SitesBLAST
Comparing HSERO_RS02645 FitnessBrowser__HerbieS:HSERO_RS02645 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 12 hits to proteins with known functional sites (download)
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
27% identity, 88% coverage: 38:463/484 of query aligns to 9:414/430 of P0AA76
- Y29 (≠ C58) binding
- D31 (= D60) mutation to N: Loss of galactonate transport activity.
- R32 (= R61) binding
- Y64 (= Y93) binding
- E118 (= E150) mutation to Q: Loss of galactonate transport activity.
- W358 (vs. gap) binding
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
27% identity, 87% coverage: 41:463/484 of query aligns to 1:395/409 of 6e9nA
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
26% identity, 88% coverage: 38:463/484 of query aligns to 1:379/393 of 6e9oA
Q9JI12 Vesicular glutamate transporter 2; VGluT2; Differentiation-associated BNPI; Differentiation-associated Na(+)-dependent inorganic phosphate cotransporter; Solute carrier family 17 member 6 from Rattus norvegicus (Rat) (see 2 papers)
24% identity, 86% coverage: 39:455/484 of query aligns to 68:481/582 of Q9JI12
- R88 (= R61) mutation to A: Impairs synaptic transmission. Abolishes the chloride ion conductance.
- H128 (≠ V86) mutation to A: Greatly lowers L-glutamate transport.
- R184 (= R143) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E150) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ M304) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
24% identity, 86% coverage: 39:455/484 of query aligns to 10:423/452 of 7t3nA
- binding (1s,3r)-1-aminocyclopentane-1,3-dicarboxylic acid: Y77 (= Y93), Y137 (≠ G154), Y165 (≠ K182), R264 (≠ M304), F268 (≠ S308), Y269 (≠ N309)
- binding (2R)-2-(methoxymethyl)-4-{[(25R)-spirost-5-en-3beta-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-beta-D-glucopyranoside: R12 (= R41), Y13 (= Y42), E152 (= E169), G163 (≠ A180)
Q9NRA2 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Membrane glycoprotein HP59; Solute carrier family 17 member 5; Vesicular excitatory amino acid transporter; VEAT from Homo sapiens (Human) (see 8 papers)
25% identity, 79% coverage: 73:454/484 of query aligns to 99:460/495 of Q9NRA2
- K136 (= K110) to E: in SD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transporter activity, but retains appreciable H(+)-coupled sialic acid transporter activity; dbSNP:rs80338795
- H183 (≠ T158) to R: in ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity; dbSNP:rs119491109
- LL 198:199 (≠ AT 173:174) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- I-----------L 266:267 (≠ ITQDVAAGPATAT 241:253) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ ASSRA 254:258) natural variant: Missing (in ISSD; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; abolishes H(+)-coupled sialic acid transporter activity; has normal L-aspartate and L-glutamate transporter activity)
- G328 (= G331) to E: in ISSD; some patients may manifest a milder phenotype consistent with Salla disease; markedly decreases H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs386833996
- P334 (= P337) to R: in ISSD; does not affect intracellular localization, targeted to lysosomes; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs119491110
- G371 (= G367) to V: in ISSD; abolishes H(+)-coupled sialic acid transporter activity; abolishes L-aspartate and L-glutamate transporter activity; dbSNP:rs777862172
Sites not aligning to the query:
- 22:23 Dileucine internalization motif; LL→AA: Targeted to plasma membrane.; LL→GG: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH.
- 39 R → C: in SD; frequent variant in Finland; alters intracellular localization, only partially targeted to lysosomes and mainly detected in LAMP1-negative vesicles and in the Golgi apparatus; completely devoid of L-aspartate and L-glutamate transport activity, but retains appreciable H(+)-coupled sialic acid and nitrate transporter activity; dbSNP:rs80338794
Q9Y2C5 Probable small intestine urate exporter; Solute carrier family 17 member 4 from Homo sapiens (Human) (see 2 papers)
24% identity, 80% coverage: 71:455/484 of query aligns to 99:464/497 of Q9Y2C5
- A372 (= A368) to T: in dbSNP:rs11754288
Sites not aligning to the query:
- 66 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-75 and A-90.
- 75 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-66 and A-90.
- 90 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: Loss of glycosylation and significant reduction in the transport of thyroid hormones T3 and T4; when associated with A-75 and A-90.
