SitesBLAST

D54 (≠ E28) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
D57 (= D31) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
R103 (= R83) mutation to A: Loss of transport activity.

Sites not aligning to the query:

309 W→V: Loss of transport activity.
312 D→A: Loss of transport activity.
313 R→A: Loss of transport activity.
317 mutation I->H,Y: Loss of transport activity.
386 R→A: Loss of transport activity.

O42885 Putative inorganic phosphate transporter C8E4.01c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 42% coverage: 10:242/549 of query aligns to 40:288/572 of O42885

query
sites
O42885

L

L

T

T

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K

G

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K

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A

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Y

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-

G

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M

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G

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H

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Y

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G

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A

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A

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D

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Y

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A

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A

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N

K

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G

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Y

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I

-

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C

-

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R

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Y

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N

N

R

E

E

A

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-

H

-

Y

F

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K

A

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E

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G

-

V

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A

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-

P

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R

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E

E

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S

P

K

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S

F

Y

Q

E

Q

N

M

S

K

K

-

A

-

L

-

N

-

S

A

A

E

E

G

G

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G

D

S

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K

T

A

P

F

F

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R

N

D

T

S

D

L

D

K

E

D

D

G

-

N

N

L

M

K

K

Sites not aligning to the query:

12 modified: Phosphoserine
14 modified: Phosphoserine
292 modified: Phosphoserine
296 modified: Phosphoserine

A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
31% identity, 31% coverage: 73:244/549 of query aligns to 58:217/446 of A0A0H2VG78

query
sites
A0A0H2VG78

G

G

A

A

A

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R

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x
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E

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Q

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-

L

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Y

-

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-

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-

N

N

E

Y

A

A

F

F

-

A

-

D

-

I

E

E

A

G

W

W

G

R

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W

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G

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A

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-

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-

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E

E

S

S

P

P

-

R

-

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L

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L

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E

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N

M

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N

A

E

E

E

G

A

-

A

-

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K

Q

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M

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T

F

Y

R

D

D

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D

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N

E

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E

M

M

R102 (= R125) mutation to A: Loss of transport activity.
I105 (≠ Q128) mutation to S: Affects symport activity. May function as an uniporter.
E122 (= E145) mutation to A: Loss of transport activity.
Q137 (= Q160) mutation to A: Loss of transport activity.

Sites not aligning to the query:

22 D→N: Affects symport activity. May function as an uniporter.
250 Q→A: Loss of transport activity.
251 Q→A: Loss of transport activity.
256 N→A: Loss of transport activity.
357 W→A: Loss of transport activity.

Q09852 Putative inorganic phosphate transporter C23D3.12 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 40% coverage: 10:226/549 of query aligns to 38:264/559 of Q09852

query
sites
Q09852

L

L

T

T

K

K

G

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E

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D

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D

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Y

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-

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Q

Q

C

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F

A

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N

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-

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A

A

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G

N

K

K

Sites not aligning to the query:

297 modified: Phosphoserine
299 modified: Phosphoserine

P36035 Carboxylic acid transporter protein homolog from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 31% coverage: 68:237/549 of query aligns to 186:338/616 of P36035

query
sites
P36035

F

F

V

V

R

R

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S

F

A

G

G

A

A

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T

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D

N

D

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-

A

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A

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G

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W

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A

-

E

-

G

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D

D

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K
|
K

K338 (= K237) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
9 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

6rw3A The molecular basis for sugar import in malaria parasites. (see paper)
24% identity, 46% coverage: 73:325/549 of query aligns to 60:333/437 of 6rw3A

