SitesBLAST
Comparing Echvi_2810 FitnessBrowser__Cola:Echvi_2810 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)
32% identity, 98% coverage: 11:450/450 of query aligns to 16:485/491 of P0AGF4
- F24 (= F19) mutation to A: Decreases xylose transport.
- G83 (= G71) mutation to A: Abolishes xylose transport.
- R133 (= R103) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E123) mutation to A: Abolishes xylose transport.
- R160 (= R130) mutation to A: Abolishes xylose transport.
- Q168 (= Q138) binding ; mutation to A: Abolishes xylose transport.
- Q288 (≠ N252) mutation to A: Abolishes xylose transport.
- QQ 288:289 (≠ NQ 252:253) binding
- Q289 (= Q253) mutation to A: Strongly decreases xylose transport.
- N294 (= N258) binding ; mutation to A: Abolishes xylose transport.
- Y298 (= Y262) mutation to A: Abolishes xylose transport.
- N325 (= N289) mutation to A: No effect on xylose transport.
- G340 (= G304) mutation to A: Abolishes xylose transport.
- R341 (= R305) mutation R->A,W: Abolishes xylose transport.
- W392 (= W356) binding ; mutation to A: Abolishes xylose transport.
- E397 (= E361) mutation to A: Abolishes xylose transport.
- R404 (= R368) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ H379) binding
- W416 (= W380) 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)
32% identity, 94% coverage: 11:434/450 of query aligns to 12:472/475 of 4gc0A
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
32% identity, 94% coverage: 11:434/450 of query aligns to 12:472/475 of 4gbzA
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
32% identity, 94% coverage: 11:434/450 of query aligns to 12:472/475 of 4gbyA
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
33% identity, 93% coverage: 22:439/450 of query aligns to 22:440/446 of A0A0H2VG78
- D22 (= D22) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R103) mutation to A: Loss of transport activity.
- I105 (≠ G106) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E123) mutation to A: Loss of transport activity.
- Q137 (= Q138) mutation to A: Loss of transport activity.
- Q250 (≠ N252) mutation to A: Loss of transport activity.
- Q251 (= Q253) mutation to A: Loss of transport activity.
- N256 (= N258) mutation to A: Loss of transport activity.
- W357 (= W356) mutation to A: Loss of transport activity.
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 95% coverage: 16:441/450 of query aligns to 42:484/509 of Q8VZR6
- ER 481:482 (≠ QK 438:439) mutation to AA: No effect on targeting.
Sites not aligning to the query:
- 479:509 mutation Missing: Leads to endoplasmic reticulum relocalization.
- 500:509 mutation Missing: Leads to endoplasmic reticulum relocalization.
- 502:504 mutation LLE->AAA,SSS: Leads to plasma membrane relocalization.
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)
28% identity, 93% coverage: 19:438/450 of query aligns to 26:469/492 of P11166
- N34 (= N30) to S: in GLUT1DS1; 55% of wild-type glucose uptake activity; dbSNP:rs80359812
- N45 (≠ T39) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to T: Loss of glycosylation site.
- R51 (≠ G45) to H: in EIG12; uncertain significance; dbSNP:rs201815571
- T60 (vs. gap) to M: in EIG12; uncertain significance; decreased glucose transport; dbSNP:rs142986731
- M77 (≠ V57) to T: in EIG12; decreased glucose transport; dbSNP:rs1187210267
- G91 (= G71) to D: in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose; dbSNP:rs80359814
- R126 (= R103) 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 (= G107) to S: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359819
- T137 (≠ S114) binding
- P149 (≠ Q126) to A: in EIG12; uncertain significance
- R153 (= R130) to C: in GLUT1DS1; 44% of wild-type glucose uptake activity
- L169 (= L146) natural variant: Missing (in GLUT1DS1; 48% of wild-type glucose uptake activity; dbSNP:rs80359832)
- I192 (≠ A170) mutation to C: Strongly decreases glucose transport.
- L204 (≠ I182) mutation to C: Abolishes glucose transport.
