Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P40394 (ADH7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase class 4 mu/sigma chain

EC=1.1.1.1
Alternative name(s):
Alcohol dehydrogenase class IV mu/sigma chain
Gastric alcohol dehydrogenase
Retinol dehydrogenase
Gene names
Name:ADH7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Could function in retinol oxidation for the synthesis of retinoic acid, a hormone important for cellular differentiation. Medium-chain (octanol) and aromatic (m-nitrobenzaldehyde) compounds are the best substrates. Ethanol is not a good substrate but at the high ethanol concentrations reached in the digestive tract, it plays a role in the ethanol oxidation and contributes to the first pass ethanol metabolism.

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

Preferentially expressed in stomach.

Miscellaneous

There are 7 different ADH's isozymes in human: three belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Class-IV subfamily.

Caution

It is uncertain whether Met-1 or Met-13 is the initiator.

Sequence caution

The sequence AAA19002.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAC51351.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAG35707.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA53960.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA53961.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processethanol catabolic process

Inferred from electronic annotation. Source: Ensembl

ethanol oxidation

Inferred from direct assay PubMed 10969996Ref.9. Source: UniProtKB

extracellular negative regulation of signal transduction

Inferred from direct assay PubMed 9600267. Source: GOC

fatty acid omega-oxidation

Inferred from direct assay PubMed 9600267. Source: UniProtKB

oxidation-reduction process

Inferred from direct assay Ref.9. Source: UniProtKB

response to bacterium

Inferred from direct assay PubMed 11410738. Source: UniProtKB

response to ethanol

Inferred from direct assay PubMed 9600267. Source: UniProtKB

retinoic acid metabolic process

Inferred from electronic annotation. Source: Ensembl

retinoid metabolic process

Inferred from direct assay PubMed 9600267. Source: UniProtKB

retinol metabolic process

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular region

Inferred from direct assay PubMed 9600267. Source: GOC

   Molecular_functionalcohol dehydrogenase (NAD) activity

Traceable author statement PubMed 8074657. Source: UniProtKB

alcohol dehydrogenase activity, zinc-dependent

Inferred from direct assay Ref.9. Source: UniProtKB

aldehyde oxidase activity

Inferred from direct assay PubMed 9600267. Source: UniProtKB

ethanol binding

Inferred from direct assay Ref.13. Source: UniProtKB

receptor antagonist activity

Inferred from direct assay PubMed 9600267. Source: UniProtKB

retinol binding

Inferred from direct assay Ref.13. Source: UniProtKB

retinol dehydrogenase activity

Inferred from direct assay PubMed 11997393Ref.9. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P40394-1)

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: P40394-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MFAEIQIQDKDRMGTAGK → MKCLVSRHTVRETLDMVFQRMSVEAG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 386386Alcohol dehydrogenase class 4 mu/sigma chain
PRO_0000160691

Regions

Nucleotide binding211 – 2166NAD
Nucleotide binding304 – 3063NAD

Sites

Metal binding591Zinc 1; catalytic
Metal binding801Zinc 1; catalytic
Metal binding1101Zinc 2
Metal binding1131Zinc 2
Metal binding1161Zinc 2
Metal binding1241Zinc 2
Metal binding1861Zinc 1; catalytic
Binding site2351NAD
Binding site2401NAD
Binding site3811NAD

Natural variations

Alternative sequence1 – 1818MFAEI…GTAGK → MKCLVSRHTVRETLDMVFQR MSVEAG in isoform 2.
VSP_043093
Natural variant921G → A.
Corresponds to variant rs1573496 [ dbSNP | Ensembl ].
VAR_024364

Experimental info

Sequence conflict91D → E in AAA19002. Ref.2
Sequence conflict321Q → R AA sequence Ref.11
Sequence conflict831T → R AA sequence Ref.11
Sequence conflict1101C → V in AAB38424. Ref.10
Sequence conflict150 – 1512HH → GR AA sequence Ref.11
Sequence conflict160 – 1612EY → VI in AAB38424. Ref.10
Sequence conflict1691V → E in AAB38424. Ref.10
Sequence conflict1751A → T in BAG35707. Ref.4
Sequence conflict2171L → V in AAB38424. Ref.10

Secondary structure

......................................................................... 386
Helix Strand Turn

Details...