query
sites
6rw3A

G

G

A

C

A

G

F

F

F

S

G

G

S

Y

L

L

G

-

D

V

R

Q

I

F

G

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K

R

Y

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F

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N

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H

N

H

Y

F

A

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F

A

A

A

-

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-

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-

I

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L

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I

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L

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R

R

L

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A

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G

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A

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|
Q

C

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A

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A

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P

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E

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D

N

N

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D

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E

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-

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-

A

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E

-

A

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-

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-

N

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E

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-

A

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K

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-

S

L

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S

L

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S

L

A

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K

A

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A

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A

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A

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I

Y

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G

-

C

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-

L

G
x
Q

Q

Q

F

F

Y

T

A

G

L
x
I

F
x
N

F

V

L

L

-

V

-

S

-

N

S

S

S

N

M

E

L

L

K

Y

V

K

D

E

A

F

T

L

T

D

S

S

Y

H

L

L

L

I

-

T

I

I

A

L

A

S

A

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L

V

A

M

L

T

G

A

V

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P

N

F

F

F

L

I

M

F

T

F

F

G

P

-

A

-

I

W

Y

L

I

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E

R

K

I

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G

G

R

R

K

K

W

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I

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L

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A

W

G

G

C

C

L

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L

G

A

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A

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V

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T

A

Y

Y

I

L

P

P

binding beta-D-glucopyranose: Q138 (= Q160), Q264 (≠ G262), N270 (≠ F268)
binding alpha-D-glucopyranose: Q138 (= Q160), Q264 (≠ G262), I269 (≠ L267), N270 (≠ F268)

Sites not aligning to the query:

8et9A Cryo-em structure of the organic cation transporter 2 in complex with 1-methyl-4-phenylpyridinium (see paper)
35% identity, 19% coverage: 31:134/549 of query aligns to 122:214/517 of 8et9A

query
sites
8et9A

D

D

F

G

F

W

L

V

Y

Y

G

D

S

T

L

P

A

G

A

S

I

S

I

I

A

V

K

T

Q

E

F

F

F

N

S

L

G

V

V

C

N

A

E

D

T

S

T

W

G

M

M

L

I

D

F

L

A

V

L

Q

L

A

A

A

F

V

A

N

A

V

G

G

F

F

V

V

R

-

P

-

F

-

G

G

A

S

A

M

F

S

F

I

G

G

S

Y

L

I

G

A

D

D

R

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I

F

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G

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R

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K

Y

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F

L

L

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T

T

I

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N

G

A

I

I

S

S

T

G

F

V

L

L

V

M

G

A

V

V

L

A

P

P

N

N

Y

Y

A

T

S

W

I

-

G

-

F

-

A

-

P

-

V

-

I

-

L

M

I

L

I

I

L

F

R

R

L

L

A

I

Q

Q

G

G

L

L

A

V

M

S

G

K

G

G

Sites not aligning to the query:

binding 1-methyl-4-phenylpyridin-1-ium: 216, 240, 243, 430

Q9R0W2 Solute carrier family 22 member 2; Organic cation transporter 2; rOCT2 from Rattus norvegicus (Rat) (see paper)
45% identity, 12% coverage: 66:130/549 of query aligns to 159:212/555 of Q9R0W2

query
sites
Q9R0W2

G

G

F

F

V

I

R

-

P

-

F

-

G

G

A

A

A

M

F

M

F

I

G

G

S

Y

L

L

G

A

D

D

R

R

I

F

G

G

R

R

K

K

Y

F

T

C

F

L

L

L

V

V

T

T

I

I

L

L

I

I

M

N

G

A

I

I

S

S

T

G

F

A

L

L

V

M

G

A

V

I

L

S

P

P

N

N

Y

Y

A

A

S

W

I

-

G

-

F

-

A

-

P

-

V

-

I

-

L

M

I

L

I

V

L

F

R

R

L

F

A

L

Q

Q

G

G

L

L

Sites not aligning to the query:

451 Involved in recognition of organic cations and participates in structural changes that occur during translocation of organic cations; C→M: Transport activity strongly reduced.

Q63089 Solute carrier family 22 member 1; Organic cation transporter 1; rOCT1 from Rattus norvegicus (Rat) (see 4 papers)
31% identity, 19% coverage: 66:167/549 of query aligns to 159:249/556 of Q63089

