SitesBLAST
Comparing 3610525 FitnessBrowser__Dino:3610525 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)
7wmvA Structure of human sglt1-map17 complex bound with lx2761 (see paper)
33% identity, 92% coverage: 12:500/533 of query aligns to 11:550/602 of 7wmvA
- binding N-[2-(dimethylamino)ethyl]-2-methyl-2-[4-[4-[[2-methyl-5-[(2S,3R,4R,5S,6R)-6-methylsulfanyl-3,4,5-tris(oxidanyl)oxan-2-yl]phenyl]methyl]phenyl]butanoylamino]propanamide: N61 (= N61), H66 (≠ S66), L70 (= L70), I81 (= I81), F84 (≠ Y84), L257 (= L235), M266 (≠ V243), L269 (= L246), T270 (≠ G247), Y273 (= Y250), W274 (= W251), F436 (= F393), D437 (≠ S394), Q440 (= Q397), H508 (= H458)
P13866 Sodium/glucose cotransporter 1; Na(+)/glucose cotransporter 1; High affinity sodium-glucose cotransporter; Solute carrier family 5 member 1 from Homo sapiens (Human) (see 6 papers)
33% identity, 92% coverage: 12:500/533 of query aligns to 28:567/664 of P13866
- N51 (≠ E35) to S: in GGM; slightly decreased activity; dbSNP:rs17683011
- W67 (= W50) mutation to A: Strong reduction in D-glucose transporter activity.
- S77 (= S60) mutation to A: Loss of activity.
- H83 (≠ S66) mutation to L: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and C-290.; mutation to Q: Loss of D-glucose transporter activity.
- R135 (= R118) to W: in GGM; loss of activity
- S159 (≠ A141) to P: in GGM; loss of activity
- A166 (≠ G148) to T: in GGM; about 90% reduction in activity
- D204 (= D187) mutation to A: Loss of activity.
- N248 (≠ H223) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Loss of N-glycosylation.
- C255 (≠ L226) modified: Disulfide link with 511
- W276 (= W237) to L: in GGM; about 95% reduction in activity
- T287 (≠ G247) mutation to A: Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with L-83 and C-290.; mutation to N: Loss of D-glucose transporter activity. Has strict selectivity for D-galactose.; mutation T->S,A: Has normal D-glucose and D-galactose transporter activity.
- Y290 (= Y250) mutation to C: Loss of D-galactose transporter activity. Has strict selectivity for D-glucose. Acquires D-mannose, D-fructose and L-sorbose transporter activity; when associated with A-287 and L-83.
- W291 (= W251) mutation to A: Loss of D-glucose transporter activity.
- C292 (≠ T252) to Y: in GGM; loss of activity; mutation to A: Has no effect on water permeability.
- Q295 (= Q255) to R: in GGM; loss of activity
- R300 (= R260) to S: in GGM; loss of activity
- A304 (= A264) to V: in GGM; impairs trafficking to the plasma membrane
- K321 (= K281) mutation to Q: Acquires D-mannose and D-allose transporter activity comparable to glucose and galactose.
- C345 (vs. gap) modified: Disulfide link with 351
- C351 (vs. gap) modified: Disulfide link with 345
- C355 (vs. gap) modified: Disulfide link with 361
- C361 (≠ T304) modified: Disulfide link with 355
- N363 (≠ D306) mutation to A: Loss of water permeation.
- L369 (= L312) to S: in GGM; loss of activity
- R379 (= R322) to Q: in GGM; loss of activity
- A388 (= A331) to V: in GGM; loss of activity
- S396 (= S339) mutation to A: Loss of activity.
- F405 (≠ V348) to S: in GGM; loss of activity
- A411 (≠ E354) to T: in GGM; slightly decreased activity; dbSNP:rs17683430
- G426 (= G368) to R: in GGM; loss of activity
- Q451 (vs. gap) mutation to A: Strong reduction in water permeation.
