SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing BWI76_RS16895 FitnessBrowser__Koxy:BWI76_RS16895 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 17 hits to proteins with known functional sites (download)

P77589 3-(3-hydroxy-phenyl)propionate transporter; 3HPP transporter; 3-(3-hydroxy-phenyl)propionate:H(+) symporter; 3HPP:H(+) symporter from Escherichia coli (strain K12) (see paper)
83% identity, 96% coverage: 12:394/398 of query aligns to 13:396/403 of P77589

query
sites
P77589

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E27 (= E26) mutation to A: Lack of 3HPP transport activity.; mutation to D: Slight decrease in 3HPP transport activity.
D75 (= D74) mutation D->A,E: Lack of 3HPP transport activity.
A272 (= A270) mutation to H: 30% increase in 3HPP transport activity.
K276 (= K274) mutation to D: Lack of 3HPP transport activity.

Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
36% identity, 87% coverage: 18:364/398 of query aligns to 33:415/448 of Q51955

query
sites
Q51955

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D41 (≠ E26) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
D44 (= D29) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
G85 (= G70) mutation to V: Abolishes 4-HBA transport and chemotaxis.
D89 (= D74) mutation to N: Abolishes 4-HBA transport and chemotaxis.
G92 (= G77) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to C: No change in 4-HBA transport and chemotaxis.; mutation G->L,V: Abolishes 4-HBA transport and chemotaxis.; mutation to Q: Decrease in 4-HBA transport and strong decrease in chemotaxis.
R124 (= R109) mutation to A: Abolishes 4-HBA transport.
E144 (= E129) mutation to A: Strong decrease in 4-HBA transport.
H183 (≠ Q167) mutation to A: Decrease in 4-HBA transport and chemotaxis.
D323 (= D273) mutation to N: Abolishes 4-HBA transport and chemotaxis.
H328 (≠ L278) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to R: Decrease in 4-HBA transport and loss of chemotaxis.
R386 (= R335) mutation to A: Strong decrease in 4-HBA transport.
R398 (= R347) mutation to A: Abolishes 4-HBA transport.

Sites not aligning to the query:

444 H→A: No change in 4-HBA transport and chemotaxis.

Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
35% identity, 87% coverage: 19:364/398 of query aligns to 27:406/452 of Q5EXK5

query
sites
Q5EXK5

C

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N

D82 (= D74) mutation to A: Loss of activity.
V311 (≠ A270) mutation to W: Loss of activity.
D314 (= D273) mutation to A: Loss of activity.

Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
28% identity, 89% coverage: 11:366/398 of query aligns to 39:405/444 of Q8NLB7