query
sites
Q63089

G

G

F

F

V

L

R

-

P

-

F

-

G

G

A

S

A

L

F

V

G

G

S

Y

L

I

G

A

D

D

R

R

I

F

G

G

R

R

K

K

Y

L

T
x
C

F

L

L

L

V

V

T

T

I

T

L

L

I

V

M

T

G

S

I

V

S

S

T

G

F

V

L

L

V

T

G

A

V

V

L

A

P

P

N

D

Y

Y

A

T

S

S

I

-

G

-

F

-

A

-

P

-

V

-

I

-

L

M

I

L

L

F

R

R

L

L

A

L

Q

Q

G

G

L
x
M

A
x
V

M
x
S

G
x
K

G
|
G

E
x
S

Y
x
W

G
x
V

G
x
S

A
x
G

A
x
Y

T
|
T

Y
x
L

V
x
I

A
x
T

E
|
E

H
x
F

A
x
V

P

G

A

S

N

G

K

Y

R

R

G

R

L

T

Y

T

T

A

S

I

F

L

I

Y

Q

Q

C

M

T

A

A

F

T

T

L

V

G

G

L

L

C179 (≠ T89) mutation to A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; S-322; A-358; A-418; S-437; A-470 and A-474.
M212 (≠ L130) mutation to L: No change in TEA and MPP(+) uptake.
V213 (≠ A131) mutation to G: Decreased TEA uptake. No change in MPP(+) uptake.
S214 (≠ M132) mutation to G: Decreased TEA and MPP(+) uptake.
K215 (≠ G133) mutation to Q: Loss of TEA and MPP(+) uptake activity.; mutation to R: Loss of TEA and MPP(+) uptake activity.
G216 (= G134) mutation to A: Decreased TEA and MPP(+) uptake.
S217 (≠ E135) mutation to G: No change in TEA and MPP(+) uptake.
W218 (≠ Y136) mutation to F: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. No change in TEA and MPP(+) affinity. Decreased TEA Vmax. No change in MPP(+) Vmax.; mutation to L: Decreased guanidine, histamine, serotonin, TEA and MPP(+) uptake. Decreased TEA affinity. No change in MPP(+) affinity. Decreased TEA and MPP(+) Vmax.; mutation to Y: Decreased guanidine, histamine, serotonin and TEA uptake. No change in MPP(+) uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax.
V219 (≠ G137) mutation to L: No change in TEA and MPP(+) uptake.
S220 (≠ G138) mutation to I: Decreased TEA and MPP(+) uptake.
G221 (≠ A139) mutation to A: Decreased TEA and MPP(+) uptake.
Y222 (≠ A140) mutation to F: No change in guanidine, histamine, serotonin, TEA and MPP(+) uptake. Increased TEA affinity. No change in MPP(+) affinity. Decreased TEA Vmax. No change in MPP(+) Vmax.; mutation to L: Decreased guanidine, serotonin, TEA and MPP(+) uptake. No change in histamine uptake. Increased TEA and MPP(+) affinity. Decreased TEA and MPP(+) Vmax.
T223 (= T141) mutation to I: Decreased TEA uptake. No change in MPP(+) uptake.
L224 (≠ Y142) mutation to V: Decreased TEA and MPP(+) uptake.
I225 (≠ V143) mutation to G: No change in TEA and MPP(+) uptake.
T226 (≠ A144) mutation to A: Decreased TEA uptake. No change in MPP(+) uptake.
E227 (= E145) mutation to D: Loss of TEA and MPP(+) uptake activity.; mutation to Q: Loss of TEA and MPP(+) uptake activity.
F228 (≠ H146) mutation to I: No change in TEA and MPP(+) uptake.
V229 (≠ A147) mutation to A: Decreased TEA and MPP(+) uptake.; mutation to L: Loss of TEA and MPP(+) uptake activity.

Sites not aligning to the query:

26 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-155; A-179; S-322; A-358; A-418; S-437; A-470 and A-474.
155 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-179; S-322; A-358; A-418; S-437; A-470 and A-474.
286 S→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-292; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-292; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-292; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-292; A-296; A-328 and A-550.
292 S→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-296; A-328 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-296; A-328 and A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-296; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-296; A-328 and A-550.
296 T→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-328; A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-328; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-328 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-328 and A-550.
322 C→S: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with M-451. Choline affinity is increased fivefold by MMTS. Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; A-358; A-418; S-437; A-470 and A-474. Choline affinity is increased four- to fivefold; when associated with M-451.
328 S→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. No effect of PKA activation on ASP uptake. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-550. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-550. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-550. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-550.
358 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-418; S-437; A-470 and A-474.
418 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; S-437; A-470 and A-474.
437 C→S: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-470 and A-474.
451 C→M: Reduces the activation by MMTS. Abolishes the activation by MMTs; when associated with S-322. Abolishes the effect of MMTs on choline-induced currents. Choline affinity is not influenced by MMTS. Choline affinity is increased four- to fivefold; when associated with S-322.
470 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-474.
474 C→A: Choline affinity is increased fourfold by MMTS; when associated with A-26; A-155; A-179; S-322; A-358; A-418; A-437 and A-470.
475 D→E: Decreased MPP(+) uptake, no change in MPP(+) affinity. Decreased NMN uptake, increased NMN affinity. Decreased choline uptake, increased choline affinity.; D→N: Decreased MPP(+) uptake.; D→R: Decreased MPP(+) uptake.
550 T→A: No effect of PKC-induced stimulation on ASP uptake. No effect of PKC-induced stimulation on ASP uptake; when associated with A-286; A-292; A-296; A-328. Significant increase of the ASP uptake by PKA activation. No effect of PKA activation on ASP uptake; when associated with A-286; A-292; A-296 and A-328. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition. Significant reduction of ASP uptake by p56(lck) tyrosine kinase-induced inhibition; when associated with A-286; A-292; A-296; A-328. No significant effect on trafficking from intracellular pools to the cell membrane; when associated with A-286; A-292; A-296 and A-328. suppresses phosphorylation by PKC; when associated with A-286; A-292; A-296 and A-328.