- L452 (= L392) mutation to A: Loss of water permeation.
- D454 (≠ S394) mutation to A: Has no effect on water permeation.
- Q457 (= Q397) mutation to A: Loss of D-glucose transporter activity.; mutation to C: Strong reduction in D-glucose transporter activity.
- T460 (≠ L400) mutation to A: Loss of D-glucose transporter activity.
- V470 (= V410) to N: in GGM; about 90% reduction in activity; requires 2 nucleotide substitutions
- R499 (≠ L439) to H: in GGM; impairs trafficking to the plasma membrane; decreases the sugar affinity
- C511 (≠ G451) modified: Disulfide link with 255
- C517 (≠ L454) modified: Disulfide link with 522
- C522 (vs. gap) modified: Disulfide link with 517
Sites not aligning to the query:
- 191:664 natural variant: Missing (in GGM; loss of activity)
- 379:664 natural variant: Missing (in GGM; loss of activity)
- 615 H → Q: in GGM; slightly decreased activity
- 641 W→A: Slightly reduced D-glucose transporter activity.
- 660:661 HA→WG: Loss of D-glucose transporter activity.
P11170 Sodium/glucose cotransporter 1; Na(+)/glucose cotransporter 1; High affinity sodium-glucose cotransporter; Solute carrier family 5 member 1 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
32% identity, 92% coverage: 12:500/533 of query aligns to 28:567/662 of P11170
- C255 (≠ L226) modified: Disulfide link with 608
- Q457 (= Q397) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ L400) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 608 modified: Disulfide link with 255
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
31% identity, 91% coverage: 12:494/533 of query aligns to 28:561/659 of Q9NY91
- E457 (≠ Q397) mutation to Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
7vsiA Structure of human sglt2-map17 complex bound with empagliflozin (see paper)
31% identity, 97% coverage: 12:526/533 of query aligns to 5:572/586 of 7vsiA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (= N61), H60 (≠ S66), G63 (= G69), L64 (= L70), V75 (≠ I81), F78 (≠ Y84), E79 (= E85), V266 (≠ L246), S267 (≠ G247), Y270 (= Y250), F433 (= F393), D434 (≠ S394), Q437 (= Q397)
8hezA Structure of human sglt2-map17 complex with dapagliflozin (see paper)
31% identity, 98% coverage: 12:533/533 of query aligns to 5:581/582 of 8hezA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (= N61), G59 (≠ S65), H60 (≠ S66), G63 (= G69), L64 (= L70), T67 (≠ G73), F78 (≠ Y84), E79 (= E85), V266 (≠ L246), S267 (≠ G247), W271 (= W251), K301 (= K281), F433 (= F393), Q437 (= Q397)
- binding sodium ion: A53 (= A59), I56 (≠ M62), G57 (≠ S63), A369 (= A332), S372 (= S335), S373 (= S336)
- binding : L568 (= L520), M571 (≠ L523), A572 (≠ S524), V575 (≠ G527), F576 (= F528), G579 (≠ W531), F580 (= F532)
8hdhA Structure of human sglt2-map17 complex with canagliflozin (see paper)
31% identity, 97% coverage: 12:526/533 of query aligns to 5:572/586 of 8hdhA
- binding (2~{S},3~{R},4~{R},5~{S},6~{R})-2-[3-[[5-(4-fluorophenyl)thiophen-2-yl]methyl]-4-methyl-phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (= N61), G59 (≠ S65), H60 (≠ S66), G63 (= G69), L64 (= L70), F78 (≠ Y84), E79 (= E85), S267 (≠ G247), W271 (= W251), F433 (= F393), D434 (≠ S394), Q437 (= Q397), Y506 (= Y459)
