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P21953 (ODBB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-oxoisovalerate dehydrogenase subunit beta, mitochondrial

EC=1.2.4.4
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase E1 component beta chain
Short name=BCKDE1B
Short name=BCKDH E1-beta
Gene names
Name:BCKDHB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activity

3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.

Subunit structure

Heterotetramer of 2 alpha and 2 beta chains.

Subcellular location

Mitochondrion matrix.

Involvement in disease

Maple syrup urine disease 1B (MSUD1B) [MIM:248600]: A metabolic disorder due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. Accumulation of these 3 amino acids and their corresponding keto acids leads to encephalopathy and progressive neurodegeneration. Clinical features include mental and physical retardation, feeding problems, and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine. If untreated, maple syrup urine disease can lead to seizures, coma, and death. The disease is often classified by its pattern of signs and symptoms. The most common and severe form of the disease is the classic type, which becomes apparent soon after birth. Variant forms of the disorder become apparent later in infancy or childhood and are typically milder, but they still involve developmental delay and other medical problems if not treated.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Maple syrup urine disease
   DomainTransit peptide
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbranched-chain amino acid catabolic process

Inferred from mutant phenotype PubMed 2022752. Source: HGNC

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial alpha-ketoglutarate dehydrogenase complex

Inferred from mutant phenotype PubMed 2022752. Source: HGNC

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from mutant phenotype PubMed 2022752. Source: HGNC

   Molecular_function3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity

Traceable author statement Ref.1. Source: ProtInc

alpha-ketoacid dehydrogenase activity

Inferred from electronic annotation. Source: Ensembl

carboxy-lyase activity

Traceable author statement PubMed 11839747. Source: HGNC

protein binding

Inferred from physical interaction PubMed 10745006PubMed 12902323PubMed 15166214PubMed 15576032. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCKDHAP1269414EBI-1029067,EBI-1029053

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5050Mitochondrion
Chain51 – 3923422-oxoisovalerate dehydrogenase subunit beta, mitochondrial
PRO_0000020470

Amino acid modifications

Modified residue2321N6-acetyllysine By similarity
Modified residue2411N6-acetyllysine Ref.10

Natural variations

Natural variant411T → I.
Corresponds to variant rs35470366 [ dbSNP | Ensembl ].
VAR_050437
Natural variant1701R → H in MSUD1B. Ref.14
VAR_068348
Natural variant1831R → P in MSUD1B. Ref.13
Corresponds to variant rs28934895 [ dbSNP | Ensembl ].
VAR_024851
Natural variant2061H → R in MSUD1B. Ref.12
VAR_004974
Natural variant2781G → S in MSUD1B. Ref.13
VAR_024852
Natural variant3461Q → R in MSUD1B. Ref.14
VAR_068349

Experimental info

Sequence conflict20 – 234EGHW → RLPP Ref.8
Sequence conflict3221T → S in CAA36685. Ref.8

Secondary structure

................................................................... 392
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21953 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: D78097834D063BB7

FASTA39243,122
        10         20         30         40         50         60 
MAVVAAAAGW LLRLRAAGAE GHWRRLPGAG LARGFLHPAA TVEDAAQRRQ VAHFTFQPDP 

        70         80         90        100        110        120 
EPREYGQTQK MNLFQSVTSA LDNSLAKDPT AVIFGEDVAF GGVFRCTVGL RDKYGKDRVF 

       130        140        150        160        170        180 
NTPLCEQGIV GFGIGIAVTG ATAIAEIQFA DYIFPAFDQI VNEAAKYRYR SGDLFNCGSL 

       190        200        210        220        230        240 
TIRSPWGCVG HGALYHSQSP EAFFAHCPGI KVVIPRSPFQ AKGLLLSCIE DKNPCIFFEP 

       250        260        270        280        290        300 
KILYRAAAEE VPIEPYNIPL SQAEVIQEGS DVTLVAWGTQ VHVIREVASM AKEKLGVSCE 

       310        320        330        340        350        360 
VIDLRTIIPW DVDTICKSVI KTGRLLISHE APLTGGFASE ISSTVQEECF LNLEAPISRV 

       370        380        390 
CGYDTPFPHI FEPFYIPDKW KCYDALRKMI NY 

« Hide

References

« Hide 'large scale' references
[1]"Maple syrup urine disease. Complete primary structure of the E1 beta subunit of human branched chain alpha-ketoacid dehydrogenase complex deduced from the nucleotide sequence and a gene analysis of patients with this disease."
Matsuda I., Asaka J., Akaboshi I., Endo F., Mitsubuchi H., Nobukuni Y.
J. Clin. Invest. 86:242-247(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Maple syrup urine disease: the E1beta gene of human branched-chain alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR in one of the two E1beta mRNAs arises from intronic sequences."
Chuang J.L., Cox R.P., Chuang D.T.
Am. J. Hum. Genet. 58:1373-1377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[3]"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].
Tissue: Hippocampus.
[4]"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].
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton 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 (SEP-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].
Tissue: Eye.
[8]"Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex."
Chuang J.L., Cox R.P., Chuang D.T.
FEBS Lett. 262:305-309(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-392.
[9]"Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence."
Wynn R.M., Kochi H., Cox R.P., Chuang D.T.
Biochim. Biophys. Acta 1201:125-128(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-62.
[10]"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-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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].
[12]"Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex."
Nobukuni Y., Mitsubuchi H., Hayashida Y., Ohta K., Indo Y., Ichiba Y., Endo F., Matsuda I.
Biochim. Biophys. Acta 1225:64-70(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MSUD1B ARG-206.
[13]"Maple syrup urine disease: identification and carrier-frequency determination of a novel founder mutation in the Ashkenazi Jewish population."
Edelmann L., Wasserstein M.P., Kornreich R., Sansaricq C., Snyderman S.E., Diaz G.A.
Am. J. Hum. Genet. 69:863-868(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MSUD1B PRO-183 AND SER-278.
[14]"Two novel mutations in the BCKDHB gene (R170H, Q346R) cause the classic form of maple syrup urine disease (MSUD)."
Wang Y.P., Qi M.L., Li T.T., Zhao Y.J.
Gene 498:112-115(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MSUD1B HIS-170 AND ARG-346.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55575 mRNA. Translation: AAA51812.1.
D90391 Genomic DNA. Translation: BAA14389.1.
AK289977 mRNA. Translation: BAF82666.1.
BT020063 mRNA. Translation: AAV38866.1.
AL049696, AL391595 Genomic DNA. Translation: CAC36881.2.
AL391595, AL049696 Genomic DNA. Translation: CAI15049.1.
CH471051 Genomic DNA. Translation: EAW48696.1.
CH471051 Genomic DNA. Translation: EAW48697.1.
BC040139 mRNA. Translation: AAH40139.1.
U50708 mRNA. Translation: AAB16763.1.
X52446 mRNA. Translation: CAA36685.1.
CCDSCCDS4994.1.
PIRA37157.
RefSeqNP_000047.1. NM_000056.3.
NP_898871.1. NM_183050.2.
UniGeneHs.654441.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DTWX-ray2.70B51-392[»]
1OLSX-ray1.85B51-392[»]
1OLUX-ray1.90B51-392[»]
1OLXX-ray2.25B51-392[»]
1U5BX-ray1.83B51-392[»]
1V11X-ray1.95B51-392[»]
1V16X-ray1.90B51-392[»]
1V1MX-ray2.00B51-392[»]
1V1RX-ray1.80B51-392[»]
1WCIX-ray1.84B51-392[»]
1X7WX-ray1.73B51-392[»]
1X7XX-ray2.10B51-392[»]
1X7YX-ray1.57B51-392[»]
1X7ZX-ray1.72B51-392[»]
1X80X-ray2.00B51-392[»]
2BEUX-ray1.89B51-392[»]
2BEVX-ray1.80B51-392[»]
2BEWX-ray1.79B51-392[»]
2BFBX-ray1.77B51-392[»]
2BFCX-ray1.64B51-392[»]
2BFDX-ray1.39B51-392[»]
2BFEX-ray1.69B51-392[»]
2BFFX-ray1.46B51-392[»]
2J9FX-ray1.88B/D51-392[»]
ProteinModelPortalP21953.
SMRP21953. Positions 64-392.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107066. 2 interactions.
DIPDIP-6147N.
IntActP21953. 1 interaction.
MINTMINT-271857.
STRING9606.ENSP00000318351.

PTM databases

PhosphoSiteP21953.

Polymorphism databases

DMDM129034.

2D gel databases

REPRODUCTION-2DPAGEIPI00011276.

Proteomic databases

MaxQBP21953.
PaxDbP21953.
PeptideAtlasP21953.
PRIDEP21953.

Protocols and materials databases

DNASU594.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320393; ENSP00000318351; ENSG00000083123.
ENST00000356489; ENSP00000348880; ENSG00000083123.
GeneID594.
KEGGhsa:594.
UCSCuc003pjd.2. human.

Organism-specific databases

CTD594.
GeneCardsGC06P080873.
GeneReviewsBCKDHB.
HGNCHGNC:987. BCKDHB.
HPAHPA031580.
MIM248600. phenotype.
248611. gene.
neXtProtNX_P21953.
Orphanet268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
268184. Thiamine-responsive maple syrup urine disease.
PharmGKBPA25298.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0022.
HOGENOMHOG000281451.
HOVERGENHBG108210.
InParanoidP21953.
KOK00167.
OMADKHRCLA.
OrthoDBEOG79SDXF.
PhylomeDBP21953.
TreeFamTF105947.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12006.
ReactomeREACT_111217. Metabolism.
SABIO-RKP21953.

Gene expression databases

ArrayExpressP21953.
BgeeP21953.
CleanExHS_BCKDHB.
GenevestigatorP21953.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProIPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetSearch...

Other

ChiTaRSBCKDHB. human.
EvolutionaryTraceP21953.
GeneWikiBCKDHB.
GenomeRNAi594.
NextBio2413.
PROP21953.
SOURCESearch...

Entry information

Entry nameODBB_HUMAN
AccessionPrimary (citable) accession number: P21953
Secondary accession number(s): Q9BQL0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 158 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

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 6

Human chromosome 6: entries, gene names and cross-references to MIM