SitesBLAST
Comparing 17022 b2943 D-galactose transporter (NCBI) 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)
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
39% identity, 91% coverage: 32:451/464 of query aligns to 22:437/446 of A0A0H2VG78
- D22 (= D32) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R112) mutation to A: Loss of transport activity.
- I105 (≠ L115) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E132) mutation to A: Loss of transport activity.
- Q137 (= Q147) mutation to A: Loss of transport activity.
- Q250 (= Q262) mutation to A: Loss of transport activity.
- Q251 (= Q263) mutation to A: Loss of transport activity.
- N256 (= N268) mutation to A: Loss of transport activity.
- W357 (= W371) mutation to A: Loss of transport activity.
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 92% coverage: 22:449/464 of query aligns to 38:477/509 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.
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)
33% identity, 94% coverage: 13:449/464 of query aligns to 23:487/514 of Q9LT15
- F39 (= F29) mutation to A: Reduces affinity for glucose 8-fold.
- L43 (≠ I33) mutation to A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
- C77 (≠ V57) modified: Disulfide link with 449; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
- E162 (= E132) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q147) binding ; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (= I154) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (= Q262) binding
- Q296 (= Q263) binding
- N301 (= N268) binding
- N332 (= N300) binding
- D344 (= D312) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W371) binding
- C449 (≠ N410) 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)
33% identity, 94% coverage: 13:449/464 of query aligns to 3:467/487 of 7aaqA
7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
32% identity, 94% coverage: 13:449/464 of query aligns to 8:472/485 of 7aarA
- binding Octyl Glucose Neopentyl Glycol : L28 (≠ I33), I90 (≠ L75), H94 (≠ L79), V98 (≠ K83), F101 (≠ M86), N138 (≠ S123), P142 (= P127), N158 (≠ I143), F161 (≠ Y146), Q162 (= Q147), I165 (= I150), D210 (= D193), G391 (= G367), P392 (= P368), W395 (= W371), M419 (≠ W395)
- binding beta-D-glucopyranose: Q280 (= Q262), N286 (= N268), M289 (= M271), G391 (= G367), W395 (= W371)
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
32% identity, 95% coverage: 9:448/464 of query aligns to 4:475/491 of P0AGF4
- F24 (= F29) mutation to A: Decreases xylose transport.
- G83 (= G80) mutation to A: Abolishes xylose transport.
- R133 (= R112) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E132) mutation to A: Abolishes xylose transport.
- R160 (= R139) mutation to A: Abolishes xylose transport.
- Q168 (= Q147) binding ; mutation to A: Abolishes xylose transport.
- Q288 (= Q262) mutation to A: Abolishes xylose transport.
- QQ 288:289 (= QQ 262:263) binding
- Q289 (= Q263) mutation to A: Strongly decreases xylose transport.
- N294 (= N268) binding ; mutation to A: Abolishes xylose transport.
- Y298 (= Y272) mutation to A: Abolishes xylose transport.
- N325 (= N300) mutation to A: No effect on xylose transport.
- G340 (= G315) mutation to A: Abolishes xylose transport.
- R341 (= R316) mutation R->A,W: Abolishes xylose transport.
- W392 (= W371) binding ; mutation to A: Abolishes xylose transport.
- E397 (= E376) mutation to A: Abolishes xylose transport.
- R404 (= R383) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ N394) binding
- W416 (= W395) 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: 11:448/464 of query aligns to 2:471/475 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: 11:448/464 of query aligns to 2:471/475 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: 11:448/464 of query aligns to 2:471/475 of 4gbyA
Q9C757 Probable inositol transporter 2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
39% identity, 70% coverage: 20:346/464 of query aligns to 33:371/580 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.
O23492 Inositol transporter 4; Myo-inositol-proton symporter INT4; Protein INOSITOL TRANSPORTER 4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 71% coverage: 22:350/464 of query aligns to 34:377/582 of O23492
Sites not aligning to the query:
- 559:561 LLE→AAA: No effect on targeting.
