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P29218 (IMPA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Protein existenceEvidence 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 componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandLithium
Magnesium
Metal-binding
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processinositol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

inositol phosphate dephosphorylation

Inferred from direct assay Ref.9. Source: MGI

inositol phosphate metabolic process

Traceable author statement. Source: Reactome

phosphate-containing compound metabolic process

Inferred from mutant phenotype Ref.1. Source: UniProtKB

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

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 16189514PubMed 19447967PubMed 21516116. Source: IntAct

inositol monophosphate 1-phosphatase activity

Inferred from mutant phenotype Ref.1. Source: UniProtKB

inositol monophosphate 3-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol monophosphate 4-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein homodimerization activity

Inferred from physical interaction Ref.9. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Inositol monophosphatase 1
PRO_0000142513

Regions

Region92 – 954Substrate binding
Region194 – 1963Substrate binding

Sites

Metal binding701Magnesium 1
Metal binding901Magnesium 1
Metal binding901Magnesium 2
Metal binding921Magnesium 1; via carbonyl oxygen
Metal binding931Magnesium 2
Metal binding2201Magnesium 2
Binding site701Substrate
Binding site2131Substrate
Binding site2201Substrate By similarity

Natural variations

Alternative sequence11M → MGQRPGPVLPAVAVLGQVAK RKVAWLLRWKAVTRTETAGN SSGVYGFGKMKIFVKYFQKM in isoform 3.
VSP_046308
Alternative sequence153 – 277125DITKS…RDDED → GSGVLEQQLLICALWQLAEQ MHIMKWEFTAGMLQELALLL LKLVAC in isoform 2.
VSP_042521
Natural variant1091I → V.
Corresponds to variant rs204781 [ dbSNP | Ensembl ].
VAR_049600

Experimental info

Mutagenesis361K → Q: 50-fold reduction in activity. Ref.15
Mutagenesis931D → N: Loss of activity. Ref.9
Isoform 3:
Sequence conflict171Q → R in BAH13340. Ref.4

Secondary structure

.............................................. 277
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 861D5617E1C04627

FASTA27730,189
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 59A26CFDC77422ED
Show »

FASTA19821,956
Isoform 3 [UniParc].

Checksum: 5838EB952D0C2FA6
Show »

FASTA33636,695

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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 expand/collapse EMBL AC list , 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.
CCDSCCDS47883.1. [P29218-3]
CCDS47884.1. [P29218-2]
CCDS6231.1. [P29218-1]
PIRS23130.
RefSeqNP_001138350.1. NM_001144878.1. [P29218-3]
NP_001138351.1. NM_001144879.1. [P29218-2]
NP_005527.1. NM_005536.3. [P29218-1]
UniGeneHs.656694.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AWBX-ray2.50A/B2-277[»]
1IMAX-ray2.30A/B1-277[»]
1IMBX-ray2.20A/B1-277[»]
1IMCX-ray2.60A/B1-277[»]
1IMDX-ray2.60A/B1-277[»]
1IMEX-ray2.25A/B1-277[»]
1IMFX-ray2.50A1-277[»]
2HHMX-ray2.10A/B2-277[»]
4AS4X-ray1.70A/B1-277[»]
ProteinModelPortalP29218.
SMRP29218. Positions 3-276.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109825. 11 interactions.
IntActP29218. 1 interaction.
MINTMINT-1480285.
STRING9606.ENSP00000408526.

Chemistry

BindingDBP29218.
ChEMBLCHEMBL1786.
DrugBankDB01356. Lithium.
GuidetoPHARMACOLOGY1463.

PTM databases

PhosphoSiteP29218.

Polymorphism databases

DMDM127717.

2D gel databases

REPRODUCTION-2DPAGEIPI00020906.
UCD-2DPAGEP29218.

Proteomic databases

MaxQBP29218.
PaxDbP29218.
PeptideAtlasP29218.
PRIDEP29218.

Protocols and materials databases

DNASU3612.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000256108; ENSP00000256108; ENSG00000133731. [P29218-1]
ENST00000311489; ENSP00000311803; ENSG00000133731. [P29218-2]
ENST00000449740; ENSP00000408526; ENSG00000133731. [P29218-3]
GeneID3612.
KEGGhsa:3612.
UCSCuc003ych.2. human. [P29218-1]
uc011lfr.1. human. [P29218-2]

Organism-specific databases

CTD3612.
GeneCardsGC08M082569.
HGNCHGNC:6050. IMPA1.
HPAHPA037489.
MIM602064. gene.
neXtProtNX_P29218.
PharmGKBPA29860.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0483.
HOGENOMHOG000282238.
HOVERGENHBG052123.
InParanoidP29218.
KOK01092.
OMAKIEFGIV.
OrthoDBEOG7RJPS8.
PhylomeDBP29218.
TreeFamTF313194.

Enzyme and pathway databases

BioCycMetaCyc:HS05783-MONOMER.
BRENDA3.1.3.25. 3474.
ReactomeREACT_111217. Metabolism.
SABIO-RKP29218.
UniPathwayUPA00823; UER00788.

Gene expression databases

ArrayExpressP29218.
BgeeP29218.
CleanExHS_IMPA1.
GenevestigatorP29218.

Family and domain databases

InterProIPR020583. Inositol_monoP_metal-BS.
IPR020552. Inositol_monoPase_Li-sen.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERPTHR20854. PTHR20854. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSPR00377. IMPHPHTASES.
PR00378. LIIMPHPHTASE.
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIMPA1. human.
EvolutionaryTraceP29218.
GeneWikiIMPA1.
GenomeRNAi3612.
NextBio14127.
PROP29218.
SOURCESearch...

Entry information

Entry nameIMPA1_HUMAN
AccessionPrimary (citable) accession number: P29218
Secondary accession number(s): B2R733 expand/collapse secondary AC list , B4DLN3, B7Z6Q4, J3KQT7, Q9UK71
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM