SitesBLAST

Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
24% identity, 40% coverage: 9:227/553 of query aligns to 32:231/444 of Q8NLB7

query
sites
Q8NLB7

T

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D

D54 (≠ E31) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
D57 (= D34) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
R103 (≠ L86) 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.

P25297 Inorganic phosphate transporter PHO84 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
22% identity, 56% coverage: 16:322/553 of query aligns to 61:428/587 of P25297

query
sites
P25297

E

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K298 (vs. gap) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Sites not aligning to the query:

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

O08966 Solute carrier family 22 member 1; Organic cation transporter 1; mOCT1 from Mus musculus (Mouse) (see paper)
28% identity, 31% coverage: 75:247/553 of query aligns to 162:313/556 of O08966

query
sites
O08966

F

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V

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.

Q63089 Solute carrier family 22 member 1; Organic cation transporter 1; rOCT1 from Rattus norvegicus (Rat) (see 4 papers)
28% identity, 29% coverage: 75:233/553 of query aligns to 162:299/556 of Q63089

query
sites
Q63089

F

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G

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A

C179 (≠ T92) 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 (≠ L133) mutation to L: No change in TEA and MPP(+) uptake.
V213 (≠ A134) mutation to G: Decreased TEA uptake. No change in MPP(+) uptake.
S214 (≠ L135) mutation to G: Decreased TEA and MPP(+) uptake.
K215 (≠ G136) mutation to Q: Loss of TEA and MPP(+) uptake activity.; mutation to R: Loss of TEA and MPP(+) uptake activity.
G216 (= G137) mutation to A: Decreased TEA and MPP(+) uptake.
S217 (≠ E138) mutation to G: No change in TEA and MPP(+) uptake.
W218 (≠ Y139) 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 (≠ G140) mutation to L: No change in TEA and MPP(+) uptake.
S220 (≠ G141) mutation to I: Decreased TEA and MPP(+) uptake.
G221 (≠ A142) mutation to A: Decreased TEA and MPP(+) uptake.
Y222 (≠ A143) 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 (= T144) mutation to I: Decreased TEA uptake. No change in MPP(+) uptake.
L224 (≠ Y145) mutation to V: Decreased TEA and MPP(+) uptake.
I225 (≠ V146) mutation to G: No change in TEA and MPP(+) uptake.
T226 (≠ A147) mutation to A: Decreased TEA uptake. No change in MPP(+) uptake.
E227 (= E148) mutation to D: Loss of TEA and MPP(+) uptake activity.; mutation to Q: Loss of TEA and MPP(+) uptake activity.
F228 (≠ H149) mutation to I: No change in TEA and MPP(+) uptake.
V229 (≠ A150) mutation to A: Decreased TEA and MPP(+) uptake.; mutation to L: Loss of TEA and MPP(+) uptake activity.
S286 (= S218) mutation to 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.
S292 (≠ A226) mutation to 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.
T296 (= T230) mutation to 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.

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.
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.

6rw3A The molecular basis for sugar import in malaria parasites. (see paper)
25% identity, 47% coverage: 68:329/553 of query aligns to 64:333/437 of 6rw3A

