SitesBLAST
Comparing BPHYT_RS17540 BPHYT_RS17540 amino acid:proton symporter to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
25% identity, 83% coverage: 3:445/531 of query aligns to 19:451/456 of 5oqtA
- binding alanine: I38 (≠ S21), G40 (≠ I23), T41 (≠ G24), G42 (≠ S25), F226 (= F212), A227 (= A213), I229 (≠ N215)
- binding : E24 (≠ N8), G26 (= G10), F28 (= F12), D29 (≠ A13), M32 (= M15), A176 (= A156), R177 (= R157), A184 (≠ I164), A188 (≠ I174), L192 (≠ M178), Q294 (≠ L287), V297 (≠ L290)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
25% identity, 83% coverage: 3:445/531 of query aligns to 21:453/458 of 6f34A
- binding arginine: I40 (≠ S21), G42 (≠ I23), T43 (≠ G24), G44 (≠ S25), E115 (≠ N93), Y116 (≠ W94), A119 (≠ I97), F228 (= F212), A229 (= A213), I231 (≠ N215), V314 (≠ T305)
- binding cholesterol: W201 (vs. gap), Y202 (vs. gap)
- binding : G28 (= G10), F30 (= F12), D31 (≠ A13), M34 (= M15), A178 (= A156), R179 (= R157), A186 (≠ I164), I187 (≠ F165), A190 (≠ I174), L194 (≠ M178), Q296 (≠ L287), V299 (≠ L290)
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
26% identity, 81% coverage: 19:447/531 of query aligns to 14:432/433 of 6f2wA
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)
25% identity, 73% coverage: 2:387/531 of query aligns to 25:431/629 of P30825
- N226 (≠ E189) modified: carbohydrate, N-linked (GlcNAc...) asparagine
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
26% identity, 74% coverage: 2:395/531 of query aligns to 5:388/469 of P46349
- G33 (= G30) mutation to D: Lack of activity.
- G42 (= G39) mutation to S: Lack of activity.
- G301 (≠ Y309) mutation to V: Lack of activity.
- G338 (≠ N347) mutation to E: Lack of activity.
- F341 (≠ V350) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
24% identity, 83% coverage: 2:442/531 of query aligns to 16:447/458 of P24207
- R26 (≠ F12) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P40) 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 (≠ M73) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y76) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ R78) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ S80) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ H81) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ L84) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F87) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W91) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ N93) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W94) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ I97) 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 (= E104) mutation E->G,L,V,N: Loss of activity.
- K168 (= K166) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ Q218) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (≠ V250) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P340) 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.
- P442 (= P437) mutation to A: 46% of wild-type phenylalanine transport activity.; mutation to G: 52% of wild-type phenylalanine transport activity.; mutation to L: 43% of wild-type phenylalanine transport activity.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
26% identity, 84% coverage: 2:446/531 of query aligns to 5:436/438 of O34739
- C94 (≠ S89) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (vs. gap) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ T173) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ T305) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ W422) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
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)
24% identity, 83% coverage: 4:445/531 of query aligns to 34:471/531 of Q9QXW9
- Y130 (≠ I101) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ E104) 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.
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)
24% identity, 83% coverage: 4:445/531 of query aligns to 35:472/535 of Q9UHI5
- I53 (= I22) binding
- Y93 (= Y60) 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 (≠ E104) 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 (≠ G127) modified: Interchain (with C-210 in SLC3A2)
- W174 (vs. gap) 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 (≠ N215) 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 (≠ F274) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (≠ S375) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (= Y376) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ S382) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (= R395) to C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
- V460 (≠ L436) to 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
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)
24% identity, 73% coverage: 3:392/531 of query aligns to 9:390/457 of P15993
- Y103 (≠ I97) 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%.