query
sites
Q8NLB7

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K

R

A

I

A

L

V

L

I

G

G

S

S

V

V

L

L

L

I

F

L

G

S

L

V

F

F

S

T

I

M

A

L

T

C

A

A

L

F

A

A

W

P

N

N

Y

P

P

W

T

V

L

F

L

G

L

A

A

F

R

R

L

F

L

I

T

A

G

G

V

L

G

G

L

L

G

G

A

G

A

L

L

V

P

P

N

S

L

V

I

N

A

A

L

M

T

T

S

S

E

D

A

L

A

V

G

P

P

R

R

K

F

T

R

M

G

S

R

A

A

W

V

A

S

T

L

V

M

M

Y

M

C

S

G

G

V

V

P

P

I

I

G

G

A

G

A

S

L

I

A

A

A

V

L

L

G

A

F

L

F

V

G

V

L

V

A

P

A

S

-

E

-

W

-

G

W

W

Q

R

T

F

V

M

F

F

W

L

V

I

G

-

G

A

I

L

V

I

P

P

L

L

L

V

-

G

V

L

P

P

L

I

L

A

L

M

R

K

W

V

L

I

P

P

E

S

S

D

P

K

V

A

F

I

Q

K

-

A

-

D

-

H

-

D

-

I

R

R

S

E

A

G

Q

H

G

D

V

E

P

P

-

A

-

G

L

F

R

K

A

D

L

L

A

V

P

D

G

R

N

Y

A

R

T

W

A

I

T

S

L

I

L

W

L

F

W

A

L

L

C

A

Y

T

F

F

F

V

T

T

L

L

V

A

V

W

Y

Y

M

G

L

L

I

G

N

T

W

W

L

L

P

P

M

R

L

L

L

M

V

E

G

T

Q

A

G

G

F

Y

S

E

A

F

S

G

E

H

A

A

A

L

G

M

V

F

M

T

F

L

V

A

L

L

Q

N

F

L

G

G

A

A

A

V

C

I

G

G

T

S

L

V

L

T

G

A

A
x
W

L

A

M

G

D
|
D

K
x
R

L

F

S

G

P

P

L
x
I

W

R

M

S

S

G

L

V

L

I

I

A

Y

A

S

G

G

I

M

A

L

G

A

I

S

A

L

L

A

L

L

L

G

L

T

T

A

Y

T

P

S

P

L

V

A

T

A

A

M

V

L

Y

F

V

S

I

G

L

F

I

V

L

A

A

G

G

L

V

F

G

A

T

T

H

G

G

G

T

Q

Q

S

I

V

L

L

I

Y

I

A

A

L

A

A

V

P

A

L

N

F

F

Y

Y

R

P

T

S

E

N

I

L

R

R

A

G

T

T

G

A

V

L

G

G

T

W

A

A

V

L

A

G

I

V

G

G

R
|
R

L

I

G

G

A

A

M

V

S

V

G

A

P

P

L

Q

L

L

A

A

G

G

K

L

M

L

L

L

A

A

L

W

G

N

T

L

G

G

D54 (≠ E26) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
D57 (= D29) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
R103 (= R75) mutation to A: Loss of transport activity.
W309 (≠ A270) mutation to V: Loss of transport activity.
D312 (= D273) mutation to A: Loss of transport activity.
R313 (≠ K274) mutation to A: Loss of transport activity.
I317 (≠ L278) mutation I->H,Y: Loss of transport activity.
R386 (= R347) mutation to A: Loss of transport activity.

Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
31% identity, 36% coverage: 52:194/398 of query aligns to 191:346/727 of Q9Z2I6

query
sites
Q9Z2I6

G

G

W

W

I

L

F

G

S

S

A

I

G

V

I

Y

L

L

G

G

L

M

P

V

G

G

A

A

L

F

A

F

G

W

G

G

M

G

L

L

A

A

D

D

R

K

Y

V

G

G

R

R

K

K

R

Q

I

S

L

L

G

I

S

C

V

M

L

S

L

V

F

N

G

G

L

F

F

F

S

A

I

F

A

L

T

S

A

S

L

F

A

V

W

Q

N

G

Y

Y

P

G

T

F

L

F

L

L

A

C

R

R

L

L

T

S

G

G

V

F

G

G

L

I

G

G

A

G

A

A

L

I

P

P

N

T

L

V

I

F

A

S

L

Y

T

F

S

A

E

E

A

V

A

L

G

A

P

R

R

E

F

K

R

R

G

G

R

E

A

H

V

L

S

S

L

W

M

L

Y

C

C

M

G

F

V

W

P

M

I

I

G

G

A

G

A

I

L

Y

A

A

A

S

A

A

L

M

G

A

F

W

-

A

-

I

-

P

-

H

-

Y

-

G

-

W

-

S

F

F

G

S

L

M

A

G

A

S

A

A

W

Y

Q

Q

-

F

-

H

-

S

-

W

T

R

V

V

F

F

W

V

V

I

G

V

G

C

I

A

V

L

P

P

L

C

L

V

L

S

V

S

P

V

L

V

L

A

L

L

R

T

W

F

L

M

P

P

E

E

S

S

P

P

V

R

F

F

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.