query
sites
6rw3A

A

S

G

G

F

Y

I

L

V

V

R

Q

P

-

F

F

G

G

A

R

L

-

V

-

F

-

G

-

R

R

L

L

G

S

D

L

L

L

V

I

G

I

R

Y

K

N

Y

F

T

F

F

F

L

L

V

V

T

S

I

I

L

L

I

-

M

-

G

-

A

-

S

-

T

-

F

-

I

-

V

T

G

S

V

I

L

T

P

H

N

H

Y

F

N

H

S

T

I

I

G

-

I

-

T

-

A

-

P

-

I

-

L

-

I

L

I

F

L

A

R

R

I

L

L

L

Q

S

G

G

L

F

A

G

L

I

G

G

G

L

E

V

Y

T

G

V

G

S

A

V

A

P

T

M

Y

Y

V

I

A

S

E

E

H

M

A

T

P

H

E

K

G

D

R

K

G

G

S

A

F

Y

T

G

A

V

W

M

I

H

Q
|
Q

T

L

T

F

A

I

T

T

M

F

G

G

L

I

F

F

L

V

S

A

L

-

V

V

I

M

L

L

G

G

V

L

R

-

T

-

A

A

V

M

G

G

E

E

A

T

A

S

F

F

A

A

D

K

W

L

G

W

W

W

R

R

I

L

P

M

F

F

L

L

-

F

-

P

-

S

-

V

V

I

S

S

I

L

L

I

-

G

L

I

L

L

A

A

I

L

S

V

V

V

W

F

I

F

R

K

M

-

S

-

M

-

N

E

E

E

S

T

P

P

A

Y

F

F

L

L

K

F

M

E

K

K

A

G

E

R

G

I

K

E

T

E

S

S

K

K

-

N

-

I

-

L

-

K

-

I

-

Y

-

E

-

T

-

D

-

N

-

V

-

D

A

E

P

P

L

L

T

N

-

A

-

I

-

K

E

E

A

A

F

V

G

E

Q

Q

W

N

K

E

N

S

L

A

K

K

-

K

-

N

-

S

L

L

V

S

I

L

L

L

A

S

L

A

V

L

G

K

L

I

T

P

A

S

G

Y

Q

R

A

Y

V

V

V

I

-

I

-

L

-

G

-

C

-

L

-

S

-

G

-

L

-
x
Q

W

Q

Y

F

T

T

G

G

Q
x
I

F
x
N

Y

V

A

L

L

V

F

S

F

N

L

S

T

N

Q

E

T

L

L

Y

K

K

V

E

D

F

G

L

P

D

T

S

A

H

N

L

I

I

L

T

I

I

A

L

A

S

A

V

L

V

L

M

L

T

A

A

T

V

P

N

F

F

F

L

L

M

F

T

F

F

G

P

S

A

-

I

-

Y

L

I

S

V

D

E

K

K

I

L

G

G

R

R

K

K

P

T

I

L

L

L

G

W

G

G

C

C

L

V

I

G

A

V

A

L

V

V

T

A

Y

Y

F

L

P

P

binding beta-D-glucopyranose: Q138 (= Q163), Q264 (vs. gap), N270 (≠ F268)
binding alpha-D-glucopyranose: Q138 (= Q163), Q264 (vs. gap), I269 (≠ Q267), N270 (≠ F268)

Sites not aligning to the query:

O15245 Solute carrier family 22 member 1; Organic cation transporter 1; hOCT1 from Homo sapiens (Human) (see 10 papers)
32% identity, 19% coverage: 68:170/553 of query aligns to 157:248/554 of O15245

query
sites
O15245

A

A

G

G

F

F

I
x
L

V

-

R

-

P

-

F

F

G

G

A

S

L

L

V

G

F

V

G

G

R

Y

L

F

G

A

D

D

L

R

V

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

A

V

S
|
S

T

G

F

V

I

L

V

M

G

A

V

F

L

S

P

P

N

N

Y

Y

N

M

S

S

I

-

G

-

I

-

T

-

A

-

P

-

I

-

L

M

I

L

L

F

R

R

I

L

L

L

Q

Q

G

G

L

L

A

V

L

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

E

S

G

G

R

S

R

R

G

R

S

T

F

V

T

A

A

I

W

M

I
x
Y

Q

Q

T

M

T

A

A

F

T

T

M

V

G

G

L

L

L160 (≠ I71) 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 (= S103) to L: no changes in MPP(+) uptake; dbSNP:rs34104736
G220 (≠ A142) to V: affects transporter activity; reduction of MPP(+) uptake when associated with V-408; dbSNP:rs36103319
Y240 (≠ I162) 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

8et8A Cryo-em structure of the organic cation transporter 1 in complex with verapamil (see paper)
28% identity, 31% coverage: 75:247/553 of query aligns to 160:311/532 of 8et8A

