SitesBLAST

R257 (= R290) mutation to C: Sodium-independent binding affinity for proline.
C281 (≠ T318) mutation to S: Does not affect proline uptake activity. Confers resistance to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
C344 (≠ G380) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
C349 (≠ G385) mutation to S: Does not affect proline uptake activity. Sensitive to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
R376 (= R413) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.

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)
24% identity, 41% coverage: 33:261/556 of query aligns to 8:237/643 of Q92911

query
sites
Q92911

E

E

R

R

Q

P

P

T

V

F

N

G

V

A

T

W

A

D

I

Y

A

G

M

V

F

F

L

A

L

L

F

M

V

L

A

L

G

V

T

S

L

T

G

G

I

I

T

G

Y

L

W

W

-

V

-

G

-

L

A

A

S

R

K

G

R

G

T

Q

R

R

S

S

A

A

S

E

D

D

F

F

Y

F

T

T

A

G

G

G

G

R

I

L

S

A

G

A

F

L

Q

P

N

V

G

G

L

L

A

S

I

L

A

S

G

A

D

S

Y

F

M

M

S

S

A

A

A

V

A

Q

F

V

L

L

G

G

L

V

S

P

G

S

M

E

V

A

F

Y

A

R

K

Y

G

G

F

L

D

K

G

F

V

L

I

W

Y

M

T

C

I

L

G

G

F

Q

L

L

V

L

G

N

W

S

P

V

L

L

M

T

L
x
A

F

L

L

L

I

F

A

M

E

P

R

V

L

F

R

Y

N

R

L

L

G

G

R

L

F

T

T

S

F

T

A

Y

D

E

V

Y

A

L

S

E

Y

M

R

R

L

F

G

S

Q

-

T

-

P

-

I

-

R

R

S

A

L

V

A

R

A

L

V

C

G

G

S

T

L

L

T

Q

V

-

C

-

F

-

Y

Y

L

I

I

V

A

A

Q

T

M

M

V

L

G

Y

A

T

G

G

K

I

L

V

I

I

-

Y

-

A

-

P

-

A

-

L

-

I

-

L

Q

N

L

Q

L

V

F

T

G

G

L

L

D

D

Y

I

T

W

Y

A

A

S

V

L

M

S

V

T

G

G

V

I

L

I

M

C

I

T

L

F

Y

Y

V

T

T

A

F

V

G

G

M

M

L

K

A

A

T

V

W

W

V

T

Q

D

I

V

I

F

K

Q

A

V

V

V

M

V

L

M

L

L

G

S

G

G

C

F

T

W

V

V

L

V

V

L

G

A

L

R

A

G

L

V

A

M

Q

L

F

V

G

G

F

-

N

G

P

P

E

R

R

Q

L

V

L

L

Q

T

Q

L

A

A

V

Q

A

N

A
x
H

H

S

A

R

A

I

N

N

A

L

A

M

I

D

L

F

R

N

P

P

S
x
D

A102 (≠ L124) natural variant: A -> P
H226 (≠ A250) mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
D237 (≠ S261) mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.

Sites not aligning to the query:

242 Required for homodimerization; Y→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.
243 Required for homodimerization; T→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.
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

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)
26% identity, 39% coverage: 20:237/556 of query aligns to 7:224/672 of P31639

