SitesBLAST
Comparing CA265_RS01275 FitnessBrowser__Pedo557:CA265_RS01275 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)
37% identity, 100% coverage: 1:462/462 of query aligns to 1:483/491 of P0AGF4
- F24 (= F24) mutation to A: Decreases xylose transport.
- G83 (= G75) mutation to A: Abolishes xylose transport.
- R133 (= R107) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E127) mutation to A: Abolishes xylose transport.
- R160 (= R134) mutation to A: Abolishes xylose transport.
- Q168 (= Q142) binding ; mutation to A: Abolishes xylose transport.
- Q288 (≠ S273) mutation to A: Abolishes xylose transport.
- QQ 288:289 (≠ SQ 273:274) binding
- Q289 (= Q274) mutation to A: Strongly decreases xylose transport.
- N294 (= N279) binding ; mutation to A: Abolishes xylose transport.
- Y298 (≠ F283) mutation to A: Abolishes xylose transport.
- N325 (= N310) mutation to A: No effect on xylose transport.
- G340 (= G325) mutation to A: Abolishes xylose transport.
- R341 (= R326) mutation R->A,W: Abolishes xylose transport.
- W392 (≠ F377) binding ; mutation to A: Abolishes xylose transport.
- E397 (= E382) mutation to A: Abolishes xylose transport.
- R404 (= R389) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ M400) binding
- W416 (= W401) 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)
37% identity, 97% coverage: 9:458/462 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)
37% identity, 97% coverage: 9:458/462 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)
37% identity, 97% coverage: 9:458/462 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)
35% identity, 93% coverage: 27:454/462 of query aligns to 22:434/446 of A0A0H2VG78
- D22 (= D27) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R107) mutation to A: Loss of transport activity.
- I105 (≠ A110) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E127) mutation to A: Loss of transport activity.
- Q137 (= Q142) mutation to A: Loss of transport activity.
- Q250 (≠ S273) mutation to A: Loss of transport activity.
- Q251 (= Q274) mutation to A: Loss of transport activity.
- N256 (= N279) mutation to A: Loss of transport activity.
- W357 (≠ F377) mutation to A: Loss of transport activity.
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 98% coverage: 6:460/462 of query aligns to 27:482/509 of Q8VZR6
- ER 481:482 (≠ SE 459:460) 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.
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, 98% coverage: 9:460/462 of query aligns to 24:492/514 of Q9LT15
- F39 (= F24) mutation to A: Reduces affinity for glucose 8-fold.
- L43 (≠ M28) 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 (= E127) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q142) binding ; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (= I149) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (≠ S273) binding
- Q296 (= Q274) binding
- N301 (= N279) binding
- N332 (= N310) binding
- D344 (= D322) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (≠ F377) binding
- C449 (≠ D416) 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, 98% coverage: 9:460/462 of query aligns to 4:472/487 of 7aaqA
7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
28% identity, 99% coverage: 5:460/462 of query aligns to 5:477/485 of 7aarA
- binding Octyl Glucose Neopentyl Glycol : L28 (≠ M28), I90 (≠ L70), H94 (≠ V74), V98 (≠ K78), F101 (= F81), N138 (≠ S118), P142 (= P122), N158 (≠ V138), F161 (≠ Y141), Q162 (= Q142), I165 (= I145), D210 (≠ E206), G391 (= G373), P392 (= P374), W395 (≠ F377), M419 (≠ W401)
- binding beta-D-glucopyranose: Q280 (≠ S273), N286 (= N279), M289 (≠ I282), G391 (= G373), W395 (≠ F377)
P43427 Solute carrier family 2, facilitated glucose transporter member 5; Fructose transporter; Glucose transporter type 5, small intestine; GLUT-5 from Rattus norvegicus (Rat) (see paper)
30% identity, 98% coverage: 12:462/462 of query aligns to 18:479/502 of P43427
- Y31 (≠ F24) binding
- Q166 (= Q142) binding ; mutation to E: Impairs D-fructose binding.
- Q287 (≠ S273) binding
- IYY 295:297 (≠ VIF 281:283) binding
- H386 (≠ F368) binding
- HW 418:419 (≠ MW 400:401) 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: 17:459/462 of query aligns to 19:469/492 of P11166
- N34 (≠ S32) to S: in GLUT1DS1; 55% of wild-type glucose uptake activity; dbSNP:rs80359812
- N45 (≠ S40) 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 (≠ I61) to T: in EIG12; decreased glucose transport; dbSNP:rs1187210267
- G91 (= G75) to D: in GLUT1DS1; significantly decreases the transport of 3-O-methyl-D-glucose; dbSNP:rs80359814
- R126 (= R107) 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 (= G111) to S: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359819
- T137 (≠ S118) binding
- P149 (= P130) to A: in EIG12; uncertain significance
- R153 (= R134) to C: in GLUT1DS1; 44% of wild-type glucose uptake activity
- L169 (= L150) natural variant: Missing (in GLUT1DS1; 48% of wild-type glucose uptake activity; dbSNP:rs80359832)
- I192 (≠ V189) mutation to C: Strongly decreases glucose transport.