O08966 Solute carrier family 22 member 1; Organic cation transporter 1; mOCT1 from Mus musculus (Mouse) (see paper)
31% identity, 19% coverage: 66:167/549 of query aligns to 159:249/556 of O08966

query
sites
O08966

G

G

F

F

V

L

R

-

P

-

F

-

G

G

A

S

A

L

F

V

G

G

S

Y

L

I

G

A

D

D

R

R

I

F

G

G

R

R

K

K

Y

L

T

C

F

L

L

L

V

V

T

T

I

T

L

L

I

V

M

T

G

S

I

L

S

S

T

G

F

V

L

L

V

T

G

A

V

V

L

A

P

P

N

D

Y

Y

A

T

S

S

I

-

G

-

F

-

A

-

P

-

V

-

I

-

L

M

I

L

L

F

R

R

L

L

A

L

Q

Q

G

G

L

M

A

V

M

S

G

K

G

G

E

S

Y

W

G

V

G

S

A

G

A

Y

T

T

Y

L

V

I

A

T

E

E

H

F

A

V

P

G

A

S

N

G

K

Y

R

R

G

R

L

T

Y

T

T

A

S

I

F

L

I

Y

Q

Q

C

V

T

A

A

F

T

T

L

V

G

G

L

L

Sites not aligning to the query:

32 L→F: Increased trospium uptake. Increased trospium affinity. No change in fenoterol uptake.
36 Y→C: Decreased fenoterol uptake. Decreased fenoterol affinity. No change in trospium uptake. No change in terbutaline affinity.

8et8A Cryo-em structure of the organic cation transporter 1 in complex with verapamil (see paper)
32% identity, 19% coverage: 66:169/549 of query aligns to 157:249/532 of 8et8A

query
sites
8et8A

G

G

F

F

V

L

R

G

P

S

F

L

G

G

A

V

A

-

F

-

G

G

S

Y

L

I

G

A

D

D

R

R

I

F

G

G

R

R

K

K

Y

L

T

C

F

L

L

L

V

A

T

T

I

T

L

L

I

I

M

S

G

A

I

V

S

S

T

G

F

V

L

L

V

M

G

A

V

V

L

A

P

P

N

D

Y

Y

A

T

S

S

I

-

G

-

F

-

A

-

P

-

V

-

I

-

L

M

I

L

L

F

R

R

L

L

A

L

Q

Q

G

G

L

L

A

V

M

S

G
x
K

G

G

E

S

Y
x
W

G

M

G

S

A

G

A

Y

T

T

Y

L

V

I

A

T

E

E

H

F

A

V

P

G

A

S

N

G

K

Y

R

R

G

R

L

T

Y

V

T

A

S

I

F

L

I

Y

Q
|
Q

C

M

T

A

A

F

T

T

L

V

G

G

L

L

F

V

M

L

binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: K213 (≠ G133), W216 (≠ Y136), Q240 (= Q160)

Sites not aligning to the query:

binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: 31, 35, 353, 360, 378, 381, 385, 449, 469

