SitesBLAST
Comparing RR42_RS11305 FitnessBrowser__Cup4G11:RR42_RS11305 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 10 hits to proteins with known functional sites (download)
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
24% identity, 92% coverage: 8:405/432 of query aligns to 3:397/409 of 6e9nA
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
24% identity, 92% coverage: 8:405/432 of query aligns to 14:416/430 of P0AA76
- Y29 (= Y23) binding
- D31 (≠ A25) mutation to N: Loss of galactonate transport activity.
- R32 (= R26) binding
- Y64 (= Y58) binding
- E118 (= E112) mutation to Q: Loss of galactonate transport activity.
- W358 (≠ Y347) binding
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
23% identity, 92% coverage: 8:405/432 of query aligns to 6:381/393 of 6e9oA
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)
26% identity, 83% coverage: 12:368/432 of query aligns to 62:424/495 of Q9NRA2
- K136 (= K75) 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 (≠ V120) 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 (≠ AI 135:136) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (= IL 202:203) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ AGQEA 204:208) 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 (≠ A266) 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 (= P272) 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 (= G309) 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
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)
26% identity, 62% coverage: 101:368/432 of query aligns to 164:424/495 of Q8BN82
- H183 (≠ V120) 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.
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)
25% identity, 62% coverage: 101:368/432 of query aligns to 164:424/495 of Q5Q0U0
- R168 (= R105) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L108) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G109) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E112) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A113) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (≠ I116) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P117) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ V120) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ T123) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ AGQEA 204:208) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P272) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (= G309) 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.
- 136 K→E: Markedly decreases H(+)-coupled sialic acid transporter activity.
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
27% identity, 50% coverage: 101:315/432 of query aligns to 139:356/493 of Q03567
Sites not aligning to the query:
- 69 modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q9Y2C5 Probable small intestine urate exporter; Solute carrier family 17 member 4 from Homo sapiens (Human) (see 2 papers)
28% identity, 57% coverage: 65:311/432 of query aligns to 128:376/497 of Q9Y2C5
- A372 (≠ L307) 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.
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)
27% identity, 47% coverage: 103:305/432 of query aligns to 182:388/582 of Q9JI12
- R184 (= R105) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E112) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ S239) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.
Sites not aligning to the query:
- 88 R→A: Impairs synaptic transmission. Abolishes the chloride ion conductance.
- 128 H→A: Greatly lowers L-glutamate transport.
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
25% identity, 47% coverage: 103:305/432 of query aligns to 124:330/452 of 7t3nA
Sites not aligning to the query:
Query Sequence
>RR42_RS11305 FitnessBrowser__Cup4G11:RR42_RS11305
MKHIKGMRWWMVSLVTMGLIVNYLARNTLSVAAPTMMSELHMTTQQYSYVVVAWQVCYAM
MQPVAGLVLDAIGTKIGFGIFALAWSLACAAAALASGWQGLAFFRGLLGLAEAAGIPGGV
KATTEWFPAKERSIAIGWFNIGSSIGALCAPPLVVWTILNGGWQRAFIIVGALGVAWTVL
WMLCYKHPKNQQRLSDQEREYILAGQEAQHKDANMAKASWLEIMRSRNFWSIAIPRFLSE
PAWQTFNAWIPLYMATERHMNIKEIAMFAWLPFLAADIGCVLGGYLSPWFHKHLKVSLFT
SRKLVMLVGCLAMIGPACVGLVDSPYSAIALLCVGGFAHQTLSGALYSITSDAFGKNEVA
TATGLAGMSGYLGATLFTLLFGIAVTHIGYSPLFVLLAVFDLIAAAIVFLMARERAAPGA
AAANLGSPALHS
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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