- P205 (≠ L183) mutation to C: Abolishes glucose transport.
- R212 (= R190) to C: in GLUT1DS1 and DYT9; dbSNP:rs387907312
- R218 (≠ Q196) to S: in EIG12; decreased glucose transport
- R223 (≠ A201) 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 (≠ K204) modified: Phosphoserine; by PKC/PRKCB; mutation to A: Abolishes phosphorylation by PKA, leading to impaired response to TPA.
- R232 (≠ T210) 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 (≠ S220) to V: in EIG12; decreased glucose transport
- A275 (= A245) to T: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909740
- Q282 (≠ N252) binding
- QQLS 282:285 (≠ NQLS 252:255) 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 (= G256) 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 (≠ P265) to M: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359823
- V303 (≠ T275) to L: found in a patient with GLUT1 deficiency syndrome; dbSNP:rs1205631854
- G314 (= G286) to S: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909739
- S324 (≠ G296) to L: in GLUT1DS2; mild phenotype; reduced transporter activity; dbSNP:rs796053253
- E329 (≠ D301) to Q: in GLUT1DS1; stabilizes the inward-open conformation
- R333 (= R305) to Q: in GLUT1DS1 and GLUT1DS2; dbSNP:rs1553155986; to W: in GLUT1DS1; 43% of wild-type glucose uptake activity; dbSNP:rs80359825
- G340 (= G312) mutation to C: Strongly decreases glucose transport.
- W388 (= W356) binding
- N411 (≠ H379) Not glycosylated; binding ; to S: in EIG12; decreased glucose transport; dbSNP:rs398123069
- I435 (≠ M404) 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 (≠ L427) 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
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, 93% coverage: 19:438/450 of query aligns to 26:469/492 of P17809
- N45 (≠ T39) 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.
Q9C757 Probable inositol transporter 2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 72% coverage: 9:332/450 of query aligns to 32:367/580 of Q9C757
Sites not aligning to the query:
- 399 C→A: Strongly decreased nickel inhibition; when associated with A-402, A-410 and A-413.; C→S: No effect on inostol transport or nickel inhibition. No effect on inostol transport or nickel inhibition; when associated with S-410.
- 402 C→A: Strongly decreased nickel inhibition; when associated with A-399, A-410 and A-413.
- 410 C→A: Strongly decreased nickel inhibition; when associated with A-399, A-402 and A-413.; C→S: No effect on inostol transport or nickel inhibition; when associated with S-399.
- 413 C→A: Strongly decreased nickel inhibition; when associated with A-399, A-402 and A-410.
5eqiA Human glut1 in complex with cytochalasin b (see paper)
28% identity, 90% coverage: 19:424/450 of query aligns to 18:447/447 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)
28% identity, 90% coverage: 19:424/450 of query aligns to 18:447/447 of 5eqhA
5eqgA Human glut1 in complex with inhibitor (2~{s})-3-(4-fluorophenyl)-2-[2- (3-hydroxyphenyl)ethanoylamino]-~{n}-[(1~{s})-1- phenylethyl]propanamide (see paper)
28% identity, 90% coverage: 19:424/450 of query aligns to 18:447/447 of 5eqgA
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, 87% coverage: 57:447/450 of query aligns to 96:502/514 of Q9LT15
- E162 (= E123) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q138) binding ; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (= I145) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (≠ N252) binding
- Q296 (= Q253) binding
- N301 (= N258) binding
- N332 (= N289) binding
- D344 (= D301) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W356) binding
- C449 (≠ T396) modified: Disulfide link with 77; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
Sites not aligning to the query:
- 39 F→A: Reduces affinity for glucose 8-fold.