8et7A Cryo-em structure of the organic cation transporter 1 in complex with diphenhydramine (see paper)
32% identity, 19% coverage: 66:169/549 of query aligns to 157:249/532 of 8et7A

query
sites
8et7A

G

G

F

F

V

L

R

G

P

S

F

L

G

G

A

V

A

-

F

-

G

G

S

Y

L

I

G

A

D

D

R

R

I

F

G

G

R

R

K

K

Y

L

T

C

F

L

L

L

V

A

T

T

I

T

L

L

I

I

M

S

G

A

I

V

S

S

T

G

F

V

L

L

V

M

G

A

V

V

L

A

P

P

N

D

Y

Y

A

T

S

S

I

-

G

-

F

-

A

-

P

-

V

-

I

-

L

M

I

L

L

F

R

R

L

L

A

L

Q

Q

G

G

L

L

A

V

M

S

G

K

G

G

E

S

Y

W

G

M

G

S

A

G

A

Y

T

T

Y

L

V

I

A

T

E

E

H

F

A

V

P

G

A

S

N

G

K

Y

R

R

G

R

L

T

Y

V

T

A

S

I

F

L

I

Y

Q

Q

C

M

T

A

A

F

T

T

L

V

G

G

L

L

F

V

M

L

Sites not aligning to the query:

binding n-[2-(benzhydryloxy)ethyl]-n,n-dimethylamine: 35, 385, 445

O15245 Solute carrier family 22 member 1; Organic cation transporter 1; hOCT1 from Homo sapiens (Human) (see 10 papers)
27% identity, 25% coverage: 31:167/549 of query aligns to 123:248/554 of O15245

query
sites
O15245

D

D

F

G

F

W

L

V

Y

Y

G

D

S

T

L

P

A

G

A

S

I

S

I

I

A

V

K

T

Q

E

F

F

F

N

S

L

G

V

V

C

N

A

E

D

T

S

T

W

G

K

M

L

I

D

F

L

A

F

L

Q

L

S

A

C

F

L

A

N

A

A

G

G

F

F

F
x
L

V

-

R

-

P

-

F

F

G

G

A

S

A

L

F

G

F

V

G

G

S

Y

L

F

G

A

D

D

R

R

I

F

G

G

R

R

K

K

Y

L

T

C

F

L

L

L

V

G

T

T

I

V

L

L

I

V

M

N

G

A

I

V

S
|
S

T

G

F

V

L

L

V

M

G

A

V

F

L

S

P

P

N

N

Y

Y

A

M

S

S

I

-

G

-

F

-

A

-

P

-

V

-

I

-

L

M

I

L

L

F

R

R

L

L

A

L

Q

Q

G

G

L

L

A

V

M

S

G

K

G

G

E

N

Y

W

G

M

G

A

A
x
G

A

Y

T

T

Y

L

V

I

A

T

E

E

H

F

A

V

P

G

A

S

N

G

K

S

R

R

G

R

L

T

Y

V

T

A

S

I

F

M

I
x
Y

Q

Q

C

M

T

A

A

F

T

T

L

V

G

G

L

L

L160 (≠ F68) to F: no changes in both MPP(+) and TEA uptake; abolishes MPP(+) uptake when associated with S-401; largely localized to the plasma membrane; dbSNP:rs683369
S189 (= S100) to L: no changes in MPP(+) uptake; dbSNP:rs34104736
G220 (≠ A139) to V: affects transporter activity; reduction of MPP(+) uptake when associated with V-408; dbSNP:rs36103319
Y240 (≠ I159) mutation to F: Decreased TEA uptake.

Sites not aligning to the query:

