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P67775 (PP2AA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform

Short name=PP2A-alpha
EC=3.1.3.16
Alternative name(s):
Replication protein C
Short name=RP-C
Gene names
Name:PPP2CA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

PP2A is the major phosphatase for microtubule-associated proteins (MAPs). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase. Cooperates with SGOL2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I By similarity. Can dephosphorylate SV40 large T antigen and p53/TP53. Activates RAF1 by dephosphorylating it at 'Ser-259'. Ref.10 Ref.11 Ref.21

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Subunit structure

PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with NXN; the interaction is direct By similarity. Interacts with TP53, SGOL1 and SGOL2. Interacts with AXIN1; the interaction dephosphorylates AXIN1. Interacts with PIM3; this interaction promotes dephosphorylation, ubiquitination and proteasomal degradation of PIM3. Interacts with RAF1. Interaction with IGBP1 protects unassembled PPP2CA from degradative ubiquitination. Interacts with GSK3B (via C2 domain). Ref.7 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Subcellular location

Cytoplasm. Nucleus. Chromosomecentromere. Cytoplasmcytoskeletonspindle pole. Note: In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles. Centromeric localization requires the presence of SGOL2 By similarity. Ref.13

Post-translational modification

Reversibly methyl esterified on Leu-309. Carboxyl methylation may play a role in holoenzyme assembly, enhancing the affinity of the PP2A core enzyme for some, but not all, regulatory subunits. It varies during the cell cycle.

Phosphorylation of either threonine (by autophosphorylation-activated protein kinase) or tyrosine results in inactivation of the phosphatase. Auto-dephosphorylation has been suggested as a mechanism for reactivation.

Sequence similarities

Belongs to the PPP phosphatase family. PP-1 subfamily.

Ontologies

Keywords
   Biological processMeiosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandIron
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMMethylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA splicing

Non-traceable author statement PubMed 11007961. Source: UniProtKB

apoptotic process

Traceable author statement PubMed 11007961. Source: UniProtKB

ceramide metabolic process

Non-traceable author statement PubMed 11007961. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

inactivation of MAPK activity

Non-traceable author statement PubMed 11007961. Source: UniProtKB

mRNA metabolic process

Traceable author statement. Source: Reactome

meiotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

mesoderm development

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear envelope reassembly

Traceable author statement. Source: Reactome

negative regulation of cell growth

Non-traceable author statement PubMed 11007961. Source: UniProtKB

negative regulation of epithelial to mesenchymal transition

Inferred from mutant phenotype Ref.19. Source: BHF-UCL

negative regulation of tyrosine phosphorylation of Stat3 protein

Non-traceable author statement PubMed 11007961. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

positive regulation of protein serine/threonine kinase activity

Inferred from mutant phenotype Ref.19. Source: BHF-UCL

protein dephosphorylation

Traceable author statement PubMed 11007961Ref.1. Source: UniProtKB

protein heterotrimerization

Inferred from electronic annotation. Source: Ensembl

regulation of DNA replication

Non-traceable author statement PubMed 11007961. Source: UniProtKB

regulation of Wnt signaling pathway

Non-traceable author statement PubMed 11007961. Source: UniProtKB

regulation of cell adhesion

Non-traceable author statement PubMed 11007961. Source: UniProtKB

regulation of cell differentiation

Non-traceable author statement PubMed 11360189. Source: UniProtKB

regulation of growth

Non-traceable author statement PubMed 11360189. Source: UniProtKB

regulation of protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of receptor activity

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Non-traceable author statement PubMed 11007961. Source: UniProtKB

response to organic substance

Non-traceable author statement PubMed 11007961. Source: UniProtKB

second-messenger-mediated signaling

Non-traceable author statement PubMed 11007961. Source: UniProtKB

   Cellular_componentchromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement PubMed 11007961. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

membrane

Non-traceable author statement PubMed 11007961. Source: UniProtKB

microtubule cytoskeleton

Non-traceable author statement PubMed 11007961. Source: UniProtKB

mitochondrion

Non-traceable author statement PubMed 11007961. Source: UniProtKB

nucleus

Non-traceable author statement PubMed 11007961. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein phosphatase type 2A complex

Inferred from direct assay PubMed 17055435PubMed 17174897. Source: UniProtKB

spindle pole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine phosphatase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P67775-1)

Also known as: PP2Acalpha1;

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: P67775-2)

Also known as: PP2Acalpha2;

The sequence of this isoform differs from the canonical sequence as follows:
     193-246: Missing.
Note: Catalytically inactive, shows enhanced binding to IGBP1, and does not interact with the scaffolding subunit PPP2R1A.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
PRO_0000058839