Sequences

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

Last modified March 23, 2010. Version 2.
Checksum: E34C959778ED6817

FASTA38641,481
        10         20         30         40         50         60 
MFAEIQIQDK DRMGTAGKVI KCKAAVLWEQ KQPFSIEEIE VAPPKTKEVR IKILATGICR 

        70         80         90        100        110        120 
TDDHVIKGTM VSKFPVIVGH EATGIVESIG EGVTTVKPGD KVIPLFLPQC RECNACRNPD 

       130        140        150        160        170        180 
GNLCIRSDIT GRGVLADGTT RFTCKGKPVH HFMNTSTFTE YTVVDESSVA KIDDAAPPEK 

       190        200        210        220        230        240 
VCLIGCGFST GYGAAVKTGK VKPGSTCVVF GLGGVGLSVI MGCKSAGASR IIGIDLNKDK 

       250        260        270        280        290        300 
FEKAMAVGAT ECISPKDSTK PISEVLSEMT GNNVGYTFEV IGHLETMIDA LASCHMNYGT 

       310        320        330        340        350        360 
SVVVGVPPSA KMLTYDPMLL FTGRTWKGCV FGGLKSRDDV PKLVTEFLAK KFDLDQLITH 

       370        380 
VLPFKKISEG FELLNSGQSI RTVLTF 

« Hide

Isoform 2 [UniParc].

Checksum: 2EBC96FC412B6729
Show »

FASTA39442,467

References

« Hide 'large scale' references
[1]"Alcohol dehydrogenase of class IV (sigma sigma-ADH) from human stomach. cDNA sequence and structure/function relationships."
Farres J., Moreno A., Crosas B., Peralba J.M., Allali-Hassani A., Hjelmqvist L., Joernvall H., Pares X.
Eur. J. Biochem. 224:549-557(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Stomach.
[2]"The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene."
Satre M.A., Zgombic-Knight M., Duester G.
J. Biol. Chem. 269:15606-15612(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Stomach.
[3]"Genomic structure and expression of the ADH7 gene encoding human class IV alcohol dehydrogenase, the form most efficient for retinol metabolism in vitro."
Zgombic-Knight M., Foglio M.H., Duester G.
J. Biol. Chem. 270:4305-4311(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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] (ISOFORMS 1 AND 2).
Tissue: Esophagus and Trachea.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [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).
[8]"Molecular characterization of a class IV human alcohol dehydrogenase gene (ADH7)."
Yokoyama S., Matsuo Y., Ramsbotham R., Yokoyama R.
FEBS Lett. 351:411-415(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-386 (ISOFORM 1), ZINC-BINDING SITES.
Tissue: Stomach.
[9]"Expression and kinetic characterization of recombinant human stomach alcohol dehydrogenase. Active-site amino acid sequence explains substrate specificity compared with liver isozymes."
Kedishvili N.Y., Bosron W.F., Stone C.L., Hurley T.D., Peggs C.F., Thomasson H.R., Popov K.M., Carr L.G., Edenberg H.J., Li T.K.
J. Biol. Chem. 270:3625-3630(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-386 (ISOFORM 1).
Tissue: Stomach.
[10]"Molecular cloning and chromosomal localization of the ADH7 gene encoding human class IV (sigma) ADH."
Yokoyama H., Baraona E., Lieber C.S.
Genomics 31:243-245(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-386.
Tissue: Foreskin.
[11]"Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis of human sigma sigma-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class."
Pares X., Cederlund E., Moreno A., Saubi N., Hoeoeg J.-O., Joernvall H.
FEBS Lett. 303:69-72(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-33; 53-58; 74-92; 97-123; 147-154 AND 181-186.
[12]"Human stomach class IV alcohol dehydrogenase: molecular genetic analysis."
Cheung B., Anderson J.K., Holmes R.S., Beacham I.R.
Alcohol. Clin. Exp. Res. 19:185-186(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 239-311 (ISOFORM 1).
Tissue: Stomach.
[13]"X-ray structure of human class IV sigmasigma alcohol dehydrogenase. Structural basis for substrate specificity."
Xie P., Parsons S.H., Speckhard D.C., Bosron W.F., Hurley T.D.
J. Biol. Chem. 272:18558-18563(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 14-386.
[14]"Methionine-141 directly influences the binding of 4-methylpyrazole in human sigma sigma alcohol dehydrogenase."
Xie P.T., Hurley T.D.
Protein Sci. 8:2639-2644(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 14-386 IN COMPLEX WITH NAD AND ZINC IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76342 mRNA. Translation: CAA53961.1. Different initiation.
X76342 mRNA. Translation: CAA53960.1. Different initiation.
U07821 mRNA. Translation: AAA19002.1. Different initiation.
U16293 expand/collapse EMBL AC list , U16286, U16287, U16288, U16289, U16290, U16291, U16292 Genomic DNA. Translation: AAC51351.1. Different initiation.
AK301696 mRNA. Translation: BAG63168.1.
AK312854 mRNA. Translation: BAG35707.1. Different initiation.
AP001960 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX06101.1.
BC131512 mRNA. Translation: AAI31513.1.
L33179 mRNA. Translation: AAA59211.1.
U09623 mRNA. Translation: AAA82165.1.
L47166 Genomic DNA. Translation: AAB38424.1.
S77168 mRNA. Translation: AAB34478.1.
CCDSCCDS34034.1. [P40394-1]
CCDS54781.1. [P40394-2]
PIRDEHUAS. A55878.
RefSeqNP_000664.2. NM_000673.4. [P40394-1]
NP_001159976.1. NM_001166504.1. [P40394-2]
UniGeneHs.389.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AGNX-ray3.00A/B/C/D14-386[»]
1D1SX-ray2.50A/B/C/D14-386[»]
1D1TX-ray2.40A/B/C/D14-386[»]
ProteinModelPortalP40394.
SMRP40394. Positions 14-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106643. 3 interactions.
STRING9606.ENSP00000209665.

