SitesBLAST
Comparing 350322 FitnessBrowser__Btheta:350322 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)
48% identity, 99% coverage: 1:481/484 of query aligns to 1:479/491 of P0AGF4
- F24 (= F27) mutation to A: Decreases xylose transport.
- G83 (= G84) mutation to A: Abolishes xylose transport.
- R133 (= R128) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E148) mutation to A: Abolishes xylose transport.
- R160 (= R155) mutation to A: Abolishes xylose transport.
- Q168 (= Q163) binding ; mutation to A: Abolishes xylose transport.
- Q288 (= Q298) mutation to A: Abolishes xylose transport.
- QQ 288:289 (= QQ 298:299) binding
- Q289 (= Q299) mutation to A: Strongly decreases xylose transport.
- N294 (= N304) binding ; mutation to A: Abolishes xylose transport.
- Y298 (= Y308) mutation to A: Abolishes xylose transport.
- N325 (= N334) mutation to A: No effect on xylose transport.
- G340 (= G349) mutation to A: Abolishes xylose transport.
- R341 (= R350) mutation R->A,W: Abolishes xylose transport.
- W392 (= W401) binding ; mutation to A: Abolishes xylose transport.
- E397 (= E406) mutation to A: Abolishes xylose transport.
- R404 (= R413) mutation to A: Strongly decreases xylose transport.
- Q415 (= Q424) binding
- W416 (= W425) 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)
49% identity, 97% coverage: 12:481/484 of query aligns to 5:475/475 of 4gc0A
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
49% identity, 97% coverage: 12:481/484 of query aligns to 5:475/475 of 4gbzA
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
49% identity, 97% coverage: 12:481/484 of query aligns to 5:475/475 of 4gbyA
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
32% identity, 93% coverage: 30:477/484 of query aligns to 22:434/446 of A0A0H2VG78
- D22 (= D30) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R128) mutation to A: Loss of transport activity.
- I105 (≠ G131) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E148) mutation to A: Loss of transport activity.
- Q137 (= Q163) mutation to A: Loss of transport activity.
- Q250 (= Q298) mutation to A: Loss of transport activity.
- Q251 (= Q299) mutation to A: Loss of transport activity.
- N256 (= N304) mutation to A: Loss of transport activity.
- W357 (= W401) mutation to A: Loss of 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)
29% identity, 96% coverage: 20:482/484 of query aligns to 19:469/492 of P17809
- N45 (≠ L46) 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.
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: 20:482/484 of query aligns to 19:469/492 of P11166
- N34 (≠ S35) to S: in GLUT1DS1; 55% of wild-type glucose uptake activity; dbSNP:rs80359812
- N45 (≠ L46) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to T: Loss of glycosylation site.
- R51 (≠ Q52) to H: in EIG12; uncertain significance; dbSNP:rs201815571
- T60 (= T61) to M: in EIG12; uncertain significance; decreased glucose transport; dbSNP:rs142986731
- M77 (≠ V70) to T: in EIG12; decreased glucose transport; dbSNP:rs1187210267
- G91 (= G84) to D: in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose; dbSNP:rs80359814
- R126 (= R128) 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 (= G132) to S: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359819
- T137 (≠ S139) binding
- P149 (= P151) to A: in EIG12; uncertain significance
- R153 (= R155) to C: in GLUT1DS1; 44% of wild-type glucose uptake activity
- L169 (= L171) natural variant: Missing (in GLUT1DS1; 48% of wild-type glucose uptake activity; dbSNP:rs80359832)
- I192 (≠ W212) mutation to C: Strongly decreases glucose transport.
- L204 (= L230) mutation to C: Abolishes glucose transport.
- P205 (≠ F231) mutation to C: Abolishes glucose transport.
- R212 (= R238) to C: in GLUT1DS1 and DYT9; dbSNP:rs387907312
- R218 (≠ Q244) to S: in EIG12; decreased glucose transport
- R223 (≠ K248) 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 (≠ T251) modified: Phosphoserine; by PKC/PRKCB; mutation to A: Abolishes phosphorylation by PKA, leading to impaired response to TPA.
- R232 (≠ N257) 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 (≠ A271) to V: in EIG12; decreased glucose transport
- A275 (≠ G291) to T: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909740
- Q282 (= Q298) binding
- QQLS 282:285 (≠ QQAI 298:301) 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 (= G302) 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 (≠ P311) to M: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359823
- V303 (≠ A319) to L: found in a patient with GLUT1 deficiency syndrome; dbSNP:rs1205631854
- G314 (= G331) to S: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909739
- S324 (≠ A341) to L: in GLUT1DS2; mild phenotype; reduced transporter activity; dbSNP:rs796053253
- E329 (≠ D346) to Q: in GLUT1DS1; stabilizes the inward-open conformation
- R333 (= R350) to Q: in GLUT1DS1 and GLUT1DS2; dbSNP:rs1553155986; to W: in GLUT1DS1; 43% of wild-type glucose uptake activity; dbSNP:rs80359825
- G340 (= G357) mutation to C: Strongly decreases glucose transport.
- W388 (= W401) binding
- N411 (≠ Q424) Not glycosylated; binding ; to S: in EIG12; decreased glucose transport; dbSNP:rs398123069
- I435 (≠ S448) 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 (≠ K471) 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
P32037 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Mus musculus (Mouse) (see paper)
30% identity, 96% coverage: 18:481/484 of query aligns to 15:466/493 of P32037
- N43 (≠ D50) modified: carbohydrate, N-linked (GlcNAc...) asparagine
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)
29% identity, 96% coverage: 19:483/484 of query aligns to 31:492/514 of Q9LT15
- F39 (= F27) mutation to A: Reduces affinity for glucose 8-fold.