query
sites
P31639

A

A

G

G

P

S

V

A

H

P

A

E

A

M

A

G

I

A

D

Q

G

K

A

A

V

L

E

I

R

D

Q

N

P

P

V

A

N

D

V

I

T

L

A

V

I

I

A

A

M

A

F

Y

L

F

L

L

F

L

V

V

A

-

G

-

T

-

L

I

G

G

I

V

T

G

Y

L

W

W

A

S

S

M

K

C

R

R

T

T

R

N

S

R

A

G

S

T

-

V

-

G

D

G

F

Y

Y

F

T

L

A

A

G

G

G

R

G

S

I

M

S

V

G

W

F

W

Q

P

N

V

G

G

L

A

A

S

I

L

A

F

G

A

D

S

Y

N

M

I

S

G

A

S

A

G

A

H

F

F

L

V

G

G

L

L

S

A

G

G

M

T

V

G

F

A

A

A

K

S

G

G

-

L

-

A

-
x
V

-

A

-

G

F
|
F

D

E

G

W

V

N

I

A

Y

L

T

F

I

V

G

V

F

L

L

L

V

L

G

G

W

W

P

-

L

-

M

-

L

-

F

-

L

L

I

F

A

A

E

P

R

V

L

Y

R

L

N

T

L

A

G

G

R

V

F

I

T

T

F

M

A

P

D

Q

V

Y

A

L

S

R

Y

K

R

R

L

F

G

G

Q

G

T

R

P

R

I

I

R

R

S

L

L

Y

A

L

A

S

V

V

G

L

S

S

L

L

T

F

V

L

V

Y

C

I

F

F

Y

T

L

K

I

I

A

S

-
x
V

Q

D

M

M

V

F

G

S

A

G

G

A

K

V

L

F

I

I

Q

Q

L

Q

L

A

F

L

G

G

L

W

D

N

-

I

Y

Y

T

A

Y

S

A

V

V

I

V

A

M

L

V

L

G

G

V

I

L

T

M

M

I

I

L

Y

Y

T

V

V

T

T

F

-

G

G

M

L

L

A

A

A

T

L

T

M

W

Y

V

T

Q

D

I

T

I

V

K

Q

A

T

V

F

M

V

L

I

L

L

G

G

C

A

T

C

V

I

L

L

V

M

G

G

L

Y

A

A

L

F

A

H

Q

E

F

V

G

G

V95 (vs. gap) mutation to A: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
F98 (= F107) mutation to A: Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.
V157 (vs. gap) mutation to A: Decreases D-glucose transporter activity.

Sites not aligning to the query:

283 L→M: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
453 F→A: Slightly decreases D-glucose transporter activity. Greatly reduces the binding to inhibitor, empagliflozin.

7vsiA Structure of human sglt2-map17 complex bound with empagliflozin (see paper)
26% identity, 37% coverage: 35:237/556 of query aligns to 2:204/586 of 7vsiA

query
sites
7vsiA

Q

N

P

P

V

A

N

D

V

I

T

L

A

V

I

I

A

A

M

A

F

Y

L

F

L

L

F

L

V

V

A

-

G

-

T

-

L

I

G

G

I

V

T

G

Y

L

W

W

A

S

S

M

K

C

R

R

T

T

R

N

S

R

A

G

S

T

-

V

-

G

D

G

F

Y

Y

F

T

L

A

A

G

G

G

R

G

S

I

M

S

V

G

W

F

W

Q

P

N

V

G

G

L

A

A

S

I

L

A

F

G

A

D

S

Y
x
N

M

I

S

G

A

S

A

G

A
x
H

F

F

L

V

G
|
G

L
|
L

S

A

G

G

M
x
T

V

G

F

A

A

A

K

S

G

G

-

L

-

A

-
x
V

-

A

-

G

F
|
F

D
x
E

G

W

V

N

I
x
A

Y

L

T

F

I

V

G

V

F

L

L

L

V

L

G

G

W

W

P

-

L

-

M

-

L

-

F

-

L

L

I

F

A

A

E

P

R

V

L

Y

R

L

N

T

L

A

G

G

R

V

F

I

T

T

F

M

A

P

D

Q

V

Y

A

L

S

R

Y

K

R

R

L

F

G

G

Q

G

T

R

P

R

I

I

R

R

S

L

L

Y

A

L

A

S

V

V

G

L

S

S

L

L

T

F

V

L

V

Y

C

I

F

F

Y

T

L

K

I

I

A

S

-
x
V

Q

D

M

M

V

F

G

S

A

G

G

A

K

V

L

F

I

I

Q

Q

L

Q

L

A

F

L

G

G

L

W

D

N

-

I

Y

Y

T

A

Y

S

A

V

V

I

V

A

M

L

V

L

G

G

V

I

L

T

M

M

I

I

L

Y

Y

T

V

V

T

T

F

-

G

G

M

L

L

A

A

A

T

L

T

M

W

Y

V

T

Q

D

I

T

I

V

K

Q

A

T

V

F

M

V

L

I

L

L

G

G

C

A

T

C

V

I

L

L

V

M

G

G

L

Y

A

A

L

F

A

H

Q

E

F

V

G

G

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 (≠ Y89), H60 (≠ A94), G63 (= G97), L64 (= L98), T67 (≠ M101), V75 (vs. gap), F78 (= F107), E79 (≠ D108), A82 (≠ I111), V137 (vs. gap)