Q496J9 Synaptic vesicle glycoprotein 2C from Homo sapiens (Human) (see 4 papers)
31% identity, 36% coverage: 52:194/398 of query aligns to 191:346/727 of Q496J9

query
sites
Q496J9

G

G

W

W

I

L

F

G

S

S

A

I

G

V

I

Y

L

L

G

G

L

M

P

V

G

G

A

A

L

F

A

F

G

W

G

G

M

G

L

L

A

A

D

D

R

K

Y

V

G

G

R

R

K

K

R

Q

I

S

L

L

G

I

S

C

V

M

L

S

L

V

F

N

G

G

L

F

F

F

S

A

I

F

A

L

T

S

A

S

L

F

A

V

W

Q

N

G

Y

Y

P

G

T

F

L

F

L

L

L

F

A

C

R

R

L

L

T

S

G

G

V

F

G

G

L

I

G

G

A

G

A

A

L

I

P

P

N

T

L

V

I

F

A

S

L

Y

T

F

S

A

E

E

A

V

A

L

G

A

P

R

R

E

F

K

R

R

G

G

R

E

A

H

V

L

S

S

L

W

M

L

Y

C

C

M

G

F

V

W

P

M

I

I

G

G

A

G

A

I

L

Y

A

A

A

S

A

A

L

M

G

A

F

W

-

A

-

I

-

P

-

H

-

Y

-

G

-

W

-

S

F

F

G

S

L

M

A

G

A

S

A

A

W

Y

Q

Q

-

F

-

H

-

S

-

W

T

R

V

V

F

F

W

V

V

I

G

V

G

C

I

A

V

L

P

P

L

C

L

V

L

S

V

S

P

V

L

V

L

A

L

L

R

T

W

F

L

M

P

P

E

E

S

S

P

P

V

R

F

F

Sites not aligning to the query:

519:563 (Microbial infection) C.botulinum neurotoxin type A-binding
534 modified: carbohydrate, N-linked (GlcNAc...) asparagine
559 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: No change in interaction with C.botulinum neurotoxin type A heavy chain (botA, BoNT/A HC). Decreased molecular weight probably due to glycosylation loss, decreased interaction with BoNT/A HC.; N→Q: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC. Greater reduction in weight; when associated with Q-565.
561 S→A: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC.
563 F→A: No longer interacts with BoNT/A HC.
565 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Decreased molecular weight probably due to glycosylation loss, no change in binding to BoNT/A heavy chain. Greater reduction in weight; when associated with Q-559.

O08966 Solute carrier family 22 member 1; Organic cation transporter 1; mOCT1 from Mus musculus (Mouse) (see paper)
30% identity, 41% coverage: 47:211/398 of query aligns to 145:310/556 of O08966

query
sites
O08966

D

D

K

A

M

W

Q

K

M

V

G

D

W

L

I

F

F

Q

S

S

A

C

G

V

I

N

L

L

G

G

L

F

P

L

G

G

A

S

L

L

A

V

G

V

G

G

M

Y

L

I

A

A

D

D

R

R

Y

F

G

G

R

R

K

K

R

L

I

C

L

L

G

V

S

T

V

T

L

L

L

V

F

T

G

S

L

L

F

S

S

G

I

V

A

L

T

T

A

A

L

V

A

A

W

P

N

D

Y

Y

P

T

T

S

L

M

L

L

A

F

R

R

L

L

T

Q

G

G

V

M

G

V

L

S

G

K

A

G

A

S

L

W

P

V

N

S

L

G

I

Y

A

T

L

L

T

I

S

T

E

E

A

F

A

V

G

G

P

S

R

G

F

Y

R

R

G

-

R

R

A

T

V

T

S

A

L

I

M

L

Y

Y

C

-

G

-

V

-

P

-

I

-

G

-

A

-

A

Q

L

V

A

A

A

F

A

T

L

V

G

G

F

L

F

V

G

G

L

L

A

A

-

G

A

V

A

A

W

Y

Q

A

T

I

V

P

F

D

W

W

-

R

-

W

-

L

-

Q

V

L

G

A

G

V

I

S

V

L

P

P

L

T

L

F

L

L

V

F

P

L

L

L

L

Y

R

W

W

F

L

V

P

P

E

E

S

S

P

P

V

R

F

W

-

L

-

S

-

Q

Q

K

R

R

S

T

A

T

Q

Q

G

A

V

V

P

R

L

I

R

M

A

E

L

Q

L

I

A

A

P

Q

G

K

N

N

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)
30% identity, 38% coverage: 60:211/398 of query aligns to 158:310/556 of Q63089

