SitesBLAST
Comparing Ga0059261_1777 FitnessBrowser__Korea:Ga0059261_1777 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)
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
35% identity, 93% coverage: 29:452/458 of query aligns to 17:475/491 of P0AGF4
- F24 (= F36) mutation to A: Decreases xylose transport.
- G83 (= G87) mutation to A: Abolishes xylose transport.
- R133 (= R119) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E139) mutation to A: Abolishes xylose transport.
- R160 (= R146) mutation to A: Abolishes xylose transport.
- Q168 (= Q154) binding ; mutation to A: Abolishes xylose transport.
- Q288 (≠ N271) mutation to A: Abolishes xylose transport.
- QQ 288:289 (≠ NQ 271:272) binding
- Q289 (= Q272) mutation to A: Strongly decreases xylose transport.
- N294 (= N277) binding ; mutation to A: Abolishes xylose transport.
- Y298 (= Y281) mutation to A: Abolishes xylose transport.
- N325 (= N308) mutation to A: No effect on xylose transport.
- G340 (= G323) mutation to A: Abolishes xylose transport.
- R341 (= R324) mutation R->A,W: Abolishes xylose transport.
- W392 (= W376) binding ; mutation to A: Abolishes xylose transport.
- E397 (= E381) mutation to A: Abolishes xylose transport.
- R404 (= R388) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ H399) binding
- W416 (= W400) mutation to A: Strongly decreases xylose transport.
4gc0A The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to 6-bromo-6-deoxy-d-glucose (see paper)
35% identity, 93% coverage: 29:452/458 of query aligns to 13:471/475 of 4gc0A
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
35% identity, 93% coverage: 29:452/458 of query aligns to 13:471/475 of 4gbzA
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
35% identity, 93% coverage: 29:452/458 of query aligns to 13:471/475 of 4gbyA
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
32% identity, 90% coverage: 39:452/458 of query aligns to 22:434/446 of A0A0H2VG78
- D22 (= D39) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R119) mutation to A: Loss of transport activity.
- I105 (≠ G122) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E139) mutation to A: Loss of transport activity.
- Q137 (= Q154) mutation to A: Loss of transport activity.
- Q250 (≠ N271) mutation to A: Loss of transport activity.
- Q251 (= Q272) mutation to A: Loss of transport activity.
- N256 (= N277) mutation to A: Loss of transport activity.
- W357 (= W376) mutation to A: Loss of transport activity.
Q9LT15 Sugar transport protein 10; AtSTP10; D-glucose-H(+) symport protein STP10; D-glucose-proton symporter STP10; Hexose transporter 10 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 95% coverage: 19:451/458 of query aligns to 22:485/514 of Q9LT15
- F39 (= F36) mutation to A: Reduces affinity for glucose 8-fold.
- L43 (≠ T40) mutation to A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
- C77 (≠ F54) modified: Disulfide link with 449; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
- E162 (= E139) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q154) binding ; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (= I161) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (≠ N271) binding
- Q296 (= Q272) binding
- N301 (= N277) binding
- N332 (= N308) binding
- D344 (= D320) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W376) binding
- C449 (≠ A415) modified: Disulfide link with 77; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
7aaqA Sugar/h+ symporter stp10 in outward occluded conformation (see paper)
27% identity, 95% coverage: 19:451/458 of query aligns to 2:465/487 of 7aaqA
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 93% coverage: 29:452/458 of query aligns to 38:476/509 of Q8VZR6
Sites not aligning to the query:
- 479:509 mutation Missing: Leads to endoplasmic reticulum relocalization.
- 481:482 ER→AA: No effect on targeting.
- 500:509 mutation Missing: Leads to endoplasmic reticulum relocalization.
- 502:504 mutation LLE->AAA,SSS: Leads to plasma membrane relocalization.
7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
27% identity, 95% coverage: 15:451/458 of query aligns to 3:470/485 of 7aarA
- binding Octyl Glucose Neopentyl Glycol : L28 (≠ T40), I90 (≠ P82), H94 (≠ F86), V98 (≠ G90), F101 (≠ L93), N138 (≠ S130), P142 (= P134), N158 (≠ V150), F161 (≠ N153), Q162 (= Q154), I165 (= I157), D210 (≠ E204), G391 (= G372), P392 (≠ A373), W395 (= W376), M419 (≠ W400)
- binding beta-D-glucopyranose: Q280 (≠ N271), N286 (= N277), M289 (≠ L280), G391 (= G372), W395 (= W376)
P11169 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Homo sapiens (Human) (see paper)
29% identity, 95% coverage: 17:452/458 of query aligns to 5:462/496 of P11169
- Q159 (= Q154) binding
- QLS 277:279 (≠ AMF 268:270) Important for selectivity against fructose; mutation to HVA: Confers moderate fructose transport activity.
