SitesBLAST
Comparing Ga0059261_2977 FitnessBrowser__Korea:Ga0059261_2977 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 14 hits to proteins with known functional sites (download)
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
28% identity, 94% coverage: 14:419/432 of query aligns to 7:423/430 of P0AA76
- Y29 (= Y36) binding D-galactonate
- D31 (= D38) mutation to N: Loss of galactonate transport activity.
- R32 (= R39) binding D-galactonate
- Y64 (= Y71) binding D-galactonate
- E118 (= E125) mutation to Q: Loss of galactonate transport activity.
- W358 (≠ Y354) binding D-galactonate
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
28% identity, 93% coverage: 19:419/432 of query aligns to 1:404/409 of 6e9nA
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
27% identity, 93% coverage: 18:419/432 of query aligns to 3:388/393 of 6e9oA
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)
26% identity, 44% coverage: 122:309/432 of query aligns to 172:353/495 of Q5Q0U0
- G172 (= G122) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E125) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ S126) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F129) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P130) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ I133) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ V136) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ ---QD 217:218) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (≠ I280) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
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.
- 168 R→C: Abolishes H(+)-coupled sialic acid transporter activity.
- 171 E→C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- 371 G→V: Remains in the endoplasmic reticulum.
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, 44% coverage: 122:309/432 of query aligns to 172:353/495 of Q8BN82
- H183 (≠ I133) 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, 78% coverage: 46:383/432 of query aligns to 69:422/493 of Q03567
- N69 (≠ K46) modified: carbohydrate, N-linked (GlcNAc...) asparagine
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)
23% identity, 66% coverage: 122:407/432 of query aligns to 172:465/495 of Q9NRA2
- H183 (≠ I133) 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 148:149) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ I- 215) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ --EQD 216:218) 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 (= G274) 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 (≠ I280) 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 (vs. gap) 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
- 136 K → 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
8u3hA Structure of fmoc-leu-oh bound sialin
24% identity, 46% coverage: 122:319/432 of query aligns to 109:300/425 of 8u3hA
Sites not aligning to the query:
8u3gA Structure of naag-bound sialin
24% identity, 46% coverage: 122:319/432 of query aligns to 111:302/427 of 8u3gA
Sites not aligning to the query:
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, 63% coverage: 118:389/432 of query aligns to 184:465/582 of Q9JI12
- R184 (= R118) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E125) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (vs. gap) 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)
22% identity, 63% coverage: 122:394/432 of query aligns to 130:412/452 of 7t3nA
Sites not aligning to the query:
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
23% identity, 95% coverage: 14:425/432 of query aligns to 13:441/452 of Q5EXK5
- D82 (= D83) mutation to A: Loss of activity.
- V311 (≠ K297) mutation to W: Loss of activity.
- D314 (≠ K300) mutation to A: Loss of activity.
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
23% identity, 38% coverage: 19:184/432 of query aligns to 25:190/448 of Q51955
- D41 (≠ N35) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (= D38) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (= G79) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D83) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G86) 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 (= R118) mutation to A: Abolishes 4-HBA transport.
- E144 (= E138) mutation to A: Strong decrease in 4-HBA transport.
- H183 (≠ R177) mutation to A: Decrease in 4-HBA transport and chemotaxis.
Sites not aligning to the query:
- 323 D→N: Abolishes 4-HBA transport and chemotaxis.
- 328 H→A: Decrease in 4-HBA transport and chemotaxis.; H→R: Decrease in 4-HBA transport and loss of chemotaxis.
- 386 R→A: Strong decrease in 4-HBA transport.
- 398 R→A: Abolishes 4-HBA transport.
- 444 H→A: No change in 4-HBA transport and chemotaxis.
Q9Y2C5 Probable small intestine urate exporter; Solute carrier family 17 member 4 from Homo sapiens (Human) (see 2 papers)
24% identity, 38% coverage: 138:300/432 of query aligns to 190:357/497 of Q9Y2C5
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.
- 372 A → T: in dbSNP:rs11754288
Query Sequence
>Ga0059261_2977 FitnessBrowser__Korea:Ga0059261_2977
MDASQAEGIRTGAAANAGRYRWMIVALLFAATVINYIDRQMIGVLKPTLMQDLHWSERDF
AGVIIWFQIAYAIGYIGFGKFVDMVGARVGYAVAFVIWQLAHIAHGGAYSMTQFAMARFG
LGIGESGNFPAGIKAVTEWFPAKERAFAIGVFNAGANIGAVITPLVVPLMVIAWGWRMAF
VVTGVISFVWLIAWWAMYRSPRQHPKVSEGELAWIEQDPADPVKPIGYATVLTRKETWAY
SLGKFFIDPIWWFFLFWLPGYLFKQYDLNLLTFGIPLAAIYLISDVGSVFGGWMSSKLMK
AGKSANYARKLTMFVCACLVLPVVFAESITSVWVAVLVIGVATAGHQAFSANLYALPSDL
FPRGAVGSVVGIGGTVGAVGGILMAFYAGEILDRLGVYWPLFWVAGSAYFVALLVVHLLS
PRLEPVKVDETA
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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