SitesBLAST
Comparing Ga0059261_1307 FitnessBrowser__Korea:Ga0059261_1307 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P60844 Aquaporin Z; Bacterial nodulin-like intrinsic protein; Water channel AqpZ from Escherichia coli (strain K12) (see paper)
68% identity, 84% coverage: 9:211/243 of query aligns to 7:209/231 of P60844
- C9 (≠ L11) mutation to S: No effect.
- C20 (= C22) mutation to S: Loss of oligomerization; no alteration of water permeability.
- T183 (= T185) mutation to C: No effect.
- R189 (= R191) mutation R->V,S: Loss of function.
2o9eA Crystal structure of aqpz mutant t183c complexed with mercury (see paper)
67% identity, 84% coverage: 9:211/243 of query aligns to 9:211/232 of 2o9eA
3nkaA Crystal structure of aqpz h174g,t183f (see paper)
67% identity, 84% coverage: 9:211/243 of query aligns to 9:211/230 of 3nkaA
P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
38% identity, 92% coverage: 4:226/243 of query aligns to 37:245/271 of P08995
Sites not aligning to the query:
- 262 modified: Phosphoserine; by CPK
8ct2D Local refinement of aqp1 tetramer (c1; refinement mask included d1 of protein 4.2 and ankyrin-1 ar1-5) in class 2 of erythrocyte ankyrin-1 complex (see paper)
37% identity, 95% coverage: 8:238/243 of query aligns to 13:242/247 of 8ct2D
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)
36% identity, 90% coverage: 9:226/243 of query aligns to 15:220/271 of P41181
- G64 (= G61) to R: in NDI2; loss of water channel activity; dbSNP:rs104894326
- G78 (= G75) mutation to A: Does not affect interaction with MIAC; when associated with A-79.
- C79 (≠ G76) mutation to A: Does not affect interaction with MIAC; when associated with A-78.
- S148 (= S154) 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 (= R191) to C: in NDI2; loss of water channel activity; mutant protein does not fold properly; dbSNP:rs104894328
- A190 (≠ G194) to T: in NDI2; mutant protein does not fold properly and is not functional; dbSNP:rs104894341
- V194 (≠ I198) to I: in dbSNP:rs772051028
- S216 (≠ G222) to P: in NDI2; loss of water channel activity; dbSNP:rs104894329
- L217 (≠ I223) mutation to A: Abolishes interaction with MIAC; when associated with A-221.
Sites not aligning to the query:
- 221 Y→A: Abolishes interaction with MIAC; when associated with A-217.
- 229 S→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; S→D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- 231 S→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; S→D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- 232 E→A: Reduces interaction with MIAC.
- 244 T→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; T→E: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- 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)
36% identity, 90% coverage: 9:226/243 of query aligns to 14:219/239 of 4nefA
P55064 Aquaporin-5; AQP-5 from Homo sapiens (Human) (see 2 papers)
37% identity, 90% coverage: 8:225/243 of query aligns to 15:221/265 of P55064
- A38 (≠ V34) to E: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123054
- I45 (≠ V41) to S: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123055
- N123 (≠ L118) to D: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123057
- S156 (≠ A159) mutation to A: No effect on location at the cell membrane.; mutation to E: Increased location at the cell membrane.
- I177 (= I180) to F: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123056
- R188 (= R191) to C: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs368292687
2evuA Crystal structure of aquaporin aqpm at 2.3a resolution (see paper)
37% identity, 92% coverage: 5:228/243 of query aligns to 6:243/245 of 2evuA
5dyeD Crystal structure of the full length s156e mutant of human aquaporin 5 (see paper)
37% identity, 90% coverage: 8:225/243 of query aligns to 14:220/253 of 5dyeD
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)
35% identity, 93% coverage: 8:234/243 of query aligns to 14:228/271 of P56402
- T126 (≠ P128) 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
P55088 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Mus musculus (Mouse) (see 2 papers)
35% identity, 90% coverage: 9:226/243 of query aligns to 40:249/323 of P55088
- S111 (≠ A79) modified: Phosphoserine; by PKG; mutation to A: Loss of phosphorylation by PKG (in vitro). No effect on location at cell membrane.
Sites not aligning to the query:
- 4 natural variant: G -> R
P30301 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Homo sapiens (Human) (see 10 papers)
36% identity, 91% coverage: 8:228/243 of query aligns to 14:222/263 of P30301
- R33 (≠ L27) to C: in CTRCT15; reduces cell-to-cell adhesion, reduces cell-to-cell gap junction coupling, no loss of cell membrane localization, no loss of water channel activity; dbSNP:rs864309693
- V107 (≠ I104) to I: in CTRCT15; likely benign; dbSNP:rs74641138
- E134 (= E140) to G: in CTRCT15; non-progressive lamellar cataract; loss of activity; dbSNP:rs121917869
- T138 (= T144) to R: in CTRCT15; progressive polymorphic and lamellar cataract; loss of activity; dbSNP:rs121917867
- D150 (= D156) to H: in CTRCT15; loss of plasma membrane expression; dbSNP:rs778327521
- G165 (= G169) to D: in CTRCT15; uncertain significance; loss of plasma membrane expression
- Y177 (≠ P181) to C: in CTRCT15; uncertain significance
Sites not aligning to the query:
- 204:263 natural variant: Missing (in CTRCT15; uncertain significance)
- 211:263 natural variant: Missing (in CTRCT15; uncertain significance)
- 235 modified: Phosphoserine
- 246 modified: Deamidated asparagine; by deterioration
- 259 modified: Deamidated asparagine; by deterioration
P09011 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Rattus norvegicus (Rat) (see 2 papers)
36% identity, 91% coverage: 8:228/243 of query aligns to 12:220/261 of P09011
Sites not aligning to the query:
- 233 modified: Phosphoserine
- 244 N→D: No effects.
