SitesBLAST
Comparing GFF1100 FitnessBrowser__WCS417:GFF1100 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)
P0AER0 Glycerol uptake facilitator protein; Aquaglyceroporin; Glycerol facilitator from Escherichia coli (strain K12) (see 3 papers)
71% identity, 98% coverage: 6:284/285 of query aligns to 3:281/281 of P0AER0
- HLN 66:68 (= HLN 69:71) binding
- Y138 (= Y141) binding
- GFA 199:201 (= GFA 202:204) binding
- N203 (= N206) binding
- R206 (= R209) binding
- PL 236:237 (≠ PI 239:240) mutation to FW: No detectable water or glycerol permeability.
1fx8A Crystal structure of the e. Coli glycerol facilitator (glpf) with substrate glycerol (see paper)
76% identity, 89% coverage: 9:262/285 of query aligns to 1:254/254 of 1fx8A
B1VB61 Propanediol uptake facilitator PduF from Citrobacter freundii (see paper)
68% identity, 93% coverage: 9:272/285 of query aligns to 4:267/269 of B1VB61
P37451 Propanediol uptake facilitator PduF from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
69% identity, 89% coverage: 9:263/285 of query aligns to 4:258/264 of P37451
Q96PS8 Aquaporin-10; AQP-10; Aquaglyceroporin-10; Small intestine aquaporin from Homo sapiens (Human) (see 2 papers)
41% identity, 92% coverage: 10:270/285 of query aligns to 20:277/301 of Q96PS8
- E27 (= E17) mutation to Q: Abolishes permeability to glycerol.
- G73 (≠ S62) mutation to A: Increased permeability to glycerol at acidic pH.; mutation to F: Abolishes permeability to glycerol.
- S77 (= S66) mutation S->A,D: Nearly abolishes permeability to glycerol.
- H80 (= H69) mutation to A: Abolishes permeability to glycerol.
- F85 (≠ V74) mutation to A: Nearly abolishes permeability to glycerol.
- R94 (≠ D83) mutation to A: Abolishes permeability to glycerol.
- N133 (≠ H122) modified: carbohydrate, N-linked (GlcNAc...) asparagine; mutation to Q: Abolishes N-glycosylation.
6f7hC Crystal structure of human aqp10 (see paper)
41% identity, 88% coverage: 10:261/285 of query aligns to 5:252/253 of 6f7hC
O14520 Aquaporin-7; AQP-7; Aquaglyceroporin-7; Aquaporin adipose; AQPap; Aquaporin-7-like from Homo sapiens (Human) (see 4 papers)
33% identity, 93% coverage: 7:272/285 of query aligns to 30:290/342 of O14520
- V59 (vs. gap) to L: in dbSNP:rs4008659
- Y135 (≠ S112) Important for permeability to glycerol; mutation to A: Strongly decreased permeability to glycerol. Mildly decreased water permeability.
- H165 (≠ L145) mutation to A: Decreased permeability to glycerol. Mildly decreased water permeability.
- G264 (= G246) to V: affects water and glycerol transport; dbSNP:rs62542743
Sites not aligning to the query:
- 1:32 mutation Missing: Decreased interaction with PLIN1.
- 12 R → C: in dbSNP:rs139297434
8c9hA Aqp7_inhibitor
35% identity, 87% coverage: 7:254/285 of query aligns to 5:247/253 of 8c9hA
6n1gA Crystal structure of aquaglyceroporin aqp7 (see paper)
35% identity, 86% coverage: 9:254/285 of query aligns to 1:241/249 of 6n1gA
I1CR68 Aquaporin-1 from Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar) (see paper)
39% identity, 84% coverage: 13:250/285 of query aligns to 60:292/306 of I1CR68
- H275 (≠ R231) mutation to A: Affects pH sensing; when associated with A-85.
3c02A X-ray structure of the aquaglyceroporin from plasmodium falciparum (see paper)
36% identity, 88% coverage: 9:259/285 of query aligns to 1:236/242 of 3c02A
2evuA Crystal structure of aquaporin aqpm at 2.3a resolution (see paper)
33% identity, 87% coverage: 9:255/285 of query aligns to 3:241/245 of 2evuA
P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
32% identity, 88% coverage: 12:261/285 of query aligns to 38:249/271 of P08995
Sites not aligning to the query:
- 262 modified: Phosphoserine; by CPK
P41181 Aquaporin-2; AQP-2; ADH water channel; Aquaporin-CD; AQP-CD; Collecting duct water channel protein; WCH-CD; Water channel protein for renal collecting duct from Homo sapiens (Human) (see 12 papers)
31% identity, 95% coverage: 5:276/285 of query aligns to 4:244/271 of P41181
- G64 (= G67) to R: in NDI2; loss of water channel activity; dbSNP:rs104894326
- G78 (≠ F81) mutation to A: Does not affect interaction with MIAC; when associated with A-79.
- C79 (≠ A82) mutation to A: Does not affect interaction with MIAC; when associated with A-78.
- S148 (≠ L169) mutation to A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; mutation to D: Retained in the endoplasmic reticulum.
- R187 (= R209) to C: in NDI2; loss of water channel activity; mutant protein does not fold properly; dbSNP:rs104894328
- A190 (≠ G212) to T: in NDI2; mutant protein does not fold properly and is not functional; dbSNP:rs104894341
- V194 (≠ M216) to I: in dbSNP:rs772051028
- S216 (≠ A251) to P: in NDI2; loss of water channel activity; dbSNP:rs104894329
- L217 (≠ A252) mutation to A: Abolishes interaction with MIAC; when associated with A-221.
- Y221 (≠ G256) mutation to A: Abolishes interaction with MIAC; when associated with A-217.
