SitesBLAST

C145 (≠ S104) mutation to S: No significant effect on transport activity; when associated with S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
F160 (≠ I119) mutation to C: Reduces phosphate binding, transport and signaling activities.
R168 (= R129) mutation to A: Reduces transport activity. No significant effects on affinity for inorganic phosphate. No significant effects on growth rates.; mutation to C: Abolishes transport and signaling activities.; mutation to E: Reduces transport activity. Moderately reduces affinity for inorganic phosphate. No significant effects on growth rates.; mutation to Q: Reduces transport activity. Moderately reduces affinity for inorganic phosphate. Moderately reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.
G172 (= G133) mutation to C: Abolishes transport and signaling activities.
G174 (≠ A135) mutation to C: Abolishes transport and signaling activities.
G176 (= G137) mutation to C: Abolishes transport and signaling activities.
D178 (≠ E139) mutation D->E,N: Reduces transport activity. No significant effects on affinity for inorganic phosphate. No significant effects on signaling activities. No significant effects on growth rates.
Y179 (= Y140) mutation to A: Significantly reduces transport activity. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. Reduces growth rates under low phosphate conditions. Slightly reduces signaling activity.; mutation to G: Abolishes transport activity. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. Reduces growth rates under low phosphate conditions. Abolishes signaling activity.; mutation Y->S,F: No significant effects on transport activity. No significant effects on growth rates under low phosphate conditions. Does not affect patterns of secreted phosphatase activities under low and high phosphate conditions. No significant effects on signaling activity.
C237 (vs. gap) mutation to S: No significant effect on transport activity; when associated with S-145, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
C241 (vs. gap) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-245, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
C245 (vs. gap) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-263, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
C263 (≠ S209) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-335, S-399, S-434, S-455, S-474, S-510 and S-519.
K298 (vs. gap) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); mutation to A: No significant effect on membrane localization under low phosphate conditions and internalization after phosphate addition. Strongly affects vacuolar sorting of the protein after internalization.
304:327 (vs. gap) mutation Missing: Increases transport activity. Has no significant effect on membrane localization under low phosphate conditions. Results in severely delayed internalization after phosphate addition.
C335 (≠ S237) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-399, S-434, S-455, S-474, S-510 and S-519.
D358 (vs. gap) mutation to E: Abolishes transport activity. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. Moderately decreases signaling activities. Significantly reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.; mutation to N: Significantly reduces transport activity. No significant effects on affinity for inorganic phosphate. Causes pronounced increase in secreted phosphatase activity under high phosphate conditions. No significant effects on signaling activities. Significantly reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.
V392 (= V286) mutation to C: Reduces transport and signaling activities.
C399 (≠ A293) mutation to S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-434, S-455, S-474, S-510 and S-519.
V408 (= V302) mutation to C: Reduces signaling activity and enhances transport activity.

Sites not aligning to the query:

6 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
434 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-455, S-474, S-510 and S-519.
455 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-474, S-510 and S-519.
473 E→K: No significant effects on transport activity. No significant effects on affinity for inorganic phosphate. No significant effects on growth rates.; E→Q: No significant effects on transport activity. Reduces affinity for inorganic phosphate. No significant effects on growth rates.
474 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-510 and S-519.
492 mutation K->A,Q: No significant effects on transport activity. Reduces affinity for inorganic phosphate. No significant effects on growth rates.; K→E: Reduces transport activity. Reduces affinity for inorganic phosphate. Significantly reduces growth rates under low phosphate conditions. No significant effects on growth rates under high phosphate conditions.
510 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474 and S-519.
519 C→S: No significant effect on transport activity; when associated with S-145, S-237, S-241, S-245, S-263, S-335, S-399, S-434, S-455, S-474 and S-510.

Q12300 High glucose sensor RGT2; Low-affinity glucose receptor RGT2; Low-affinity transporter-like sensor RGT2; Restores glucose transport protein 2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
25% identity, 39% coverage: 76:320/628 of query aligns to 158:426/763 of Q12300

query
sites
Q12300

F

F

G

G

A

A

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L

V

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S

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S

-

F

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R231 (= R156) mutation to K: In RGT2-1; constitutively signaling glucose receptor.

Sites not aligning to the query:

684:690 SIISDST→AIIADAA: In Rgt2(4SA); Abolishes Yck-dependent phosphorylation, interaction with MTH1 and STD1, and glucose signaling, but does not affect protein stability.

Q496J9 Synaptic vesicle glycoprotein 2C from Homo sapiens (Human) (see 4 papers)
27% identity, 25% coverage: 77:234/628 of query aligns to 204:356/727 of Q496J9

query
sites
Q496J9

G

G

A

A

L

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V

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F

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G

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R

G

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D

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A

A

Sites not aligning to the query:

519:563 (Microbial infection) C.botulinum neurotoxin type A-binding
534 modified: carbohydrate, N-linked (GlcNAc...) asparagine
559 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: No change in interaction with C.botulinum neurotoxin type A heavy chain (botA, BoNT/A HC). Decreased molecular weight probably due to glycosylation loss, decreased interaction with BoNT/A HC.; N→Q: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC. Greater reduction in weight; when associated with Q-565.
561 S→A: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC.
563 F→A: No longer interacts with BoNT/A HC.
565 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Decreased molecular weight probably due to glycosylation loss, no change in binding to BoNT/A heavy chain. Greater reduction in weight; when associated with Q-559.