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
24% identity, 80% coverage: 19:445/531 of query aligns to 10:432/457 of 7b00A
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
24% identity, 80% coverage: 19:445/531 of query aligns to 10:432/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
24% identity, 80% coverage: 19:445/531 of query aligns to 10:432/458 of 7cmhB
P82251 b(0,+)-type amino acid transporter 1; b(0,+)AT1; Glycoprotein-associated amino acid transporter b0,+AT1; Solute carrier family 7 member 9 from Homo sapiens (Human) (see 11 papers)
23% identity, 75% coverage: 3:400/531 of query aligns to 24:410/487 of P82251
- V40 (≠ L19) to M: in CSNU; uncertain significance
- IIGSG 43:47 (= IIGSG 22:26) binding
- I44 (= I23) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ A31) to F: in CSNU; uncertain significance
- P52 (≠ W32) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ V47) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y76) to H: in CSNU; uncertain significance
- G105 (= G82) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W91) to R: in CSNU; uncertain significance
- I120 (= I97) to L: in CSNU; uncertain significance
- T123 (≠ A107) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ D126) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ S128) modified: Interchain (with C-114 in SLC3A1)
- V170 (= V152) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ I164) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (vs. gap) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ T203) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A204) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ T207) to D: in CSNU; decreased amino acid transport activity
- W230 (≠ F212) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ N215) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F217) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ S219) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S241) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ L243) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ G268) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ T308) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ T313) to E: in CSNU; uncertain significance
- V330 (≠ A319) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M320) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R322) to Q: in CSNU; decreased amino acid transport activity; dbSNP:rs769576205; to W: in CSNU; severe loss of amino acid transport activity; dbSNP:rs121908484
- A354 (= A343) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (= S369) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ T372) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ V373) mutation to A: Complete loss of amino acid transport activity.
- Y386 (= Y376) mutation to A: Loss of amino acid transport activity.
- K401 (≠ T391) to E: in CSNU; uncertain significance; dbSNP:rs760264924
Sites not aligning to the query:
- 426 L → P: in CSNU; uncertain significance
- 482 P → L: in CSNU; severe loss of amino acid transport activity; no effect on localization to the apical membrane; dbSNP:rs146815072; mutation P->A,G,S,V: No effect on amino acid transport activity.; mutation P->F,I,M,W: Decreased amino acid transport activity.
Q01650 Large neutral amino acids transporter small subunit 1; 4F2 light chain; 4F2 LC; 4F2LC; CD98 light chain; Integral membrane protein E16; E16; L-type amino acid transporter 1; hLAT1; Solute carrier family 7 member 5; y+ system cationic amino acid transporter from Homo sapiens (Human) (see 3 papers)
23% identity, 82% coverage: 4:441/531 of query aligns to 45:474/507 of Q01650
- Y117 (≠ V74) mutation to A: Strongly decreased leucine transport activity.
- C164 (≠ W115) modified: Interchain (with C-210 in SLC3A2)
- D223 (≠ E189) to V: in dbSNP:rs17853937
- N230 (≠ G197) to K: in dbSNP:rs1060250
- A246 (vs. gap) mutation to V: Nearly abolishes leucine transport activity.
- F252 (= F212) mutation to A: Nearly abolishes leucine transport activity.
- W257 (≠ F217) mutation to A: Nearly abolishes leucine transport activity.
- N258 (≠ Q218) mutation to A: Decreased leucine transport activity.; mutation to D: Nearly abolishes leucine transport activity.
- Y259 (≠ S219) mutation to A: Strongly decreased leucine transport activity.
- E303 (≠ S263) mutation to K: Decreased leucine transport activity.
- P375 (≠ Q342) mutation to L: Nearly abolishes leucine transport activity.
Sites not aligning to the query:
- 483:507 mutation Missing: Nearly abolishes leucine transport activity.
