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Q9UBK8 (MTRR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine synthase reductase
Short name=MSR
EC=1.16.1.8
Gene names
Name:MTRR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length725 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the reductive regeneration of cob(I)alamin (vitamin B12) cofactor required for the maintenance of methionine synthase in a functional state. Necessary for utilization of methylgroups from the folate cycle, thereby affecting transgenerational epigenetic inheritance. Folate pathway donates methyl groups necessary for cellular methylation and affects different pathways such as DNA methylation, possibly explaining the transgenerational epigenetic inheritance effects. Ref.8

Catalytic activity

2 [methionine synthase]-methylcob(I)alamin + 2 S-adenosylhomocysteine + NADP+ = 2 [methionine synthase]-cob(II)alamin + NADPH + 2 S-adenosyl-L-methionine. Ref.8

Cofactor

FAD. Ref.8

FMN. Ref.8

Subcellular location

Isoform B: Cytoplasm Ref.5.

Isoform C: Cytoplasm Ref.5.

Isoform A: Cytoplasm Ref.5.

Tissue specificity

Found in all tissues tested, particularly abundant in skeletal muscle.

Polymorphism

Variant Met-49 has been associated with an increased risk for spina bifida and may be associated with chromosomal non-disjunction and Down syndrome.

Involvement in disease

Homocystinuria-megaloblastic anemia, cblE complementation type (HMAE) [MIM:236270]: 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. Cells from patients with HMAE fail to incorporate methyltetrahydrofolate into methionine in whole cells, but cell extracts show normal methionine synthase activity in the presence of a reducing agent.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.9

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.10 Ref.11 Ref.12

Sequence similarities

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Biophysicochemical properties

Kinetic parameters:

KM=2.89 µM for NADPH Ref.8

KM=3540 µM for NADH

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Methionine biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandFAD
Flavoprotein
FMN
NADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from sequence or structural similarity. Source: UniProtKB

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cobalamin metabolic process

Traceable author statement. Source: Reactome

folic acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

methionine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

methionine metabolic process

Traceable author statement Ref.2. Source: UniProtKB

methylation

Traceable author statement. Source: Reactome

oxidation-reduction process

Traceable author statement Ref.2. Source: UniProtKB

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_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement Ref.2. Source: UniProtKB

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionFMN binding

Traceable author statement Ref.2. Source: UniProtKB

NADP binding

Traceable author statement Ref.2. Source: UniProtKB

[methionine synthase] reductase activity

Traceable author statement Ref.8Ref.2. Source: UniProtKB

flavin adenine dinucleotide binding

Inferred from direct assay Ref.8. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen

Inferred from Biological aspect of Ancestor. Source: RefGenome

oxidoreductase activity, oxidizing metal ions, NAD or NADP as acceptor

Inferred from direct assay Ref.8. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9UBK8-1)

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 B (identifier: Q9UBK8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.
Isoform C (identifier: Q9UBK8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: Missing.
     71-85: YDLKTETAPLVVVVS → VSVIQNTPTFAMGGR
     86-725: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 725725Methionine synthase reductase
PRO_0000021785

Regions

Domain32 – 174143Flavodoxin-like
Domain298 – 560263FAD-binding FR-type
Nucleotide binding120 – 15132FMN By similarity
Nucleotide binding478 – 4814FAD
Nucleotide binding514 – 5174FAD
Nucleotide binding637 – 6382NADP
Nucleotide binding651 – 6533NADP
Region193 – 27482Hinge

Sites

Binding site3181NADP
Binding site6861NADP
Binding site7241FAD

Amino acid modifications

Modified residue1981Phosphoserine Ref.6

Natural variations

Alternative sequence1 – 2727Missing in isoform B and isoform C.
VSP_003910
Alternative sequence71 – 8515YDLKT…VVVVS → VSVIQNTPTFAMGGR in isoform C.
VSP_003911
Alternative sequence86 – 725640Missing in isoform C.
VSP_003912
Natural variant491I → M May be associated with susceptibility to folate-sensitive NTD. Ref.10 Ref.11 Ref.12
Corresponds to variant rs1801394 [ dbSNP | Ensembl ].
VAR_012836
Natural variant811Missing in HMAE. Ref.9
VAR_012837
Natural variant831V → M in HMAE. Ref.9
VAR_012838
Natural variant1561A → T in HMAE. Ref.9
VAR_012839
Natural variant2021S → L. Ref.1 Ref.2 Ref.12
Corresponds to variant rs1532268 [ dbSNP | Ensembl ].
VAR_034595
Natural variant2841S → T.
Corresponds to variant rs2303080 [ dbSNP | Ensembl ].
VAR_034596
Natural variant3601L → V. Ref.9
Corresponds to variant rs10064631 [ dbSNP | Ensembl ].
VAR_012840
Natural variant3771K → R. Ref.12
Corresponds to variant rs162036 [ dbSNP | Ensembl ].
VAR_034597
Natural variant4321C → R in HMAE. Ref.9
VAR_012841
Natural variant4421R → C.
Corresponds to variant rs2287780 [ dbSNP | Ensembl ].
VAR_034598
Natural variant4771P → R.
Corresponds to variant rs16879334 [ dbSNP | Ensembl ].
VAR_034599
Natural variant5141G → R in HMAE. Ref.9
VAR_012842
Natural variant5421A → V.
Corresponds to variant rs16879355 [ dbSNP | Ensembl ].
VAR_056947
Natural variant5811G → R in HMAE. Ref.9
VAR_015731
Natural variant6031Missing in HMAE. Ref.2
VAR_012843
Natural variant6221H → Y.
Corresponds to variant rs10380 [ dbSNP | Ensembl ].
VAR_014944