14 S → F: exclusively found in the African American population; increased MPP(+) uptake when associated with V-408; dbSNP:rs34447885
24 I→L: No change in fenoterol uptake. No change in trospium uptake. No change in terbutaline uptake.
28 L→I: No change in fenoterol uptake. No change in trospium uptake. No change in terbutaline uptake.
31 A→S: No change in fenoterol uptake. No change in trospium uptake. No change in terbutaline uptake.
32 F→L: No change in fenoterol uptake. Decreased trospium uptake. Decreased trospium affinity.
36 C→Y: Increased fenoterol uptake. Increased fenoterol affinity. No change in trospium uptake. No change in terbutaline uptake. No change in terbutaline affinity.
41 F → L: in dbSNP:rs2297373
61 R → C: affects transporter activity; reduction of MPP(+) uptake; reduction of serum O-isobutanoyl-(R)-carnitine levels; reduction of MPP(+) uptake when associated with V-408; dbSNP:rs12208357
85 L → F: no changes in MPP(+) uptake; when associated with V-408; dbSNP:rs35546288
88 C → R: affects transporter activity; reduction of MPP(+), serotonin and TEA uptake; dbSNP:rs55918055
283 P → L: in dbSNP:rs4646277; P→A: Decreased TEA uptake.
287 R → G: in dbSNP:rs4646278
341 P → L: affects transporter activity; reduction of TEA uptake; reduction o MPP(+) uptake when associated with V-408; largely localized to the plasma membrane; dbSNP:rs2282143
342 R → H: no changes in MPP(+) uptake when associated with V-408; dbSNP:rs34205214
361 Y→F: Decreased TEA uptake.
376 Y→F: Decreased TEA uptake.
401 G → S: affects transporter activity; reduction of MPP(+), serotonin and TEA uptake; no MPP(+) uptake when associated with L-160; dbSNP:rs34130495
408 M → V: does not affect transporter activity; no changes in MPP(+) uptake when associated with F-14; no changes in MPP(+) uptake when associated with F-85; no changes in MPP(+) uptake when associated with L-189; no changes in MPP(+) uptake when associated with H-342; no changes in MPP(+) uptake when associated with M-420 del; no changes in MPP(+) uptake when associated with I-440; no changes in MPP(+) uptake when associated with I-461; no changes in MPP(+) uptake when associated with M-488; reduction of MPP uptake when associated with C-61; no MPP(+) uptake when associated with V-220; reduction of MPP(+) uptake when associated with L-341; no MPP(+) uptake when associated with S-401; no MPP(+) uptake when associated with R-465; dbSNP:rs628031
420 natural variant: Missing (reduction of serum O-isobutanoyl-(R)-carnitine levels; no change in MPP(+) uptake; no changes in MPP(+) uptake when associated with V-408; dbSNP:rs72552763)
440 M → I: in dbSNP:rs35956182
461 V → I: no changes in MPP(+) uptake when associated with V-408; dbSNP:rs34295611
465 G → R: reduction of the localization to the basolateral membrane; no MPP(+) uptake when associated with V-408; dbSNP:rs34059508; G→A: No changes in MPP(+) uptake.
488 R → M: no changes in MPP(+) uptake when associated with V-408; dbSNP:rs35270274

8fvzA Pipt y150a
25% identity, 29% coverage: 16:175/549 of query aligns to 4:160/433 of 8fvzA

query
sites
8fvzA

K

K

V

L

I

V

F

L

A

L

S

A

S

G

L

V

G

G

T

F

V

F

F

L

E

D

W

A

Y

Y

D

D

F

L

F

F

L

I

Y

I

G

N

S

Q

L

V

A

A

A

P

I

M

I

L

A

A

K

Q

Q

V

F

Y

F

F

S

-

G

-

V

-

N

-

E

P

T

K

T

T

G

G

M

L

-

P

-

A

I

Q

F

R

A

Q

L

D

L

L

A

M

F

K

A

A

G

A

F

N

F

I

V

G

R

C

P

V

F

V

G

G

A

Q

A

V

F

M

F

F

G

G

S

V

L

L

G

G

D

D

R

S

I

F

G

G

R

R

K

K

Y

F

T

V

F

Y

L

G

V

K

T

E

I

L

L

I

I

L

M

I

G

I

I

V

S

A

T

T

F

I

L

F

V

Q

G

M

V

S

L

A

P

P

N

S

Y

H

A

W

S

D

I

-

G

G

F

N

A

R

A

V

P

L

V

T

I

W

L

I

I

T

I

I

L

C

R

R

L

V

A

F

Q

L

G

G

L

I

A

G

M

I

G

G

E

D

Y

A

G

P

G

M

A

S

A

A

T

T

Y

V

V

V

A

S

E

D

H

R

A

A

P

N

A

I

N

H

K

R

R

R

G

G

L

T

Y

L

T

L

S

C

F

F

I

I

Q
x
F

C

A

T

N

A

Q

T

G

L

W

G

G

L

S

F

F

M

V

S

G

L

S

L

L

I

V

I

T

L

I

binding phosphate ion: F145 (≠ Q160)

Sites not aligning to the query:

binding phosphate ion: 235, 239, 243, 346

8jtzA Hoct1 in complex with spironolactone in outward facing partially occluded conformation (see paper)
27% identity, 25% coverage: 31:167/549 of query aligns to 121:246/530 of 8jtzA

query
sites
8jtzA

D

D

F

G

F

W

L

V

Y

Y

G

D

S

T

L

P

A

G

A

S

I

S

I

I

A

V

K

T

Q

E

F

F

F

N

S

L

G

V

V

C

N

A

E

D

T

S

T

W

G

K

M

L

I

D

F

L

A

F

L

Q

L

S

A

C

F

L

A

N

A

A

G

G

F

F

F

L

V

-

R

-

P

-

F

F

G

G

A

S

A

L

F

G

F

V

G

G

S

Y

L

F

G

A

D

D

R

R

I

F

G

G

R

R

K

K

Y

L

T

C

F

L

L

L

V

G

T

T

I

V

L

L

I

V

M

N

G

A

I

V

S

S

T

G

F

V

L

L

V

M

G

A

V

F

L

S

P

P

N

N

Y

Y

A

M

S

S

I

-

G

-

F

-

A

-

P

-

V

-

I

-

L

M

I

L

L

F

R

R

L

L

A

L

Q

Q

G

G

L

L

A

V

M

S

G
x
K

G

G

E

N

Y
x
W

G

M

G

A

A

G

A

Y

T

T

Y

L

V

I

A

T

E

E

H

F

A

V

P

G

A

S

N

G

K

S

R

R

G

R

L

T

Y

V

T

A

S

I

F

M

I

Y

Q
|
Q

C

M

T

A

A
x
F

T

T

L

V

G

G

L

L

binding spironolactone: K212 (≠ G133), W215 (≠ Y136), Q239 (= Q160), F242 (≠ A163)

Sites not aligning to the query:

binding spironolactone: 441, 444, 445, 471

8jttA Hoct1 in complex with metformin in outward occluded conformation (see paper)
32% identity, 19% coverage: 65:167/549 of query aligns to 79:170/454 of 8jttA

query
sites
8jttA

A

A

G

G

F

F

F

L

V

-

R

-

P

-

F

F

G

G

A

S

A

L

F

G

F

V

G

G

S

Y

L

F

G

A

D

D

R

R

I

F

G

G

R

R

K

K

Y

L

T

C

F

L

L

L

V

G

T

T

I

V

L

L

I

V

M

N

G

A

I

V

S

S

T

G

F

V

L

L

V

M

G

A

V

F

L

S

P

P

N

N

Y

Y

A

M

S

S

I

-

G

-

F

-

A

-

P

-

V

-

I

-

L

M

I

L

L

F

R

R

L

L

A

L

Q

Q

G

G

L

L

A

V

M

S

G

K

G

G

E

N

Y

W

G

M

G

A

A

G

A

Y

T

T

Y

L

V

I

A

T

E

E

H

F

A

V

P

G

A

S

N

G

K

S

R

R

G

R

L

T

Y

V

T

A

S

I

F

M

I

Y

Q

Q

C

M

T

A

A

F

T

T

L

V

G

G

L

L

Sites not aligning to the query:

binding Metformin: 34, 283

Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
25% identity, 26% coverage: 78:219/549 of query aligns to 78:204/452 of Q5EXK5

query
sites
Q5EXK5

G

G

S

P

L

L

G

S

D
|
D

R

R

I

F

G

G

R

R

K

K

Y

R

T

V

F

I

L

E

V

F

T

C

I

V

L

A

I

L

M

F

G

G

I

L

S

F

T

S

F

L

L

L

V

S

G

A

V

F

L

A

P

P

N

D

Y

L

A

Q

S

-

I

-

G

-

F

-

A

-

P

-

V

-

I

M

L

L

I

V

I

F

L

L

R

R

L

F

A

L

Q

T

G

G

L

L

A

G

M

L

G

G

E

A

Y

M

G

P

G

N

A

T

A

I

T

T

Y

M

V

T

A

S

E

E

H

Y

A

L

P

P

A

A

N

R

K

R

R

R

G

G

L

A

Y

L

T

V

S

T

F

L

I

M

Q

F

C

C

T

G

A

F

T

T

L

L

G

G

L

S

F

A

M

F

S

G

L

G

L

V

I

V

I

S

L

A

A

Q

C

L

R

V

Y

P

F

L

L

I

G

G

N

W

E

H

A

G

F

I

E

L

A

V

W

L

G

G

W

G

R

V

I

L

P

P

F

L

L

I

V

L

S

A

I

V

V

A

L

L

L

V

G

P

I

L

S

-

V

-

W

-

I

-

R

-

L

-

Q

-

L

L

S

P

E

E

S

S

P

P

L

R

F

W

Q

Q

D82 (= D82) mutation to A: Loss of activity.