- L204 (= L201) mutation to C: Abolishes glucose transport.
- P205 (≠ L202) mutation to C: Abolishes glucose transport.
- R212 (= R209) to C: in GLUT1DS1 and DYT9; dbSNP:rs387907312
- R218 (= R216) 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 (≠ N222) modified: Phosphoserine; by PKC/PRKCB; mutation to A: Abolishes phosphorylation by PKA, leading to impaired response to TPA.
- R232 (≠ N228) 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 (≠ S239) to V: in EIG12; decreased glucose transport
- A275 (= A266) to T: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909740
- Q282 (≠ S273) binding
- QQLS 282:285 (≠ SQFS 273:276) 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 (= G277) 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 (≠ P286) to M: in GLUT1DS1; 75% of wild-type glucose uptake activity; dbSNP:rs80359823
- V303 (≠ I294) to L: found in a patient with GLUT1 deficiency syndrome; dbSNP:rs1205631854
- G314 (= G307) to S: in GLUT1DS2; the mutation decreases glucose transport but does not affect cation permeability; dbSNP:rs121909739
- S324 (≠ A317) to L: in GLUT1DS2; mild phenotype; reduced transporter activity; dbSNP:rs796053253
- E329 (≠ D322) to Q: in GLUT1DS1; stabilizes the inward-open conformation
- R333 (= R326) to Q: in GLUT1DS1 and GLUT1DS2; dbSNP:rs1553155986; to W: in GLUT1DS1; 43% of wild-type glucose uptake activity; dbSNP:rs80359825
- G340 (= G333) mutation to C: Strongly decreases glucose transport.
- W388 (≠ F377) binding
- N411 (≠ M400) Not glycosylated; binding ; to S: in EIG12; decreased glucose transport; dbSNP:rs398123069
- I435 (≠ F425) 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 (≠ K448) 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)
29% identity, 96% coverage: 17:459/462 of query aligns to 19:469/492 of P17809
- N45 (≠ S40) 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.
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)
30% identity, 96% coverage: 10:453/462 of query aligns to 26:471/478 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.
P11168 Solute carrier family 2, facilitated glucose transporter member 2; Glucose transporter type 2, liver; GLUT-2 from Homo sapiens (Human) (see 6 papers)
29% identity, 89% coverage: 51:460/462 of query aligns to 99:502/524 of P11168
- T110 (≠ V62) to I: in dbSNP:rs5400
- V197 (≠ T146) to I: in NIDDM; abolishes transport activity of the transporter expressed in Xenopus oocytes; dbSNP:rs121909741
- I322 (≠ V281) mutation to V: Reduced fructose transport.
Sites not aligning to the query:
- 68 P → L: in dbSNP:rs7637863
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, 98% coverage: 10:462/462 of query aligns to 11:470/493 of P32037
- N43 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q9C757 Probable inositol transporter 2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 71% coverage: 7:332/462 of query aligns to 25:346/580 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.
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)
29% identity, 96% coverage: 10:453/462 of query aligns to 26:470/477 of Q9JIF3
Sites not aligning to the query:
- 12:13 Dileucine internalization motif; LL→AA: Abolishes interaction with AP2B1.
O23492 Inositol transporter 4; Myo-inositol-proton symporter INT4; Protein INOSITOL TRANSPORTER 4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 70% coverage: 9:332/462 of query aligns to 26:348/582 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.
5eqiA Human glut1 in complex with cytochalasin b (see paper)
29% identity, 93% coverage: 17:445/462 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: 17:445/462 of query aligns to 11:447/447 of 5eqhA
Query Sequence
>CA265_RS01275 FitnessBrowser__Pedo557:CA265_RS01275
MRKQGANYFIFLITLIAALGGFLFGFDMAVVSGIIEPLKSQYGLSSAQEGLFVSCALLGC
IVGVSFSGYLSDKVGRRKVLFLAAILFLVSAVGFAFSVAYPVLIFFRVLAGMGVGVASNV
SPLYISEVAPSQKRGRLVVFYQLAITIGILAAYISNLFLQRYATVHAGAGEGILHWLFVE
NVWRGMFIVGVVPAAAFCLLLLIVPESPRWLVQYGRNEEALNTLIKINGAETGRLELDSI
KEMASQKSGGYKELMRLPLSKLLALATILTALSQFSGINGVIFYGPTILKSAGIVTSDAL
FYQVILGSANVLFTFIAISKVDTWGRRPLYIIGSLCAAGALALTGFCFLMDITGWFMLFS
IILFLLFFAFSLGPLKFVISTEIFPTHIRGTALSMCIMTMWVSDWVVNMLFPIMRDGLGI
ATTFFIFSFFCILSFLYAKKKLFETKGKSLEEIEKAWNSEVK
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