Secondary structure

1 ...................................................................... 725
Helix Strand Turn

Details...

Sequences

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

Last modified May 18, 2010. Version 3.
Checksum: C3EF82DAC388BAF1

FASTA72580,410
        10         20         30         40         50         60 
MGAASVRAGA RLVEVALCSF TVTCLEVMRR FLLLYATQQG QAKAIAEEIC EQAVVHGFSA 

        70         80         90        100        110        120 
DLHCISESDK YDLKTETAPL VVVVSTTGTG DPPDTARKFV KEIQNQTLPV DFFAHLRYGL 

       130        140        150        160        170        180 
LGLGDSEYTY FCNGGKIIDK RLQELGARHF YDTGHADDCV GLELVVEPWI AGLWPALRKH 

       190        200        210        220        230        240 
FRSSRGQEEI SGALPVASPA SSRTDLVKSE LLHIESQVEL LRFDDSGRKD SEVLKQNAVN 

       250        260        270        280        290        300 
SNQSNVVIED FESSLTRSVP PLSQASLNIP GLPPEYLQVH LQESLGQEES QVSVTSADPV 

       310        320        330        340        350        360 
FQVPISKAVQ LTTNDAIKTT LLVELDISNT DFSYQPGDAF SVICPNSDSE VQSLLQRLQL 

       370        380        390        400        410        420 
EDKREHCVLL KIKADTKKKG ATLPQHIPAG CSLQFIFTWC LEIRAIPKKA FLRALVDYTS 

       430        440        450        460        470        480 
DSAEKRRLQE LCSKQGAADY SRFVRDACAC LLDLLLAFPS CQPPLSLLLE HLPKLQPRPY 

       490        500        510        520        530        540 
SCASSSLFHP GKLHFVFNIV EFLSTATTEV LRKGVCTGWL ALLVASVLQP NIHASHEDSG 

       550        560        570        580        590        600 
KALAPKISIS PRTTNSFHLP DDPSIPIIMV GPGTGIAPFI GFLQHREKLQ EQHPDGNFGA 

       610        620        630        640        650        660 
MWLFFGCRHK DRDYLFRKEL RHFLKHGILT HLKVSFSRDA PVGEEEAPAK YVQDNIQLHG 

       670        680        690        700        710        720 
QQVARILLQE NGHIYVCGDA KNMAKDVHDA LVQIISKEVG VEKLEAMKTL ATLKEEKRYL 


QDIWS

« Hide

Isoform B [UniParc].

Checksum: D4B394F0B24A07E5
Show »

FASTA69877,674
Isoform C [UniParc].

Checksum: 5FDB3101DE6A9453
Show »

FASTA586,368

References

« Hide 'large scale' references
[1]"Molecular cloning, expression and physical mapping of the human methionine synthase reductase gene."
Leclerc D., Odievre M.-H., Wu Q., Wilson A., Huizenga J., Rozen R., Scherer S.W., Gravel R.A.
Gene 240:75-88(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A; B AND C), VARIANT LEU-202.
[2]"Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria."
Leclerc D., Wilson A., Dumas R., Gafuik C., Song D., Watkins D., Heng H.H.Q., Rommens J.M., Scherer S.W., Rosenblatt D.S., Gravel R.A.
Proc. Natl. Acad. Sci. U.S.A. 95:3059-3064(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), VARIANT LEU-202, VARIANT HMAE LEU-603 DEL.
[3]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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] (ISOFORMS A AND B).
Tissue: Lung.
[5]"Restricted role for methionine synthase reductase defined by subcellular localization."
Froese D.S., Wu X., Zhang J., Dumas R., Schoel W.M., Amrein M., Gravel R.A.
Mol. Genet. Metab. 94:68-77(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION (ISOFORM A).
[6]"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-198, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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]"Mechanism of coenzyme binding to human methionine synthase reductase revealed through the crystal structure of the FNR-like module and isothermal titration calorimetry."
Wolthers K.R., Lou X., Toogood H.S., Leys D., Scrutton N.S.
Biochemistry 46:11833-11844(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 192-725 IN COMPLEX WITH FAD AND NADP, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, FUNCTION.
[9]"Molecular basis for methionine synthase reductase deficiency in patients belonging to the cblE complementation group of disorders in folate/cobalamin metabolism."
Wilson A., Leclerc D., Rosenblatt D.S., Gravel R.A.
Hum. Mol. Genet. 8:2009-2016(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HMAE VAL-81 DEL; MET-83; THR-156; ARG-432; ARG-514 AND ARG-581, VARIANT VAL-360.
[10]"A common variant in methionine synthase reductase combined with low cobalamin (vitamin B12) increases risk for spina bifida."
Wilson A., Platt R., Wu Q., Leclerc D., Christensen B., Yang H., Gravel R.A., Rozen R.
Mol. Genet. Metab. 67:317-323(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION OF VARIANT MET-49 WITH SUSCEPTIBILITY TO FS-NTD.
[11]"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 MET-49 WITH SUSCEPTIBILITY TO FS-NTD.
[12]"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 VARIANTS MET-49; LEU-202 AND ARG-377 WITH SUSCEPTIBILITY TO FS-NTD.
+Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF121213 expand/collapse EMBL AC list , AF121202, AF121203, AF121204, AF121205, AF121206, AF121207, AF121208, AF121209, AF121210, AF121211, AF121212 Genomic DNA. Translation: AAF17303.1.
AF121214 mRNA. Translation: AAF16876.1.
AF121213 expand/collapse EMBL AC list , AF121202, AF121203, AF121204, AF121205, AF121206, AF121207, AF121208, AF121209, AF121210, AF121211, AF121212 Genomic DNA. Translation: AAF17304.1.
AF025794 mRNA. Translation: AAC39667.1.
AC010346 Genomic DNA. No translation available.
AC025174 Genomic DNA. No translation available.
BC054816 mRNA. Translation: AAH54816.2.
BC109216 mRNA. Translation: AAI09217.1.
RefSeqNP_002445.2. NM_002454.2.
NP_076915.2. NM_024010.2.
UniGeneHs.481551.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QTLX-ray1.90A192-725[»]
2QTZX-ray1.90A192-725[»]
ProteinModelPortalQ9UBK8.
SMRQ9UBK8. Positions 29-725.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110645. 5 interactions.
STRING9606.ENSP00000264668.

Chemistry

DrugBankDB00115. Cyanocobalamin.
DB00200. Hydroxocobalamin.
DB00134. L-Methionine.

PTM databases

PhosphoSiteQ9UBK8.

Polymorphism databases

DMDM296439300.

Proteomic databases

PaxDbQ9UBK8.
PRIDEQ9UBK8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264668; ENSP00000264668; ENSG00000124275. [Q9UBK8-1]
ENST00000341013; ENSP00000341918; ENSG00000124275. [Q9UBK8-3]
ENST00000440940; ENSP00000402510; ENSG00000124275. [Q9UBK8-2]
ENST00000510279; ENSP00000427200; ENSG00000124275. [Q9UBK8-3]
ENST00000514369; ENSP00000426132; ENSG00000124275. [Q9UBK8-3]
GeneID4552.
KEGGhsa:4552.
UCSCuc003jed.3. human. [Q9UBK8-1]

Organism-specific databases

CTD4552.
GeneCardsGC05P007851.
H-InvDBHIX0031952.
HGNCHGNC:7473. MTRR.
HPAHPA038113.
MIM236270. phenotype.
601634. phenotype.
602568. gene.
neXtProtNX_Q9UBK8.
Orphanet2169. Methylcobalamin deficiency type cblE.
PharmGKBPA31277.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHOG000007485.
HOVERGENHBG108376.
InParanoidQ9UBK8.
KOK00597.
OMAPSCQPPL.
OrthoDBEOG7NCV31.
PhylomeDBQ9UBK8.
TreeFamTF105716.

Enzyme and pathway databases

BioCycMetaCyc:HS04756-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ9UBK8.

Gene expression databases

ArrayExpressQ9UBK8.
BgeeQ9UBK8.
CleanExHS_MTRR.
GenevestigatorQ9UBK8.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UBK8.
GeneWikiMTRR_(gene).
GenomeRNAi4552.
NextBio17541.
PROQ9UBK8.
SOURCESearch...

Entry information

Entry nameMTRR_HUMAN
AccessionPrimary (citable) accession number: Q9UBK8
Secondary accession number(s): O60471, Q32MA9, Q7Z4M8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 137 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

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

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