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P54868 (HMCS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hydroxymethylglutaryl-CoA synthase, mitochondrial

Short name=HMG-CoA synthase
EC=2.3.3.10
Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase
Gene names
Name:HMGCS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.

Catalytic activity

Acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA.

Pathway

Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.

Subunit structure

Homodimer. Ref.11

Subcellular location

Mitochondrion.

Tissue specificity

Expression in liver is 200-fold higher than in any other tissue. Low expression in colon, kidney, testis, and pancreas. Very low expression in heart and skeletal muscle. Not detected in brain. The relative expression of isoform 3 (at mRNA level) is highest in heart (70%) and skeletal muscle (60%). Ref.1 Ref.9 Ref.10

Involvement in disease

HMG-CoA synthase deficiency (HMGCS deficiency) [MIM:605911]: Affected individuals present with severe hypoketotic hypoglycemia, mild hepatomegaly, or fatty liver, and a nondiagnostic pattern of urinary organic acids with increase of medium and short chain dicarboxylic acids.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the HMG-CoA synthase family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P54868-1)

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: P54868-2)

The sequence of this isoform differs from the canonical sequence as follows:
     187-228: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P54868-3)

Also known as: HMGCS2delta4;

The sequence of this isoform differs from the canonical sequence as follows:
     229-283: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Mitochondrion Probable
Chain38 – 508471Hydroxymethylglutaryl-CoA synthase, mitochondrial
PRO_0000013483

Sites

Active site1321Proton donor/acceptor Probable
Active site1661Nucleophile Ref.11
Active site3011Proton donor/acceptor Probable
Binding site801Substrate
Binding site2041Substrate
Binding site2581Substrate
Binding site3801Substrate

Amino acid modifications

Modified residue521N6-succinyllysine By similarity
Modified residue831N6-acetyllysine; alternate By similarity
Modified residue831N6-succinyllysine; alternate By similarity
Modified residue2211N6-succinyllysine By similarity
Modified residue2431N6-acetyllysine By similarity
Modified residue2561N6-acetyllysine; alternate By similarity
Modified residue2561N6-succinyllysine; alternate By similarity
Modified residue3061N6-acetyllysine By similarity
Modified residue3101N6-acetyllysine; alternate By similarity
Modified residue3101N6-succinyllysine; alternate By similarity
Modified residue3331N6-succinyllysine By similarity
Modified residue3421N6-acetyllysine; alternate By similarity
Modified residue3421N6-succinyllysine; alternate By similarity
Modified residue3501N6-acetyllysine; alternate By similarity
Modified residue3501N6-succinyllysine; alternate By similarity
Modified residue3541N6-acetyllysine; alternate By similarity
Modified residue3541N6-succinyllysine; alternate By similarity
Modified residue3581N6-acetyllysine; alternate By similarity
Modified residue3581N6-succinyllysine; alternate By similarity
Modified residue4371N6-acetyllysine By similarity
Modified residue4471N6-acetyllysine; alternate By similarity
Modified residue4471N6-succinyllysine; alternate By similarity
Modified residue4731N6-acetyllysine; alternate By similarity
Modified residue4731N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence187 – 22842Missing in isoform 2.
VSP_042892
Alternative sequence229 – 28355Missing in isoform 3.
VSP_047445
Natural variant541V → M in HMGCS deficiency. Ref.14
Corresponds to variant rs28937320 [ dbSNP | Ensembl ].
VAR_032757
Natural variant1671Y → C in HMGCS deficiency. Ref.14
VAR_032758
Natural variant1741F → L in HMGCS deficiency; reduced peptide level; no enzymatic activity. Ref.13
VAR_032711
Natural variant2121G → R in HMGCS deficiency. Ref.12
VAR_032759
Natural variant5001R → H in HMGCS deficiency. Ref.12
VAR_032760

Experimental info

Sequence conflict2341H → Y in CAG33131. Ref.3
Sequence conflict3851S → T in CAG33131. Ref.3

Secondary structure

................................................................................ 508
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1996. Version 1.
Checksum: BD362D631F7C3C80

