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P22234 (PUR6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. 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:
Multifunctional protein ADE2

Including the following 2 domains:

  1. Phosphoribosylaminoimidazole-succinocarboxamide synthase
    EC=6.3.2.6
    Alternative name(s):
    SAICAR synthetase
  2. Phosphoribosylaminoimidazole carboxylase
    EC=4.1.1.21
    Alternative name(s):
    AIR carboxylase
    Short name=AIRC
Gene names
Name:PAICS
Synonyms:ADE2, AIRC, PAIS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate.

5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2.

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.

Subunit structure

Homooctamer. Ref.19

Sequence similarities

In the N-terminal section; belongs to the SAICAR synthetase family.

In the C-terminal section; belongs to the AIR carboxylase family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionDecarboxylase
Ligase
Lyase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

purine nucleobase biosynthetic process

Traceable author statement Ref.1. Source: ProtInc

purine nucleobase metabolic process

Traceable author statement. Source: Reactome

purine ribonucleoside monophosphate biosynthetic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction PubMed 16169070PubMed 16189514PubMed 21988832. Source: IntAct

phosphoribosylaminoimidazole carboxylase activity

Traceable author statement. Source: Reactome

phosphoribosylaminoimidazolesuccinocarboxamide synthase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P22234-1)

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: P22234-2)

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: G → VTSYKSNR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 425424Multifunctional protein ADE2
PRO_0000075030

Regions

Region2 – 260259SAICAR synthetase
Region261 – 2666Linker
Region267 – 425159AIR carboxylase

Sites

Active site1011For SAICAR synthetase activity Ref.19
Active site1071For SAICAR synthetase activity Ref.19
Active site2151For SAICAR synthetase activity Ref.19
Active site3031For AIR carboxylase activity Ref.19
Active site3321For AIR carboxylase activity Ref.19
Site3341Essential for AIR carboxylase activity

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.11 Ref.18
Modified residue221Phosphotyrosine By similarity
Modified residue271Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.17
Modified residue361N6-acetyllysine By similarity
Modified residue1071Phosphoserine Ref.10
Modified residue2381Phosphothreonine Ref.9
Modified residue2471N6-acetyllysine Ref.14

Natural variations

Alternative sequence721G → VTSYKSNR in isoform 2.
VSP_041265
Natural variant2011K → N.
Corresponds to variant rs11549976 [ dbSNP | Ensembl ].
VAR_051884

Experimental info

Mutagenesis3031H → Y: Loss of AIR carboxylase activity. Ref.19
Mutagenesis3321S → A: Loss of AIR carboxylase activity. Ref.19
Mutagenesis3341G → A: Loss of AIR carboxylase activity. Ref.19
Mutagenesis4001S → A: No change of AIR carboxylase activity.
Sequence conflict2171W → R in CAH18683. Ref.3
Sequence conflict3401S → T in CAH18683. Ref.3

Secondary structure

............................................................... 425
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: E08CF19BC8898F29

FASTA42547,079
        10         20         30         40         50         60 
MATAEVLNIG KKLYEGKTKE VYELLDSPGK VLLQSKDQIT AGNAARKNHL EGKAAISNKI 

        70         80         90        100        110        120 
TSCIFQLLQE AGIKTAFTRK CGETAFIAPQ CEMIPIEWVC RRIATGSFLK RNPGVKEGYK 

       130        140        150        160        170        180 
FYPPKVELFF KDDANNDPQW SEEQLIAAKF CFAGLLIGQT EVDIMSHATQ AIFEILEKSW 

       190        200        210        220        230        240 
LPQNCTLVDM KIEFGVDVTT KEIVLADVID NDSWRLWPSG DRSQQKDKQS YRDLKEVTPE 

       250        260        270        280        290        300 
GLQMVKKNFE WVAERVELLL KSESQCRVVV LMGSTSDLGH CEKIKKACGN FGIPCELRVT 

       310        320        330        340        350        360 
SAHKGPDETL RIKAEYEGDG IPTVFVAVAG RSNGLGPVMS GNTAYPVISC PPLTPDWGVQ 

       370        380        390        400        410        420 
DVWSSLRLPS GLGCSTVLSP EGSAQFAAQI FGLSNHLVWS KLRASILNTW ISLKQADKKI 


RECNL 

« Hide

Isoform 2 [UniParc].

