SitesBLAST
Comparing BWI76_RS13565 FitnessBrowser__Koxy:BWI76_RS13565 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 20 (the maximum) hits to proteins with known functional sites (download)
P0AA76 D-galactonate transporter; D-galactonate/H(+) symporter from Escherichia coli (strain K12) (see paper)
41% identity, 97% coverage: 6:429/436 of query aligns to 9:429/430 of P0AA76
- Y29 (= Y26) binding
- D31 (= D28) mutation to N: Loss of galactonate transport activity.
- R32 (= R29) binding
- Y64 (= Y61) binding
- E118 (= E119) mutation to Q: Loss of galactonate transport activity.
- W358 (= W357) binding
6e9nA E. Coli d-galactonate:proton symporter in the inward open form (see paper)
42% identity, 96% coverage: 11:428/436 of query aligns to 3:409/409 of 6e9nA
6e9oA E. Coli d-galactonate:proton symporter mutant e133q in the outward substrate-bound form (see paper)
39% identity, 97% coverage: 6:428/436 of query aligns to 1:393/393 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)
26% identity, 92% coverage: 10:408/436 of query aligns to 83:481/582 of Q9JI12
- R88 (≠ L15) mutation to A: Impairs synaptic transmission. Abolishes the chloride ion conductance.
- H128 (≠ F54) mutation to A: Greatly lowers L-glutamate transport.
- R184 (= R112) mutation R->A,E,K: Greatly lowers L-glutamate transport.
- E191 (= E119) mutation to A: Greatly lowers L-glutamate transport.; mutation E->D,Q: Lowers L-glutamate transport.
- R322 (≠ V251) mutation to A: Loss of L-glutamate release. Abolishes the chloride ion conductance.
7t3nA R184q/e191q mutant of rat vesicular glutamate transporter 2 (vglut2)
26% identity, 92% coverage: 10:408/436 of query aligns to 25:423/452 of 7t3nA
Sites not aligning to the query:
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)
24% identity, 94% coverage: 25:432/436 of query aligns to 77:488/495 of Q9NRA2
- K136 (≠ R78) 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 (≠ S127) 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 (≠ VT 142:143) mutation to AA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- IL 266:267 (≠ IR 209:210) mutation to LA: Localizes in vesicular structures mainly concentrated in the perinuclear region.
- S-SLRN 268:272 (≠ EGGGEP 211:216) 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 (= G278) 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 (= P284) 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 (= G320) 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
Q03567 Uncharacterized transporter slc-17.2 from Caenorhabditis elegans (see paper)
26% identity, 87% coverage: 42:421/436 of query aligns to 75:457/493 of Q03567
Sites not aligning to the query:
- 69 modified: carbohydrate, N-linked (GlcNAc...) asparagine
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, 90% coverage: 41:434/436 of query aligns to 99:490/495 of Q5Q0U0
- K136 (≠ R78) mutation to E: Markedly decreases H(+)-coupled sialic acid transporter activity.
- R168 (= R112) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- E171 (≠ M115) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-175.
- G172 (= G116) mutation to C: Decreases protein levels and alters subcellular localization.
- E175 (= E119) mutation to C: Decreases H(+)-coupled sialic acid transporter activity; when associated with C-171.
- G176 (≠ A120) mutation to C: Decreases protein levels and alters subcellular localization.
- F179 (= F123) mutation to C: Decreases the affinity and transport rate for D-glucuronate. Does not affect H(+)-coupled sialic acid transporter activity.
- P180 (= P124) mutation to C: Decreases protein levels and alters subcellular localization.
- H183 (≠ S127) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- W186 (≠ S130) mutation to C: Abolishes H(+)-coupled sialic acid transporter activity.
- S-----SLKN 268:272 (≠ EGGGEPELGT 211:220) mutation Missing: Abolishes H(+)-coupled sialic acid transporter activity.
- P334 (= P284) mutation to R: Abolishes H(+)-coupled sialic acid transporter activity.
- G371 (= G320) 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)
27% identity, 84% coverage: 41:405/436 of query aligns to 99:453/495 of Q8BN82
- H183 (≠ S127) 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.
Q9Y2C5 Probable small intestine urate exporter; Solute carrier family 17 member 4 from Homo sapiens (Human) (see 2 papers)
23% identity, 88% coverage: 39:420/436 of query aligns to 99:478/497 of Q9Y2C5
- A372 (≠ I318) 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.
A2SWM2 Sphingosine-1-phosphate transporter SPNS2; Protein spinster homolog 2; Protein two of hearts from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
21% identity, 81% coverage: 10:362/436 of query aligns to 56:398/504 of A2SWM2
- R153 (= R112) mutation to S: In ko157; displays cardia bifida (2 hearts).