- 559:582 mutation Missing: No effect on targeting.
- 564:565 FK→AA: No effect on targeting.
- 570:575 RRREKK→AAAAAA: No effect on targeting.
Q9JJZ1 Solute carrier family 2, facilitated glucose transporter member 8; Glucose transporter type 8; GLUT-8; Glucose transporter type X1 from Rattus norvegicus (Rat) (see paper)
33% identity, 98% coverage: 2:455/464 of query aligns to 16:478/478 of Q9JJZ1
Sites not aligning to the query:
- 12:13 Dileucine internalization motif; LL→AA: Changes subcellular location mainly to the plasma membrane, threreby increasing transport activity.
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)
30% identity, 93% coverage: 22:454/464 of query aligns to 19:470/492 of P17809
- N45 (≠ Q48) 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.
Q9JIF3 Solute carrier family 2, facilitated glucose transporter member 8; Glucose transporter type 8; GLUT-8; Glucose transporter type X1 from Mus musculus (Mouse) (see paper)
31% identity, 98% coverage: 2:455/464 of query aligns to 15:477/477 of Q9JIF3
Sites not aligning to the query:
- 12:13 Dileucine internalization motif; LL→AA: Abolishes interaction with AP2B1.
4zw9A Crystal structure of human glut3 bound to d-glucose in the outward- occluded conformation at 1.5 angstrom (see paper)
29% identity, 93% coverage: 17:449/464 of query aligns to 12:463/470 of 4zw9A
- binding beta-D-glucopyranose: Q159 (= Q147), I166 (= I154), Q280 (= Q262), Q281 (= Q263), N286 (= N268), F377 (= F362), W386 (= W371)
- binding alpha-D-glucopyranose: Q159 (= Q147), I162 (= I150), I166 (= I154), Q280 (= Q262), Q281 (= Q263), N286 (= N268), W386 (= W371)
7crzA Crystal structure of human glucose transporter glut3 bound with c3361 (see paper)
29% identity, 93% coverage: 17:449/464 of query aligns to 10:461/469 of 7crzA
- binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: T26 (≠ I33), A66 (≠ M61), S69 (vs. gap), Q157 (= Q147), I164 (= I154), Q278 (= Q262), Q279 (= Q263), N284 (= N268), N313 (= N300), F375 (= F362), W384 (= W371), N411 (= N398), F412 (≠ M399), G415 (= G402)
7spsA Crystal structure of human glucose transporter glut3 bound with exofacial inhibitor sa47 (see paper)
29% identity, 93% coverage: 17:449/464 of query aligns to 9:460/468 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 (= F29), T25 (≠ I33), N29 (≠ G38), Q156 (= Q147), I163 (= I154), Q278 (= Q263), F286 (≠ M271), A308 (≠ V296), N312 (= N300), F374 (= F362), E375 (≠ A363), N406 (= N394), W407 (= W395), N410 (= N398)
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, 93% coverage: 22:454/464 of query aligns to 19:470/492 of P11166
- N34 (≠ A37) to S: in GLUT1DS1; 55% of wild-type glucose uptake activity; dbSNP:rs80359812
- N45 (≠ Q48) 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 (≠ S51) to M: in EIG12; uncertain significance; decreased glucose transport; dbSNP:rs142986731
- M77 (≠ A66) to T: in EIG12; decreased glucose transport; dbSNP:rs1187210267
- G91 (= G80) to D: in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose; dbSNP:rs80359814
- R126 (= R112) 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 (= G116) to S: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359819
- T137 (≠ S123) binding
- P149 (= P135) to A: in EIG12; uncertain significance
- R153 (= R139) to C: in GLUT1DS1; 44% of wild-type glucose uptake activity
- L169 (= L155) natural variant: Missing (in GLUT1DS1; 48% of wild-type glucose uptake activity; dbSNP:rs80359832)
- I192 (≠ V176) mutation to C: Strongly decreases glucose transport.
