SitesBLAST
Comparing BPHYT_RS19040 FitnessBrowser__BFirm:BPHYT_RS19040 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)
66% identity, 95% coverage: 5:237/246 of query aligns to 3:231/231 of P60844
- C9 (≠ L11) mutation to S: No effect.
- C20 (= C22) mutation to S: Loss of oligomerization; no alteration of water permeability.
- T183 (= T189) mutation to C: No effect.
- R189 (= R195) mutation R->V,S: Loss of function.
2o9eA Crystal structure of aqpz mutant t183c complexed with mercury (see paper)
65% identity, 94% coverage: 5:236/246 of query aligns to 5:232/232 of 2o9eA
3nkaA Crystal structure of aqpz h174g,t183f (see paper)
66% identity, 87% coverage: 2:215/246 of query aligns to 2:211/230 of 3nkaA
P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
38% identity, 93% coverage: 5:232/246 of query aligns to 38:247/271 of P08995
Sites not aligning to the query:
- 262 modified: Phosphoserine; by CPK
P55088 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Mus musculus (Mouse) (see 2 papers)
36% identity, 93% coverage: 5:232/246 of query aligns to 36:251/323 of P55088
- S111 (≠ P83) 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
2evuA Crystal structure of aquaporin aqpm at 2.3a resolution (see paper)
36% identity, 93% coverage: 1:229/246 of query aligns to 2:240/245 of 2evuA
P47863 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Rattus norvegicus (Rat) (see 4 papers)
34% identity, 93% coverage: 5:232/246 of query aligns to 36:251/323 of P47863
- S180 (≠ K161) modified: Phosphoserine; by PKC; mutation to A: Decreases internalization from the cell membrane in response to PKC activation.
- H201 (= H180) 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
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)
35% identity, 96% coverage: 5:239/246 of query aligns to 10:235/247 of 8ct2D
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, 92% coverage: 4:229/246 of query aligns to 10:219/271 of P56402
- T126 (≠ S136) 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
Q9XF58 Aquaporin PIP2-5; Plasma membrane intrinsic protein 2-5; ZmPIP2-5; ZmPIP2;5; ZmPIP2a from Zea mays (Maize) (see paper)
33% identity, 79% coverage: 39:232/246 of query aligns to 77:269/285 of Q9XF58
- G104 (≠ C66) mutation to W: Loss of water transport.
P06624 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Bos taurus (Bovine) (see 4 papers)
35% identity, 91% coverage: 5:229/246 of query aligns to 11:219/263 of P06624
- Y149 (≠ T159) 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
P55064 Aquaporin-5; AQP-5 from Homo sapiens (Human) (see 2 papers)
36% identity, 91% coverage: 5:229/246 of query aligns to 12:221/265 of P55064
- A38 (= A32) to E: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123054
- I45 (≠ V45) to S: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123055
- N123 (≠ F122) to D: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123057
- S156 (≠ A163) mutation to A: No effect on location at the cell membrane.; mutation to E: Increased location at the cell membrane.
- I177 (= I184) to F: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123056
- R188 (= R195) to C: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs368292687
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)
33% identity, 92% coverage: 4:229/246 of query aligns to 10:219/271 of P41181
- G64 (= G65) to R: in NDI2; loss of water channel activity; dbSNP:rs104894326
- G78 (≠ A79) mutation to A: Does not affect interaction with MIAC; when associated with A-79.
- C79 (≠ G80) mutation to A: Does not affect interaction with MIAC; when associated with A-78.
- S148 (= S158) 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 (= R195) to C: in NDI2; loss of water channel activity; mutant protein does not fold properly; dbSNP:rs104894328
- A190 (≠ G198) to T: in NDI2; mutant protein does not fold properly and is not functional; dbSNP:rs104894341
- V194 (≠ F202) to I: in dbSNP:rs772051028
- S216 (≠ G226) to P: in NDI2; loss of water channel activity; dbSNP:rs104894329
- L217 (≠ V227) 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.
P43286 Aquaporin PIP2-1; Plasma membrane intrinsic protein 2-1; AtPIP2;1; Plasma membrane intrinsic protein 2a; PIP2a from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
31% identity, 92% coverage: 6:232/246 of query aligns to 44:269/287 of P43286
Sites not aligning to the query:
- 3 modified: N6,N6-dimethyllysine; partial; K→A: 2-fold decrease in water transport activity.; K→R: No effect.
- 6 E→A: No effect.
- 280 modified: Phosphoserine; S→A: Normal subcellular localization.
- 283 modified: Phosphoserine; S→A: Intracellular reticulation pattern, probably corresponding to the endoplasmic reticulum.; S→D: Normal subcellular localization.
5dyeD Crystal structure of the full length s156e mutant of human aquaporin 5 (see paper)
36% identity, 91% coverage: 5:229/246 of query aligns to 11:220/253 of 5dyeD
4nefA X-ray structure of human aquaporin 2 (see paper)
33% identity, 92% coverage: 4:229/246 of query aligns to 9:218/239 of 4nefA
Q6Z2T3 Aquaporin NIP2-1; Low silicon protein 1; NOD26-like intrinsic protein 2-1; OsNIP2;1; Silicon influx transporter LSI1 from Oryza sativa subsp. japonica (Rice) (see paper)
31% identity, 99% coverage: 2:244/246 of query aligns to 46:272/298 of Q6Z2T3
- A132 (= A93) mutation to T: In lsi; impairs silicon uptake. Grain discoloration. Reduces grain yield 10-fold.
P61837 Aquaporin PIP1-1; AtPIP1;1; Plasma membrane aquaporin-1; Plasma membrane intrinsic protein 1a; PIP1a from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 78% coverage: 40:232/246 of query aligns to 85:276/286 of P61837
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
P09011 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Rattus norvegicus (Rat) (see 2 papers)
33% identity, 94% coverage: 5:236/246 of query aligns to 9:224/261 of P09011
Sites not aligning to the query:
- 233 modified: Phosphoserine
- 244 N→D: No effects.
Q06611 Aquaporin PIP1-2; AtPIP1;2; Plasma membrane intrinsic protein 1b; PIP1b; Transmembrane protein A; AthH2; TMP-A from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 78% coverage: 40:232/246 of query aligns to 85:275/286 of Q06611
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
Query Sequence
>BPHYT_RS19040 FitnessBrowser__BFirm:BPHYT_RS19040
MQLSKRLVAELFGTFWLVLGGCGSAVLAANFAGPVHGLGIGFVGVSLAFGLTVLTMAFAI
GHISGCHLNPAVSVGLTVAGRFPARDLLPYIVAQLIGAVLGALVLSLIASGKPGFDLVAS
GFASNGYGERSPGHYSLAAAFICEVVMTGFFLFVILGSTDKRAPAGFAPIAIGLCLTLIH
LISIPVTNTSVNPARSTGPALFVGGAAMDQLWLFWVAPILGAVIAGVLYPVIAESRSGNA
QKLALD
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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