Q8IVW8 Sphingosine-1-phosphate transporter SPNS2; Protein spinster homolog 2 from Homo sapiens (Human) (see 2 papers)
22% identity, 79% coverage: 18:362/436 of query aligns to 108:445/549 of Q8IVW8
- R200 (= R112) mutation to S: Loss of function; does not rescue the cardia bifida phenotype in the morpholino knockdown in zebrafish.
- S319 (≠ Y245) natural variant: Missing (in DFNB115; uncertain significance; dbSNP:rs749994718)
8jhqA Cryo-em structure of human s1p transporter spns2 bound with s1p (see paper)
22% identity, 79% coverage: 18:362/436 of query aligns to 14:350/446 of 8jhqA
Sites not aligning to the query:
7yubR S1p-bound human spns2 (see paper)
22% identity, 79% coverage: 18:362/436 of query aligns to 16:333/429 of 7yubR
Q9GQQ0 Protein spinster; Protein benchwarmer; Protein diphthong from Drosophila melanogaster (Fruit fly) (see paper)
23% identity, 79% coverage: 18:362/436 of query aligns to 120:448/605 of Q9GQQ0
- E217 (= E119) mutation to K: In bnch(N); leads to storage in yolk spheres during oogenesis and results in widespread accumulation of enlarged lysosomal and late endosomal inclusions.
8g92A Structure of inhibitor 16d-bound spns2 (see paper)
22% identity, 79% coverage: 18:362/436 of query aligns to 10:321/415 of 8g92A
7yudR Fty720p-bound human spns2 (see paper)
22% identity, 79% coverage: 18:362/436 of query aligns to 9:321/417 of 7yudR
Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
20% identity, 70% coverage: 2:305/436 of query aligns to 20:324/448 of Q51955
- D41 (≠ N25) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- D44 (= D28) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
- G85 (= G69) mutation to V: Abolishes 4-HBA transport and chemotaxis.
- D89 (= D73) mutation to N: Abolishes 4-HBA transport and chemotaxis.
- G92 (= G76) 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 (= R112) mutation to A: Abolishes 4-HBA transport.
- E144 (≠ Q132) mutation to A: Strong decrease in 4-HBA transport.
- H183 (= H171) mutation to A: Decrease in 4-HBA transport and chemotaxis.
- D323 (≠ K304) mutation to N: Abolishes 4-HBA transport and chemotaxis.
Sites not aligning to the query:
- 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.
Q9UPI3 Heme transporter FLVCR2; Calcium-chelate transporter; CCT; Feline leukemia virus subgroup C receptor-related protein 2 from Homo sapiens (Human) (see 2 papers)
23% identity, 78% coverage: 59:397/436 of query aligns to 132:463/526 of Q9UPI3
Sites not aligning to the query:
- 16 V → A: in dbSNP:rs2287015
- 30:66 HPSVSVHPSVSINPSVSVHPSSSAHPSALAQPSGLAH→APSVSVAPSVSINPSVSVAPSSSAAPSALAQPSGLAA: Loss of heme-binding activity.
Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
21% identity, 92% coverage: 1:402/436 of query aligns to 7:410/452 of Q5EXK5
- D82 (= D73) mutation to A: Loss of activity.
- V311 (= V297) mutation to W: Loss of activity.
- D314 (= D300) mutation to A: Loss of activity.
Query Sequence
>BWI76_RS13565 FitnessBrowser__Koxy:BWI76_RS13565
MQQQLKRSNVRYGILLFLFLATVFNYADRATLSVVAPIMSKELGFDPEAMGLAFSVFGIS
YVIMQIPGGWLLDKYGSRLVYGCALIGWSIVTMFQGTIYMFASPLVALVILRLMMGAIEA
PAFPANSRLSVQWFPNKERGFVTSVYQAAQYISLGIITPLMTIILHNLSWHYVFYYIGAI
GVVLGIFWLVKVRDPSHHPKINQQELDYIREGGGEPELGTKKTQQKLTLAQIKSVCVNRM
MIGVYIGQFCVTSITWFFLTWFPTYLYQAKGMSILKVGFVASIPAIAGFIGGLLGGVFSD
WLLKRGYSLTTARKLPVICGMLLSCVIVVANYTTSEVVVIAAMSVAFFAKGFGNLGWCVL
SDTSPKEMLGIAGGVFNMCGNLASIITPLVIGVIIANTHSFDYAILYVGSMGVLGLFSYL
FIVGPLDRLTLTPRAA
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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