SitesBLAST
Comparing PP_4461 FitnessBrowser__Putida:PP_4461 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 6 hits to proteins with known functional sites (download)
O08966 Solute carrier family 22 member 1; Organic cation transporter 1; mOCT1 from Mus musculus (Mouse) (see paper)
25% identity, 81% coverage: 68:416/430 of query aligns to 162:518/556 of O08966
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.
Q9Y7Q9 Probable metabolite transporter C2H8.02 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 49% coverage: 7:218/430 of query aligns to 35:255/583 of Q9Y7Q9
Sites not aligning to the query:
- 267 modified: Phosphoserine
- 269 modified: Phosphoserine
- 289 modified: Phosphoserine
- 290 modified: Phosphoserine
- 292 modified: Phosphoserine
- 330 modified: Phosphoserine
O23492 Inositol transporter 4; Myo-inositol-proton symporter INT4; Protein INOSITOL TRANSPORTER 4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 48% coverage: 16:223/430 of query aligns to 33:222/582 of O23492
Sites not aligning to the query:
- 559:561 LLE→AAA: No effect on targeting.
- 559:582 mutation Missing: No effect on targeting.
- 564:565 FK→AA: No effect on targeting.
- 570:575 RRREKK→AAAAAA: No effect on targeting.
Q63089 Solute carrier family 22 member 1; Organic cation transporter 1; rOCT1 from Rattus norvegicus (Rat) (see 4 papers)
24% identity, 81% coverage: 68:416/430 of query aligns to 162:518/556 of Q63089
- C179 (≠ A85) 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 (≠ F126) mutation to L: No change in TEA and MPP(+) uptake.
- V213 (≠ A127) mutation to G: Decreased TEA uptake. No change in MPP(+) uptake.
- S214 (≠ A128) mutation to G: Decreased TEA and MPP(+) uptake.
- K215 (≠ G129) mutation to Q: Loss of TEA and MPP(+) uptake activity.; mutation to R: Loss of TEA and MPP(+) uptake activity.
- G216 (= G130) mutation to A: Decreased TEA and MPP(+) uptake.
- S217 (≠ E131) mutation to G: No change in TEA and MPP(+) uptake.
- W218 (= W132) 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 (≠ G133) mutation to L: No change in TEA and MPP(+) uptake.
- S220 (≠ T134) mutation to I: Decreased TEA and MPP(+) uptake.
- G221 (≠ S135) mutation to A: Decreased TEA and MPP(+) uptake.
- Y222 (≠ A136) 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 (≠ S137) mutation to I: Decreased TEA uptake. No change in MPP(+) uptake.
- L224 (≠ Y138) mutation to V: Decreased TEA and MPP(+) uptake.
- I225 (= I139) mutation to G: No change in TEA and MPP(+) uptake.
- T226 (≠ V140) mutation to A: Decreased TEA uptake. No change in MPP(+) uptake.
- E227 (= E141) mutation to D: Loss of TEA and MPP(+) uptake activity.; mutation to Q: Loss of TEA and MPP(+) uptake activity.
- F228 (≠ W142) mutation to I: No change in TEA and MPP(+) uptake.
- V229 (≠ S143) mutation to A: Decreased TEA and MPP(+) uptake.; mutation to L: Loss of TEA and MPP(+) uptake activity.
- S286 (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-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 (≠ R205) 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.
- C322 (≠ V231) mutation to 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.
- S328 (≠ F237) 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-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.
- C358 (≠ Y253) mutation to 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.
- C418 (≠ S323) mutation to 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.
- C437 (≠ A336) mutation to 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.
- C451 (= C350) mutation to 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.
- C470 (≠ T367) mutation to 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.
- C474 (= C371) mutation to 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.
- D475 (≠ C372) mutation to E: Decreased MPP(+) uptake, no change in MPP(+) affinity. Decreased NMN uptake, increased NMN affinity. Decreased choline uptake, increased choline affinity.; mutation to N: Decreased MPP(+) uptake.; mutation to R: Decreased MPP(+) uptake.
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.
- 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.
8et8A Cryo-em structure of the organic cation transporter 1 in complex with verapamil (see paper)
27% identity, 36% coverage: 68:220/430 of query aligns to 160:293/532 of 8et8A
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)
27% identity, 36% coverage: 68:220/430 of query aligns to 160:293/532 of 8et7A
Sites not aligning to the query:
Query Sequence
>PP_4461 FitnessBrowser__Putida:PP_4461
MTKTISTRKTWFAVATSGSGNLLEVYDFAVYAFFATTIAKLFFPNVDETTSLLQTFAAYG
AGFIARPLGSYVIGRIGDKRGRKPAMLLTIICMAIGSIGIGLIPTYETIGVGAPILLVML
RCLQGFAAGGEWGTSASYIVEWSPAGRKGFFGSFQSVSSSGGALLASLVASALLLIPAED
LLDWGWRVPFIAGGLAIFAFSLFLRAHAEETPEYVNSKAEVVNPTDSKPYVLGLQAFGFT
IFWTTLSYLVSAYMVTYTQNHAGLTRTEALISSNIALLLQITLIPVAGALSDRFGRKPLL
LLACLGTATLAYPILNLMSGGASFHQVVMLQCCLSALFAMYSGPGPATICEIFPTRLRNT
WMTVGYTLAVCCFGGFAPLISTWLISVTKIAASPAFLLIPAAVVSALVILKLPSTRISGF
KSAAKAEASY
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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