8fvzA Pipt y150a
24% identity, 49% coverage: 18:326/628 of query aligns to 2:318/433 of 8fvzA

query
sites
8fvzA

E

Q

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F

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E

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W

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D

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Y

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binding phosphate ion: F145 (≠ Q164), W235 (vs. gap), D239 (vs. gap), Y243 (≠ F254)

Sites not aligning to the query:

binding phosphate ion: 346

Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
27% identity, 25% coverage: 77:234/628 of query aligns to 204:356/727 of Q9Z2I6

query
sites
Q9Z2I6

G

G

A

A

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F

F

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G

G

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G

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D

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-

F

F

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G

C

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F

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M

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K

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G

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K

E

A

A

Sites not aligning to the query:

1:57 Interaction with SYT1
529:566 (Microbial infection) C.botulinum neurotoxin type A-binding
559 N→A: Loss of one glycosylation site. No effect on C.botulinum neurotoxin type A (BoNT/A, botA) binding, but reduces the uptake of BoNT/A.

Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534) (see paper)
22% identity, 28% coverage: 30:206/628 of query aligns to 52:209/444 of Q8NLB7

query
sites
Q8NLB7

V

I

F

F

E
x
D

W

G

Y

Y

D
|
D

F

L

Y

I

L

V

Y

Y

G

G

S

T

L

-

A

-

F

-

I

V

G

Q

A

S

A

A

F

L

F

A

S

K

E

E

Y

W

P

N

E

L

A

S

T

S

R

A

N

T

I

L

F

G

A

T

L

I

L

G

A

S

F

T

A

A

A

-

G

-

F

F

L

F

V

G

R

M

P

A

F

I

G

G

A

A

L

V

V

F

F

I

G

G

R

R

I

L

G

S

D

D

L
x
R

V

V

G

G

R

R

K

K

Y

A

T

A

F

V

L

I

V

G

T

S

I

V

M

L

I

I

M

L

G

S

L

V

S

F

T

T

F

M

L

L

V

C

G

A

V

F

L

A

P

P

G

N

S

-

A

-

S

-

W

-

G

-

I

-

A

-

P

P

I

W

I

V

L

F

I

G

G

A

L

F

R

R

M

F

L

I

Q

A

G

G

L

L

A

G

L

L

G

G

E

L

Y

V

G

P

G

S

A

V

A

N

T

A

Y

M

V

T

A

S

E

D

H

L

A

V

P

P

D

R

N

K

K

T

R

M

G

S

Y

A

Y

W

T

A

S

T

W

V

I

M

Q

M

T

S

T

G

A

V

T

P

L

I

G

G

L

G

F

S

L

I

S

A

L

A

I

V

V

L

I

A

L

L

V

V

I

V

Q

V

N

-

W

-

L

-

G

-

K

-

D

P

A

S

F

S

A

E

W

W

G

G

W

W

R

R

I

F

P

M

F

F

I

L

L

I

S

A

F

L

V

I

L

P

L

L

D54 (≠ E32) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
D57 (= D35) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
R103 (≠ L87) mutation to A: Loss of transport activity.

Sites not aligning to the query:

309 W→V: Loss of transport activity.
312 D→A: Loss of transport activity.
313 R→A: Loss of transport activity.
317 mutation I->H,Y: Loss of transport activity.
386 R→A: Loss of transport activity.

Query Sequence

>WP_106712722.1 NCBI__GCF_003010955.1:WP_106712722.1
MATTSVADTSSRGMTREEKKVIFASSLGTVFEWYDFYLYGSLAAFIGAAFFSEYPEATRN
IFALLAFAAGFLVRPFGALVFGRIGDLVGRKYTFLVTIMIMGLSTFLVGVLPGSASWGIA
APIILIGLRMLQGLALGGEYGGAATYVAEHAPDNKRGYYTSWIQTTATLGLFLSLIVILV
IQNWLGKDAFAAWGWRIPFILSFVLLGISVWIRLSLSESPTFQRMKEEGKGSKAPLSEAF
GQWKNAKIALLALFGLTAGQAVVWYSGQFYALFFLQNVLKVDGQAVNIMIAIALLLGTGF
FVFFGWLSDKIGRKPIIMAGLALAILTYFPLFKALTWAANPALAAAQQDVRATVTAAPGD
CKFQFNPTGTAKFTTSCDIATSFLTRNSVPYDVVATAAPGTAATVKIGQETVESYDAAAA
GADAKTKEAAFAKAVNIALQDGGYPLVRDPVKVADSKLDALVTANPKLALDTAAIRAGEK
TMVPVDQAIKDKLITAEEAAGATEVAVYTVPGAGAFKMVADPAAVSWTKVIAILFVLVIY
VTMVYGPIAAILVEMFPTRIRYTGMSLPYHIGNGWFGGLLPATVFAMSAFKGDIYYGLWY
PIVIAAMTLIIGLIFVRDTKDTDLHEVK

Or try a new SitesBLAST search

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