query
sites
8et8A

F

L

G

G

A

S

L

L

V

G

F

V

G

G

R

Y

L

I

G

A

D

D

L

R

V

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

A

V

S

S

T

G

F

V

I

L

V

M

G

A

V

V

L

A

P

P

N

D

Y

Y

N

T

S

S

I

-

G

-

I

-

T

-

A

-

P

-

I

-

L

M

I

L

L

F

R

R

I

L

L

L

Q

Q

G

G

L

L

A

V

L

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

E

S

G

G

R

Y

R

R

G

R

S

T

F

V

T

A

A

I

W

L

I

Y

Q
|
Q

T

M

T

A

A

F

T

T

M

V

G

G

L

L

F

V

L

L

S

-

L

-

V

-

I

L

L

S

G

G

V

V

R

A

T

Y

A

A

V

I

G

-

E

-

A

-

F

-

A

P

D

H

W

W

G

R

W

W

-

L

R

Q

I

L

P

A

F

V

L

S

V

L

S

P

I

T

L

F

L

L

L

F

A

L

I

L

S

Y

V

Y

W

W

I

-

R

-

M

-

S

C

M

V

N

P

E

E

S

S

P

P

A

R

F

W

L

L

K

-

M

L

K

S

A

Q

E

K

G

R

K

N

T

T

S

Q

K

A

A

I

P

K

L

I

T

M

E

D

A

H

F

I

G

A

Q

Q

W

-

K

K

N

N

L

G

K

K

L

L

binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: K213 (≠ G136), W216 (≠ Y139), Q240 (= Q163)

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)
28% identity, 31% coverage: 75:247/553 of query aligns to 160:311/532 of 8et7A

query
sites
8et7A

F

L

G

G

A

S

L

L

V

G

F

V

G

G

R

Y

L

I

G

A

D

D

L

R

V

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

A

V

S

S

T

G

F

V

I

L

V

M

G

A

V

V

L

A

P

P

N

D

Y

Y

N

T

S

S

I

-

G

-

I

-

T

-

A

-

P

-

I

-

L

M

I

L

L

F

R

R

I

L

L

L

Q

Q

G

G

L

L

A

V

L

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

E

S

G

G

R

Y

R

R

G

R

S

T

F

V

T

A

A

I

W

L

I

Y

Q

Q

T

M

T

A

A

F

T

T

M

V

G

G

L

L

F

V

L

L

S

-

L

-

V

-

I

L

L

S

G

G

V

V

R

A

T

Y

A

A

V

I

G

-

E

-

A

-

F

-

A

P

D

H

W

W

G

R

W

W

-

L

R

Q

I

L

P

A

F

V

L

S

V

L

S

P

I

T

L

F

L

L

L

F

A

L

I

L

S

Y

V

Y

W

W

I

-

R

-

M

-

S

C

M

V

N

P

E

E

S

S

P

P

A

R

F

W

L

L

K

-

M

L

K

S

A

Q

E

K

G

R

K

N

T

T

S

Q

K

A

A

I

P

K

L

I

T

M

E

D

A

H

F

I

G

A

Q

Q

W

-

K

K

N

N

L

G

K

K

L

L

Sites not aligning to the query:

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

8sc2A Human oct1 bound to diltiazem in inward-open conformation (see paper)
32% identity, 19% coverage: 68:170/553 of query aligns to 139:230/453 of 8sc2A

query
sites
8sc2A

A

A

G

G

F

F

I

L

V

-

R

-

P

-

F

F

G

G

A

S

L

L

V

G

F

V

G

G

R

Y

L

F

G

A

D

D

L

R

V

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

A

V

S

S

T

G

F

V

I

L

V

M

G

A

V

F

L

S

P

P

N

N

Y

Y

N

M

S

S

I

-

G

-

I

-

T

-

A

-

P

-

I

-

L

M

I

L

L

F

R

R

I

L

L

L

Q

Q

G

G

L

L

A

V

L

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

E

S

G

G

R

S

R

R

G

R

S

T

F

V

T

A

A

I

W

M

I

Y

Q
|
Q

T

M

T

A

A
x
F

T

T

M

V

G

G

L

L

binding Diltiazem: W199 (≠ Y139), Q223 (= Q163), F226 (≠ A166)