- 43 L→A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
- 77 modified: Disulfide link with 449; C→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, 87% coverage: 57:447/450 of query aligns to 76:482/487 of 7aaqA
7spsA Crystal structure of human glucose transporter glut3 bound with exofacial inhibitor sa47 (see paper)
27% identity, 94% coverage: 11:432/450 of query aligns to 13:458/468 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 (= F19), T25 (= T23), N29 (≠ S27), Q156 (= Q138), I163 (= I145), Q278 (= Q253), F286 (≠ L261), A308 (≠ I285), N312 (= N289), F374 (≠ H347), E375 (≠ G348), N406 (≠ H379), W407 (= W380), N410 (≠ A383)
7crzA Crystal structure of human glucose transporter glut3 bound with c3361 (see paper)
27% identity, 94% coverage: 11:432/450 of query aligns to 14:459/469 of 7crzA
- binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: T26 (= T23), A66 (≠ F47), S69 (= S50), Q157 (= Q138), I164 (= I145), Q278 (≠ N252), Q279 (= Q253), N284 (= N258), N313 (= N289), F375 (≠ H347), W384 (= W356), N411 (≠ A383), F412 (≠ A384), G415 (≠ T387)
4zw9A Crystal structure of human glut3 bound to d-glucose in the outward- occluded conformation at 1.5 angstrom (see paper)
27% identity, 94% coverage: 11:432/450 of query aligns to 16:461/470 of 4zw9A
- binding beta-D-glucopyranose: Q159 (= Q138), I166 (= I145), Q280 (≠ N252), Q281 (= Q253), N286 (= N258), F377 (≠ H347), W386 (= W356)
- binding alpha-D-glucopyranose: Q159 (= Q138), I162 (= I141), I166 (= I145), Q280 (≠ N252), Q281 (= Q253), N286 (= N258), W386 (= W356)
P11169 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Homo sapiens (Human) (see paper)
27% identity, 94% coverage: 11:432/450 of query aligns to 16:461/496 of P11169
- Q159 (= Q138) binding
- QLS 277:279 (≠ AIF 249:251) Important for selectivity against fructose; mutation to HVA: Confers moderate fructose transport activity.
- QQ 280:281 (≠ NQ 252:253) binding
- N286 (= N258) binding
- N315 (= N289) binding
- E378 (≠ G348) binding
- W386 (= W356) binding
5c65A Structure of the human glucose transporter glut3 / slc2a3
28% identity, 94% coverage: 11:432/450 of query aligns to 12:449/457 of 5c65A
- binding Octyl Glucose Neopentyl Glycol : L42 (vs. gap), L58 (≠ D41), F75 (≠ L61), S76 (≠ L62), L79 (≠ I65), R87 (≠ K73), L95 (≠ V81), L96 (≠ M82), L121 (≠ F104), P199 (≠ L183)
- binding cholesterol hemisuccinate: I270 (≠ G246), S396 (≠ V378), T399 (≠ G381)
7sptA Crystal structure of exofacial state human glucose transporter glut3 (see paper)
27% identity, 94% coverage: 11:432/450 of query aligns to 16:461/470 of 7sptA
Query Sequence
>Echvi_2810 FitnessBrowser__Cola:Echvi_2810
MKNLTTYYAFIVSLTGFLFGFDTAVISGANLPLKALWQTSDWFHGFFIMSVALWGTVIGA
LLGGIPCHHLGRKNTLFWIGVMFLVSALGTALATDPFVFSFYRFVGGVAIGASSIAAPTY
VSEISQAYQRGRRVGLYQINIVSGILVAYVSNYLLQGVGDHNDWRWMLAAEIIPAIIYLA
FILDIPESPRWLILKQKDESAAQKVLKKITTGKIDQLLLSIKHDSLRSKKMKLFSAKNRL
PLFLAGIIAIFNQLSGINFILYYAPEIMEKAGFVTTTSLLGAVCIGFTNLIFTLIGMSLI
DKTGRKQLMLIGSMGYIISLGLVSYGFYDSSSPLFILTSILIFIAAHGIGQGAVIWVFIS
EIFPNKVRAMGQSFGAGVHWGGAAMITLFGAVLIDTLMPFQIFMVFMALMILQFVFVWRY
MPETKGLELENLHSKLAQKLYEKFPSDHKT
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