Sites

Active site1181Proton donor By similarity
Metal binding571Iron By similarity
Metal binding591Iron By similarity
Metal binding851Iron By similarity
Metal binding851Manganese By similarity
Metal binding1171Manganese By similarity
Metal binding1671Manganese By similarity
Metal binding2411Manganese By similarity

Amino acid modifications

Modified residue3071Phosphotyrosine
Modified residue3091Leucine methyl ester Ref.6

Natural variations

Alternative sequence193 – 24654Missing in isoform 2.
VSP_044320
Natural variant521V → A.
Corresponds to variant rs11552681 [ dbSNP | Ensembl ].
VAR_051735

Experimental info

Mutagenesis3091L → A: Loss of binding to PP2A B-alpha regulatory subunit. Ref.8

Secondary structure

......................................................... 309
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PP2Acalpha1) [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: C602291F78F34555

FASTA30935,594
        10         20         30         40         50         60 
MDEKVFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC PVTVCGDVHG 

        70         80         90        100        110        120 
QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYRER ITILRGNHES 

       130        140        150        160        170        180 
RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI 

       190        200        210        220        230        240 
RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA 

       250        260        270        280        290        300 
HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV 


TRRTPDYFL 

« Hide

Isoform 2 (PP2Acalpha2) [UniParc].

Checksum: B50450F64CB286AB
Show »

FASTA25529,735

References

« Hide 'large scale' references
[1]"The nucleotide sequence of the cDNA encoding the human lung protein phosphatase 2A alpha catalytic subunit."
Stone S.R., Mayer R., Wernet W., Maurer F., Hofsteenge J., Hemmings B.A.
Nucleic Acids Res. 16:11365-11365(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fibroblast.
[2]"Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes."
Arino J., Woon C.W., Brautigan D.L., Miller T.B. Jr., Johnson G.L.
Proc. Natl. Acad. Sci. U.S.A. 85:4252-4256(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[3]"Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes."
Khew-Goodall Y., Mayer R.E., Maurer F., Stone S.R., Hemmings B.A.
Biochemistry 30:89-97(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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, Placenta and Uterus.
[5]"Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: inhibition by small-t antigen."
Scheidtmann K.H., Mumby M.C., Rundell K., Walter G.
Mol. Cell. Biol. 11:1996-2003(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DEPHOSPHORYLATION OF SV40 LARGE-T ANTIGEN AND P53 PROTEIN.
[6]"The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo."
Favre B., Zolnierowicz S., Turowski P., Hemmings B.A.
J. Biol. Chem. 269:16311-16317(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LEU-309.
[7]"Alpha 4 associates with protein phosphatases 2A, 4, and 6."
Chen J., Peterson R.T., Schreiber S.L.
Biochem. Biophys. Res. Commun. 247:827-832(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGBP1.
[8]"Methylated C-terminal leucine residue of PP2A catalytic subunit is important for binding of regulatory Balpha subunit."
Bryant J.C., Westphal R.S., Wadzinski B.E.
Biochem. J. 339:241-246(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LEU-309.
[9]"Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A."
Virshup D.M., Kauffman M.G., Kelly T.J.
EMBO J. 8:3891-3898(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, ACTIVATION OF SV40 REPLICATION.
[10]"Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain."
Hsu W., Zeng L., Costantini F.
J. Biol. Chem. 274:3439-3445(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AXIN1, FUNCTION.
[11]"Raf-1-associated protein phosphatase 2A as a positive regulator of kinase activation."
Abraham D., Podar K., Pacher M., Kubicek M., Welzel N., Hemmings B.A., Dilworth S.M., Mischak H., Kolch W., Baccarini M.
J. Biol. Chem. 275:22300-22304(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAF1.
[12]"PP2A is required for centromeric localization of Sgo1 and proper chromosome segregation."
Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.
Dev. Cell 10:575-585(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SGOL1.
[13]"Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SGOL1.
[14]"Protein phosphatase 2A regulates the stability of Pim protein kinases."
Losman J.A., Chen X.P., Vuong B.Q., Fay S., Rothman P.B.
J. Biol. Chem. 278:4800-4805(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIM3.
[15]"A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55."
Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.
EMBO J. 26:402-411(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TP53.
[16]"Tripin/hSgo2 recruits MCAK to the inner centromere to correct defective kinetochore attachments."
Huang H., Feng J., Famulski J., Rattner J.B., Liu S.T., Kao G.D., Muschel R., Chan G.K., Yen T.J.
J. Cell Biol. 177:413-424(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SGOL2.
[17]"Alpha4 is an essential regulator of PP2A phosphatase activity."
Kong M., Ditsworth D., Lindsten T., Thompson C.B.
Mol. Cell 36:51-60(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGBP1.
[18]"Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination."
McConnell J.L., Watkins G.R., Soss S.E., Franz H.S., McCorvey L.R., Spiller B.W., Chazin W.J., Wadzinski B.E.
Biochemistry 49:1713-1718(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGBP1.
[19]"Role of DAB2IP in modulating epithelial-to-mesenchymal transition and prostate cancer metastasis."
Xie D., Gore C., Liu J., Pong R.C., Mason R., Hao G., Long M., Kabbani W., Yu L., Zhang H., Chen H., Sun X., Boothman D.A., Min W., Hsieh J.T.
Proc. Natl. Acad. Sci. U.S.A. 107:2485-2490(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GSK3B.
[20]"Identification and characterization of an alternatively spliced isoform of the human protein phosphatase 2Aalpha catalytic subunit."
Migueleti D.L., Smetana J.H., Nunes H.F., Kobarg J., Zanchin N.I.
J. Biol. Chem. 287:4853-4862(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
[21]"Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit alpha4, altering PP2A stability and microtubule-associated protein phosphorylation."
Watkins G.R., Wang N., Mazalouskas M.D., Gomez R.J., Guthrie C.R., Kraemer B.C., Schweiger S., Spiller B.W., Wadzinski B.E.
J. Biol. Chem. 287:24207-24215(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"Structural mechanism of demethylation and inactivation of protein phosphatase 2A."
Xing Y., Li Z., Chen Y., Stock J.B., Jeffrey P.D., Shi Y.
Cell 133:154-163(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH PPP2R1A AND PPME1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12646 mRNA. Translation: CAA31176.1.
J03804 mRNA. Translation: AAB38019.1.
M60483 Genomic DNA. Translation: AAA36466.1.
BC000400 mRNA. Translation: AAH00400.1.
BC002657 mRNA. Translation: AAH02657.1.
BC019275 mRNA. Translation: AAH19275.1.
BC031696 mRNA. Translation: AAH31696.1.
PIRPAHU2A. S01986.
RefSeqNP_002706.1. NM_002715.2.
UniGeneHs.105818.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IAEX-ray3.50C/F1-309[»]
2IE3X-ray2.80C1-309[»]
2IE4X-ray2.60C1-309[»]
2NPPX-ray3.30C/F1-309[»]
2NYLX-ray3.80C/F2-294[»]
2NYMX-ray3.60C/F2-294[»]
3C5WX-ray2.80C1-309[»]
3DW8X-ray2.85C/F1-309[»]
3FGAX-ray2.70C1-309[»]
3K7VX-ray2.85C1-309[»]
3K7WX-ray2.96C1-309[»]
3P71X-ray2.70C1-309[»]
4I5LX-ray2.43C/F1-309[»]
4I5NX-ray2.80C/F1-309[»]
4IYPX-ray2.80C6-153[»]
4LACX-ray2.82C1-309[»]
ProteinModelPortalP67775.
SMRP67775. Positions 2-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111507. 154 interactions.
DIPDIP-29395N.
IntActP67775. 115 interactions.
MINTMINT-215645.
STRING9606.ENSP00000418447.