Sites not aligning to the query:

binding Diltiazem: 18, 293, 297, 385

8sc3A Human oct1 bound to fenoterol in inward-open conformation (see paper)
32% identity, 19% coverage: 68:170/553 of query aligns to 139:230/445 of 8sc3A

query
sites
8sc3A

A

A

G

G

F

F

I

L

V

-

R

-

P

-

F

F

G

G

A

S

L

L

V

G

F

V

G

G

R

Y

L

F

G

A

D

D

L

R

V

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

A

V

S

S

T

G

F

V

I

L

V

M

G

A

V

F

L

S

P

P

N

N

Y

Y

N

M

S

S

I

-

G

-

I

-

T

-

A

-

P

-

I

-

L

M

I

L

L

F

R

R

I

L

L

L

Q

Q

G

G

L

L

A

V

L

S

G

K

G

G

E

N

Y
x
W

G
x
M

G

A

A

G

A

Y

T

T

Y

L

V

I

A

T

E

E

H

F

A

V

P

G

E

S

G

G

R

S

R

R

G

R

S

T

F

V

T

A

A

I

W

M

I

Y

Q
|
Q

T

M

T

A

A
x
F

T

T

M

V

G

G

L

L

binding Fenoterol: W199 (≠ Y139), M200 (≠ G140), Q223 (= Q163), F226 (≠ A166)

Sites not aligning to the query:

binding Fenoterol: 284, 291, 376, 380

8sc6A Human oct1 bound to thiamine in inward-open conformation (see paper)
32% identity, 19% coverage: 68:170/553 of query aligns to 139:230/447 of 8sc6A

query
sites
8sc6A

A

A

G

G

F

F

I

L

V

-

R

-

P

-

F

F

G

G

A

S

L

L

V

G

F

V

G

G

R

Y

L

F

G

A

D

D

L

R

V

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

A

V

S

S

T

G

F

V

I

L

V

M

G

A

V

F

L

S

P

P

N

N

Y

Y

N

M

S

S

I

-

G

-

I

-

T

-

A

-

P

-

I

-

L

M

I

L

L

F

R

R

I

L

L

L

Q

Q

G

G

L

L

A

V

L

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

E

S

G

G

R

S

R

R

G

R

S

T

F

V

T

A

A

I

W

M

I

Y

Q
|
Q

T

M

T

A

A
x
F

T

T

M

V

G

G

L

L

binding 3-(4-amino-2-methyl-pyrimidin-5-ylmethyl)-5-(2-hydroxy-ethyl)-4-methyl-thiazol-3-ium: Q223 (= Q163), F226 (≠ A166)

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

P36035 Carboxylic acid transporter protein homolog from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
24% identity, 28% coverage: 72:224/553 of query aligns to 187:325/616 of P36035

query
sites
P36035

V

V

R

R

P

S

F

A

G

G

A

A

L

V

V

I

F

F

G

G

R

L

L

W

G

T

D

D

L

K

V

S

G

S

R

R

K

K

Y

W

T

P

F

Y

L

I

V

T

T

C

I

L

L

F

I

L

M

F

G

V

A

I

S

A

T

Q

F

L

I

C

V

T

G

P

V

W

L

C

P

D

N

T

Y

Y

N

E

S

K

I

-

G

-

I

-

T

-

A

-

P

-

I

-

L

F

I

L

I

G

L

V

R

R

I

W

L

I

Q

T

G

G

L

I

A

A

L

M

G

G

E

I

Y

Y

G

G

G

C

A

A

A

S

T

A

Y

T

V

A

A

I

E

E

H

D

A

A

P

P

E

V

G

K

R

A

R

R

G

S

S

F

F

L

T

S

A

G

W

L

I

F

Q

F

T

S

T

A

A

Y

T

A

M

M

G

G

L

F

F

I

L

F

S

A

L

I

V

F

I

Y

L

R

G

A

V

F

R

-

T

-

A

-

V

-

G

-

E

-

A

G

A

Y

F

F

A

R

D

D

W

D

G

G

W

W

R

K

I

I

P

L

F

F

L

W

V

F

S

S

I

I

L

F

L

L

L

P

A

I

I

L

S

L

V

I

W

F

I

W

R

R

M

L

S

L

M

W

N

P

E

E

S

T

P

K

A

Y

F

F

L

T

K

K

M

V

Sites not aligning to the query:

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

Q9C757 Probable inositol transporter 2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
23% identity, 53% coverage: 85:376/553 of query aligns to 93:425/580 of Q9C757

query
sites
Q9C757

D

D

L

K

V

L

G

G

R

R

K

R

Y

S

T

A

F

I

L

L

V

M

T

A

I

D

L

F

I

L

M

F

G

L

A

L

S

G

T

A

F

I

I

I

V

M

G

A

V

A

L

A

P

P

N

N

Y

-

N

-

S

-

I

-

G

-

I

-

T

-

A

-

P

P

I

S

I

L

L

L

I

V

L

G

R

R

I

V

L

F

Q

V

G

G

L

L

A

G

L

V

G

G

G

M

E

A

Y

S

G

M

G

T

A

A

A

P

T

L

Y

Y

V

I

A

S

E

E

H

A

A

S

P

P

E

A

G

K

R

I

R

R

G

G

S

A

F

L

T

V

A

S

W

T

I

N

Q

G

T

F

T

L

A

I

T

T

M

G

G

G

L

Q

F

F

L

L

S

S

L

Y

L

L

V

I

I

N

L

L

G

A

V

F

R

T

T

D

A

V

V

T

G

G

E

-

A

-

F

-

A

-

D

T

W

W

G

R

W

W

R

M

-

L

-

G

-

I

-

A

-

G

I

I

P

P

F

A

L

L

V

L

S

Q

I

F

L

V

L

L

L

M

A

-

I

-

S

-

V

-

W

-

I

-

R

-

M

F

S

T

M

L

N

P

E

E

S

S

P

P

A

R

F

W

L

L

K

Y

M

R

K

K

A

G

E

R

G

E

K

E

T

E

S

A

K

K

A

A

P

I

L

L

-

R

-

I

-

Y

-

S

-

A

-

E

-

D

-

V

-

E

-

Q

-

E

-

I

-

R

-

A

-

L

-

K

-

D

-

S

-

V

-

E

T

T

E

E

A

I

F

L

G

E

Q

E

W

G

K

S

N

S

L

E

K

K

L

I

V

N

I

M

L

I

A

K

L

L

V

C

-

K

-

A

-

K

-

T

-

V

-

R

G

G

L

L

T

I

A

A

G

G

-

V

-

G

-

L

Q

Q

A

V

V

F

V

Q

W

Q

Y

F

T

V

G

G

Q

I

F

N

Y

T

A

V

L

M

F

Y

L

S

T

P

Q

T

T

I

L

V

K

Q

V

L

D

A

G

G

P

F

T

A

A

S

N

N

I

-

L

R

I

T

A

A

A

L

L

L

L

S

L

L

A

V

T

T

P

A

F

G

F

L

L

N

F

A

F

F

G

G

S

S

L

I

-

I

-

S

-

I

-

Y

-

F

S

I

D

D

K

R

I

I

G

G

R

R

K

K

P

K

I

L

-

L

-

I

-

S

-

L

-

F

-

G

-

V

-

I

-

S

-

L

-

G

I

I

L

L

G

T

G

G

C

V

L

F

I

Y

A

E

A

A

V

A

T

T

Y

H

F

A

P

P

I

A

F

I

S

S

G

S

L

L

-

E

-

T

-

Q

-

R

-

F

T

N

H

N

F

I

A

S

N

C

P

P

A

D

L

Y

E

K

A

S

A

A

L

M

Q

N

K

T

S

N

P

A

-

W

-

D

-
x
C

-

M

V

T

I
x
C

V

L

T

K

A

A

D

S

P

S

A

P

S

S

C
|
C

Q

G

F

Y

Q
x
C

F

S

N

S

P

P

T

I

G

G

T

-

K

K

K

E

F

H

T

P

S

G

S

A

C

C

C399 (vs. gap) mutation to A: Strongly decreased nickel inhibition; when associated with A-402, A-410 and A-413.; mutation to S: No effect on inostol transport or nickel inhibition. No effect on inostol transport or nickel inhibition; when associated with S-410.
C402 (≠ I352) mutation to A: Strongly decreased nickel inhibition; when associated with A-399, A-410 and A-413.
C410 (= C360) mutation to A: Strongly decreased nickel inhibition; when associated with A-399, A-402 and A-413.; mutation to S: No effect on inostol transport or nickel inhibition; when associated with S-399.
C413 (≠ Q363) mutation to A: Strongly decreased nickel inhibition; when associated with A-399, A-402 and A-410.

Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
26% identity, 27% coverage: 76:222/553 of query aligns to 204:347/727 of Q9Z2I6

query
sites
Q9Z2I6

G

G

A

A

L

F

V

F

F

W

G

G

R

G

L

L

G

A

D

D

L

K

V

V

G

G

R

R

K

K

Y

Q

T

S

F

L

L

L

V

I

T

C

I

M

L

S

I

V

M

N

G

G

A

F

S

F

T

A

F

F

I

L

V

S

G

S

V

F

L

V

P

Q

N

G

Y

Y

N

G

S

-

I

-

G

-

I

-

T

-

A

-

P

-

I

-

I

F

L

F

I

L

L

C

R

R

I

L

L

L

Q

S

G

G

L

F

A

G

L

I

G

G

E

A

Y

I

G

P

G

T

A

V

A

F

T

S

Y

Y

V

F

A

A

E

E

H

V

A

L

P

A

E

R

G

E

R

K

R

R

G

G

S

E

F

H

T

L

A

S

W

W

I

L

Q

C

T

M

T

F

A

W

T

M

M

I

G

G

-

G

-

I

-

Y

-

A

-

S

-

A

L

M

F

A

L

W

S

A

L

I

V

P

I

H

L

Y

G

G

V

W

R

S

T

F

A

S

V

M

G

G

E

-

A

S

A

A

F

Y

A

Q

D

F

W

H

G

S

W

W

R

R

I

V

P

F

F

V

L

I

V

V

S

C

I

A

L

L

L

P

L

C

A

V

I

S

S

S

V

V

W

V

I

A

R

L

M

T

S

F

M

M

N

P

E

E

S

S

P

P

A

R

F

F

L

L

Sites not aligning to the query:

1:57 Interaction with SYT1
529:566 (Microbial infection) C.botulinum neurotoxin type A-binding
559 N→A: Loss of one glycosylation site. No effect on C.botulinum neurotoxin type A (BoNT/A, botA) binding, but reduces the uptake of BoNT/A.

A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
26% identity, 43% coverage: 81:319/553 of query aligns to 63:310/446 of A0A0H2VG78

query
sites
A0A0H2VG78

G

G

R

P

L

L

G

A

D

D

L

K

V

L

G

G

R

R

K

R

Y

-

T

-

F

-

L

-

V

-

T

R

I

L

L

V

I

M

M

L

G

I

A

A

S

I

T

V

F

F

I

I

V

I

G

G

V

A

L

L

P

I

N

L

Y

A

N

A

S

S

I

T

G

N

I

L

T

A

A

-

P

-

I

-

I

L

L

L

I

I

L

G

R
|
R

I

L

L

I

Q
x
I

G

G

L

L

A

A

L

V

G

G

E

S

Y

M

G

S

G

T

A

V

A

P

T

V

Y

Y

V

L

A

S

E
|
E

H

M

A

A

P

P

E

T

G

E

R

Y

R

R

G

G

S

S

F

L

T

G

A

S

W

L

I

N

Q
|
Q

T

L

T

M

A

I

T

T

M

I

G

G

L

I

F

L

L

A

S

A

L

Y

L

L

V

V

I

-

L

-

G

-

V

-

R

-

T

-

A

-

V

-

G

-

E

N

A

Y

A

A

F

F

A

A

D

D

-

I

-

E

-

G

W

W

G

R

W

W

R

M

I

L

P

G

F

L

L

A

V

V

-

V

-

P

-

S

S

V

I

I

L

L

L

V

A

G

I

I

S

Y

V

F

-

M

-

P

-

E

-

S

-

P

-

R

W

W

I

L

R

L

M

E

S

N

M

R

N

N

E

E

S

E

P

A

A

A

-

R

-

Q

-

V

-

M

-

K

-

I

-

T

-

Y

-

D

-

S

-

E

-

I

-

D

-

K

-

E

F

L

L

K

K

E

M

M

K

K

A

E

E

I

G

N

K

A

T

I

S

S

K

E

A

S

P

T

L

W

T

T

E

V

A

I

F

K

G

S

Q

P

W

W

K

L

N

G

L

R

K

I

L

L

V

I

I

V

L

G

A

C

L

I

V

F

G

A

L

I

-

F

-
x
Q

-

F

T

I

A

G

G

I

Q
x
N

A

A

V

V

V

I

W

F

Y

Y

T

S

G

S

Q

S

F

I

Y

F

A

A

L

K

F

A

F

G

L

L

T

G

Q

E

T

A

L

A

K

S

V

I

D

L

G

G

P

S

T

V

A

G

N

-

I

-

L

-

I

I

A

G

A

T

A

I

L

N

L

V

L

L

A

V

T

T

P

I

F

V

F

A

L

I

F

F

F

-

G

-

S

-

L

V

S

V

D

D

K

K

I

I

G

D

R

R

K

K

P

K

I

L

L

V

G

G

R102 (= R128) mutation to A: Loss of transport activity.
I105 (≠ Q131) 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 (vs. gap) mutation to A: Loss of transport activity.
Q251 (vs. gap) mutation to A: Loss of transport activity.
N256 (≠ Q259) mutation to A: Loss of transport activity.