Q5Q0U0 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Solute carrier family 17 (Anion/sugar transporter), member 5; Vesicular excitatory amino acid transporter; VEAT from Rattus norvegicus (Rat) (see 2 papers)
23% identity, 82% coverage: 58:454/484 of query aligns to 83:460/495 of Q5Q0U0
- K136 (= K110) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R143) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L146) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G147) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E150) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (= G151) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (≠ G154) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (≠ I155) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ T158) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ I161) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLK------------------------N 268:272 (≠ QDVAAGPATATASSRAHVGAQVTPMPWLD 243:271) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P337) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (= G367) mutation to V: Remains in the endoplasmic reticulum.
Sites not aligning to the query:
- 22:23 Dileucine internalization motif; LL→AA: Targeted to plasma membrane; sialic acid uptake strongly activated at acidic pH.
- 39 R→C: Markedly decreases H(+)-coupled sialic acid transporter activity.
Q8BN82 Sialin; H(+)/nitrate cotransporter; H(+)/sialic acid cotransporter; AST; Solute carrier family 17 member 5; Vesicular excitatory amino acid transporter; VEAT from Mus musculus (Mouse) (see paper)
24% identity, 82% coverage: 58:454/484 of query aligns to 83:460/495 of Q8BN82
- H183 (≠ T158) mutation to R: Abolishes sialic acid transporter activity. Does not affect L-aspartate and L-glutamate transporter activity.
Sites not aligning to the query:
- 39 R→C: Completely abolishes L-aspartate and L-glutamate transporter activity. Retains appreciable H(+)-coupled sialic acid transporter activity.
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
24% identity, 60% coverage: 74:365/484 of query aligns to 75:352/493 of Q03567
Sites not aligning to the query:
- 69 modified: carbohydrate, N-linked (GlcNAc...) asparagine
P11551 L-fucose-proton symporter; 6-deoxy-L-galactose permease; L-fucose permease; L-fucose-H(+) symport protein from Escherichia coli (strain K12) (see 3 papers)
33% identity, 25% coverage: 50:171/484 of query aligns to 34:151/438 of P11551
- W38 (= W54) mutation W->F,I,Y: Strong decrease in L-fucose transport.
- D46 (≠ G65) Important for activity; mutation D->A,N: Loss of L-fucose transport.
- E135 (≠ N159) Important for activity; mutation E->A,D,Q: Loss of L-fucose transport.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 278 mutation W->F,Y: Slight decrease in L-fucose transport.; W→I: 30% decrease in L-fucose transport.
P0AGC0 Hexose-6-phosphate:phosphate antiporter from Escherichia coli (strain K12) (see paper)
25% identity, 87% coverage: 61:479/484 of query aligns to 46:453/463 of P0AGC0
- C108 (vs. gap) mutation to S: No change in activity.
- C143 (≠ G156) mutation to S: 30% of wild-type sugar phosphate transport activity.
- C265 (= C303) mutation to S: No change in activity.
- C331 (≠ L365) mutation to S: No change in activity.
- C436 (≠ L462) mutation to S: No change in activity.
- C438 (= C464) mutation to S: No change in activity.
Query Sequence
>HSERO_RS02645 FitnessBrowser__HerbieS:HSERO_RS02645
MHHVDAADPVGRGSSAASVAPAASAASNAPAAAQIGQKPTRYRWVVMGLIFLIWAIACAD
RANFGIALPYMKKEYGITNTEAGLIVSLFSFAYGLVQIPVGLMYKRLSEKTTGILFSVFM
LLTSLFTGLMGTTSSVLLLQLYRVGLGLSEGPLGIGCTNVINRWFPPEEKGTATGLWIAA
SKLGPLIVPTVCIIVIQLWGWREIFYVFAVPGIFLAILWFFLVTNSPSENRFCNEAERRY
ITQDVAAGPATATASSRAHVGAQVTPMPWLDGINRTRRVPRLETLRQVFTSWNVIGVAIG
YGCMIGISNIFMSWIPTYLVTVKGFASVKMGFLASAPFIGAVAGNMLGGVISDRLLGGRR
KPMMLLGALGTALMTLLLVEAPDSVLYLGAMLMLSGLMLGIGFAGYSAYPMGLATKATYP
AAFGIVNSLGQIGGACAPLAVGMLLDRYDWSSVFLYMVGTSLLCLALLLSVVEPITVRKA
GEEA
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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