- L204 (≠ V188) mutation to C: Abolishes glucose transport.
- P205 (≠ F189) mutation to C: Abolishes glucose transport.
- R212 (= R196) to C: in GLUT1DS1 and DYT9; dbSNP:rs387907312
- R218 (= R202) to S: in EIG12; decreased glucose transport
- R223 (vs. gap) 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 (≠ R209) modified: Phosphoserine; by PKC/PRKCB; mutation to A: Abolishes phosphorylation by PKA, leading to impaired response to TPA.
- R232 (= R215) 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 (= E227) to V: in EIG12; decreased glucose transport
- A275 (≠ G255) to T: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909740
- Q282 (= Q262) binding
- QQLS 282:285 (≠ QQFT 262:265) 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 (= G266) 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 (≠ P275) to M: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359823
- V303 (≠ T286) to L: found in a patient with GLUT1 deficiency syndrome; dbSNP:rs1205631854
- G314 (= G297) to S: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909739
- S324 (≠ A307) to L: in GLUT1DS2; mild phenotype; reduced transporter activity; dbSNP:rs796053253
- E329 (≠ D312) to Q: in GLUT1DS1; stabilizes the inward-open conformation
- R333 (= R316) to Q: in GLUT1DS1 and GLUT1DS2; dbSNP:rs1553155986; to W: in GLUT1DS1; 43% of wild-type glucose uptake activity; dbSNP:rs80359825
- G340 (= G323) mutation to C: Strongly decreases glucose transport.
- W388 (= W371) binding
- N411 (= N394) Not glycosylated; binding ; to S: in EIG12; decreased glucose transport; dbSNP:rs398123069
- I435 (≠ W419) 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 (≠ V442) 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
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, 93% coverage: 17:449/464 of query aligns to 12:463/496 of P11169
- Q159 (= Q147) binding
- QLS 277:279 (≠ QVM 259:261) Important for selectivity against fructose; mutation to HVA: Confers moderate fructose transport activity.
- QQ 280:281 (= QQ 262:263) binding
- N286 (= N268) binding
- N315 (= N300) binding
- E378 (≠ A363) binding
- W386 (= W371) binding
5c65A Structure of the human glucose transporter glut3 / slc2a3
29% identity, 93% coverage: 17:449/464 of query aligns to 8:451/457 of 5c65A
- binding Octyl Glucose Neopentyl Glycol : L42 (≠ S51), L58 (≠ E55), F75 (≠ V70), S76 (≠ G71), L79 (≠ W74), R87 (≠ K82), L95 (≠ I90), L96 (= L91), L121 (≠ V113), P199 (≠ F189)
- binding cholesterol hemisuccinate: I270 (≠ V256), S396 (≠ T393), T399 (≠ I396)
Query Sequence
>17022 b2943 D-galactose transporter (NCBI)
MPDAKKQGRSNKAMTFFVCFLAALAGLLFGLDIGVIAGALPFIADEFQITSHTQEWVVSS
MMFGAAVGAVGSGWLSFKLGRKKSLMIGAILFVAGSLFSAAAPNVEVLILSRVLLGLAVG
VASYTAPLYLSEIAPEKIRGSMISMYQLMITIGILGAYLSDTAFSYTGAWRWMLGVIIIP
AILLLIGVFFLPDSPRWFAAKRRFVDAERVLLRLRDTSAEAKRELDEIRESLQVKQSGWA
LFKENSNFRRAVFLGVLLQVMQQFTGMNVIMYYAPKIFELAGYTNTTEQMWGTVIVGLTN
VLATFIAIGLVDRWGRKPTLTLGFLVMAAGMGVLGTMMHIGIHSPSAQYFAIAMLLMFIV
GFAMSAGPLIWVLCSEIQPLKGRDFGITCSTATNWIANMIVGATFLTMLNTLGNANTFWV
YAALNVLFILLTLWLVPETKHVSLEHIERNLMKGRKLREIGAHD
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