query
sites
Q63089

L

L

G

G

L

F

P

L

G

G

A

S

L

L

A

V

G

V

G

G

M

Y

L

I

A

A

D

D

R

R

Y

F

G

G

R

R

K

K

R

L

I
x
C

L

L

G

V

S

T

V

T

L

L

L

V

F

T

G

S

L

V

F

S

S

G

I

V

A

L

T

T

A

A

L

V

A

A

W

P

N

D

Y

Y

P

T

T

S

L

M

L

L

A

F

R

R

L

L

T

Q

G

G

V
x
M

G
x
V

L
x
S

G
x
K

A
x
G

A
x
S

L
x
W

P
x
V

N
x
S

L
x
G

I
x
Y

A
x
T

L
|
L

T
x
I

S
x
T

E
|
E

A
x
F

A
x
V

G

G

P

S

R

G

F

Y

R

R

G

-

R

R

A

T

V

T

S

A

L

I

M

L

Y

Y

C

-

G

-

V

-

P

-

I

-

G

-

A

-

A

Q

L

M

A

A

A

F

A

T

L

V

G

G

F

L

F

V

G

G

L

L

A

A

-

G

A

V

A

A

W

Y

Q

A

T

I

V

P

F

D

W

W

-

R

-

W

-

L

-

Q

V

L

G

A

G

V

I

S

V

L

P

P

L

T

L

F

L

L

V

F

P

L

L

L

L

Y

R

W

W

F

L

V

P

P

E

E

S
|
S

P

P

V

R

F

W

-

L

-
x
S

-

Q

Q

K

R

R

S
x
T

A

T

Q

R

G

A

V

V

P

R

L

I

R

M

A

E

L

Q

L

I

A

A

P

Q

G

K

N

N

C179 (≠ I81) 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 (≠ V114) mutation to L: No change in TEA and MPP(+) uptake.
V213 (≠ G115) mutation to G: Decreased TEA uptake. No change in MPP(+) uptake.
S214 (≠ L116) mutation to G: Decreased TEA and MPP(+) uptake.
K215 (≠ G117) mutation to Q: Loss of TEA and MPP(+) uptake activity.; mutation to R: Loss of TEA and MPP(+) uptake activity.
G216 (≠ A118) mutation to A: Decreased TEA and MPP(+) uptake.
S217 (≠ A119) mutation to G: No change in TEA and MPP(+) uptake.
W218 (≠ L120) 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 (≠ P121) mutation to L: No change in TEA and MPP(+) uptake.
S220 (≠ N122) mutation to I: Decreased TEA and MPP(+) uptake.
G221 (≠ L123) mutation to A: Decreased TEA and MPP(+) uptake.
Y222 (≠ I124) 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 (≠ A125) mutation to I: Decreased TEA uptake. No change in MPP(+) uptake.
L224 (= L126) mutation to V: Decreased TEA and MPP(+) uptake.
I225 (≠ T127) mutation to G: No change in TEA and MPP(+) uptake.
T226 (≠ S128) mutation to A: Decreased TEA uptake. No change in MPP(+) uptake.
E227 (= E129) mutation to D: Loss of TEA and MPP(+) uptake activity.; mutation to Q: Loss of TEA and MPP(+) uptake activity.
F228 (≠ A130) mutation to I: No change in TEA and MPP(+) uptake.
V229 (≠ A131) mutation to A: Decreased TEA and MPP(+) uptake.; mutation to L: Loss of TEA and MPP(+) uptake activity.
S286 (= S191) 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 (vs. gap) 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 (≠ S197) 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.

O74899 Uncharacterized transporter C576.17c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 36% coverage: 59:203/398 of query aligns to 127:278/525 of O74899