Chemistry

BindingDBP67775.
ChEMBLCHEMBL4703.
DrugBankDB00163. Vitamin E.

PTM databases

PhosphoSiteP67775.

Polymorphism databases

DMDM54038809.

Proteomic databases

PaxDbP67775.
PRIDEP67775.

Protocols and materials databases

DNASU5515.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000481195; ENSP00000418447; ENSG00000113575. [P67775-1]
GeneID5515.
KEGGhsa:5515.
UCSCuc003kze.3. human. [P67775-1]

Organism-specific databases

CTD5515.
GeneCardsGC05M133530.
HGNCHGNC:9299. PPP2CA.
HPACAB003848.
MIM176915. gene.
neXtProtNX_P67775.
PharmGKBPA33663.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172696.
HOVERGENHBG000216.
InParanoidP67775.
KOK04382.
OMALMACKQL.
OrthoDBEOG74N5H2.
PhylomeDBP67775.
TreeFamTF105559.

Enzyme and pathway databases

BioCycMetaCyc:HS03696-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
REACT_71. Gene Expression.
SignaLinkP67775.

Gene expression databases

ArrayExpressP67775.
BgeeP67775.
CleanExHS_PPP2CA.
GenevestigatorP67775.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP67775.
GeneWikiPPP2CA.
GenomeRNAi5515.
NextBio21330.
PROP67775.
SOURCESearch...

Entry information

Entry namePP2AA_HUMAN
AccessionPrimary (citable) accession number: P67775
Secondary accession number(s): P05323, P13197
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 106 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

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 5

Human chromosome 5: entries, gene names and cross-references to MIM