Sites not aligning to the query:

311 V→W: Loss of activity.
314 D→A: Loss of activity.

8sc2A Human oct1 bound to diltiazem in inward-open conformation (see paper)
32% identity, 19% coverage: 65:167/549 of query aligns to 139:230/453 of 8sc2A

query
sites
8sc2A

A

A

G

G

F

F

F

L

V

-

R

-

P

-

F

F

G

G

A

S

A

L

F

G

F

V

G

G

S

Y

L

F

G

A

D

D

R

R

I

F

G

G

R

R

K

K

Y

L

T

C

F

L

L

L

V

G

T

T

I

V

L

L

I

V

M

N

G

A

I

V

S

S

T

G

F

V

L

L

V

M

G

A

V

F

L

S

P

P

N

N

Y

Y

A

M

S

S

I

-

G

-

F

-

A

-

P

-

V

-

I

-

L

M

I

L

L

F

R

R

L

L

A

L

Q

Q

G

G

L

L

A

V

M

S

G

K

G

G

E

N

Y
x
W

G

M

G

A

A

G

A

Y

T

T

Y

L

V

I

A

T

E

E

H

F

A

V

P

G

A

S

N

G

K

S

R

R

G

R

L

T

Y

V

T

A

S

I

F

M

I

Y

Q
|
Q

C

M

T

A

A
x
F

T

T

L

V

G

G

L

L

binding Diltiazem: W199 (≠ Y136), Q223 (= Q160), F226 (≠ A163)

Sites not aligning to the query:

binding Diltiazem: 18, 293, 297, 385

8sc6A Human oct1 bound to thiamine in inward-open conformation (see paper)
32% identity, 19% coverage: 65:167/549 of query aligns to 139:230/447 of 8sc6A

query
sites
8sc6A

A

A

G

G

F

F

F

L

V

-

R

-

P

-

F

F

G

G

A

S

A

L

F

G

F

V

G

G

S

Y

L

F

G

A

D

D

R

R

I

F

G

G

R

R

K

K

Y

L

T

C

F

L

L

L

V

G

T

T

I

V

L

L

I

V

M

N

G

A

I

V

S

S

T

G

F

V

L

L

V

M

G

A

V

F

L

S

P

P

N

N

Y

Y

A

M

S

S

I

-

G

-

F

-

A

-

P

-

V

-

I

-

L

M

I

L

L

F

R

R

L

L

A

L

Q

Q

G

G

L

L

A

V

M

S

G

K

G

G

E

N

Y

W

G

M

G

A

A

G

A

Y

T

T

Y

L

V

I

A

T

E

E

H

F

A

V

P

G

A

S

N

G

K

S

R

R

G

R

L

T

Y

V

T

A

S

I

F

M

I

Y

Q
|
Q

C

M

T

A

A
x
F

T

T

L

V

G

G

L

L

binding 3-(4-amino-2-methyl-pyrimidin-5-ylmethyl)-5-(2-hydroxy-ethyl)-4-methyl-thiazol-3-ium: Q223 (= Q160), F226 (≠ A163)

Sites not aligning to the query:

binding 3-(4-amino-2-methyl-pyrimidin-5-ylmethyl)-5-(2-hydroxy-ethyl)-4-methyl-thiazol-3-ium: 293, 294, 318, 378, 379

Query Sequence

>WP_057507085.1 NCBI__GCF_001431535.1:WP_057507085.1
MSTTPAPAQLTKGHKKVIFASSLGTVFEWYDFFLYGSLAAIIAKQFFSGVNETTGMIFAL
LAFAAGFFVRPFGAAFFGSLGDRIGRKYTFLVTILIMGISTFLVGVLPNYASIGFAAPVI
LIILRLAQGLAMGGEYGGAATYVAEHAPANKRGLYTSFIQCTATLGLFMSLLIILACRYF
LGNEAFEAWGWRIPFLVSIVLLGISVWIRLQLSESPLFQQMKAEGKGSKTPFRDSLKDGN
LKLMLLVLLGAAAGQAVVWYGGQFYALFFLSSMLKVDATTSYLLIAAALALGVPFFIFFG
WLSDRIGRKWIILAGCLLAAVTYIPVFKGLTHFANPAIEEARSSSPALVIADPNTCSFQF
DPVGLRKFTSSCDVATAALTKAGVPYDVQPAPAGSLAVVNVGTSKVSSYEAAGLAKEDGK
AKADAFGTELKAALVEAGYPAKADNARINIPGTIFMLWILVLYVTMVYGPIAAYLVELFP
TRIRYTSMSLPYHIGNGWFGGFLPAISFALVAGTGNLYYGLWYPIAIALMTVVIGGLFLH
DTKNVDITK

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