Chemistry

BindingDBP40394.
ChEMBLCHEMBL3867.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP40394.

Polymorphism databases

DMDM292495000.

Proteomic databases

PaxDbP40394.
PRIDEP40394.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000209665; ENSP00000209665; ENSG00000196344. [P40394-1]
ENST00000437033; ENSP00000414254; ENSG00000196344.
ENST00000476959; ENSP00000420269; ENSG00000196344. [P40394-2]
GeneID131.
KEGGhsa:131.
UCSCuc003huv.2. human. [P40394-1]
uc021xqj.1. human. [P40394-2]

Organism-specific databases

CTD131.
GeneCardsGC04M100333.
HGNCHGNC:256. ADH7.
HPAHPA039695.
MIM600086. gene.
neXtProtNX_P40394.
PharmGKBPA24577.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1062.
HOGENOMHOG000294674.
HOVERGENHBG000195.
KOK13951.
OMAPFKQINE.
OrthoDBEOG72NRQ6.
PhylomeDBP40394.
TreeFamTF300429.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP40394.
BgeeP40394.
CleanExHS_ADH7.
GenevestigatorP40394.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR028635. Zinc_ADH_IV.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PTHR11695:SF406. PTHR11695:SF406. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 2 hits.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP40394.
GeneWikiADH7.
GenomeRNAi131.
NextBio523.
PROP40394.
SOURCESearch...

Entry information

Entry nameADH7_HUMAN
AccessionPrimary (citable) accession number: P40394
Secondary accession number(s): A2RRB6 expand/collapse secondary AC list , A8MVN9, B2R760, B4DWV6, Q13713
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: March 23, 2010
Last modified: July 9, 2014
This is version 142 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

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 4

Human chromosome 4: entries, gene names and cross-references to MIM