- QQ 280:281 (≠ NQ 271:272) binding
- N286 (= N277) binding
- N315 (= N308) binding
- E378 (≠ A368) binding
- W386 (= W376) binding
P11166 Solute carrier family 2, facilitated glucose transporter member 1; Glucose transporter type 1, erythrocyte/brain; GLUT-1; HepG2 glucose transporter from Homo sapiens (Human) (see 23 papers)
29% identity, 96% coverage: 16:454/458 of query aligns to 6:466/492 of P11166
- N34 (≠ S44) to S: in GLUT1DS1; 55% of wild-type glucose uptake activity; dbSNP:rs80359812
- N45 (≠ G55) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to T: Loss of glycosylation site.
- R51 (vs. gap) to H: in EIG12; uncertain significance; dbSNP:rs201815571
- T60 (vs. gap) to M: in EIG12; uncertain significance; decreased glucose transport; dbSNP:rs142986731
- M77 (≠ V73) to T: in EIG12; decreased glucose transport; dbSNP:rs1187210267
- G91 (= G87) to D: in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose; dbSNP:rs80359814
- R126 (= R119) to C: in GLUT1DS1, GLUT1DS2 and DYT9; reduced transporter activity; dbSNP:rs80359818; to H: in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose and dehydroascorbic acid; 57% of wild-type glucose uptake activity; dbSNP:rs80359816
- G130 (= G123) to S: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359819
- T137 (≠ S130) binding
- P149 (= P142) to A: in EIG12; uncertain significance
- R153 (= R146) to C: in GLUT1DS1; 44% of wild-type glucose uptake activity
- L169 (= L162) natural variant: Missing (in GLUT1DS1; 48% of wild-type glucose uptake activity; dbSNP:rs80359832)
- I192 (= I187) mutation to C: Strongly decreases glucose transport.
- L204 (≠ T199) mutation to C: Abolishes glucose transport.
- P205 (≠ L200) mutation to C: Abolishes glucose transport.
- R212 (= R207) to C: in GLUT1DS1 and DYT9; dbSNP:rs387907312
- R218 (vs. gap) to S: in EIG12; decreased glucose transport
- R223 (= R217) to P: in EIG12; mild phenotype; reduced transporter activity; impaired phosphorylation by PKC; dbSNP:rs397514564; to Q: in EIG12; uncertain significance; no effect on glucose transport; impaired phosphorylation by PKC; dbSNP:rs397514564; to W: in GLUT1DS1; impaired phosphorylation by PKC; dbSNP:rs796053248
- S226 (≠ D220) modified: Phosphoserine; by PKC/PRKCB; mutation to A: Abolishes phosphorylation by PKA, leading to impaired response to TPA.
- R232 (vs. gap) to C: in EIG12; the mutant protein is expressed at the cell surface but has mildly decreased glucose uptake (70%) compared to wild-type; dbSNP:rs387907313
- E243 (≠ R236) to V: in EIG12; decreased glucose transport
- A275 (= A264) to T: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909740
- Q282 (≠ N271) binding
- QQLS 282:285 (≠ NQLS 271:274) natural variant: Missing (in GLUT1DS2; accompanied by hemolytic anemia and altered erythrocyte ion concentrations; the mutation decreases glucose transport and causes a cation leak that alteres intracellular concentrations of sodium potassium and calcium)
- G286 (= G275) to D: in SDCHCN; no effect on protein abundance; no effect on localization to the plasma membrane; loss of D-glucose transporter activity; increased cation leakage; dbSNP:rs864309514
- T295 (≠ P284) to M: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359823
- V303 (≠ A294) to L: found in a patient with GLUT1 deficiency syndrome; dbSNP:rs1205631854
- G314 (= G305) to S: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909739
- S324 (≠ A315) to L: in GLUT1DS2; mild phenotype; reduced transporter activity; dbSNP:rs796053253
- E329 (≠ D320) to Q: in GLUT1DS1; stabilizes the inward-open conformation
- R333 (= R324) to Q: in GLUT1DS1 and GLUT1DS2; dbSNP:rs1553155986; to W: in GLUT1DS1; 43% of wild-type glucose uptake activity; dbSNP:rs80359825
- G340 (= G331) mutation to C: Strongly decreases glucose transport.