Checksum: 1F8F3B240AD1C137
Show »

FASTA43247,958

References

« Hide 'large scale' references
[1]"Cloning and sequencing of a human cDNA coding for a multifunctional polypeptide of the purine pathway by complementation of the ade2-101 mutant in Saccharomyces cerevisiae."
Minet M., Lacroute F.
Curr. Genet. 18:287-291(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Retina.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Lung and Placenta.
[6]Bienvenut W.V., Potts A., Brablan J., Quadroni M.
Submitted (JUL-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[7]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND THR-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis."
Li S.-X., Tong Y.-P., Xie X.-C., Wang Q.-H., Zhou H.-N., Han Y., Zhang Z.-Y., Gao W., Li S.-G., Zhang X.C., Bi R.-C.
J. Mol. Biol. 366:1603-1614(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, ACTIVE SITE, MUTAGENESIS OF HIS-303; SER-332 AND GLY-334.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53793 mRNA. Translation: CAA37801.1.
BT006988 mRNA. Translation: AAP35634.1.
CR749824 mRNA. Translation: CAH18683.1.
AC068620 Genomic DNA. No translation available.
AC114766 Genomic DNA. No translation available.
BC010273 mRNA. Translation: AAH10273.1.
BC019255 mRNA. Translation: AAH19255.1.
PIRS14147.
RefSeqNP_001072992.1. NM_001079524.1.
NP_001072993.1. NM_001079525.1.
NP_006443.1. NM_006452.3.
UniGeneHs.518774.
Hs.709570.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H31X-ray2.80A1-425[»]
ProteinModelPortalP22234.
SMRP22234. Positions 7-425.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115852. 49 interactions.
IntActP22234. 16 interactions.
MINTMINT-5006326.
STRING9606.ENSP00000382595.

Chemistry

ChEMBLCHEMBL5922.
DrugBankDB00128. L-Aspartic Acid.

PTM databases

PhosphoSiteP22234.

Polymorphism databases

DMDM131628.

Proteomic databases

PaxDbP22234.
PRIDEP22234.

Protocols and materials databases

DNASU10606.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264221; ENSP00000264221; ENSG00000128050. [P22234-1]
ENST00000399688; ENSP00000382595; ENSG00000128050. [P22234-2]
ENST00000512576; ENSP00000421096; ENSG00000128050. [P22234-1]
GeneID10606.
KEGGhsa:10606.
UCSCuc003hbs.1. human. [P22234-1]
uc003hbt.1. human. [P22234-2]

Organism-specific databases

CTD10606.
GeneCardsGC04P057301.
HGNCHGNC:8587. PAICS.
HPAHPA035895.
HPA041538.
MIM172439. gene.
neXtProtNX_P22234.
PharmGKBPA32914.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0041.
HOGENOMHOG000082628.
HOVERGENHBG008335.
InParanoidP22234.
KOK01587.
OMATAFTRKC.
PhylomeDBP22234.
TreeFamTF106384.

Enzyme and pathway databases

BioCycMetaCyc:HS05155-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00074; UER00130.
UPA00074; UER00131.

Gene expression databases

ArrayExpressP22234.
BgeeP22234.
CleanExHS_PAICS.
GenevestigatorP22234.

Family and domain databases

Gene3D3.30.470.20. 1 hit.
3.40.50.7700. 1 hit.
InterProIPR013816. ATP_grasp_subdomain_2.
IPR000031. PurE_dom.
IPR028923. SAICAR_synt/ADE2_N.
IPR018236. SAICAR_synthetase_CS.
[Graphical view]
PfamPF00731. AIRC. 1 hit.
PF01259. SAICAR_synt. 1 hit.
[Graphical view]
SMARTSM01001. AIRC. 1 hit.
[Graphical view]
SUPFAMSSF52255. SSF52255. 1 hit.
TIGRFAMsTIGR01162. purE. 1 hit.
PROSITEPS01057. SAICAR_SYNTHETASE_1. 1 hit.
PS01058. SAICAR_SYNTHETASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPAICS. human.
EvolutionaryTraceP22234.
GenomeRNAi10606.
NextBio40280.
PROP22234.
SOURCESearch...

Entry information

Entry namePUR6_HUMAN
AccessionPrimary (citable) accession number: P22234
Secondary accession number(s): E9PDH9, Q68CQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 151 of the entry and version 3 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 4

Human chromosome 4: entries, gene names and cross-references to MIM