P-POD: Princeton Protein Orthology Database: GO3/Nens390

This family has 38 members: 6 Arabidopsis thaliana, 2 Caenorhabditis elegans, 3 Danio rerio, 2 Dictyostelium discoideum, 7 Drosophila melanogaster, 2 Escherichia coli, 3 Gallus gallus, 3 Homo sapiens, 3 Mus musculus, 3 Rattus norvegicus, 3 Saccharomyces cerevisiae, 1 Schizosaccharomyces pombe.

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GO3/Nens390
38 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaTAIR:locus:2160831 (MBM17.9 · AT5G63990 · MBM17_9) · NCBI:NP_568983.1⌘
A. thalianaNCBI:NP_186936.1 · TAIR:locus:2075392 (F13E7_19 · F13E7.19 · VTC4 · AT3G02870)⌘
A. thalianaNCBI:NP_201203.2 · TAIR:locus:2160826 (ATSAL1 · FIERY1 · HOS2 · MBM17_8 · FRY1 · AT5G63980 · ALX8 · MBM17.8 · SAL1)ALTERED EXPRESSION OF APX2 8 · HIGH EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 2⌘
A. thalianaNCBI:NP_196491.2 · TAIR:locus:2184812 (T5E8.90 · AT5G09290 · T5E8_90)⌘
A. thalianaNCBI:NP_200250.1 · TAIR:locus:2147279 (F24B18_1 · ATAHL · F24B18.1 · AT5G54390 · AHL)ARABIDOPSIS HAL2-LIKE⌘
A. thalianaNCBI:NP_201205.1 · TAIR:locus:2160836 (MBM17.10 · ATSAL2 · SAL2 · MBM17_10 · AT5G64000)⌘
C. elegansWB:WBGene00008765 (F13G3.5 · ttx-7) · UniProtKB:Q19420⌘
C. elegansWB:WBGene00012390 (Y6B3B.5) · UniProtKB:Q5ZEQ3⌘
D. rerioZFIN:ZDB-GENE-051127-23 (zgc:123256) · UniProtKB:Q2YDR3⌘
D. rerioZFIN:ZDB-GENE-050522-349 (zgc:110201) · UniProtKB:Q503S9⌘
D. rerioENSEMBL:ENSDARG00000003517 · UniProtKB:Q6DGB2
D. discoideumUniProtKB:Q55F34 · dictyBase:DDB_G0268652 (DDB_G0268652)3'(2'),5'-bisphosphate nucleotidase, 3'(2'),5'-bisphosphonucleoside 3'(2')-phosphohydrolase, inositol monophosphatase, HAL2 family protein⌘
D. discoideumUniProtKB:Q54U72 · dictyBase:DDB_G0281239 (impa1)inositol-phosphate phosphatase, inositol monophosphatase (IMPase)⌘
D. melanogasterFB:FBgn0030465 (CG15743) · UniProtKB:Q9VYF2⌘
D. melanogasterFB:FBgn0036551 (CG17029 · IMP) · UniProtKB:Q8MQN7⌘
D. melanogasterFB:FBgn0037064 (CG9389 · IMP · 142336_at) · UniProtKB:Q9VP62⌘
D. melanogasterFB:FBgn0037063 (CG9391 · 142335_at · IMP) · UniProtKB:Q9VP63⌘
D. melanogasterFB:FBgn0036550 (CG17026) · UniProtKB:Q9VUW1⌘
D. melanogasterFB:FBgn0036552 (CG17028 · IMP) · UniProtKB:Q9VUW3⌘
D. melanogasterFB:FBgn0036553 (IMP · CG17027 · 152392_at) · UniProtKB:Q9VUW4⌘
E. coliUniProtKB:P22255 · ECOLI:EG10043-MONOMER (cysQ · b4214 · CysQ · amtA · amt · ECK4210)adenosine-3'(2'),5'-bisphosphate nucleotidase⌘
E. coliUniProtKB:P0ADG4 · ECOLI:EG10983-MONOMER (b2533 · ssyA · suhB · ECK2530 · SuhB)inositol monophosphatase⌘
G. gallusNCBI:XP_419214 · ENTREZ:421132
G. gallusNCBI:XP_419118 · ENTREZ:421032
G. gallusNCBI:XP_418310 · ENTREZ:420199
H. sapiensENSEMBL:ENSG00000133731 · UniProtKB:P29218 (IPI00020906 · IMPA1 · P29218 · IMPA · IMPA1_HUMAN)Inositol monophosphatase⌘
H. sapiensENSEMBL:ENSG00000141401 · UniProtKB:O14732 (IMPA2_HUMAN · IPI00023635 · IMPA2 · O14732 · IPI00555726 · IMP.18P)Inositol monophosphatase 2⌘
H. sapiensENSEMBL:ENSG00000104331 · UniProtKB:Q9NX62 (IPI00787853 · IMPA3_HUMAN · Q9NX62 · IMPA3 · IMPAD1)Inositol monophosphatase 3⌘
M. musculusUniProtKB:O55023 · MGI:MGI:1933158 (Impa1)lithium-sensitive myo-inositol monophosphatase A1 · inositol (myo)-1(or 4)-monophosphatase 1⌘
M. musculusUniProtKB:Q91UZ5 · MGI:MGI:2149728 (Impa2)inositol (myo)-1(or 4)-monophosphatase 2⌘
M. musculusUniProtKB:Q80V26 · MGI:MGI:1915720 (gPAPP · Impad1 · Jaws)inositol monophosphatase domain containing 1⌘
