mutation to L: 26% of wild-type phenylalanine transport activity.
- F87 (= F78) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y81) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ D83) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ A85) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ I86) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ W89) mutation to L: No effect on phenylalanine transport activity.
- F101 (≠ Y92) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W96) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y98) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W99) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ W102) mutation to L: 60% of wild-type phenylalanine transport activity.; mutation to Y: Enables the transport of tryptophan to almost the same steady-state level as that of phenylalanine.
- E118 (= E109) mutation E->G,L,V,N: Loss of activity.
- K168 (= K159) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E218) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R244) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P334) mutation to A: 5% of wild-type phenylalanine transport activity.; mutation P->G,Q,K,R: Loss of activity.; mutation to S: 3% of wild-type phenylalanine transport activity.; mutation to T: 17% of wild-type phenylalanine transport activity.
Sites not aligning to the query:
- 442 P→A: 46% of wild-type phenylalanine transport activity.; P→G: 52% of wild-type phenylalanine transport activity.; P→L: 43% of wild-type phenylalanine transport activity.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
34% identity, 82% coverage: 14:397/466 of query aligns to 17:408/489 of P25737
- Y102 (= Y98) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (= W102) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K159) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F212) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E218) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E226) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (vs. gap) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-278.
- D278 (vs. gap) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 90% coverage: 6:423/466 of query aligns to 80:515/590 of P04817
- P113 (≠ A39) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P73) mutation to L: In CAN1-337; confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, 3-chloro-L-alanine, L-ethionine, L-allylglycine, and D-histidine, but not sensitivity to L-aspartic acid alpha-hydroxamate or p-fluoro-L-phenylalanine.
- V149 (≠ D74) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S77) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y98) mutation to D: In CAN1-306; confers citrulline transport activity in GAP1-deleted cells.; mutation to H: In CAN1-327; confers citrulline transport activity in GAP1-deleted cells.
- G308 (≠ A225) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P230) mutation to S: In CAN1-329; confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, 3-chloro-L-alanine, L-ethionine, L-allylglycine, and D-histidine, L-aspartic acid alpha-hydroxamate and p-fluoro-L-phenylalanine.
- TS 354:355 (≠ GS 271:272) mutation Missing: In CAN1-318; confers citrulline transport activity in GAP1-deleted cells.
- Y356 (= Y273) mutation to H: In CAN1-340; confers citrulline transport activity in GAP1-deleted cells.; mutation to N: In CAN1-339; confers citrulline transport activity in GAP1-deleted cells.
- W451 (≠ F362) mutation to C: In CAN1-328; confers citrulline transport activity in GAP1-deleted cells.; mutation to L: In CAN1-316; confers citrulline transport activity in GAP1-deleted cells.; mutation to S: In CAN1-335; confers citrulline transport activity in GAP1-deleted cells.
- F461 (≠ L372) mutation to S: In CAN1-307; confers citrulline transport activity in GAP1-deleted cells.
Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 88% coverage: 14:421/466 of query aligns to 84:502/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
31% identity, 85% coverage: 14:408/466 of query aligns to 90:497/602 of P19145
- A297 (≠ M215) mutation to V: Impairs basic amino-acids transport and regulation by these amino-acids.
Sites not aligning to the query:
- 76 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
P48813 High-affinity glutamine permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 85% coverage: 3:396/466 of query aligns to 138:544/663 of P48813
Sites not aligning to the query:
- 132 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Q03770 SPS-sensor component SSY1; Amino-acid permease homolog SSY1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
23% identity, 86% coverage: 3:405/466 of query aligns to 270:747/852 of Q03770
- T382 (≠ A114) mutation T->H,L: Constitutively active, up-regulates amino acid permease transcription in response to subthreshold concentrations of amino acids.; mutation to K: In SSY1-102; constitutively active, up-regulates amino acid permease transcription in the absence of amino-acids.; mutation to R: Constitutively active, up-regulates amino acid permease transcription in the absence of amino acids.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