- W388 (= W376) binding
- N411 (≠ H399) Not glycosylated; binding ; to S: in EIG12; decreased glucose transport; dbSNP:rs398123069
- I435 (≠ A423) natural variant: Missing (in SDCHCN; no effect on protein abundance; no effect on localization to the plasma membrane; loss of D-glucose transporter activity; increased cation leakage)
- R458 (≠ I446) to W: in EIG12; decreased glucose transport; dbSNP:rs13306758
Sites not aligning to the query:
- 485 P → L: in GLUT1DS1; creates a dileucine internalization motif that promotes recruitment of clathrin and mislocalization of the protein to endocytic compartments
4zw9A Crystal structure of human glut3 bound to d-glucose in the outward- occluded conformation at 1.5 angstrom (see paper)
29% identity, 95% coverage: 17:452/458 of query aligns to 5:462/470 of 4zw9A
- binding beta-D-glucopyranose: Q159 (= Q154), I166 (= I161), Q280 (≠ N271), Q281 (= Q272), N286 (= N277), F377 (= F367), W386 (= W376)
- binding alpha-D-glucopyranose: Q159 (= Q154), I162 (= I157), I166 (= I161), Q280 (≠ N271), Q281 (= Q272), N286 (= N277), W386 (= W376)
7spsA Crystal structure of human glucose transporter glut3 bound with exofacial inhibitor sa47 (see paper)
29% identity, 95% coverage: 17:452/458 of query aligns to 2:459/468 of 7spsA
- binding methyl N-[(2-{4-[4-(5-fluoro-2-methoxyphenyl)piperazin-1-yl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}phenyl)methyl]-beta-alaninate: F21 (= F36), T25 (= T40), N29 (≠ S44), Q156 (= Q154), I163 (= I161), Q278 (= Q272), F286 (≠ L280), A308 (≠ V304), N312 (= N308), F374 (= F367), E375 (≠ A368), N406 (≠ H399), W407 (= W400), N410 (≠ A403)
7crzA Crystal structure of human glucose transporter glut3 bound with c3361 (see paper)
29% identity, 95% coverage: 17:452/458 of query aligns to 3:460/469 of 7crzA
- binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: T26 (= T40), A66 (= A66), S69 (≠ L69), Q157 (= Q154), I164 (= I161), Q278 (≠ N271), Q279 (= Q272), N284 (= N277), N313 (= N308), F375 (= F367), W384 (= W376), N411 (≠ A403), F412 (≠ A404), G415 (≠ T407)
5c65A Structure of the human glucose transporter glut3 / slc2a3
30% identity, 95% coverage: 17:452/458 of query aligns to 1:450/457 of 5c65A
- binding Octyl Glucose Neopentyl Glycol : L42 (= L56), L58 (≠ M60), F75 (≠ L77), S76 (≠ I78), L79 (≠ A81), R87 (≠ K89), L95 (≠ I97), L96 (≠ A98), L121 (≠ F120), P199 (≠ L200)
- binding cholesterol hemisuccinate: I270 (= I265), S396 (≠ T398), T399 (≠ V401)
7sptA Crystal structure of exofacial state human glucose transporter glut3 (see paper)
29% identity, 95% coverage: 17:452/458 of query aligns to 5:462/470 of 7sptA
P17809 Solute carrier family 2, facilitated glucose transporter member 1; Glucose transporter type 1, erythrocyte/brain; GLUT-1; GT1 from Mus musculus (Mouse) (see 3 papers)
28% identity, 96% coverage: 16:454/458 of query aligns to 6:466/492 of P17809
- N45 (≠ G55) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Sites not aligning to the query:
- 485 P→L: Lethality immediately after birth in knockin mice; caused by creation of a dileucine internalization motif that promotes mislocalization of the protein.
P32037 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Mus musculus (Mouse) (see paper)
28% identity, 95% coverage: 16:451/458 of query aligns to 4:461/493 of P32037
- N43 (≠ Q53) modified: carbohydrate, N-linked (GlcNAc...) asparagine
5eqiA Human glut1 in complex with cytochalasin b (see paper)
29% identity, 92% coverage: 22:443/458 of query aligns to 4:447/447 of 5eqiA
5eqhA Human glut1 in complex with inhibitor (2~{s})-3-(2-bromophenyl)-2-[2- (4-methoxyphenyl)ethanoylamino]-~{n}-[(1~{s})-1- phenylethyl]propanamide (see paper)
29% identity, 92% coverage: 22:443/458 of query aligns to 4:447/447 of 5eqhA
Query Sequence
>Ga0059261_1777 FitnessBrowser__Korea:Ga0059261_1777
MHSVSASFAGAPDEEARATVAIILSAAGAALGGLLFGFDTAVISGATQALQLQFGLTDAM
LGFTVASALIGTVLGSLIAGAPADRFGRKGVMLTVAIAYVVSSLGTGLAPDLNAFLVFRF
MGGLAIGAASVVTPIYIAEVSPARFRGRLVAMNQLNIVLGILIAFLSNYIIAGLVQYDVA
WRWMFGIVAVPSTIFLLVTLLLPESPRWLAIHGQADRARDVMQRLGFADPRAELARIELA
EAREEAAGKPRLFQRSHFTPVACAIAIAMFNQLSGINALLYYAPRIFELAGAGADSALLQ
SIAVGGTNLVFTVAALFLIDRFGRRPLLFVGSVICAATLLLVGWQLESAKPDGTLILFGL
LGFIAAFAMSQGAVIWVFISEVFPSAVRGKGQALGSTTHWVMAAAITWAFPVFAASVGGW
VFAFFGAMMLLQLLWTWKFMPETNGIALEDMNLGSARA
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