- binding sodium ion: A53 (= A59), S54 (= S60), I56 (≠ M62), G57 (≠ S63), A369 (= A332), S372 (= S335), S373 (= S336)
Sites not aligning to the query:
8hb0A Structure of human sglt2-map17 complex with ta1887 (see paper)
31% identity, 97% coverage: 12:526/533 of query aligns to 5:572/586 of 8hb0A
- binding (2R,3R,4S,5S,6R)-2-[3-[(4-cyclopropylphenyl)methyl]-4-fluoranyl-indol-1-yl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (= N61), H60 (≠ S66), G63 (= G69), L64 (= L70), T67 (≠ G73), V75 (≠ I81), F78 (≠ Y84), E79 (= E85), V137 (≠ G142), V266 (≠ L246), S267 (≠ G247), W271 (= W251), F433 (= F393), Q437 (= Q397)
- binding sodium ion: A53 (= A59), I56 (≠ M62), G57 (≠ S63), A369 (= A332), S372 (= S335), S373 (= S336)
Sites not aligning to the query:
8hg7A Structure of human sglt2-map17 complex with sotagliflozin (see paper)
32% identity, 92% coverage: 12:500/533 of query aligns to 5:547/590 of 8hg7A
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: N55 (= N61), G59 (≠ S65), H60 (≠ S66), G63 (= G69), L64 (= L70), E79 (= E85), V266 (≠ L246), S267 (≠ G247), Y270 (= Y250), W271 (= W251), K301 (= K281), F433 (= F393), Q437 (= Q397)
- binding sodium ion: A53 (= A59), S54 (= S60), I56 (≠ M62), G57 (≠ S63), A369 (= A332), S372 (= S335), S373 (= S336)
Sites not aligning to the query:
P31639 Sodium/glucose cotransporter 2; Na(+)/glucose cotransporter 2; Low affinity sodium-glucose cotransporter; Solute carrier family 5 member 2 from Homo sapiens (Human) (see paper)
32% identity, 92% coverage: 12:500/533 of query aligns to 25:567/672 of P31639
- V95 (≠ I81) mutation to A: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F98 (≠ Y84) mutation to A: Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.
- V157 (≠ G142) mutation to A: Decreases D-glucose transporter activity.
- L283 (≠ V243) mutation to M: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F453 (= F393) mutation to A: Slightly decreases D-glucose transporter activity. Greatly reduces the binding to inhibitor, empagliflozin.
Q9ET37 Solute carrier family 5 member 4A; SGLT3-a from Mus musculus (Mouse) (see paper)
32% identity, 92% coverage: 12:500/533 of query aligns to 28:567/656 of Q9ET37
- E457 (≠ Q397) mutation to Q: Confers sodium-dependent sugar transport activity not found in the wild type protein.
7sl8A Cryoem structure of sglt1 at 3.4 a resolution (see paper)
32% identity, 94% coverage: 12:512/533 of query aligns to 9:552/582 of 7sl8A
Sites not aligning to the query:
7slaA Cryoem structure of sglt1 at 3.15 angstrom resolution (see paper)
32% identity, 94% coverage: 12:512/533 of query aligns to 10:555/585 of 7slaA
8hinA Structure of human sglt2-map17 complex with phlorizin (see paper)
30% identity, 98% coverage: 12:533/533 of query aligns to 12:587/588 of 8hinA
- binding 1-[2-[(2S,3R,4S,5S,6R)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-4,6-bis(oxidanyl)phenyl]-3-(4-hydroxyphenyl)propan-1-one: S46 (= S56), A49 (= A59), S50 (= S60), G53 (≠ S63), D177 (= D187), T181 (≠ A191), R276 (= R260), S369 (= S336)
- binding : L574 (= L520), A578 (≠ S524), V581 (≠ G527), F582 (= F528), G585 (≠ W531), F586 (= F532)
7yniA Structure of human sglt1-map17 complex bound with substrate 4d4fdg in the occluded conformation (see paper)