Sites not aligning to the query:

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

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)
24% identity, 30% coverage: 77:240/553 of query aligns to 95:248/514 of Q9LT15

query
sites
Q9LT15

A

A

L

L

V

V

F

A

G

S

R

F

L

M

G

A

D

S

L

V

V

I

G

T

R

R

K

K

Y

H

T

G

F

R

L

K

V

V

T

S

I

M

L

F

I

I

M

-

G

G

A

G

S

L

T

A

F

F

I

L

V

I

G

G

V

A

L

L

P

F

N

N

Y

A

N

F

S

A

I

V

G

N

I

V

T

S

A

-

P

-

I

-

I

M

L

L

I

I

L

G

R

R

I

L

L

L

Q

L

G

G

L

V

A

G

L

V

G

G

G

F

E

A

Y

N

G

Q

G

S

A

T

A

P

T

V

Y

Y

V

L

A

S

E
|
E

H

M

A

A

P

P

E

A

G

K

R

I

R

R

G

G

S

A

F

L

T

N

A

I

W

G

I

F

Q
|
Q

T

M

T

A

A

I

T

T

M

I

G

G

L
x
I

F

L

L

V

S

A

L

N

L

L

V

I

I

-

L

-

G

-

V

-

R

-

T

-

A

N

V

Y

G

G

E

T

A

S

A

K

F

M

A

A

D

Q

W

H

G

G

W

W

R

R

I

V

P

S

F

L

L

G

V

L

S

A

I

A

L

V

L

P

L

A

A

V

I

V

S

M

V

V

W

I

I

G

R

S

M

F

S

I

M

L

N

P

E

D

S

T

P

P

A

N

F

S

L

M

K

L

M

E

K

R

A

G

E

K

G

N

K

E

T

E

S

A

K

K

A

Q

P

M

L

L

T

K

E

K

A

I

F

R

G

G

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 (≠ L170) mutation to A: Reduces affinity for glucose 3-fold.

Sites not aligning to the query:

39 F→A: Reduces affinity for glucose 8-fold.
43 L→A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
77 modified: Disulfide link with 449; C→A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
295 binding
296 binding
301 binding
332 binding
344 D→N: Abolishes glucose transport activity; when associated with Q-162.
410 binding
449 modified: Disulfide link with 77; C→A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).

Query Sequence

>HSERO_RS11125 FitnessBrowser__HerbieS:HSERO_RS11125
MTTASVNTTARGITPEEKKVIFASSLGTVFEWYDFYLYGSLAAIIAKQFFAGTDPNTAFI
FALLAFAAGFIVRPFGALVFGRLGDLVGRKYTFLVTILIMGASTFIVGVLPNYNSIGITA
PIILIILRILQGLALGGEYGGAATYVAEHAPEGRRGSFTAWIQTTATMGLFLSLLVILGV
RTAVGEAAFADWGWRIPFLVSILLLAISVWIRMSMNESPAFLKMKAEGKTSKAPLTEAFG
QWKNLKLVILALVGLTAGQAVVWYTGQFYALFFLTQTLKVDGPTANILIAAALLLATPFF
LFFGSLSDKIGRKPIILGGCLIAAVTYFPIFSGLTHFANPALEAALQKSPVIVTADPASC
QFQFNPTGTKKFTSSCDIVKAKLSAASVNYQNVAGAPGSVATVKIGDRIITSYDAAGLSK
EDAAAKDKQLSKDLADDIKAAGYPSKADPEQMNKPMVLLLLFILVIYVTMVYGPIAACLV
EMFPTRIRYTSMSMPYHIGNGWFGGLLPTTSFALVAFKGDIYYGLWYPIVIAMITFVIGM
LFVKETVRNNIHD

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