SitesBLAST
Comparing Ga0059261_1053 FitnessBrowser__Korea:Ga0059261_1053 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)
47% identity, 95% coverage: 5:489/512 of query aligns to 3:456/456 of 5oqtA
- binding alanine: I38 (≠ V38), G40 (= G40), T41 (= T41), G42 (= G42), F226 (= F227), A227 (= A228), I229 (≠ V230)
- binding : E24 (≠ S24), G26 (= G26), F28 (= F28), D29 (≠ Q29), M32 (= M32), A176 (= A177), R177 (≠ F178), A184 (≠ L185), A188 (≠ S189), L192 (= L193), Q294 (≠ W327), V297 (≠ I330)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
47% identity, 95% coverage: 5:489/512 of query aligns to 5:458/458 of 6f34A
- binding arginine: I40 (≠ V38), G42 (= G40), T43 (= T41), G44 (= G42), E115 (= E112), Y116 (= Y113), A119 (= A116), F228 (= F227), A229 (= A228), I231 (≠ V230), V314 (= V345)
- binding cholesterol: W201 (≠ P200), Y202 (≠ V201)
- binding : G28 (= G26), F30 (= F28), D31 (≠ Q29), M34 (= M32), A178 (= A177), R179 (≠ F178), A186 (≠ L185), I187 (≠ V186), A190 (≠ S189), L194 (= L193), Q296 (≠ W327), V299 (≠ I330)
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)
31% identity, 82% coverage: 5:426/512 of query aligns to 15:431/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
26% identity, 88% coverage: 35:485/512 of query aligns to 14:430/433 of 6f2wA
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
25% identity, 92% coverage: 17:486/512 of query aligns to 4:437/438 of O34739
- C94 (≠ V105) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ G163) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L193) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V345) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ V468) 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, 90% coverage: 20:479/512 of query aligns to 34:463/531 of Q9QXW9
- Y130 (= Y113) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ A116) 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 (= F227) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
Q9UPY5 Cystine/glutamate transporter; Amino acid transport system xc-; Calcium channel blocker resistance protein CCBR1; Solute carrier family 7 member 11; xCT from Homo sapiens (Human) (see 4 papers)
26% identity, 75% coverage: 57:442/512 of query aligns to 77:427/501 of Q9UPY5
- C86 (≠ A65) mutation to S: Does not affect L-cystine transport activity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- R135 (≠ A114) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ L138) modified: Interchain (with C-210 in SLC3A2); mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- Q191 (≠ L183) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ S189) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435.
- K198 (≠ A190) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ F227) binding
- F254 (≠ T237) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ I254) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C327 (≠ M350) mutation to A: Does not affect L-glutamate transport activity. Does not affect location at cell membrane Does not affect expression level.; mutation to L: Loss of L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Loss of inhibitio nof L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid. Decrease L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to T: Does not affect L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.
- F336 (vs. gap) mutation to A: Decreases L-cystine transport activity about 50%. Increases sensitivity to erastin-induced ferroptosis. Significantly decreases the L-cystine transport activity.; mutation to Y: Does not affect L-cystine transport activity.
- R396 (≠ L412) mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.; mutation to N: Loss of L-cystine transport activity.