R. norvegicusUniProtKB:P97697 · RGD:69254 (Impa1)Inositol (myo)-1(or 4)-monophosphatase 1⌘
R. norvegicusUniProtKB:Q8CIN7 · RGD:628692 (Impa2)inositol (myo)-1(or 4)-monophosphatase 2⌘
R. norvegicusUniProtKB:Q7TPJ5 · RGD:1306455 (Impad1)inositol monophosphatase domain containing 1⌘
S. cerevisiaeUniProtKB:P32179 · SGD:S000005425 (MET22 · HAL2 · YOL064C)Bisphosphate-3'-nucleotidase, involved in salt tolerance and methionine biogenesis⌘
S. cerevisiaeUniProtKB:P38710 · SGD:S000001088 (INM1 · YHR046C)Inositol monophosphatase, involved in biosynthesis of inositol and in phosphoinositide second messenger signaling⌘
S. cerevisiaeUniProtKB:Q05533 · SGD:S000002695 (YDR287W · INM2)Inositol monophosphatase, involved in biosynthesis of inositol⌘
S. pombeGeneDB_Spombe:SPCC1753.04 (SPCC1753.04 · 3' · tol1) · UniProtKB:O94505⌘
ProteinPublicationCurator Notes
UniProtKB:P32179 · SGD:S000005425PMID:15849794 Aggarwal M, et al. Molecular cloning and biochemical characterization of a 3'(2'),5'-bisphosphate nucleotidase from Debaryomyces hansenii. Yeast. 2005 Apr 30;22(6):457-70.The D. hansenii protein DHAL2 complements a homologous mutation in S. cerevisiae.
UniProtKB:P32179 · SGD:S000005425PMID:17420146 Vaupotic T, et al. Novel 3'-phosphoadenosine-5'-phosphatases from extremely halotolerant Hortaea werneckii reveal insight into molecular determinants of salt tolerance of black yeasts. Fungal Genet Biol. 2007 Nov;44(11):1109-22.The H. werneckii protein HxHAL2A complements a homologous mutation in S. cerevisiae.
UniProtKB:P32179 · SGD:S000005425PMID:15583009 Spiegelberg BD, et al. Alteration of lithium pharmacology through manipulation of phosphoadenosine phosphate metabolism. J Biol Chem. 2005 Feb 18;280(7):5400-5.The H. sapiens protein O95861 was expressed in S. cerevisiae, but complementation was not directly tested. This paper describes the biochemical characterization of human BPNT1 in a yeast strain where its homolog, MET22, has been deleted.
UniProtKB:P32179 · SGD:S000005425PMID:17420146 Vaupotic T, et al. Novel 3'-phosphoadenosine-5'-phosphatases from extremely halotolerant Hortaea werneckii reveal insight into molecular determinants of salt tolerance of black yeasts. Fungal Genet Biol. 2007 Nov;44(11):1109-22.The H. werneckii protein HxHAL2B complements a homologous mutation in S. cerevisiae.
DescriptionSuffix
Sequences in this family.fasta
mafft aligned Fasta file.afasta
phyml newick file.newick
Notung rooted & rearranged newick file.newick.rooting.0.rearrange.0
Notung Homolog Table.newick.rooting.0.rearrange.0.homologs.csv
SGD Disease Papers (4)
UniProtKB:P32179 · SGD:S000005425PMID:15583009 Spiegelberg BD, et al. (2005) Alteration of lithium pharmacology through manipulation of phosphoadenosine phosphate metabolism. J Biol Chem 280(7):5400-5
UniProtKB:P38710 · SGD:S000001088PMID:9384595 Dichtl B, et al. (1997) Lithium toxicity in yeast is due to the inhibition of RNA processing enzymes. EMBO J 16(23):7184-95
PMID:7761465 York JD, et al. (1995) Definition of a metal-dependent/Li(+)-inhibited phosphomonoesterase protein family based upon a conserved three-dimensional core structure. Proc Natl Acad Sci U S A 92(11):5149-53
UniProtKB:P38710 · SGD:S000001088PMID:12479670 Agam G, et al. (2002) Myo-inositol-1-phosphate (MIP) synthase: a possible new target for antibipolar drugs. Bipolar Disord 4 Suppl 1:15-20
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