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
24% identity, 82% coverage: 4:441/531 of query aligns to 2:431/464 of 7dsqB
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
24% identity, 82% coverage: 4:441/531 of query aligns to 2:431/464 of 7dsnB
- binding (2~{S})-2-azanyl-7-[[2-(1,3-benzoxazol-2-yl)phenyl]methoxy]-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ S21), I20 (= I22), G22 (= G24), S23 (= S25), G24 (= G26), I97 (= I97), I104 (≠ M112), F209 (= F212), A210 (= A213), G212 (≠ N215), I354 (= I368), N361 (≠ S375)
- binding cholesterol hemisuccinate: F109 (≠ Y117), Y145 (≠ W150), K148 (= K153), V153 (≠ A158), Q326 (≠ F336)
Sites not aligning to the query:
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
24% identity, 82% coverage: 4:441/531 of query aligns to 2:431/464 of 7dslB
7dskB Overall structure of the lat1-4f2hc bound with jx-075 (see paper)
24% identity, 82% coverage: 4:441/531 of query aligns to 2:431/464 of 7dskB
- binding (2~{S})-2-azanyl-7-(naphthalen-1-ylmethoxy)-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ S21), I20 (= I22), S23 (= S25), G24 (= G26), I97 (= I97), S100 (= S108), S101 (≠ I109), F209 (= F212), G212 (≠ N215), Y216 (≠ S219), V353 (= V367), I354 (= I368), N361 (≠ S375)
- binding cholesterol hemisuccinate: K148 (= K153), A149 (≠ L154), V153 (≠ A158), F157 (≠ I162), H324 (= H334)
Sites not aligning to the query:
Q7YQK4 Large neutral amino acids transporter small subunit 1; 4F2 light chain; 4F2 LC; 4F2LC; L-type amino acid transporter 1; LAT1; Solute carrier family 7 member 5 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
23% identity, 82% coverage: 4:441/531 of query aligns to 41:470/503 of Q7YQK4
- C88 (≠ G49) mutation to S: No significant effect on inhibition by HgCl(2). Decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-183.
- C98 (≠ T59) mutation to S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Slightly less decreased KM and Vmax for Phe; when associated with S-183.
- C160 (≠ W115) mutation to S: No change to KM or Vmax for Phe.
- C172 (≠ A138) mutation to S: No change to KM or Vmax for Phe.
- C174 (≠ L140) mutation to S: No change to KM or Vmax for Phe.
- C183 (≠ Y149) mutation to S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-88. Slightly less decreased KM and Vmax for Phe; when associated with S-98.
- G219 (≠ E189) mutation to D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- W234 (= W198) mutation to L: Decreased KM and Vmax for Trp. Increased KM but decreased Vmax for Phe. Increased KM and Vmax for Phe; when associated with D-219.
- C331 (≠ A298) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ L348) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ T378) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (≠ S414) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
- C454 (≠ T425) mutation to S: No significant effect on inhibition by HgCl(2). Slightly increased KM but slightly decreased Vmax for Phe.
Sites not aligning to the query:
- 492 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe.
Query Sequence
>BPHYT_RS17540 BPHYT_RS17540 amino acid:proton symporter
MKSSIQRNIGPFALMLTGLGSIIGSGWLFGAWKAAKIAGPAAVCAWVIGAVVILAIALTY
AELGAMFPESGGMVRYARYSHGALVGFISAWANWIAIVSVIPIEAEASIQYMSTWPYPWA
HALFVDGSLTTNGLLLSAALVIIYFMLNYWGVKLFARANSAITIFKFLIPGATILGLMFA
GFHKENFGEASTFAPYGWSAVLTAVSTSGIVFAFNGFQSPINLAGEARNPAKSVPFAVIG
SILLALVIYVLLQIAYIGAVNPSDVMKGWSHFNFASPFAELAIALNLNWLAILLYVDAFV
SPSGTGTTYMATTSRMIYAMERNNTMPKMFGNVHPFYGVPRQAMWFNLLVSFIFLFFFRG
WSSLAAVISVATVISYLTGPISLMALRRAATDLERPLHIPGMKIIAPFAFVCASLILYWA
KWPLTGEIILLMVVALPVYFYFQAKSGFAGWGRDLKAAWWLVAYLPVMAILSLIGSKQFG
GHDLIPYGWDMVVVIAFSLVFYYWGVTSGYRSEYLDERSEHDEVLEGMGAH
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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