P29218 (IMPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inositol monophosphatase 1
Short name=IMP 1
Short name=IMPase 1
EC=3.1.3.25

Alternative name(s):
Inositol-1(or 4)-monophosphatase 1
Lithium-sensitive myo-inositol monophosphatase A1

Gene names

Name:	IMPA1
Synonyms:	IMPA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. Ref.9
Catalytic activity	Myo-inositol phosphate + H2O = myo-inositol + phosphate.
Cofactor	Magnesium. Ref.9
Enzyme regulation	Inhibited by Li+. Ref.9
Pathway	Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the inositol monophosphatase family.
Biophysicochemical properties	pH dependence: Optimum pH is 7.0-7.5. Ref.9

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Lithium Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inositol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway inositol phosphate dephosphorylation Inferred from direct assay Ref.9. Source: MGI phosphatidylinositol biosynthetic process Inferred from mutant phenotype Ref.1. Source: UniProtKB phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: InterPro signal transduction Inferred from mutant phenotype Ref.1. Source: UniProtKB
Cellular_component	mitochondrion Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	inositol monophosphate 1-phosphatase activity Inferred from mutant phenotype Ref.1. Source: UniProtKB inositol monophosphate 3-phosphatase activity Inferred from electronic annotation. Source: EC inositol monophosphate 4-phosphatase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-752410,EBI-752410

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P29218-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P29218-2)

The sequence of this isoform differs from the canonical sequence as follows:
     153-277: DITKSLLVTE...VIPLQRDDED → GSGVLEQQLL...ALLLLKLVAC

Note: No experimental confirmation available.

Isoform 3 (identifier: P29218-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGQRPGPVLPAVAVLGQVAKRKVAWLLRWKAVTRTETAGNSSGVYGFGKMKIFVKYFQKM

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 277

277

Inositol monophosphatase 1

PRO_0000142513

Regions

Region

92 – 95

4

Substrate binding

Region

194 – 196

3

Substrate binding

Sites

Metal binding

70

1

Magnesium 1

Metal binding

90

1

Magnesium 1

Metal binding

90

1

Magnesium 2

Metal binding

92

1

Magnesium 1; via carbonyl oxygen

Metal binding

93

1

Magnesium 2

Metal binding

220

1

Magnesium 2

Binding site

70

1

Substrate

Binding site

213

1

Substrate

Binding site

220

1

Substrate By similarity

Natural variations

Alternative sequence

1

1

M → MGQRPGPVLPAVAVLGQVAK RKVAWLLRWKAVTRTETAGN SSGVYGFGKMKIFVKYFQKM in isoform 3.

VSP_046308

Alternative sequence

153 – 277

125

DITKS…RDDED → GSGVLEQQLLICALWQLAEQ MHIMKWEFTAGMLQELALLL LKLVAC in isoform 2.

VSP_042521

Natural variant

109

1

I → V.
Corresponds to variant rs204781 [ dbSNP | Ensembl ].

VAR_049600

Experimental info

Mutagenesis

36

1

K → Q: 50-fold reduction in activity. Ref.15

Mutagenesis

93

1

D → N: Loss of activity. Ref.9

Isoform 3:

Sequence conflict

17

1

Q → R in BAH13340. Ref.4

Secondary structure

1

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277

Helix Strand Turn

Details...

