SitesBLAST
Comparing HSERO_RS11250 FitnessBrowser__HerbieS:HSERO_RS11250 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
P53322 High-affinity nicotinic acid transporter; Nicotinic acid permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
24% identity, 67% coverage: 17:306/435 of query aligns to 81:371/534 of P53322
- K283 (≠ E221) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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, 83% coverage: 69:431/435 of query aligns to 113:479/495 of Q9NRA2
- K136 (≠ R92) 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 (≠ I137) 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 (≠ IT 152:153) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ LE 227:228) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- SSLRN 268:272 (≠ ANISH 229:233) 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 (= G289) 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 (= P295) 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 (= G327) 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)
24% identity, 87% coverage: 55:431/435 of query aligns to 99:479/495 of Q8BN82
- H183 (≠ I137) 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)
24% identity, 72% coverage: 120:431/435 of query aligns to 166:479/495 of Q5Q0U0
- R168 (= R122) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ L125) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G126) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E129) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A130) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F133) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P134) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ I137) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ L140) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- SSLKN 268:272 (≠ ANISH 229:233) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P295) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (= G327) 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.
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
22% identity, 90% coverage: 29:419/435 of query aligns to 7:395/409 of 6e9nA
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
21% identity, 90% coverage: 29:419/435 of query aligns to 18:414/430 of P0AA76
- Y29 (= Y40) binding
- D31 (= D42) mutation to N: Loss of galactonate transport activity.
- R32 (= R43) binding
- Y64 (= Y75) binding
- E118 (= E129) mutation to Q: Loss of galactonate transport activity.
- W358 (= W363) binding
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)
22% identity, 90% coverage: 34:424/435 of query aligns to 79:492/582 of Q9JI12
- R88 (= R43) mutation to A: Impairs synaptic transmission. Abolishes the chloride ion conductance.
- H128 (≠ A68) mutation to A: Greatly lowers L-glutamate transport.
- R184 (= R122) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E129) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ F262) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
22% identity, 90% coverage: 29:419/435 of query aligns to 10:379/393 of 6e9oA
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
21% identity, 90% coverage: 34:424/435 of query aligns to 21:434/452 of 7t3nA
Sites not aligning to the query:
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
23% identity, 45% coverage: 87:283/435 of query aligns to 82:287/452 of Q5EXK5
- D82 (≠ H87) mutation to A: Loss of activity.
Sites not aligning to the query:
- 311 V→W: Loss of activity.
- 314 D→A: Loss of activity.
Q9Y2C5 Probable small intestine urate exporter; Solute carrier family 17 member 4 from Homo sapiens (Human) (see 2 papers)
22% identity, 81% coverage: 74:424/435 of query aligns to 120:475/497 of Q9Y2C5
- A372 (≠ C328) 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.
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
24% identity, 54% coverage: 55:288/435 of query aligns to 35:277/446 of A0A0H2VG78
- R102 (= R122) mutation to A: Loss of transport activity.
- I105 (≠ L125) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (≠ Y142) mutation to A: Loss of transport activity.
- Q137 (≠ M157) mutation to A: Loss of transport activity.
- Q250 (vs. gap) mutation to A: Loss of transport activity.
- Q251 (vs. gap) mutation to A: Loss of transport activity.
- N256 (≠ Y267) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 22 D→N: Affects symport activity. May function as an uniporter.
- 357 W→A: Loss of transport activity.
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
21% identity, 60% coverage: 22:283/435 of query aligns to 24:296/448 of Q51955
- D41 (≠ S39) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (= D42) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (≠ N83) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (≠ H87) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G90) 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 (= R122) mutation to A: Abolishes 4-HBA transport.
- E144 (≠ Y142) mutation to A: Strong decrease in 4-HBA transport.
- H183 (≠ Q188) 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.
Query Sequence
>HSERO_RS11250 FitnessBrowser__HerbieS:HSERO_RS11250
MSYQAGAAADGARASFEDATYSKVTWRLLPLLFLCYVASYLDRVNVGFAKLQMLQDLKFS
DTVYGLGAGIFFLGYFVFEVPSNMILHKVGARLWIARIMITWGIISGAMAYVTTPEMFYI
MRFLLGVAEAGFFPGVILYLTYWYPAARRGKITALFMTGIALSGVIGGPLSGWIMHAMPG
VWGHTGWQWMFILEAIPSLILGVMVILYMKDRIRDADWLSEEEKRLLEANISHEESQKEH
LSLGAMFANGRVWLGALIYFCFVMGLYGVSFWLPTIIKATGVSDPLNVGLLTAIPYAFAA
AAMVLIGRSADARRERRWHVAIPAFIGCIGLLLSTQYGHNTTLAMASLTLASVGILTTLP
LFWSLPTAFLSGTAAAAGIALINSLGNLAGFVSPFLVGWLKDATQSTNAGMYVLAASLVI
GGLLTLTLPAKLVNR
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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