- C414 (≠ D429) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
Sites not aligning to the query:
- 435 C→S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
26% identity, 76% coverage: 52:442/512 of query aligns to 27:383/455 of 7p9uB
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
26% identity, 76% coverage: 52:442/512 of query aligns to 27:383/453 of 7epzB
Sites not aligning to the query:
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)
23% identity, 90% coverage: 20:479/512 of query aligns to 35:464/535 of Q9UHI5
- I53 (≠ V38) binding
- Y93 (= Y76) 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 (≠ A116) 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 (≠ D139) modified: Interchain (with C-210 in SLC3A2)
- W174 (= W167) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F227) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ V230) 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 (≠ A286) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (= N408) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ F413) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ S419) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (= R434) to C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
- V460 (≠ L475) 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
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
23% identity, 79% coverage: 35:441/512 of query aligns to 10:385/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
23% identity, 79% coverage: 35:441/512 of query aligns to 10:385/458 of 7cmhB
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
23% identity, 79% coverage: 35:441/512 of query aligns to 10:385/457 of 7b00A
Sites not aligning to the query:
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
23% identity, 91% coverage: 7:474/512 of query aligns to 5:434/461 of P76037
- Y110 (= Y113) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
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, 83% coverage: 17:442/512 of query aligns to 22:413/487 of P82251
- V40 (≠ I35) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ VIGTG 38:42) binding
- I44 (= I39) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ L46) to F: in CSNU; uncertain significance
- P52 (≠ T47) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ V63) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y92) to H: in CSNU; uncertain significance
- G105 (= G98) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W107) to R: in CSNU; uncertain significance
- I120 (≠ E112) to L: in CSNU; uncertain significance
- T123 (≠ V115) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ F136) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ L138) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ L169) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ N180) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (≠ L193) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ A220) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A221) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ S224) to D: in CSNU; decreased amino acid transport activity
- W230 (≠ F227) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ V230) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F232) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A234) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S256) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ A258) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ P283) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ A341) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ Q353) to E: in CSNU; uncertain significance
- V330 (= V359) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M360) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R362) 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 (≠ I383) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ A414) mutation to A: Markedly reduces amino acid transport activity.
- A382 (= A417) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (vs. gap) mutation to A: Complete loss of amino acid transport activity.
- Y386 (vs. gap) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P430) 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.
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)
26% identity, 45% coverage: 227:455/512 of query aligns to 248:442/503 of Q7YQK4
- C331 (≠ L342) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ G388) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ A417) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (= C452) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
Sites not aligning to the query:
- 88 C→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.
- 98 C→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.
- 160 C→S: No change to KM or Vmax for Phe.
- 172 C→S: No change to KM or Vmax for Phe.
- 174 C→S: No change to KM or Vmax for Phe.
- 183 C→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.
- 219 G→D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- 234 W→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.
- 454 C→S: No significant effect on inhibition by HgCl(2). Slightly increased KM but slightly decreased Vmax for Phe.
- 492 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
23% identity, 80% coverage: 35:442/512 of query aligns to 11:384/458 of 6li9B
6irtB Human lat1-4f2hc complex bound with bch (see paper)
26% identity, 49% coverage: 203:455/512 of query aligns to 173:396/457 of 6irtB
Sites not aligning to the query:
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
26% identity, 49% coverage: 203:455/512 of query aligns to 180:403/464 of 7dsqB
Sites not aligning to the query:
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
26% identity, 49% coverage: 203:455/512 of query aligns to 180:403/464 of 7dsnB
Sites not aligning to the query:
- binding (2~{S})-2-azanyl-7-[[2-(1,3-benzoxazol-2-yl)phenyl]methoxy]-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: 19, 20, 22, 23, 24, 97, 104
- binding cholesterol hemisuccinate: 109, 145, 148, 153, 457
Query Sequence
>Ga0059261_1053 FitnessBrowser__Korea:Ga0059261_1053
MIFGRVKPLDAILATAEKKSLHRSLGAFQLTMLGIGAVIGTGIFVLTAEAAQKAGPGMML
SFVIAGVVCAVAALCYAEMAAMVPVSGSAYTYSYAVMGELIAWMVGWALILEYAVAAGAV
SVGWSGYVVGLIENAFALDIPDALVRGPYDGGIINLPAMLIAGLVTWLLVIGTKESAFVN
SVLVLVKVSALSLFIILAIPVMNMQNFEPFSPLGFAGVSAAAASIFFAYVGFDAVSTAAE
ETKNPQRNMPIGLIGSLAICTIFYLLVAAGVIGSVGAQPILGPDGAALPPGSTELTKACV
ETAAATGKEAVVCSKEALAWTLREIGWPQIGNLIGLAAGLALPSVILMMMFGQTRIFFVM
SRDGLLPAVFSKVHPKFHTPHVITILTGVFVALFAAFFPVGKLADISNSGTLFAFAAVSI
AVLVLRRTDPDRKRPFRTPLIIITAPIAILGCAYLFYSLGHDTKMMFVGWAALGLLVYFG
YSRRKSHVGRGIVETPEHEAYQELDPPVPGTH
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