Helix

4 – 26

23

Beta strand

34 – 38

5

Beta strand

41 – 43

3

Helix

45 – 61

17

Beta strand

66 – 69

4

Helix

70 – 74

5

Beta strand

86 – 93

8

Helix

95 – 100

6

Beta strand

106 – 113

8

Beta strand

116 – 124

9

Turn

125 – 128

4

Beta strand

129 – 134

6

Turn

135 – 137

3

Beta strand

138 – 141

4

Helix

154 – 156

3

Beta strand

158 – 160

3

Helix

169 – 183

15

Turn

184 – 186

3

Beta strand

188 – 192

5

Helix

196 – 204

9

Beta strand

207 – 215

9

Helix

218 – 230

13

Beta strand

234 – 236

3

Beta strand

240 – 242

3

Beta strand

247 – 255

9

Helix

256 – 265

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 861D5617E1C04627	FASTA	277	30,189
	10 20 30 40 50 60 MADPWQECMD YAVTLARQAG EVVCEAIKNE MNVMLKSSPV DLVTATDQKV EKMLISSIKE 70 80 90 100 110 120 KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH RFPFVAVSIG FAVNKKIEFG 130 140 150 160 170 180 VVYSCVEGKM YTARKGKGAF CNGQKLQVSQ QEDITKSLLV TELGSSRTPE TVRMVLSNME 190 200 210 220 230 240 KLFCIPVHGI RSVGTAAVNM CLVATGGADA YYEMGIHCWD VAGAGIIVTE AGGVLMDVTG 250 260 270 GPFDLMSRRV IAANNRILAE RIAKEIQVIP LQRDDED
	Isoform 2 [UniParc]. Checksum: 59A26CFDC77422ED	FASTA	198	21,956
	10 20 30 40 50 60 MADPWQECMD YAVTLARQAG EVVCEAIKNE MNVMLKSSPV DLVTATDQKV EKMLISSIKE 70 80 90 100 110 120 KYPSHSFIGE ESVAAGEKSI LTDNPTWIID PIDGTTNFVH RFPFVAVSIG FAVNKKIEFG 130 140 150 160 170 180 VVYSCVEGKM YTARKGKGAF CNGQKLQVSQ QEGSGVLEQQ LLICALWQLA EQMHIMKWEF 190 TAGMLQELAL LLLKLVAC
	Isoform 3 [UniParc]. Checksum: 5838EB952D0C2FA6	FASTA	336	36,695
	10 20 30 40 50 60 MGQRPGPVLP AVAVLGQVAK RKVAWLLRWK AVTRTETAGN SSGVYGFGKM KIFVKYFQKM 70 80 90 100 110 120 ADPWQECMDY AVTLARQAGE VVCEAIKNEM NVMLKSSPVD LVTATDQKVE KMLISSIKEK 130 140 150 160 170 180 YPSHSFIGEE SVAAGEKSIL TDNPTWIIDP IDGTTNFVHR FPFVAVSIGF AVNKKIEFGV 190 200 210 220 230 240 VYSCVEGKMY TARKGKGAFC NGQKLQVSQQ EDITKSLLVT ELGSSRTPET VRMVLSNMEK 250 260 270 280 290 300 LFCIPVHGIR SVGTAAVNMC LVATGGADAY YEMGIHCWDV AGAGIIVTEA GGVLMDVTGG 310 320 330 PFDLMSRRVI AANNRILAER IAKEIQVIPL QRDDED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme." McAllister G., Whiting P., Hammond E.A., Knowles M.R., Atack J.R., Bailey F.J., Maigetter R., Ragan C.I. Biochem. J. 284:749-754(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Hippocampus.
[2]	"Genomic structure and chromosomal localization of a human myo-inositol monophosphatase gene (IMPA)." Sjoeholt G., Molven A., Loevlie R., Wilcox A., Sikela J.M., Steen V.M. Genomics 45:113-122(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Molecular cloning and expression of human cerebral cortex myo-inositol monophosphatase A1 cDNA." Parthasarathy R., Parthasarathy L., Vadnal R.E. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Tissue: Thymus and Umbilical cord blood.
[5]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Urinary bladder.
[8]	"Molecular cloning, genomic organization and promoter analysis of the human brain lithium-sensitive myo-inositol monophosphatase A1 isoenzyme." Parthasarathy L., Parthasarathy R. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
[9]	"Spatial expression patterns and biochemical properties distinguish a second myo-inositol monophosphatase IMPA2 from IMPA1." Ohnishi T., Ohba H., Seo K.-C., Im J., Sato Y., Iwayama Y., Furuichi T., Chung S.-K., Yoshikawa T. J. Biol. Chem. 282:637-646(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, MUTAGENESIS OF ASP-93.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Structure of inositol monophosphatase, the putative target of lithium therapy." Bone R., Springer J.P., Atack J.R. Proc. Natl. Acad. Sci. U.S.A. 89:10031-10035(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
[14]	"Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis." Bone R., Frank L., Springer J.P., Atack J.R. Biochemistry 33:9468-9476(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
[15]	"The contribution of lysine-36 to catalysis by human myo-inositol monophosphatase." Ganzhorn A.J., Lepage P., Pelton P.D., Strasser F., Vincendon P., Rondeau J.-M. Biochemistry 35:10957-10966(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT GLN-36, MUTAGENESIS OF LYS-36.
[16]	"Structure of an enzyme-substrate complex and the catalytic mechanism of human brain myo-inositol monophosphatase." Ganzhorn A.J., Rondeau J.-M. Protein Eng. 10:61-70(1997) Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X66922 mRNA. Translation: CAA47359.1.
Y11360 , Y11361, Y11362, Y11367, Y11363, Y11364, Y11365, Y11366 Genomic DNA. Translation: CAA72195.1.
AF042729 mRNA. Translation: AAB97468.1.
AK297078 mRNA. Translation: BAG59595.1.
AK300750 mRNA. Translation: BAH13340.1.
AK312823 mRNA. Translation: BAG35680.1.
AC090255 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW87095.1.
BC008381 mRNA. Translation: AAH08381.1.
BC009565 mRNA. Translation: AAH09565.1.
AF178754 Genomic DNA. Translation: AAD52997.1.