- S229 (≠ H261) mutation to A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; mutation to D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- S231 (≠ P263) mutation to A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; mutation to D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- E232 (≠ S264) mutation to A: Reduces interaction with MIAC.
- T244 (= T276) mutation to A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; mutation to E: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
Sites not aligning to the query:
- 254 R → L: in NDI2; results in the loss of arginine vasopressin-mediated phosphorylation at S-256; R → Q: in NDI2; exerts a dominant-negative effect on wild-type-AQP2 in that it interferes with its trafficking to the apical membrane; is a loss of function instead of a gain of function mutation on dominant nephrogenic diabetes insipidus
- 256 modified: Phosphoserine; by PKA; S→A: Retained in vesicles.; S→D: Expressed in the apical membrane.
- 258 E → K: in NDI2; retained in the Golgi compartment; dbSNP:rs104894332
- 262 P → L: in NDI2; mutant protein folds properly and is functional but is retained in intracellular vesicles; able to assemble into tetramers with wild-type AQP2 that properly localize to the apical membrane; dbSNP:rs104894339; P→A: No effect on expression at the apical cell membrane.
4nefA X-ray structure of human aquaporin 2 (see paper)
32% identity, 89% coverage: 3:255/285 of query aligns to 1:219/239 of 4nefA
P56402 Aquaporin-2; AQP-2; ADH water channel; Aquaporin-CD; AQP-CD; Collecting duct water channel protein; WCH-CD; Water channel protein for renal collecting duct from Mus musculus (Mouse) (see 2 papers)
30% identity, 95% coverage: 5:276/285 of query aligns to 4:244/271 of P56402
- T126 (≠ S147) mutation to M: Does not cause loss of water channel activity, but impairs trafficking from cytoplasmic vesicles to the cell membrane.
Sites not aligning to the query:
- 256 modified: Phosphoserine; S → L: in cph; loss of a phosphorylation site and loss of trafficking to the apical cell membrane; causes aberrant location at the basolateral cell membrane
Q9SAI4 Aquaporin NIP6-1; NOD26-like intrinsic protein 6-1; AtNIP6;1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 89% coverage: 1:254/285 of query aligns to 67:285/305 of Q9SAI4
- A119 (≠ W51) mutation to W: 6-fold increase in water transport activity, but impaired in urea transport.
- V252 (≠ A208) mutation to A: No effect.
O94778 Aquaporin-8; AQP-8 from Homo sapiens (Human) (see 4 papers)
30% identity, 71% coverage: 14:216/285 of query aligns to 38:220/261 of O94778
- C38 (= C14) mutation to S: Does not affect loss of hydrogen peroxide transport after stress.
- F48 (≠ L24) mutation to A: Loss of hydrogen peroxide transport activity under stress condition.
- C53 (= C31) modified: Cysteine persulfide; modified: Cysteine sulfenic acid (-SOH); mutation to S: Does not affect hydrogen peroxide transport under stress condition.
- H72 (≠ W51) mutation to A: Does not affect hydrogen peroxide transport activity under stress condition.
- C173 (≠ I166) mutation to A: Loss of hydrogen peroxide transporter activity.; mutation to S: Slightly affect hydrogen peroxide transport after stress.
- C208 (≠ A204) mutation to S: Does not affect loss of hydrogen peroxide transport after stress.
- R213 (= R209) mutation to A: Does not affect hydrogen peroxide transport activity under stress condition.
Sites not aligning to the query:
- 8 C→S: Does not affect loss of hydrogen peroxide transport after stress.
- 229 I → M: in a breast cancer sample; somatic mutation
- 247 C→S: Does not affect loss of hydrogen peroxide transport after stress.
P09011 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 93% coverage: 5:270/285 of query aligns to 2:233/261 of P09011
- S233 (≠ D270) modified: Phosphoserine
Sites not aligning to the query:
- 244 N→D: No effects.
P06624 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Bos taurus (Bovine) (see 4 papers)
27% identity, 99% coverage: 5:285/285 of query aligns to 4:252/263 of P06624
- Y149 (≠ T170) mutation to G: Increases constitutive water permeability. Abolishes regulation by cytoplasmic calcium levels.; mutation to L: Strongly decreases water permeability. Abolishes regulation by cytoplasmic calcium levels.; mutation to S: Slightly decreases water permeability, but has a minor effect on the regulation by cytoplasmic calcium levels.
- L227 (= L262) mutation to A: Strongly reduced CALM binding.
- 227:237 (vs. 262:270, 27% identical) Interaction with CALM
- V230 (≠ A265) mutation to A: Strongly reduced CALM binding.
- S235 (≠ A268) modified: Phosphoserine
- S243 (≠ T276) modified: Phosphoserine; by PKA
- S245 (≠ V278) modified: Phosphoserine
- N246 (= N279) Interaction with BFSP1; modified: Deamidated asparagine
- E250 (≠ R283) interaction with BFSP1
Query Sequence
>GFF1100 FitnessBrowser__WCS417:GFF1100
MTTALQQPSLSSQCMAEFLGTALLIFFGTGCVAALKVAGASFGLWEISIIWGVGVSMAIY
LSAGISGAHLNPAVSIALCIFADFDKRKLPFYILAQIAGAFCSAALVYTLYSNLFFDYEQ
THHMVRGSQASLELASVFSTYPHALLSTAQAFLVEMVITAILMGVIMALTDDNNGLPRGP
LAPLLIGLLIAVIGSAMGPLTGFAMNPARDFGPKLMTFFAGWGEMAFTGGRDIPYFLVPI
FAPIVGACLGAAAYRGLIARHLPSAAPAIDEETPDTAVNGKTRIS
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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