P47863 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Rattus norvegicus (Rat) (see 4 papers)
36% identity, 79% coverage: 36:226/243 of query aligns to 68:249/323 of P47863
- S180 (= S157) modified: Phosphoserine; by PKC; mutation to A: Decreases internalization from the cell membrane in response to PKC activation.
- H201 (= H176) mutation to P: Partial loss of transport activity.
Sites not aligning to the query:
- 13 modified: S-palmitoyl cysteine; C→A: Reduced palmitoylation. Loss of palmitoylation; when associated with A-17.
- 17 modified: S-palmitoyl cysteine; C→A: Reduced palmitoylation. Loss of palmitoylation; when associated with A-13.
- 285 modified: Phosphoserine
Q9SAI4 Aquaporin NIP6-1; NOD26-like intrinsic protein 6-1; AtNIP6;1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 95% coverage: 9:239/243 of query aligns to 84:299/305 of Q9SAI4
- A119 (≠ F45) mutation to W: 6-fold increase in water transport activity, but impaired in urea transport.
- V252 (≠ A190) mutation to A: No effect.
P43287 Aquaporin PIP2-2; Plasma membrane intrinsic protein 2-2; AtPIP2;2; Plasma membrane intrinsic protein 2b; PIP2b; TMP2b from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
35% identity, 82% coverage: 35:234/243 of query aligns to 75:274/285 of P43287
- R194 (≠ G162) mutation to A: Reduced sensitivity to cytosolic acidification. Insensitive to cytosolic acidification; when associated with A-197.
- D195 (vs. gap) mutation to A: Reduced sensitivity to cytosolic acidification. Insensitive to cytosolic acidification; when associated with A-197.
- H197 (vs. gap) mutation to A: Reduced water transport activity. Reduced sensitivity to cytosolic acidification. Insensitive to cytosolic acidification; when associated with A-194 or A-195.; mutation to D: Reduced water transport activity. Insensitive to cytosolic acidification.; mutation to K: Very low water transport activity. Insensitive to cytosolic acidification.
- H264 (≠ Y225) mutation to A: No effect.
Sites not aligning to the query:
- 3 modified: N6,N6-dimethyllysine; partial
P06624 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Bos taurus (Bovine) (see 4 papers)
35% identity, 91% coverage: 9:228/243 of query aligns to 15:222/263 of P06624
- Y149 (≠ T155) 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.
Sites not aligning to the query:
- 227 L→A: Strongly reduced CALM binding.
- 227:237 Interaction with CALM
- 230 V→A: Strongly reduced CALM binding.
- 235 modified: Phosphoserine
- 243 modified: Phosphoserine; by PKA
- 245 modified: Phosphoserine
- 246 Interaction with BFSP1; modified: Deamidated asparagine
- 250 interaction with BFSP1
Q08733 Aquaporin PIP1-3; AtPIP1;3; Plasma membrane intrinsic protein 1c; PIP1c; Transmembrane protein B; TMP-B from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 91% coverage: 5:226/243 of query aligns to 52:274/286 of Q08733
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
P30302 Aquaporin PIP2-3; Plasma membrane intrinsic protein 2-3; AtPIP2;3; Plasma membrane intrinsic protein 2c; PIP2c; RD28-PIP; TMP2C; Water stress-induced tonoplast intrinsic protein; WSI-TIP from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 82% coverage: 35:234/243 of query aligns to 75:274/285 of P30302
- T223 (= T185) mutation to C: Creates some mercury-sensitivity.
Query Sequence
>Ga0059261_1307 FitnessBrowser__Korea:Ga0059261_1307
MTNVQRGLAELVGTFWLVFGGCGSAVLAAAFPEVGIGLLGVSFAFGLTVLTMAYSIGHIS
GCHLNPAVTFGLWAGGRFAGKDIPLYVVAQVIGAVIAAWLLYCIASGAPGGYDLAGGLAA
NGFGEHSPGKFNLQSALAIEVVLTFMFVVIIMGSTDSRAPAGFAPIAIGLALMLIHLISI
PVTNTSVNPARSTGPALIVGGWAISQLWLFWVAPIVGGVLGGIFYKALGADASKRPPVEG
APL
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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