SitesBLAST

D54 (≠ E32) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
D57 (= D35) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
R103 (= R87) 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.

8fvzA Pipt y150a
24% identity, 82% coverage: 27:383/433 of query aligns to 11:375/433 of 8fvzA

query
sites
8fvzA

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C

binding phosphate ion: F145 (≠ L164), W235 (vs. gap), D239 (≠ T248), Y243 (≠ M252), N346 (≠ S354)

8sc3A Human oct1 bound to fenoterol in inward-open conformation (see paper)
33% identity, 35% coverage: 45:195/433 of query aligns to 116:245/445 of 8sc3A

query
sites
8sc3A

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binding Fenoterol: W199 (≠ F140), M200 (≠ G141), Q223 (= Q163), F226 (vs. gap)

Sites not aligning to the query:

binding Fenoterol: 284, 291, 376, 380

8sc2A Human oct1 bound to diltiazem in inward-open conformation (see paper)
33% identity, 35% coverage: 45:195/433 of query aligns to 116:245/453 of 8sc2A

query
sites
8sc2A

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binding Diltiazem: W199 (≠ F140), Q223 (= Q163), F226 (vs. gap)

Sites not aligning to the query:

binding Diltiazem: 18, 293, 297, 385

8sc6A Human oct1 bound to thiamine in inward-open conformation (see paper)
33% identity, 35% coverage: 45:195/433 of query aligns to 116:245/447 of 8sc6A

query
sites
8sc6A

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

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

O15245 Solute carrier family 22 member 1; Organic cation transporter 1; hOCT1 from Homo sapiens (Human) (see 10 papers)
33% identity, 35% coverage: 45:195/433 of query aligns to 134:263/554 of O15245

query
sites
O15245

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W

L160 (≠ I72) 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 (= S104) to L: no changes in MPP(+) uptake; dbSNP:rs34104736
G220 (≠ A143) to V: affects transporter activity; reduction of MPP(+) uptake when associated with V-408; dbSNP:rs36103319
Y240 (≠ W162) 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)
36% identity, 24% coverage: 76:181/433 of query aligns to 160:257/532 of 8et8A

query
sites
8et8A

L

L

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G

T

Y

R

R

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R

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A

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W

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Q
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M

A

A

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G

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G

G

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A

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L

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-

S

S

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binding (2S)-2-(3,4-dimethoxyphenyl)-5-{[2-(3,4-dimethoxyphenyl)ethyl](methyl)amino}-2-(propan-2-yl)pentanenitrile: K213 (≠ G137), W216 (≠ F140), 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)
36% identity, 24% coverage: 76:181/433 of query aligns to 160:257/532 of 8et7A

query
sites
8et7A

L

L

G

G

S

S

V

L

M

G

L

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G

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Y

I

A

A

D

D

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K

F

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E

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A

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G

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A

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Y

A

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L

I

Sites not aligning to the query:

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

8et9A Cryo-em structure of the organic cation transporter 2 in complex with 1-methyl-4-phenylpyridinium (see paper)
25% identity, 82% coverage: 76:432/433 of query aligns to 160:505/517 of 8et9A

query
sites
8et9A

L

V

G

G

S

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M

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L

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G

G

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Y

Y

I

A

A

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K

K

A

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x
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Q

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x
F

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K

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L

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binding 1-methyl-4-phenylpyridin-1-ium: W216 (≠ E139), Q240 (= Q163), F243 (≠ T166), F430 (= F358)

Query Sequence

>BPHYT_RS29430 FitnessBrowser__BFirm:BPHYT_RS29430
MSTTTHPSHAVDANQPASRGAIAAAVIGNWLEFFDFTVYGFFAVIIGKLYFPSADPTTSL
LLSVATFAAGFITRPLGSVMLGVYADRKGRKAALNLTIMLMAVSTGLIAIAPTYAQIGLA
APLLIVFARLVQGFSQGGEFGAATSTLLEQGGGTRRGFRASWQLATQGGAALMGSGIAAA
LSGALPKDSLESWGWRIPFLLGVLIAPVGMYLRRRLADDAASAHSHAIERGVLHELFTQH
VRTLVLITLTVMGGTVSTYILTFYMPTYAIHTLGLPMSLSMLVGVAAGFVMLITCPLFGM
LSDRIGSRKRPILFGRGVLVLLLFPAFMLINRFPQLPVIMSLTALMLLFYSMGSASEFAL
MCESFPRRVRATGISIAYALSVCVFGGTAQLVATWLIKLTGSKLAPAGYVAACVVVSLIA
VSMLKETADKPID

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