query
sites
O74899

I

V

L

L

G

G

L

V

L

A

P

L

G

G

A

P

L

L

A

F

G

L

G

G

M

P

L

L

A

S

D

D

R

L

Y

L

G

G

R

R

K

K

R

L

I

V

L

Y

L

I

G

G

S

S

V

L

L

I

F

Y

G

V

L

C

F

F

S

C

I

I

A

S

T

C

A

A

L

L

A

A

W

R

N

N

Y

Y

P

A

T

Q

L

L

L

V

L

I

A

S

R

M

L

L

L

I

T

M

G

G

V

V

G

V

L

G

G

S

A

T

A

A

L

L

P

G

N

N

L

V

I

A

A

G

L

A

T

V

S

A

E

D

A

V

A

L

G

G

P

D

R

E

F

D

R

S

-

N

-

W

G

G

R

M

A

Y

V

M

S

F

L

I

M

F

Y

M

C

C

G

S

V

V

-

A

-

S

-

V

-

G

-

S

P

P

I

M

G

G

A

T

A

G

L

V

A

A

A

E

A

-

L

-

G

-

F

-

G

N

L

P

A

K

A

L

A

T

W

W

Q

R

T

W

V

L

F

Y

W

W

V

I

G

D

G

V

I

I

V

V

P

G

L

G

L

F

V

I

P

-

L

I

L

L

L

F

R

V

W

F

L

T

P

P

E

E

S

T

-

L

-

P

-

A

-

I

-

V

-

I

P

Q

V

R

F

Y

Q

E

R

Q

S

K

A

R

Q

Q

G

G

V

L

P

P

L

V

Sites not aligning to the query:

55 modified: Phosphoserine

8et8A Cryo-em structure of the organic cation transporter 1 in complex with verapamil (see paper)
28% identity, 41% coverage: 47:211/398 of query aligns to 143:308/532 of 8et8A

query
sites
8et8A

D

D

K

S

M

W

Q

K

M

V

G

D

W

L

I

F

F

Q

S

S

A

C

G

V

I

N

L

V

G

G

L

F

P

L

G

G

A

S

L

L

A

G

G

V

G

G

M

Y

L

I

A

A

D

D

R

R

Y

F

G

G

R

R

K

K

R

L

I

C

L

L

G

A

S

T

V

T

L

L

L

I

F

S

G

A

L

V

F

S

S

G

I

V

A

L

T

M

A

A

L

V

A

A

W

P

N

D

Y

Y

P

T

T

S

L

M

L

L

A

F

R

R

L

L

T

Q

G

G

V

L

G

V

L

S

G
x
K

A

G

A

S

L
x
W

P

M

N

S

L

G

I

Y

A

T

L

L

T

I

S

T

E

E

A

F

A

V

G

G

P

S

R

G

F

Y

R

R

G

-

R

R

A

T

V

V

S

A

L

I

M

L

Y

Y

C

-

G

-

V

-

P

-

I

-

G

-

A

-

A
x
Q

L

M

A

A

A

F

A

T

L

V

G

G

F

L

F

V

-

L

-

S

G

G

L

V

A

A

A

Y

A

A

W

I

Q

P

T

H

V

W

F

R

W

W

V

L

G

Q

G

L

I

A

V

V

-

S

-

L

P

P

L

T

L

F

L

L

V

F

P

L

L

L

L

Y

R

W

W

C

L

V

P

P

E

E

S

S

P

P

V

R

F

W

-

L

-

S

-

Q

Q

K

R

R

S

N

A

T

Q

Q

G

A

V

I

P

K

L

I

R

M

A

D

L

H

L

I

A

A

P

Q

G

K

N

N

binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: K213 (≠ G117), W216 (≠ L120), Q240 (≠ A152)

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, 41% coverage: 47:211/398 of query aligns to 143:308/532 of 8et7A