- L43 (≠ T31) mutation to A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
- C77 (vs. gap) modified: Disulfide link with 449; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
- E162 (= E148) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q163) binding ; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (≠ M170) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (= Q298) binding
- Q296 (= Q299) binding
- N301 (= N304) binding
- N332 (= N334) binding
- D344 (= D346) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W401) binding
- C449 (≠ D440) 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)
29% identity, 96% coverage: 19:483/484 of query aligns to 11:472/487 of 7aaqA
5eqiA Human glut1 in complex with cytochalasin b (see paper)
29% identity, 93% coverage: 20:468/484 of query aligns to 11:447/447 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, 93% coverage: 20:468/484 of query aligns to 11:447/447 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)
29% identity, 93% coverage: 20:468/484 of query aligns to 11:447/447 of 5eqgA
7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
29% identity, 96% coverage: 19:483/484 of query aligns to 16:477/485 of 7aarA
- binding Octyl Glucose Neopentyl Glycol : L28 (≠ T31), I90 (≠ F79), H94 (≠ L83), V98 (≠ N87), F101 (≠ R90), N138 (≠ S139), P142 (= P143), N158 (≠ V159), F161 (≠ N162), Q162 (= Q163), I165 (= I166), D210 (≠ K235), G391 (= G397), P392 (= P398), W395 (= W401), M419 (≠ W425)
- binding beta-D-glucopyranose: Q280 (= Q298), N286 (= N304), M289 (≠ L307), G391 (= G397), W395 (= W401)
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 98% coverage: 12:483/484 of query aligns to 30:482/509 of Q8VZR6
- ER 481:482 (≠ KN 482:483) 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.
7crzA Crystal structure of human glucose transporter glut3 bound with c3361 (see paper)
29% identity, 99% coverage: 5:481/484 of query aligns to 1:464/469 of 7crzA
- binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: T26 (= T31), A66 (≠ L66), S69 (vs. gap), Q157 (= Q163), I164 (≠ M170), Q278 (= Q298), Q279 (= Q299), N284 (= N304), N313 (= N334), F375 (= F392), W384 (= W401), N411 (= N428), F412 (≠ Y429), G415 (≠ S432)
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, 99% coverage: 5:481/484 of query aligns to 3:466/496 of P11169
- Q159 (= Q163) binding
- QLS 277:279 (≠ SVF 295:297) Important for selectivity against fructose; mutation to HVA: Confers moderate fructose transport activity.
- QQ 280:281 (= QQ 298:299) binding
- N286 (= N304) binding
- N315 (= N334) binding
- E378 (≠ M393) binding
- W386 (= W401) binding
4zw9A Crystal structure of human glut3 bound to d-glucose in the outward- occluded conformation at 1.5 angstrom (see paper)
29% identity, 99% coverage: 5:481/484 of query aligns to 3:466/470 of 4zw9A
- binding beta-D-glucopyranose: Q159 (= Q163), I166 (≠ M170), Q280 (= Q298), Q281 (= Q299), N286 (= N304), F377 (= F392), W386 (= W401)
- binding alpha-D-glucopyranose: Q159 (= Q163), I162 (= I166), I166 (≠ M170), Q280 (= Q298), Q281 (= Q299), N286 (= N304), W386 (= W401)
7spsA Crystal structure of human glucose transporter glut3 bound with exofacial inhibitor sa47 (see paper)
29% identity, 97% coverage: 13:481/484 of query aligns to 8:463/468 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 (= F27), T25 (= T31), N29 (≠ S35), Q156 (= Q163), I163 (≠ M170), Q278 (= Q299), F286 (≠ L307), A308 (≠ M330), N312 (= N334), F374 (= F392), E375 (≠ M393), N406 (≠ Q424), W407 (= W425), N410 (= N428)
7sptA Crystal structure of exofacial state human glucose transporter glut3 (see paper)
29% identity, 99% coverage: 5:481/484 of query aligns to 3:466/470 of 7sptA
Query Sequence
>350322 FitnessBrowser__Btheta:350322
MNNTTNEGSKLYLYSITSVAILGGLLFGYDTAVISGAEKGLEAFFLSASDFQYNKVMHGI
TSSSALIGCVLGGALSGVFASRLGRRNSLRLAAVLFFLSALGSYYPEVLFFEYGKPNMDL
LIAFNLYRVLGGIGVGLASAVCPMYIAEIAPSNIRGTLVSCNQFAIIFGMLVVYFVNYLI
MGDHQNPIILKDAAGVLSVSAESDMWTVQEGWRYMFGSEAFPAAFFGLLLFFVPKTPRYL
VLVQQEEKAYTILEKINGKKKAQEILNDIKATAQEKTEKLFTYGVTVIVIGILLSVFQQA
IGINAVLYYAPRIFENAGAEGGGMMQTVIMGIVNIIFTLVAIFTVDRFGRKPLLIIGSIG
MAVGAFAVAMCDSMAIKGVLPVLSIIVYAAFFMMSWGPICWVLISEIFPNTIRGKAVAIA
VAFQWIFNYIVSSTFPALYDFSPMFAYSLYGIICVAAAIFVWRWVPETKGKTLEDMSKLW
KKNK
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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