IPI

IPI00020906.
IPI00791997.
IPI00921428.

PIR

S23130.

RefSeq

NP_001138350.1. NM_001144878.1.
NP_001138351.1. NM_001144879.1.
NP_005527.1. NM_005536.3.

UniGene

Hs.656694.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AWB	X-ray	2.50	A/B	2-277	[»]
1IMA	X-ray	2.30	A/B	1-277	[»]
1IMB	X-ray	2.20	A/B	1-277	[»]
1IMC	X-ray	2.60	A/B	1-277	[»]
1IMD	X-ray	2.60	A/B	1-277	[»]
1IME	X-ray	2.25	A/B	1-277	[»]
1IMF	X-ray	2.50	A	1-277	[»]
2HHM	X-ray	2.10	A/B	2-277	[»]
4AS4	X-ray	1.70	A/B	1-277	[»]

ProteinModelPortal

P29218.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1480285.

STRING

9606.ENSP00000408526.

PTM databases

PhosphoSite

P29218.

Polymorphism databases

DMDM

127717.

2D gel databases

REPRODUCTION-2DPAGE

IPI00020906.

UCD-2DPAGE

P29218.

Proteomic databases

PaxDb

P29218.

PeptideAtlas

P29218.

PRIDE

P29218.

Protocols and materials databases

DNASU

3612.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000256108; ENSP00000256108; ENSG00000133731.
ENST00000311489; ENSP00000311803; ENSG00000133731.
ENST00000449740; ENSP00000408526; ENSG00000133731.

GeneID

3612.

KEGG

hsa:3612.

UCSC

uc003ych.2. human.

Organism-specific databases

CTD

3612.

GeneCards

GC08M082569.

HGNC

HGNC:6050. IMPA1.

HPA

HPA037489.

MIM

602064. gene.

neXtProt

NX_P29218.

PharmGKB

PA29860.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0483.

HOGENOM

HOG000282238.

HOVERGEN

HBG052123.

InParanoid

P29218.

KO

K01092.

OrthoDB

EOG42FSJ2.

PhylomeDB

P29218.

Enzyme and pathway databases

BioCyc

MetaCyc:HS05783-MONOMER.

BRENDA

3.1.3.25. 3474.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P29218.

UniPathway

UPA00823; UER00788.

Gene expression databases

ArrayExpress

P29218.

Bgee

P29218.

CleanEx

HS_IMPA1.

Genevestigator

P29218.

GermOnline

ENSG00000133731. Homo sapiens.

Family and domain databases

InterPro

IPR020583. Inositol_monoP_metal-BS.
IPR020552. Inositol_monoPase_Li-sen.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]

PANTHER

PTHR20854. PTHR20854. 1 hit.

Pfam

PF00459. Inositol_P. 1 hit.
[Graphical view]

PRINTS

PR00377. IMPHPHTASES.
PR00378. LIIMPHPHTASE.

PROSITE

PS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P29218.

ChEMBL

CHEMBL1786.

ChiTaRS

IMPA1. human.

DrugBank

DB01356. Lithium.

EvolutionaryTrace

P29218.

GenomeRNAi

3612.

NextBio

14127.

SOURCE

Search...

Entry information

Entry name

IMPA1_HUMAN

Accession

Primary (citable) accession number: P29218
Secondary accession number(s): B2R733 , B4DLN3, B7Z6Q4, J3KQT7, Q9UK71

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	May 1, 2013
This is version 145 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.