query
sites
8et7A

D

D

K

S

M

W

Q

K

M

V

G

D

W

L

I

F

F

Q

S

S

A

C

G

V

I

N

L

V

G

G

L

F

P

L

G

G

A

S

L

L

A

G

G

V

G

G

M

Y

L

I

A

A

D

D

R

R

Y

F

G

G

R

R

K

K

R

L

I

C

L

L

G

A

S

T

V

T

L

L

L

I

F

S

G

A

L

V

F

S

S

G

I

V

A

L

T

M

A

A

L

V

A

A

W

P

N

D

Y

Y

P

T

T

S

L

M

L

L

A

F

R

R

L

L

T

Q

G

G

V

L

G

V

L

S

G

K

A

G

A

S

L

W

P

M

N

S

L

G

I

Y

A

T

L

L

T

I

S

T

E

E

A

F

A

V

G

G

P

S

R

G

F

Y

R

R

G

-

R

R

A

T

V

V

S

A

L

I

M

L

Y

Y

C

-

G

-

V

-

P

-

I

-

G

-

A

-

A

Q

L

M

A

A

A

F

A

T

L

V

G

G

F

L

F

V

-

L

-

S

G

G

L

V

A

A

A

Y

A

A

W

I

Q

P

T

H

V

W

F

R

W

W

V

L

G

Q

G

L

I

A

V

V

-

S

-

L

P

P

L

T

L

F

L

L

V

F

P

L

L

L

L

Y

R

W

W

C

L

V

P

P

E

E

S

S

P

P

V

R

F

W

-

L

-

S

-

Q

Q

K

R

R

S

N

A

T

Q

Q

G

A

V

I

P

K

L

I

R

M

A

D

L

H

L

I

A

A

P

Q

G

K

N

N

Sites not aligning to the query:

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

P9WJY3 Probable triacylglyceride transporter Rv1410c; MFS-type drug efflux transporter P55 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
29% identity, 38% coverage: 50:199/398 of query aligns to 46:197/518 of P9WJY3

query
sites
P9WJY3

Q

R

M

I

G

T

W

W

I

I

F

V

S

T

A

M

G

Y

I

L

L

L

G

G

L

Y

L

I

P

A

G

A

A

M

L

P

A

L

G

L

G

G

M

R

L

A

A

S

D

D

R

R

Y

F

G

G

R

R

K

K

R

L

I

M

L

L

L

Q

G

V

S

S

V

L

L

A

L

G

F

F

G

I

L

I

F

G

S

S

I

V

A

V

T

T

A

A

L

L

A

A

-

G

-

H

-

F

W

G

N

D

Y

F

P

H

T

M

L

L

L

I

L

A

A

G

R

R

L

T

L

I

T

Q

G

G

V

V

G

A

L

S

G

G

A

A

A

L

L

L

P

P

N

I

L

T

I

L

A

A

L

L

T

G

S

A

E

D

A

L

A

W

G

S

P

Q

R

R

F

N

R

R

G

A

R

G

A

V

V

L

S

G

L

G

M

I

Y

G

C

A

G

A

V

Q

P

E

I

L

G

G

A

S

A

V

L

L

A

G

A

P

A

L

L

Y

G

G

F

I

F

F

-

I

-

V

G

W

L

L

A

L

A

H

A

D

W

W

Q

R

T

D

V

V

F

F

W

W

V

I

G

N

G

-

I

-

V

V

P

P

L

L

L

T

L

A

V

I

P

A

L

M

L

V

L

M

R

I

W

H

L

F

P

-

E

S

S

L

P

P

V

S

F

H

Q

D

R

R

S

S

A

T

Q

E

Sites not aligning to the query:

22 D→A: Susceptible to ethidium bromide, tested in M.smegmatis.; D→E: Decreases resistance to ethidium bromide, tested in M.smegmatis.

O15245 Solute carrier family 22 member 1; Organic cation transporter 1; hOCT1 from Homo sapiens (Human) (see 10 papers)
32% identity, 38% coverage: 61:211/398 of query aligns to 158:309/554 of O15245