31% identity, 94% coverage: 12:512/533 of query aligns to 10:544/566 of 7yniA
- binding (2R,3R,4R,5S,6R)-5-fluoranyl-6-(hydroxymethyl)oxane-2,3,4-triol: H51 (≠ S66), E70 (= E85), L248 (= L246), Y252 (= Y250), F415 (= F393), Q419 (= Q397)
Sites not aligning to the query:
7ynjA Structure of human sglt2-map17 complex bound with substrate amg in the occluded conformation (see paper)
31% identity, 91% coverage: 43:526/533 of query aligns to 19:550/564 of 7ynjA
Sites not aligning to the query:
3dh4A Crystal structure of sodium/sugar symporter with bound galactose from vibrio parahaemolyticus (see paper)
34% identity, 74% coverage: 45:438/533 of query aligns to 19:430/512 of 3dh4A
Q92911 Sodium/iodide cotransporter; Na(+)/I(-) cotransporter; Natrium iodide transporter; Sodium-iodide symporter; Na(+)/I(-) symporter; Solute carrier family 5 member 5 from Homo sapiens (Human) (see 3 papers)
25% identity, 77% coverage: 12:424/533 of query aligns to 16:444/643 of Q92911
- A102 (= A96) natural variant: A -> P
- H226 (= H223) mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- D237 (vs. gap) mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- Y242 (vs. gap) Required for homodimerization; mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471. Loss of iodide transport activity; when associated with F-535.
- T243 (vs. gap) Required for homodimerization; mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471.
Sites not aligning to the query:
- 471 Required for homodimerization; Q→A: No effect on localization to the cell membrane, iodide transport activity and homodimerization. Significant loss of homodimerization; when associated with A-242 or A243.
- 525 A→F: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Loss of iodide transport activity; when associated with A-242.
- 536 T → Q: requires 2 nucleotide substitutions
- 556 S → Q: requires 2 nucleotide substitutions
Q8N695 Sodium-coupled monocarboxylate transporter 1; Apical iodide transporter; Electrogenic sodium monocarboxylate cotransporter; Sodium iodide-related cotransporter; Solute carrier family 5 member 8 from Homo sapiens (Human) (see 3 papers)
25% identity, 79% coverage: 35:456/533 of query aligns to 39:468/610 of Q8N695
- V193 (≠ A191) to I: in dbSNP:rs1709189
- F251 (≠ Y249) to V: in dbSNP:rs11834933
Sites not aligning to the query:
- 608 T→A: Loss of interaction with PDZK1.
- 608:610 PDZ-binding
- 610 L→A: Loss of interaction with PDZK1.
7sl9A Cryoem structure of smct1 (see paper)
26% identity, 76% coverage: 53:456/533 of query aligns to 36:447/497 of 7sl9A
Query Sequence
>3610525 FitnessBrowser__Dino:3610525
MGDAKFDLHWIDYAIVVIYFIGVIAHGVYVSRKNEEGADGYFLAGRSLPWYLIGFSLFAS
NMSGSSFVGLMGGAYANGIVIFNYEWTAALVLILFAIFVLPSFLKAKISTVPEFLEQRYD
VRSRRAFSIFTILAILFIDTAGALYAGGLVISNVTGYLNLWTAVAVLALVAGIYTILGGL
SAVVVTDTVQAILLIIGAAILFWLGLDEIGGWEQLFVDIPEGHDQLILPADDDFLPWTGL
WGVVLLGFYYWTINQFVVQRTLGAKNLKEGQIGALFAGFLKLPNIFLMIIPGVIALKLYP
ELETPDLAFPTLAFELMPIGVRGLIMAALIAAIMSSLDSAMNSASTLVVKDFVEPIWEVD
EGKQVWIGRLVTGAVMVFGAIYAPSIAGFESLFSYFQSSLSYIIPTIVVVYIVGLFVPWL
NGNGAFWTIILGLVVGIPLFIMKEVTGVWAGMGLPEIHYTIMSTLMMCLGLATHFGISAL
TRKADKENIEDLVWSAADTKAIFTQWEEPLWQDRTIWAGLLILSTIGFVAWFW
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