FASTA50856,635
        10         20         30         40         50         60 
MQRLLTPVKR ILQLTRAVQE TSLTPARLLP VAHQRFSTAS AVPLAKTDTW PKDVGILALE 

        70         80         90        100        110        120 
VYFPAQYVDQ TDLEKYNNVE AGKYTVGLGQ TRMGFCSVQE DINSLCLTVV QRLMERIQLP 

       130        140        150        160        170        180 
WDSVGRLEVG TETIIDKSKA VKTVLMELFQ DSGNTDIEGI DTTNACYGGT ASLFNAANWM 

       190        200        210        220        230        240 
ESSSWDGRYA MVVCGDIAVY PSGNARPTGG AGAVAMLIGP KAPLALERGL RGTHMENVYD 

       250        260        270        280        290        300 
FYKPNLASEY PIVDGKLSIQ CYLRALDRCY TSYRKKIQNQ WKQAGSDRPF TLDDLQYMIF 

       310        320        330        340        350        360 
HTPFCKMVQK SLARLMFNDF LSASSDTQTS LYKGLEAFGG LKLEDTYTNK DLDKALLKAS 

       370        380        390        400        410        420 
QDMFDKKTKA SLYLSTHNGN MYTSSLYGCL ASLLSHHSAQ ELAGSRIGAF SYGSGLAASF 

       430        440        450        460        470        480 
FSFRVSQDAA PGSPLDKLVS STSDLPKRLA SRKCVSPEEF TEIMNQREQF YHKVNFSPPG 

       490        500 
DTNSLFPGTW YLERVDEQHR RKYARRPV 

« Hide

Isoform 2 [UniParc].

Checksum: 9D3C527559B74618
Show »

FASTA46652,482
Isoform 3 (HMGCS2delta4) [UniParc].

Checksum: 80C1D1EBB7403EC0
Show »

FASTA45350,050

References

« Hide 'large scale' references
[1]"Molecular cloning and tissue expression of human mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase."
Mascaro C., Buesa C., Ortiz J.A., Haro D., Hegardt F.G.
Arch. Biochem. Biophys. 317:385-390(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"Cloning and characterization of the human mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase gene."
Boukaftane Y., Mitchell G.A.
Gene 195:121-126(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[3]"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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"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] (ISOFORM 2).
Tissue: Liver.
[5]"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].
[6]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].
[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] (ISOFORM 1).
Tissue: Brain.
[8]"Human mitochondrial HMG CoA synthase: liver cDNA and partial genomic cloning, chromosome mapping to 1p12-p13, and possible role in vertebrate evolution."
Boukaftane Y., Duncan A., Wang S., Labuda D., Robert M.-F., Sarrazin J., Schappert K.T., Mitchell G.A.
Genomics 23:552-559(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-508 (ISOFORM 1).
Tissue: Liver.
[9]"Characterization of splice variants of the genes encoding human mitochondrial HMG-CoA lyase and HMG-CoA synthase, the main enzymes of the ketogenesis pathway."
Puisac B., Ramos M., Arnedo M., Menao S., Gil-Rodriguez M.C., Teresa-Rodrigo M.E., Pie A., de Karam J.C., Wesselink J.J., Gimenez I., Ramos F.J., Casals N., Gomez-Puertas P., Hegardt F.G., Pie J.
Mol. Biol. Rep. 39:4777-4785(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 91-316 (ISOFORM 3), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[10]"Ketogenic HMGCS2 Is a c-Myc target gene expressed in differentiated cells of human colonic epithelium and down-regulated in colon cancer."
Camarero N., Mascaro C., Mayordomo C., Vilardell F., Haro D., Marrero P.F.
Mol. Cancer Res. 4:645-653(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Crystal structures of human HMG-CoA synthase isoforms provide insights into inherited ketogenesis disorders and inhibitor design."
Shafqat N., Turnbull A., Zschocke J., Oppermann U., Yue W.W.
J. Mol. Biol. 398:497-506(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 51-508, SUBUNIT, ACTIVE SITE, SUBSTRATE-BINDING SITES.
[12]"Genetic basis of mitochondrial HMG-CoA synthase deficiency."
Aledo R., Zschocke J., Pie J., Mir C., Fiesel S., Mayatepek E., Hoffmann G.F., Casals N., Hegardt F.G.
Hum. Genet. 109:19-23(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HMGCS DEFICIENCY ARG-212 AND HIS-500.
[13]"Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase deficiency: clinical course and description of causal mutations in two patients."
Bouchard L., Robert M.-F., Vinarov D., Stanley C.A., Thompson G.N., Morris A., Leonard J.V., Quant P., Hsu B.Y.L., Boneh A., Boukaftane Y., Ashmarina L., Wang S., Miziorko H., Mitchell G.A.
Pediatr. Res. 49:326-331(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HMGCS DEFICIENCY LEU-174, CHARACTERIZATION OF VARIANT HMGCS DEFICIENCY LEU-174.
[14]"Mitochondrial HMG-CoA synthase deficiency: identification of two further patients carrying two novel mutations."
Wolf N.I., Rahman S., Clayton P.T., Zschocke J.
Eur. J. Pediatr. 162:279-280(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HMGCS DEFICIENCY MET-54 AND CYS-167.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83618 mRNA. Translation: CAA58593.1.
U81859 expand/collapse EMBL AC list , U81851, U81852, U81853, U81854, U81855, U81856, U81857, U81858 Genomic DNA. Translation: AAB72036.1.
CR456850 mRNA. Translation: CAG33131.1.
AK303777 mRNA. Translation: BAH14049.1.
AL589734 Genomic DNA. Translation: CAI22408.1.
CH471122 Genomic DNA. Translation: EAW56709.1.
BC044217 mRNA. Translation: AAH44217.1.
U12788 mRNA. Translation: AAA92673.1.
U12789 mRNA. Translation: AAA92674.1.
GU433940 mRNA. Translation: ADD21696.1.
PIRS71623.
RefSeqNP_001159579.1. NM_001166107.1.
NP_005509.1. NM_005518.3.
UniGeneHs.59889.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2WYAX-ray1.70A/B/C/D51-508[»]
ProteinModelPortalP54868.
SMRP54868. Positions 51-508.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109401. 3 interactions.
IntActP54868. 1 interaction.
STRING9606.ENSP00000358414.

PTM databases

PhosphoSiteP54868.

Polymorphism databases

DMDM1708234.

2D gel databases

REPRODUCTION-2DPAGEIPI00008934.

Proteomic databases

PaxDbP54868.
PeptideAtlasP54868.
PRIDEP54868.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369406; ENSP00000358414; ENSG00000134240. [P54868-1]
ENST00000544913; ENSP00000439495; ENSG00000134240. [P54868-2]
GeneID3158.
KEGGhsa:3158.
UCSCuc001eid.3. human. [P54868-1]
uc010oxj.2. human. [P54868-2]

Organism-specific databases

CTD3158.
GeneCardsGC01M120290.
H-InvDBHIX0160007.
HGNCHGNC:5008. HMGCS2.
HPAHPA027423.
HPA027442.
MIM600234. gene.
605911. phenotype.
neXtProtNX_P54868.
Orphanet35701. 3-hydroxy-3-methylglutaryl-CoA synthase deficiency.
PharmGKBPA29338.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3425.
HOGENOMHOG000012351.
HOVERGENHBG051912.
InParanoidP54868.
KOK01641.
OMAACFGLTA.
OrthoDBEOG741Z1W.
PhylomeDBP54868.
TreeFamTF105361.

Enzyme and pathway databases

BioCycMetaCyc:HS05836-MONOMER.
BRENDA2.3.3.10. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00058; UER00102.

Gene expression databases

BgeeP54868.
CleanExHS_HMGCS2.
GenevestigatorP54868.

Family and domain databases

Gene3D3.40.47.10. 1 hit.
InterProIPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMSSF53901. SSF53901. 3 hits.
TIGRFAMsTIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEPS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54868.
GenomeRNAi3158.
NextBio12510.
PROP54868.
SOURCESearch...

Entry information

Entry nameHMCS2_HUMAN
AccessionPrimary (citable) accession number: P54868
Secondary accession number(s): B7Z8R3 expand/collapse secondary AC list , D3Y5K6, Q5SZU2, Q6IBF4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 138 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

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