query
sites
O15245

G

G

L

F

L
|
L

P

F

G

G

A

S

L

L

A

G

G

V

G

G

M

Y

L

F

A

A

D

D

R

R

Y

F

G

G

R

R

K

K

R

L

I

C

L

L

G

G

S

T

V

V

L

L

L

V

F

N

G

A

L

V

F
x
S

S

G

I

V

A

L

T

M

A

A

L

F

A

S

W

P

N

N

Y

Y

P

M

T

S

L

M

L

L

A

F

R

R

L

L

T

Q

G

G

V

L

G

V

L

S

G

K

A

G

A

N

L

W

P

M

N

A

L
x
G

I

Y

A

T

L

L

T

I

S

T

E

E

A

F

A

V

G

G

P

S

R

G

F

S

R

R

G

-

R

R

A

T

V

V

S

A

L

I

M

M

Y
|
Y

C

-

G

-

V

-

P

-

I

-

G

-

A

-

A

Q

L

M

A

A

A

F

A

T

L

V

G

G

F

L

F

V

-

A

-

L

-

T

G

G

L

L

A

A

A

Y

A

A

W

L

Q

P

T

H

V

W

F

R

W

W

V

L

G

Q

G

L

I

A

V

V

-

S

-

L

P

P

L

T

L

F

L

L

V

F

P

L

L

L

L

Y

R

W

W

C

L

V

P
|
P

E

E

S

S

P

P

V
x
R

F

W

-

L

-

S

-

Q

Q

K

R

R

S

N

A

T

Q

E

G

A

V

I

P

K

L

I

R

M

A

D

L

H

L

I

A

A

P

Q

G

K

N

N

L160 (= L63) 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 (≠ F92) to L: no changes in MPP(+) uptake; dbSNP:rs34104736
G220 (≠ L123) to V: affects transporter activity; reduction of MPP(+) uptake when associated with V-408; dbSNP:rs36103319
Y240 (= Y144) mutation to F: Decreased TEA uptake.
P283 (= P189) to L: in dbSNP:rs4646277; mutation to A: Decreased TEA uptake.
R287 (≠ V193) to G: in dbSNP:rs4646278

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
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

Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
27% identity, 33% coverage: 43:175/398 of query aligns to 75:213/493 of Q03567

query
sites
Q03567

A

E

F

F

A

D

L

W

D

D

K

K

M

Q

Q

T

M

T

G

G

W

M

I

V

F

L

S

S

A

S

G

F

I

F

L

Y

G

G

L

Y

L

I

P

G

G

S

A

Q

L

I

A

I

G

G

M

H

L

L

A

A

D

S

R

R

Y

Y

G

G

R

G

K

K

R

R

I

V

L

V

L

F

G

V

S

T

V

I

L

L

L

G

F

S

G

A

L

L

F

L

S

T

I

L

A

L

T

N

A

P

L

V

A

A

W

A

N

R

Y

T

P

S

T

E

L

Y

L

A

L

L

A

A

R

I

L

L

L

R

T

A

G

A

V

I

G

G

L

F

-

L

-

Q

G

G

A

A

A

T

L

F

P

P

N

A

L

M

I

H

A

T

L

M

T

W

S

S

E

V

A

W

A

G

G

P

P

P

R

L

F

E

R

L

G

S

R

V

A

L

V

T

S

G

L

V

M

T

Y

Y

C

A

G

G

V

A

P

Q

I

I

G

G

A

N

A

V

L

I

A

V

A

L

A

P

L

L

-

S

G

G

F

F

-

L

-

C

-

E

F

Y

G

G

L

F

A

D

A

G

W

W

Q

P

T

S

V

I

F

F

W

Y

V

I

G

I

G

G

I

V

Sites not aligning to the query:

69 modified: carbohydrate, N-linked (GlcNAc...) asparagine

8sc6A Human oct1 bound to thiamine in inward-open conformation (see paper)
37% identity, 26% coverage: 41:144/398 of query aligns to 125:222/447 of 8sc6A

query
sites
8sc6A

A

A

Q

D

A

S

F

W

A

K

L

L

D

D

K

L

M

F

Q

Q

M

-

G

-

W

-

I

-

F

-

S

S

A

C

G

L

I

N

L

A

G

G

L

F

L

L

P

F

G

G

A

S

L

L

A

G

G

V

G

G

M

Y

L

F

A

A

D

D

R

R

Y

F

G

G

R

R

K

K

R

L

I

C

L

L

G

G

S

T

V

V

L

L

L

V

F

N

G

A

L

V

F

S

S

G

I

V

A

L

T

M

A

A

L

F

A

S

W

P

N

N

Y

Y

P

M

T

S

L

M

L

L

A

F

R

R

L

L

T

Q

G

G

V

L

G

V

L

S

G

K

A

G

A

N

L

W

P

M

N

A

L

G

I

Y

A

T

L

L

T

I

S

T

E

E

A

F

A

V

G

G

P

S

R

G

F

S

R

R

G

-

R

R

A

T

V

V

S

A

L

I

M

M

Y

Y

Sites not aligning to the query:

binding 3-(4-amino-2-methyl-pyrimidin-5-ylmethyl)-5-(2-hydroxy-ethyl)-4-methyl-thiazol-3-ium: 223, 226, 293, 294, 318, 378, 379