26% identity, 71% coverage: 14:345/466 of query aligns to 27:359/458 of 6f34A
- binding arginine: I40 (≠ V27), G42 (= G29), T43 (≠ A30), G44 (≠ S31), E115 (vs. gap), Y116 (vs. gap), A119 (vs. gap), F228 (= F212), A229 (≠ S213), I231 (≠ M215), V314 (≠ C300)
- binding cholesterol: W201 (≠ V172), Y202 (≠ A173)
- binding : G28 (≠ K15), F30 (≠ R17), D31 (≠ H18), M34 (= M21), A178 (≠ G149), R179 (≠ E150), A186 (≠ L157), I187 (≠ C158), A190 (≠ I161), L194 (≠ A165), Q296 (≠ A285), V299 (≠ I288)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
26% identity, 71% coverage: 14:345/466 of query aligns to 25:357/456 of 5oqtA
- binding alanine: I38 (≠ V27), G40 (= G29), T41 (≠ A30), G42 (≠ S31), F226 (= F212), A227 (≠ S213), I229 (≠ M215)
- binding : G26 (≠ K15), F28 (≠ R17), D29 (≠ H18), M32 (= M21), A176 (≠ G149), R177 (≠ E150), A184 (≠ L157), A188 (≠ I161), L192 (≠ A165), Q294 (≠ A285), V297 (≠ I288)
Sites not aligning to the query:
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 88% coverage: 8:418/466 of query aligns to 2:404/438 of O34739
- C94 (≠ I94) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ T138) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ A165) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (= C300) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
Sites not aligning to the query:
- 415 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
23% identity, 72% coverage: 4:340/466 of query aligns to 10:346/461 of P76037
- Y110 (≠ W102) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
P30825 High affinity cationic amino acid transporter 1; CAT-1; CAT1; Ecotropic retroviral leukemia receptor homolog; Ecotropic retrovirus receptor homolog; Solute carrier family 7 member 1; System Y+ basic amino acid transporter from Homo sapiens (Human) (see paper)
22% identity, 82% coverage: 4:386/466 of query aligns to 22:431/629 of P30825
- N226 (≠ E182) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q9UHI5 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; hLAT2; Solute carrier family 7 member 8 from Homo sapiens (Human) (see 3 papers)
25% identity, 83% coverage: 2:386/466 of query aligns to 19:410/535 of Q9UHI5
- I53 (vs. gap) binding
- Y93 (≠ L65) mutation to A: Nearly complete reduction of glycine, L-alanine, and L-glutamine uptake. Minimal effect on the transport of L-isoleucine, L-histidine and L-tryptophan.
- N134 (≠ E109) Important for substrate specificity; binding ; mutation to Q: Reduces L-leucine uptake activity. Abolishes L-tryptophan uptake.; mutation to S: The substrate specificity changed dramatically reducing L-glutamine, glycine and L-alanine uptake activity thus mimicking the selectivity of SLC7A5.
- C154 (≠ W127) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ G139) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F212) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ M215) Important for substrate specificity; binding ; mutation to S: Strong decrease in the uptake of large substrates L-tryptophan, L-glutamine, and L-histidine but increases the uptake of small neutral amino acids glycine and L-alanine.
- V302 (= V270) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (≠ A371) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ L372) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ I378) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
Sites not aligning to the query:
- 418 R → C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
- 460 V → E: found in a patient with age-related hearing loss; strongly decreases L-alanine transport activity. Decreases L-tyrosine transport activity. Decreases cell membrane localization
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
25% identity, 78% coverage: 24:386/466 of query aligns to 10:370/457 of 7b00A
Sites not aligning to the query:
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
25% identity, 78% coverage: 24:386/466 of query aligns to 10:370/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
25% identity, 78% coverage: 24:386/466 of query aligns to 10:370/458 of 7cmhB
Q9QXW9 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; mLAT2; Solute carrier family 7 member 8 from Mus musculus (Mouse) (see paper)
25% identity, 81% coverage: 11:386/466 of query aligns to 30:409/531 of Q9QXW9
- Y130 (vs. gap) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ E109) mutation to S: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake. Increases the export of both L-leucine and L-phenylalanine.
- F242 (= F212) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
27% identity, 45% coverage: 27:236/466 of query aligns to 17:223/433 of 6f2wA
Query Sequence
>16753 b2663 gamma-aminobutyrate transporter (NCBI)
MGQSSQPHELGGGLKSRHVTMLSIAGVIGASLFVGSSVAIAEAGPAVLLAYLFAGLLVVM
IMRMLAEMAVATPDTGSFSTYADKAIGRWAGYTIGWLYWWFWVLVIPLEANIAAMILHSW
VPGIPIWLFSLVITLALTGSNLLSVKNYGEFEFWLALCKVIAILAFIFLGAVAISGFYPY
AEVSGISRLWDSGGFMPNGFGAVLSAMLITMFSFMGAEIVTIAAAESDTPEKHIVRATNS
VIWRISIFYLCSIFVVVALIPWNMPGLKAVGSYRSVLELLNIPHAKLIMDCVILLSVTSC
LNSALYTASRMLYSLSRRGDAPAVMGKINRSKTPYVAVLLSTGAAFLTVVVNYYAPAKVF
KFLIDSSGAIALLVYLVIAVSQLRMRKILRAEGSEIRLRMWLYPWLTWLVIGFITFVLVV
MLFRPAQQLEVISTGLLAIGIICTVPIMARWKKLVLWQKTPVHNTR
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory