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Q99707 (METH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine synthase

EC=2.1.1.13
Alternative name(s):
5-methyltetrahydrofolate--homocysteine methyltransferase
Vitamin-B12 dependent methionine synthase
Short name=MS
Gene names
Name:MTR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1265 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate By similarity.

Catalytic activity

5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine.

Cofactor

Methylcobalamin (MeCBL).

Binds 1 zinc ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.

Subcellular location

Cytoplasm.

Tissue specificity

Widely expressed. Expressed at the highest levels in pancreas, heart, brain, skeletal muscle and placenta. Expressed at lower levels in lung, liver and kidney.

Domain

Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin By similarity.

Involvement in disease

Homocystinuria-megaloblastic anemia, cblG complementation type (HMAG) [MIM:250940]: An autosomal recessive inborn error of metabolism resulting from defects in the cobalamin-dependent pathway that converts homocysteine to methionine. It causes delayed psychomotor development, megaloblastic anemia, homocystinuria, and hypomethioninemia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.8

Folate-sensitive neural tube defects (FS-NTD) [MIM:601634]: The most common NTDs are open spina bifida (myelomeningocele) and anencephaly.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.9 Ref.10

Miscellaneous

L-homocysteine is bound via the zinc atom By similarity.

Sequence similarities

Belongs to the vitamin-B12 dependent methionine synthase family.

Contains 1 AdoMet activation domain.

Contains 1 B12-binding domain.

Contains 1 B12-binding N-terminal domain.

Contains 1 Hcy-binding domain.

Contains 1 pterin-binding domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Methionine biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainRepeat
   LigandCobalamin
Cobalt
Metal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cobalamin metabolic process

Traceable author statement. Source: Reactome

methylation

Traceable author statement. Source: Reactome

nervous system development

Traceable author statement Ref.1. Source: ProtInc

pteridine-containing compound metabolic process

Inferred from electronic annotation. Source: InterPro

small molecule metabolic process

Traceable author statement. Source: Reactome

sulfur amino acid metabolic process

Traceable author statement. Source: Reactome

vitamin metabolic process

Traceable author statement. Source: Reactome

water-soluble vitamin metabolic process

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionS-adenosylmethionine-homocysteine S-methyltransferase activity

Inferred from electronic annotation. Source: InterPro

cobalamin binding

Inferred from electronic annotation. Source: UniProtKB-KW

methionine synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TSC22D1Q157141EBI-1045782,EBI-712609

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12651265Methionine synthase
PRO_0000204530

Regions

Domain19 – 338320Hcy-binding
Domain371 – 632262Pterin-binding
Domain662 – 75998B12-binding N-terminal
Domain772 – 907136B12-binding
Domain923 – 1265343AdoMet activation
Region860 – 8612Cobalamin-binding By similarity
Region1227 – 12282S-adenosyl-L-methionine binding By similarity

Sites

Metal binding2601Zinc By similarity
Metal binding3231Zinc By similarity
Metal binding3241Zinc By similarity
Metal binding7851Cobalt (cobalamin axial ligand) By similarity
Binding site8301Cobalamin By similarity
Binding site9741S-adenosyl-L-methionine By similarity
Binding site11721S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site11761Cobalamin; via carbonyl oxygen By similarity

Natural variations

Natural variant521R → Q.
Corresponds to variant rs12749581 [ dbSNP | Ensembl ].
VAR_050033
Natural variant611R → K. Ref.8
VAR_004326
Natural variant2551C → Y. Ref.3
VAR_004327
Natural variant3141D → N.
Corresponds to variant rs2229274 [ dbSNP | Ensembl ].
VAR_061338
Natural variant8811Missing in HMAG. Ref.1 Ref.8
VAR_004328
Natural variant9191D → G May be associated with susceptibility to FS-NTD. Ref.3 Ref.6 Ref.9 Ref.10
Corresponds to variant rs1805087 [ dbSNP | Ensembl ].
VAR_004329
Natural variant9201H → D in HMAG. Ref.1
Corresponds to variant rs28933097 [ dbSNP | Ensembl ].
VAR_004330
Natural variant11731P → L in HMAG. Ref.8
VAR_004331

Secondary structure

................................................................................................................................................ 1265
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99707 [UniParc].

Last modified July 1, 1997. Version 2.
Checksum: B04C26BCBE9A57C2

FASTA1,265140,527
        10         20         30         40         50         60 
MSPALQDLSQ PEGLKKTLRD EINAILQKRI MVLDGGMGTM IQREKLNEEH FRGQEFKDHA 

        70         80         90        100        110        120 
RPLKGNNDIL SITQPDVIYQ IHKEYLLAGA DIIETNTFSS TSIAQADYGL EHLAYRMNMC 

       130        140        150        160        170        180 
SAGVARKAAE EVTLQTGIKR FVAGALGPTN KTLSVSPSVE RPDYRNITFD ELVEAYQEQA 

       190        200        210        220        230        240 
KGLLDGGVDI LLIETIFDTA NAKAALFALQ NLFEEKYAPR PIFISGTIVD KSGRTLSGQT 

       250        260        270        280        290        300 
GEGFVISVSH GEPLCIGLNC ALGAAEMRPF IEIIGKCTTA YVLCYPNAGL PNTFGDYDET 

       310        320        330        340        350        360 
PSMMAKHLKD FAMDGLVNIV GGCCGSTPDH IREIAEAVKN CKPRVPPATA FEGHMLLSGL 

       370        380        390        400        410        420 
EPFRIGPYTN FVNIGERCNV AGSRKFAKLI MAGNYEEALC VAKVQVEMGA QVLDVNMDDG 

       430        440        450        460        470        480 
MLDGPSAMTR FCNLIASEPD IAKVPLCIDS SNFAVIEAGL KCCQGKCIVN SISLKEGEDD 

       490        500        510        520        530        540 
FLEKARKIKK YGAAMVVMAF DEEGQATETD TKIRVCTRAY HLLVKKLGFN PNDIIFDPNI 

       550        560        570        580        590        600 
LTIGTGMEEH NLYAINFIHA TKVIKETLPG ARISGGLSNL SFSFRGMEAI REAMHGVFLY 

       610        620        630        640        650        660 
HAIKSGMDMG IVNAGNLPVY DDIHKELLQL CEDLIWNKDP EATEKLLRYA QTQGTGGKKV 

       670        680        690        700        710        720 
IQTDEWRNGP VEERLEYALV KGIEKHIIED TEEARLNQKK YPRPLNIIEG PLMNGMKIVG 

       730        740        750        760        770        780 
DLFGAGKMFL PQVIKSARVM KKAVGHLIPF MEKEREETRV LNGTVEEEDP YQGTIVLATV 

       790        800        810        820        830        840 
KGDVHDIGKN IVGVVLGCNN FRVIDLGVMT PCDKILKAAL DHKADIIGLS GLITPSLDEM 

       850        860        870        880        890        900 
IFVAKEMERL AIRIPLLIGG ATTSKTHTAV KIAPRYSAPV IHVLDASKSV VVCSQLLDEN 

       910        920        930        940        950        960 
LKDEYFEEIM EEYEDIRQDH YESLKERRYL PLSQARKSGF QMDWLSEPHP VKPTFIGTQV 

       970        980        990       1000       1010       1020 
FEDYDLQKLV DYIDWKPFFD VWQLRGKYPN RGFPKIFNDK TVGGEARKVY DDAHNMLNTL 

      1030       1040       1050       1060       1070       1080 
ISQKKLRARG VVGFWPAQSI QDDIHLYAEA AVPQAAEPIA TFYGLRQQAE KDSASTEPYY 

      1090       1100       1110       1120       1130       1140 
CLSDFIAPLH SGIRDYLGLF AVACFGVEEL SKAYEDDGDD YSSIMVKALG DRLAEAFAEE 

      1150       1160       1170       1180       1190       1200 
LHERVRRELW AYCGSEQLDV ADLRRLRYKG IRPAPGYPSQ PDHTEKLTMW RLADIEQSTG 

      1210       1220       1230       1240       1250       1260 
IRLTESLAMA PASAVSGLYF SNLKSKYFAV GKISKDQVED YALRKNISVA EVEKWLGPIL 


GYDTD 

« Hide

References

« Hide 'large scale' references
[1]"Human methionine synthase: cDNA cloning and identification of mutations in patients of the cblG complementation group of folate/cobalamin disorders."
Leclerc D., Campeau E., Goyette P., Adjalla C.E., Christensen B., Ross M., Eydoux P., Rosenblatt D.S., Rozen R., Gravel R.A.
Hum. Mol. Genet. 5:1867-1874(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HMAG ILE-881 DEL AND ASP-920.
Tissue: Fibroblast.
[2]"Cloning, mapping and RNA analysis of the human methionine synthase gene."
Li Y.N., Gulati S., Baker P.J., Brody L.C., Banerjee R., Kruger W.D.
Hum. Mol. Genet. 5:1851-1858(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Human methionine synthase. cDNA cloning, gene localization, and expression."
Chen L.H., Liu M.-L., Hwang H.-Y., Chen L.-S., Korenberg J., Shane B.
J. Biol. Chem. 272:3628-3634(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS TYR-255 AND GLY-919.
Tissue: Fetal liver.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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], VARIANT GLY-919.
Tissue: Testis.
[7]"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].
[8]"Defects in human methionine synthase in cblG patients."
Gulati S., Baker P.J., Li Y.N., Fowler B., Kruger W.D., Brody L.C., Banerjee R.
Hum. Mol. Genet. 5:1859-1865(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HMAG ILE-881 DEL AND LEU-1173, VARIANT LYS-61.
[9]"Maternal genetic effects, exerted by genes involved in homocysteine remethylation, influence the risk of spina bifida."
Doolin M.-T., Barbaux S., McDonnell M., Hoess K., Whitehead A.S., Mitchell L.E.
Am. J. Hum. Genet. 71:1222-1226(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF VARIANT GLY-919 WITH SUSCEPTIBILITY TO FS-NTD.
[10]"Analysis of methionine synthase reductase polymorphisms for neural tube defects risk association."
O'Leary V.B., Mills J.L., Pangilinan F., Kirke P.N., Cox C., Conley M., Weiler A., Peng K., Shane B., Scott J.M., Parle-McDermott A., Molloy A.M., Brody L.C.
Mol. Genet. Metab. 85:220-227(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NO ASSOCIATION OF VARIANT GLY-919 WITH SUSCEPTIBILITY TO FS-NTD.
+Additional computationally mapped references.

Web resources

Wikipedia

5-methyltetrahydrofolate-homocysteine methyltransferase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U71285 mRNA. Translation: AAC51188.1.
U75743 mRNA. Translation: AAB58906.1.
U73338 mRNA. Translation: AAB39704.1.
AL359185, AL359259 Genomic DNA. Translation: CAH73198.1.
AL359259, AL359185 Genomic DNA. Translation: CAH70983.1.
CH471098 Genomic DNA. Translation: EAW70066.1.
BC130616 mRNA. Translation: AAI30617.1.
BC136440 mRNA. Translation: AAI36441.1.
CCDSCCDS1614.1.
RefSeqNP_000245.2. NM_000254.2.
NP_001278869.1. NM_001291940.1.
UniGeneHs.498187.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O2KX-ray1.60A/B925-1265[»]
4CCZX-ray2.70A16-657[»]
ProteinModelPortalQ99707.
SMRQ99707. Positions 17-651, 665-920, 926-1264.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110642. 17 interactions.
IntActQ99707. 2 interactions.
STRING9606.ENSP00000355536.

Chemistry

ChEMBLCHEMBL2150844.
DrugBankDB00200. Hydroxocobalamin.
DB00134. L-Methionine.
DB00116. Tetrahydrofolic acid.

PTM databases

PhosphoSiteQ99707.

Polymorphism databases

DMDM2842762.

Proteomic databases

MaxQBQ99707.
PaxDbQ99707.
PRIDEQ99707.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366577; ENSP00000355536; ENSG00000116984.
GeneID4548.
KEGGhsa:4548.
UCSCuc001hyi.4. human.

Organism-specific databases

CTD4548.
GeneCardsGC01P236958.
GeneReviewsMTR.
HGNCHGNC:7468. MTR.
HPAHPA044474.
MIM156570. gene.
250940. phenotype.
601634. phenotype.
603174. phenotype.
neXtProtNX_Q99707.
Orphanet2170. Methylcobalamin deficiency type cblG.
PharmGKBPA31272.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1410.
HOGENOMHOG000251409.
HOVERGENHBG006347.
InParanoidQ99707.
KOK00548.
OMAKAQPMVT.
OrthoDBEOG7TF786.
PhylomeDBQ99707.
TreeFamTF312829.

Enzyme and pathway databases

BioCycMetaCyc:HS04076-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00051; UER00081.

Gene expression databases

ArrayExpressQ99707.
BgeeQ99707.
CleanExHS_MTR.
GenevestigatorQ99707.

Family and domain databases

Gene3D1.10.1240.10. 1 hit.
3.10.196.10. 1 hit.
3.20.20.20. 1 hit.
3.20.20.330. 1 hit.
3.40.50.280. 1 hit.
InterProIPR003759. Cbl-bd_cap.
IPR006158. Cobalamin-bd.
IPR011005. Dihydropteroate_synth-like.
IPR011822. MetH.
IPR000489. Pterin-binding.
IPR003726. S_MeTrfase.
IPR004223. VitB12-dep_Met_synth_activ_dom.
[Graphical view]
PfamPF02310. B12-binding. 1 hit.
PF02607. B12-binding_2. 1 hit.
PF02965. Met_synt_B12. 1 hit.
PF00809. Pterin_bind. 1 hit.
PF02574. S-methyl_trans. 1 hit.
[Graphical view]
PIRSFPIRSF000381. MetH. 1 hit.
SMARTSM01018. B12-binding_2. 1 hit.
[Graphical view]
SUPFAMSSF47644. SSF47644. 1 hit.
SSF51717. SSF51717. 1 hit.
SSF52242. SSF52242. 1 hit.
SSF56507. SSF56507. 1 hit.
SSF82282. SSF82282. 1 hit.
TIGRFAMsTIGR02082. metH. 1 hit.
PROSITEPS50974. ADOMET_ACTIVATION. 1 hit.
PS51332. B12_BINDING. 1 hit.
PS51337. B12_BINDING_NTER. 1 hit.
PS50970. HCY. 1 hit.
PS50972. PTERIN_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMTR. human.
EvolutionaryTraceQ99707.
GeneWikiMethionine_synthase.
GenomeRNAi4548.
NextBio17533.
PROQ99707.
SOURCESearch...

Entry information

Entry nameMETH_HUMAN
AccessionPrimary (citable) accession number: Q99707
Secondary accession number(s): A1L4N8 expand/collapse secondary AC list , A9Z1W4, B9EGF7, Q99713, Q99723
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 149 of the entry and version 2 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 1

Human chromosome 1: entries, gene names and cross-references to MIM