Sites not aligning to the query:

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: 266, 267, 270, 271, 301, 433, 434, 437, 506

5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
20% identity, 52% coverage: 48:338/556 of query aligns to 13:304/480 of 5nv9A

query
sites
5nv9A

F

Y

V

L

A

A

G

A

T

M

L

L

G

L

I

V

T

G

Y

V

W

Y

A

F

S

S

K

K

R

R

T

Q

R

K

S

T

A

A

S

D

D

D

F

Y

Y

F

T

R

A

G

G

G

G

R

I

V

S

P

G

G

F

W

Q

A

N

A

G

G

L

V

A

S

I

V

A

F

G
x
A

D
x
T

Y
x
T

M
x
L

S
|
S

A

S

A
x
I

A
x
T

F

F

L

M

G

S

L

I

S

P

G

A

M

K

V

A

F

Y

A

T

K

S

G

D

F

W

D

T

G

F

V

I

I

I

Y
x
G

T
x
Q

I

Y

G

L

F

A

L

I

V

A

G

I

W

L

P

P

L

L

M

V

L

F

F

Y

L

F

I

Y

A

I

E

P

R

F

L

F

R

R

N

K

L

L

G

-

R

-

F

-

T

K

F

I

A

T

D

S

V

A

A

Y

S

E

Y

Y

R

L

L

E

G

A

Q

R

T

F

P

D

I

V

R

R

S

S

L

-

A

R

A

L

V

F

G

A

S

S

L

L

T

S

V

F

V

M

C

L

F

F

Y

H

L

I

-

G

-
x
R

I

V

A

A

Q

I

M

I

V

T

G

Y

A

L

G

T

K

V

L

L

-

A

I

L

Q

R

L

P

L

F

F

M

G

G

L

I

D

D

Y

P

T

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Y

V

A

L

V

I

V

V

M

L

V

I

G

S

V

L

L

L

M

C

I

I

L

I

Y

Y

V

T

T

W

F

M

G

G

M

I

L

E

A

G

T
x
V

T

I

W

W

V

T

Q
x
D

I

V

I

I

K

Q

A

G

V

L

M

L

L

L

L

S

G

G

C

A

T

V

-

L

V

I

L

F

V

I

G

M

L

I

A

C

L

F

A

K

Q

V

F

D

G

G

F

G

N

I

P

S

E

E

R

I

L

F

L

T

Q

T

A

A

V

Q

A

A

A

D

H

K

A

F

N

P

A

T

I

Q

L

W

R

R

P

W

S

S

A

W

A

T

M

D

A

S

D

T

-

I

P

P

I

V

A

L

A

M

V

I

S

G

L
x
F

S

L

L

F

A

A

L

N

M

I

C

Q

G

Q

P

F

A

T

G

A

L

S

P

Q

H

D

I

V

L

V

M

Q

R

R

F

Y

F

I

T

V

V

T

P

D

D

S

A

I

K

K

E

E

A

T

R

K

K

R

S

T

V

L

V

I

Y

T

A

N

T

A

G

K

F

L

I
x
V

G

A

Y

I

F

I

F

P

I

I

L

F

T

F

V

F

T

A

I

I

G

G

F

S

L

A

A

L

I

F

V

V

I

Y

V

Y

G

Q

T

Q

N

N

P

P

A

S

Y

L

L

L

D

P

A

A

binding sodium ion: A52 (≠ G87), T53 (≠ D88), L55 (≠ M90), S56 (= S91), V174 (≠ T210), D178 (≠ Q214)
binding N-acetyl-beta-neuraminic acid: T54 (≠ Y89), L55 (≠ M90), S56 (= S91), I58 (≠ A93), T59 (≠ A94), G77 (≠ Y112), Q78 (≠ T113), R131 (vs. gap), F239 (≠ L273), V277 (≠ I311)