8sc3A Human oct1 bound to fenoterol in inward-open conformation (see paper)
37% identity, 26% coverage: 41:144/398 of query aligns to 125:222/445 of 8sc3A

query
sites
8sc3A

A

A

Q

D

A

S

F

W

A

K

L

L

D

D

K

L

M

F

Q

Q

M

-

G

-

W

-

I

-

F

-

S

S

A

C

G

L

I

N

L

A

G

G

L

F

L

L

P

F

G

G

A

S

L

L

A

G

G

V

G

G

M

Y

L

F

A

A

D

D

R

R

Y

F

G

G

R

R

K

K

R

L

I

C

L

L

G

G

S

T

V

V

L

L

L

V

F

N

G

A

L

V

F

S

S

G

I

V

A

L

T

M

A

A

L

F

A

S

W

P

N

N

Y

Y

P

M

T

S

L

M

L

L

A

F

R

R

L

L

T

Q

G

G

V

L

G

V

L

S

G

K

A

G

A

N

L
x
W

P
x
M

N

A

L

G

I

Y

A

T

L

L

T

I

S

T

E

E

A

F

A

V

G

G

P

S

R

G

F

S

R

R

G

-

R

R

A

T

V

V

S

A

L

I

M

M

Y

Y

binding Fenoterol: W199 (≠ L120), M200 (≠ P121)

Sites not aligning to the query:

binding Fenoterol: 223, 226, 284, 291, 376, 380

8sc2A Human oct1 bound to diltiazem in inward-open conformation (see paper)
37% identity, 26% coverage: 41:144/398 of query aligns to 125:222/453 of 8sc2A

query
sites
8sc2A

A

A

Q

D

A

S

F

W

A

K

L

L

D

D

K

L

M

F

Q

Q

M

-

G

-

W

-

I

-

F

-

S

S

A

C

G

L

I

N

L

A

G

G

L

F

L

L

P

F

G

G

A

S

L

L

A

G

G

V

G

G

M

Y

L

F

A

A

D

D

R

R

Y

F

G

G

R

R

K

K

R

L

I

C

L

L

G

G

S

T

V

V

L

L

L

V

F

N

G

A

L

V

F

S

S

G

I

V

A

L

T

M

A

A

L

F

A

S

W

P

N

N

Y

Y

P

M

T

S

L

M

L

L

A

F

R

R

L

L

T

Q

G

G

V

L

G

V

L

S

G

K

A

G

A

N

L
x
W

P

M

N

A

L

G

I

Y

A

T

L

L

T

I

S

T

E

E

A

F

A

V

G

G

P

S

R

G

F

S

R

R

G

-

R

R

A

T

V

V

S

A

L

I

M

M

Y

Y

binding Diltiazem: W199 (≠ L120)

Sites not aligning to the query:

binding Diltiazem: 18, 223, 226, 293, 297, 385

Query Sequence

>BWI76_RS16895 FitnessBrowser__Koxy:BWI76_RS16895
MTQTTTASNSRLMVTVGLCFMVALMEGLDLQAAGIAAVGMAQAFALDKMQMGWIFSAGIL
GLLPGALAGGMLADRYGRKRILLGSVLLFGLFSIATALAWNYPTLLLARLLTGVGLGAAL
PNLIALTSEAAGPRFRGRAVSLMYCGVPIGAALAAALGFFGLAAAWQTVFWVGGIVPLLL
VPLLLRWLPESPVFQRSAQGVPLRALLAPGNATATLLLWLCYFFTLLVVYMLINWLPMLL
VGQGFSASEAAGVMFVLQFGAACGTLLLGALMDKLSPLWMSLLIYSGMLASLLALGTATS
LAAMLFSGFVAGLFATGGQSVLYALAPLFYRTEIRATGVGTAVAIGRLGAMSGPLLAGKM
LALGTGTVGVMAASAPGILLAGVAVFWLMNRQKRAALA

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