Sites not aligning to the query:

binding sodium ion: 335, 338, 338, 339, 341, 342

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)
20% identity, 79% coverage: 34:471/556 of query aligns to 24:488/662 of P11170

query
sites
P11170

R

R

Q

N

P

A

V

A

N

D

V

I

T

S

A

V

I

I

A

V

M

I

F

Y

L

F

L

L

F

V

V

V

A

-

G

-

T

-

L

M

G

A

I

V

T

G

Y

L

W

W

A

A

-

M

-

F

S

S

K

T

R

N

T

R

R

G

S

T

A

V

S

G

D

G

F

F

Y

F

T

L

A

A

G

G

G

R

G

S

I

M

S

V

G

W

F

W

Q

P

N

I

G

G

L

A

A

S

I

L

A

F

G

A

D

S

Y

N

M

I

S

G

A

S

A

G

A

H

F

F

L

V

G

G

L

L

S

A

G

G

M

T

-

G

-

A

-

S

-

G

V

I

F

A

A

T

K

G

G

G

F

F

D

E

G

W

V

N

I

A

Y

L

T

I

I

M

G

V

F

V

L

V

V

L

G

G

W

W

P

V

L

F

M

V

L

P

F

I

L

Y

I

I

A

-

E

-

R

-

L

-

R

-

N

R

L

A

G

G

R

V

F

V

T

T

F

M

A

P

D

E

V

Y

A

L

S

Q

Y

K

R

R

L

F

G

G

Q

G

T

K

P

R

I

I

R

Q

S

I

L

Y

A

L

A

S

V

I

G

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x
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C255 (≠ A263) modified: Disulfide link with 608
Q457 (≠ F443) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
T460 (≠ A446) mutation to W: Decreased affinity for glucose and phlorizin.

Sites not aligning to the query:

608 modified: Disulfide link with 255

Q9NY91 Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
22% identity, 37% coverage: 34:237/556 of query aligns to 24:227/659 of Q9NY91

query
sites
Q9NY91

R

R

Q

N

P

A

V

A

N

D

V

I

T

S

A

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I

I

A

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Y

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L

L

F

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V

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-

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T

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A

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Y

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W

A

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T

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A

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Y

F

T

L

A

A

G

G

G

R

G

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A

G

W

F

W

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M

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G

L

A

A

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I

L

A

F

G

A

D

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M

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A

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A

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A

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A

A

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-

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G

Sites not aligning to the query:

457 E→Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.

Query Sequence

>AZOBR_RS19235 AZOBR_RS19235 actetate permease
MSAARLLAAASAALLPVLVAGPVHAAAIDGAVERQPVNVTAIAMFLLFVAGTLGITYWAS
KRTRSASDFYTAGGGISGFQNGLAIAGDYMSAAAFLGLSGMVFAKGFDGVIYTIGFLVGW
PLMLFLIAERLRNLGRFTFADVASYRLGQTPIRSLAAVGSLTVVCFYLIAQMVGAGKLIQ
LLFGLDYTYAVVMVGVLMILYVTFGGMLATTWVQIIKAVMLLGGCTVLVGLALAQFGFNP
ERLLQQAVAAHAANAAILRPSAAMADPIAAVSLSLALMCGPAGLPHILMRFFTVPDAKEA
RKSVVYATGFIGYFFILTVTIGFLAIVIVGTNPAYLDAAGKILGGGNMAAIHLSKAIGGN
LFLGFISAVAFATILAVVAGLTLAGASAVSHDLYARVLKKGNATEASEMRVSRLATLALG
VIAITLGLLFENQNIAFMVGLAFGLAASVNFPVLILSIFWKGLTTRGAFIGGFAGLVSCV
AFVVLGPTVWVSVFKFPAPIFPYEHPALFSMVIAFATTWLFSVTDRSARAAAEAKAYEYQ
YIRSETGLGAASAASH

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